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Conserved domains on  [gi|1878746647|gb|KAF5928721|]
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hypothetical protein HPG69_016722, partial [Diceros bicornis minor]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
400-560 7.98e-94

NADH-quinone oxidoreductase subunit NuoI;


:

Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 287.16  E-value: 7.98e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 400 RAAQTLLWTELIRGLGMTLSYLFREPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAVCPAQAITIEAEPR 479
Cdd:PRK05888    3 QYLKSMLLKELLKGLGVTLKYFFKKKVTIQYPEEKLPLSPRFRGRHALRRDPNGEERCIACKLCAAICPADAITIEAAER 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 480 ADGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEELLYNKEKLLNNGDKWEAEITANIQADYLYRPKM 559
Cdd:PRK05888   83 EDGRRRTTRYDINFGRCIFCGFCEEACPTDAIVETPDFELATETREELIYDKEKLLANGDRVEREIAPGKAADANYRGEA 162


                  .
gi 1878746647 560 Q 560
Cdd:PRK05888  163 E 163
ALDH-SF super family cl11961
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
 17-283 3.14e-77

NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.


The actual alignment was detected with superfamily member cd07132:

Pssm-ID: 448367 [Multi-domain]  Cd Length: 443  Bit Score: 253.68  E-value: 3.14e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  17 QQQLAALGTDAQPWAQDWMSAV---------ELEVSEISIVQTEINLALRNLRAWMRDEQVRRNLATQLDSAFIRKEPFG 87
Cdd:cd07132    23 IQQLEALLRMLEENEDEIVEALakdlrkpkfEAVLSEILLVKNEIKYAISNLPEWMKPEPVKKNLATLLDDVYIYKEPLG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  88 LVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLPRYLDQ------AGGPPSglsgwgpsgalTVR 161
Cdd:cd07132   103 VVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKecypvvLGGVEE-----------TTE 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 162 LaellcrgagrargdraaagaqvrlhLLHRPSHLVQVieghsgflprpGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYV 241
Cdd:cd07132   172 L-------------------------LKQRFDYIFYT-----------GSTSVGKIVMQAAAKHLTPVTLELGGKSPCYV 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 242 DDNCDPQT------------------------------------------------------------------------ 249
Cdd:cd07132   216 DKSCDIDVaarriawgkfinagqtciapdyvlctpevqekfvealkktlkefygedpkespdygriindrhfqrlkklls 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 250 -------------------------------------------------------------------------VVEQVLA 256
Cdd:cd07132   296 ggkvaiggqtdekeryiaptvltdvkpsdpvmqeeifgpilpivtvnnldeaiefinsrekplalyvfsnnkkVINKILS 375

                         410       420
                  ....*....|....*....|....*..
gi 1878746647 257 RTSSGGFCGNDGFMHMTLPSLPFGGVG 283
Cdd:cd07132   376 NTSSGGVCVNDTIMHYTLDSLPFGGVG 402
ALDH-SF super family cl11961
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
 552-675 2.31e-70

NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.


The actual alignment was detected with superfamily member cd07132:

Pssm-ID: 448367 [Multi-domain]  Cd Length: 443  Bit Score: 235.58  E-value: 2.31e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 552 DY-LYRPKMQERLLPALQSAITRFYGEDPRSSPDLGRIINEKHFQRLQGLLGCGRVAIGGQSDESDRYIAPTVLVDVQET 630
Cdd:cd07132   244 DYvLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVLTDVKPS 323

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1878746647 631 EPVMQEEIFGPILPIVNVRSLDEAIDFIKRREKPLALYAFSNSNQ 675
Cdd:cd07132   324 DPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKK 368
 
Name Accession Description Interval E-value
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
400-560 7.98e-94

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 287.16  E-value: 7.98e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 400 RAAQTLLWTELIRGLGMTLSYLFREPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAVCPAQAITIEAEPR 479
Cdd:PRK05888    3 QYLKSMLLKELLKGLGVTLKYFFKKKVTIQYPEEKLPLSPRFRGRHALRRDPNGEERCIACKLCAAICPADAITIEAAER 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 480 ADGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEELLYNKEKLLNNGDKWEAEITANIQADYLYRPKM 559
Cdd:PRK05888   83 EDGRRRTTRYDINFGRCIFCGFCEEACPTDAIVETPDFELATETREELIYDKEKLLANGDRVEREIAPGKAADANYRGEA 162


                  .
gi 1878746647 560 Q 560
Cdd:PRK05888  163 E 163
ALDH_F3AB cd07132
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ...
 17-283 3.14e-77

Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.


Pssm-ID: 143450 [Multi-domain]  Cd Length: 443  Bit Score: 253.68  E-value: 3.14e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  17 QQQLAALGTDAQPWAQDWMSAV---------ELEVSEISIVQTEINLALRNLRAWMRDEQVRRNLATQLDSAFIRKEPFG 87
Cdd:cd07132    23 IQQLEALLRMLEENEDEIVEALakdlrkpkfEAVLSEILLVKNEIKYAISNLPEWMKPEPVKKNLATLLDDVYIYKEPLG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  88 LVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLPRYLDQ------AGGPPSglsgwgpsgalTVR 161
Cdd:cd07132   103 VVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKecypvvLGGVEE-----------TTE 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 162 LaellcrgagrargdraaagaqvrlhLLHRPSHLVQVieghsgflprpGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYV 241
Cdd:cd07132   172 L-------------------------LKQRFDYIFYT-----------GSTSVGKIVMQAAAKHLTPVTLELGGKSPCYV 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 242 DDNCDPQT------------------------------------------------------------------------ 249
Cdd:cd07132   216 DKSCDIDVaarriawgkfinagqtciapdyvlctpevqekfvealkktlkefygedpkespdygriindrhfqrlkklls 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 250 -------------------------------------------------------------------------VVEQVLA 256
Cdd:cd07132   296 ggkvaiggqtdekeryiaptvltdvkpsdpvmqeeifgpilpivtvnnldeaiefinsrekplalyvfsnnkkVINKILS 375

                         410       420
                  ....*....|....*....|....*..
gi 1878746647 257 RTSSGGFCGNDGFMHMTLPSLPFGGVG 283
Cdd:cd07132   376 NTSSGGVCVNDTIMHYTLDSLPFGGVG 402
ALDH_F3AB cd07132
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ...
 552-675 2.31e-70

Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.


Pssm-ID: 143450 [Multi-domain]  Cd Length: 443  Bit Score: 235.58  E-value: 2.31e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 552 DY-LYRPKMQERLLPALQSAITRFYGEDPRSSPDLGRIINEKHFQRLQGLLGCGRVAIGGQSDESDRYIAPTVLVDVQET 630
Cdd:cd07132   244 DYvLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVLTDVKPS 323

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1878746647 631 EPVMQEEIFGPILPIVNVRSLDEAIDFIKRREKPLALYAFSNSNQ 675
Cdd:cd07132   324 DPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKK 368
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
 413-534 1.91e-62

NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes "I" subunits from the closely related F420H2 dehydrogenase and formate hydrogenlyase complexes. [Energy metabolism, Electron transport]


Pssm-ID: 273902 [Multi-domain]  Cd Length: 122  Bit Score: 203.42  E-value: 1.91e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 413 GLGMTLSYLFREPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAVCPAQAITIEAEPRADGSRRTTRYDID 492
Cdd:TIGR01971   1 GLGLTLKYFFSKPVTVQYPEEKLYLPPRFRGRIVLTRDPNGEEKCIGCTLCAAVCPADAIRVVPAEGEDGKRRLKFYEIN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1878746647 493 MTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEELLYNKEKL 534
Cdd:TIGR01971  81 FGRCIFCGLCEEACPTDAIVLTPEFELATYTRSDLVYGKEDL 122
PTZ00381 PTZ00381
aldehyde dehydrogenase family protein; Provisional
 38-246 1.11e-53

aldehyde dehydrogenase family protein; Provisional


Pssm-ID: 240392  Cd Length: 493  Bit Score: 191.78  E-value: 1.11e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  38 VELEVSEISIVQTEINLALRNLRAWMRDEQVRRNLATQLDSAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVV 117
Cdd:PTZ00381   62 FETKMTEVLLTVAEIEHLLKHLDEYLKPEKVDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVV 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 118 LKPSEISKSTEKVLAEVLPRYLDQAggppsglsgwgpsgalTVRLAEllcrgagrargdraaAGAQVRLHLLHRPShlvq 197
Cdd:PTZ00381  142 LKPSELSPHTSKLMAKLLTKYLDPS----------------YVRVIE---------------GGVEVTTELLKEPF---- 186

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1878746647 198 vieGHSGFlprPGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCD 246
Cdd:PTZ00381  187 ---DHIFF---TGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCN 229
PTZ00381 PTZ00381
aldehyde dehydrogenase family protein; Provisional
 533-675 9.58e-46

aldehyde dehydrogenase family protein; Provisional


Pssm-ID: 240392  Cd Length: 493  Bit Score: 169.82  E-value: 9.58e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 533 KLLNNGDKWeaeitanIQADYLYRPK-MQERLLPALQSAITRFYGEDPRSSPDLGRIINEKHFQRLQGLLGC--GRVAIG 609
Cdd:PTZ00381  241 KFLNAGQTC-------VAPDYVLVHRsIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKDhgGKVVYG 313

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1878746647 610 GQSDESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLDEAIDFIKRREKPLALYAFSNSNQ 675
Cdd:PTZ00381  314 GEVDIENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKR 379
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
 38-256 3.76e-29

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation


Pssm-ID: 440636 [Multi-domain]  Cd Length: 479  Bit Score: 121.39  E-value: 3.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  38 VELEVSE----ISIVQTEINLALRNLRAWMrdEQVRRNLATQLDS------AFIRKEPFGLVLIVAPWNYPVNLTLLPLV 107
Cdd:COG1012    86 AALLTLEtgkpLAEARGEVDRAADFLRYYA--GEARRLYGETIPSdapgtrAYVRREPLGVVGAITPWNFPLALAAWKLA 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 108 GALAAGNCVVLKPSEISKSTEKVLAEVlpryLDQAGGPPsglsgwgpsGALTVrlaellcrgagrargdraaagaqvrlh 187
Cdd:COG1012   164 PALAAGNTVVLKPAEQTPLSALLLAEL----LEEAGLPA---------GVLNV--------------------------- 203

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1878746647 188 LLHRPSHLVQVIEGHsgflPRP------GSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDPQTVVEQVLA 256
Cdd:COG1012   204 VTGDGSEVGAALVAH----PDVdkisftGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVR 274
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
 39-264 7.03e-29

Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.


Pssm-ID: 425500 [Multi-domain]  Cd Length: 459  Bit Score: 120.33  E-value: 7.03e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  39 ELEVSE----ISIVQTEINLALRNLR---AWMR--DEQVRRNLATQLdsAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGA 109
Cdd:pfam00171  73 ELETLEngkpLAEARGEVDRAIDVLRyyaGLARrlDGETLPSDPGRL--AYTRREPLGVVGAITPWNFPLLLPAWKIAPA 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 110 LAAGNCVVLKPSEISKSTEKVLAEVlpryLDQAGGPPsglsgwgpsGAltvrlaellcrgagrargdraaagaqvrLHLL 189
Cdd:pfam00171 151 LAAGNTVVLKPSELTPLTALLLAEL----FEEAGLPA---------GV----------------------------LNVV 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 190 HRPSHLV-QVIEGHsgflPRP------GSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDpqtvVEQVLARTSSGG 262
Cdd:pfam00171 190 TGSGAEVgEALVEH----PDVrkvsftGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDAD----LDAAVEAAVFGA 261


                  ..
gi 1878746647 263 FC 264
Cdd:pfam00171 262 FG 263
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 454-526 2.52e-24

Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 96.35  E-value: 2.52e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEAEpradgsRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPnFEFSTETHEE 526
Cdd:COG1143     1 EDKCIGCGLCVRVCPVDAITIEDG------EPGKVYVIDPDKCIGCGLCVEVCPTGAISMTP-FELAVEDREE 66
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
 576-673 1.81e-18

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation


Pssm-ID: 440636 [Multi-domain]  Cd Length: 479  Bit Score: 88.64  E-value: 1.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 576 GEDPrsSPDLGRIINEKHFQRLQGLLGCG-----RVAIGGQ--SDESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNV 648
Cdd:COG1012   316 PLDP--GTDMGPLISEAQLERVLAYIEDAvaegaELLTGGRrpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPF 393

                          90       100
                  ....*....|....*....|....*
gi 1878746647 649 RSLDEAIDFIKRREKPLALYAFSNS 673
Cdd:COG1012   394 DDEEEAIALANDTEYGLAASVFTRD 418
BADH TIGR01804
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...
 77-266 2.86e-18

betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 200131 [Multi-domain]  Cd Length: 467  Bit Score: 88.33  E-value: 2.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  77 DSAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLpryldQAGGPPSGLSG--WGP 154
Cdd:TIGR01804 125 SFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIM-----EEAGLPKGVFNvvQGD 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 155 SGALTVRLAEllcrgagrargdraaagaqvrlhllHRPSHLVQVIeghsgflprpGSPRVGKIVMAAAAKHLTPVTLELG 234
Cdd:TIGR01804 200 GAEVGPLLVN-------------------------HPDVAKVSFT----------GGVPTGKKIMAAAAGHLKHVTMELG 244

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1878746647 235 GKNPCYVDDNCDPQTVVEQVLART--SSGGFCGN 266
Cdd:TIGR01804 245 GKSPLIVFDDADLESAVDGAMLGNffSAGQVCSN 278
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 454-512 3.68e-18

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 80.90  E-value: 3.68e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEAEPRADgsrrttrydIDMTKCIYCGFCQEACPVDAIV 512
Cdd:cd10549    77 EEKCIGCGLCVKVCPVDAITLEDELEIV---------IDKEKCIGCGICAEVCPVNAIK 126
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
 559-656 1.42e-15

Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.


Pssm-ID: 425500 [Multi-domain]  Cd Length: 459  Bit Score: 79.50  E-value: 1.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 559 MQERLLPALQSAITRFYGEDPR-SSPDLGRIINEKHFQRLQGLL-----GCGRVAIGGQSDESD-RYIAPTVLVDVQETE 631
Cdd:pfam00171 281 IYDEFVEKLVEAAKKLKVGDPLdPDTDMGPLISKAQLERVLKYVedakeEGAKLLTGGEAGLDNgYFVEPTVLANVTPDM 360

                          90       100
                  ....*....|....*....|....*
gi 1878746647 632 PVMQEEIFGPILPIVNVRSLDEAID 656
Cdd:pfam00171 361 RIAQEEIFGPVLSVIRFKDEEEAIE 385
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 457-510 1.03e-14

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 68.71  E-value: 1.03e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1878746647 457 CIACKLCEAVCPAQAITIEAEPRADGsrrTTRYDIDMTKCIYCGFCQEACPVDA 510
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKKG---TKTVVIDPERCVGCGACVAVCPTGA 51
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 421-511 1.56e-06

EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 49.86  E-value: 1.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 421 LFREPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAVCPAQAITIEAE-PRADGsrrttrydidmtKCIYC 499
Cdd:NF038196  151 GPEKKKGFIPRLLSKLVNPLFYKFKVKDKKFHVTDKCIGCGICAKVCPVNNIEMEDGkPVWGH------------NCTHC 218

                          90
                  ....*....|..
gi 1878746647 500 GFCQEACPVDAI 511
Cdd:NF038196  219 LACIHRCPKEAI 230
 
Name Accession Description Interval E-value
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
400-560 7.98e-94

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 287.16  E-value: 7.98e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 400 RAAQTLLWTELIRGLGMTLSYLFREPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAVCPAQAITIEAEPR 479
Cdd:PRK05888    3 QYLKSMLLKELLKGLGVTLKYFFKKKVTIQYPEEKLPLSPRFRGRHALRRDPNGEERCIACKLCAAICPADAITIEAAER 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 480 ADGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEELLYNKEKLLNNGDKWEAEITANIQADYLYRPKM 559
Cdd:PRK05888   83 EDGRRRTTRYDINFGRCIFCGFCEEACPTDAIVETPDFELATETREELIYDKEKLLANGDRVEREIAPGKAADANYRGEA 162


                  .
gi 1878746647 560 Q 560
Cdd:PRK05888  163 E 163
ALDH_F3AB cd07132
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ...
 17-283 3.14e-77

Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.


Pssm-ID: 143450 [Multi-domain]  Cd Length: 443  Bit Score: 253.68  E-value: 3.14e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  17 QQQLAALGTDAQPWAQDWMSAV---------ELEVSEISIVQTEINLALRNLRAWMRDEQVRRNLATQLDSAFIRKEPFG 87
Cdd:cd07132    23 IQQLEALLRMLEENEDEIVEALakdlrkpkfEAVLSEILLVKNEIKYAISNLPEWMKPEPVKKNLATLLDDVYIYKEPLG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  88 LVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLPRYLDQ------AGGPPSglsgwgpsgalTVR 161
Cdd:cd07132   103 VVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKecypvvLGGVEE-----------TTE 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 162 LaellcrgagrargdraaagaqvrlhLLHRPSHLVQVieghsgflprpGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYV 241
Cdd:cd07132   172 L-------------------------LKQRFDYIFYT-----------GSTSVGKIVMQAAAKHLTPVTLELGGKSPCYV 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 242 DDNCDPQT------------------------------------------------------------------------ 249
Cdd:cd07132   216 DKSCDIDVaarriawgkfinagqtciapdyvlctpevqekfvealkktlkefygedpkespdygriindrhfqrlkklls 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 250 -------------------------------------------------------------------------VVEQVLA 256
Cdd:cd07132   296 ggkvaiggqtdekeryiaptvltdvkpsdpvmqeeifgpilpivtvnnldeaiefinsrekplalyvfsnnkkVINKILS 375

                         410       420
                  ....*....|....*....|....*..
gi 1878746647 257 RTSSGGFCGNDGFMHMTLPSLPFGGVG 283
Cdd:cd07132   376 NTSSGGVCVNDTIMHYTLDSLPFGGVG 402
ALDH_F3AB cd07132
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ...
 552-675 2.31e-70

Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.


Pssm-ID: 143450 [Multi-domain]  Cd Length: 443  Bit Score: 235.58  E-value: 2.31e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 552 DY-LYRPKMQERLLPALQSAITRFYGEDPRSSPDLGRIINEKHFQRLQGLLGCGRVAIGGQSDESDRYIAPTVLVDVQET 630
Cdd:cd07132   244 DYvLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVLTDVKPS 323

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1878746647 631 EPVMQEEIFGPILPIVNVRSLDEAIDFIKRREKPLALYAFSNSNQ 675
Cdd:cd07132   324 DPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKK 368
ALDH_F3-13-14_CALDH-like cd07087
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ...
 5-246 1.35e-65

ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.


Pssm-ID: 143406 [Multi-domain]  Cd Length: 426  Bit Score: 222.40  E-value: 1.35e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647   5 RKLRAVV-TKATQ-----QQQLAALGTDAQPWAQDWMSAV---------ELEVSEISIVQTEINLALRNLRAWMRDEQVR 69
Cdd:cd07087     5 ARLRETFlTGKTRslewrKAQLKALKRMLTENEEEIAAALyadlgkppaEAYLTEIAVVLGEIDHALKHLKKWMKPRRVS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  70 RNLATQLDSAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLPRYLDqaggppsgl 149
Cdd:cd07087    85 VPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFD--------- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 150 sgwgpsgaltvrlaellcrgagrargdraaagaqvrlhllhrpSHLVQVIEG----HSGFLPRP-------GSPRVGKIV 218
Cdd:cd07087   156 -------------------------------------------PEAVAVVEGgvevATALLAEPfdhifftGSPAVGKIV 192

                         250       260
                  ....*....|....*....|....*...
gi 1878746647 219 MAAAAKHLTPVTLELGGKNPCYVDDNCD 246
Cdd:cd07087   193 MEAAAKHLTPVTLELGGKSPCIVDKDAN 220
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
 413-534 1.91e-62

NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes "I" subunits from the closely related F420H2 dehydrogenase and formate hydrogenlyase complexes. [Energy metabolism, Electron transport]


Pssm-ID: 273902 [Multi-domain]  Cd Length: 122  Bit Score: 203.42  E-value: 1.91e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 413 GLGMTLSYLFREPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAVCPAQAITIEAEPRADGSRRTTRYDID 492
Cdd:TIGR01971   1 GLGLTLKYFFSKPVTVQYPEEKLYLPPRFRGRIVLTRDPNGEEKCIGCTLCAAVCPADAIRVVPAEGEDGKRRLKFYEIN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1878746647 493 MTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEELLYNKEKL 534
Cdd:TIGR01971  81 FGRCIFCGLCEEACPTDAIVLTPEFELATYTRSDLVYGKEDL 122
ALDH_YwdH-P39616 cd07136
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ...
 5-246 3.98e-58

Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.


Pssm-ID: 143454 [Multi-domain]  Cd Length: 449  Bit Score: 202.73  E-value: 3.98e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647   5 RKLRAVVtKATQQQQLAALGTDAQPwaqdwmSAVELEVSEISIVQTEINLALRNLRAWMRDEQVRRNLATQLDSAFIRKE 84
Cdd:cd07136    27 KKLKQAI-KKYENEILEALKKDLGK------SEFEAYMTEIGFVLSEINYAIKHLKKWMKPKRVKTPLLNFPSKSYIYYE 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  85 PFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLPRYLDqaggppsglsgwgpsgaltvrlae 164
Cdd:cd07136   100 PYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFD------------------------ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 165 llcrgagrargdraaagaqvrlhllhrPSHlVQVIEG----HSGFLPRP-------GSPRVGKIVMAAAAKHLTPVTLEL 233
Cdd:cd07136   156 ---------------------------EEY-VAVVEGgveeNQELLDQKfdyifftGSVRVGKIVMEAAAKHLTPVTLEL 207

                         250
                  ....*....|...
gi 1878746647 234 GGKNPCYVDDNCD 246
Cdd:cd07136   208 GGKSPCIVDEDAN 220
ALDH_F3-13-14_CALDH-like cd07087
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ...
 552-675 1.47e-56

ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.


Pssm-ID: 143406 [Multi-domain]  Cd Length: 426  Bit Score: 198.13  E-value: 1.47e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 552 DYLY-RPKMQERLLPALQSAITRFYGEDPRSSPDLGRIINEKHFQRLQGLLGCGRVAIGGQSDESDRYIAPTVLVDVQET 630
Cdd:cd07087   244 DYVLvHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGKVVIGGQVDKEERYIAPTILDDVSPD 323

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1878746647 631 EPVMQEEIFGPILPIVNVRSLDEAIDFIKRREKPLALYAFSNSNQ 675
Cdd:cd07087   324 SPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKA 368
PTZ00381 PTZ00381
aldehyde dehydrogenase family protein; Provisional
 38-246 1.11e-53

aldehyde dehydrogenase family protein; Provisional


Pssm-ID: 240392  Cd Length: 493  Bit Score: 191.78  E-value: 1.11e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  38 VELEVSEISIVQTEINLALRNLRAWMRDEQVRRNLATQLDSAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVV 117
Cdd:PTZ00381   62 FETKMTEVLLTVAEIEHLLKHLDEYLKPEKVDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVV 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 118 LKPSEISKSTEKVLAEVLPRYLDQAggppsglsgwgpsgalTVRLAEllcrgagrargdraaAGAQVRLHLLHRPShlvq 197
Cdd:PTZ00381  142 LKPSELSPHTSKLMAKLLTKYLDPS----------------YVRVIE---------------GGVEVTTELLKEPF---- 186

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1878746647 198 vieGHSGFlprPGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCD 246
Cdd:PTZ00381  187 ---DHIFF---TGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCN 229
ALDH_F14-YMR110C cd07135
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ...
 36-249 3.58e-53

Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.


Pssm-ID: 143453 [Multi-domain]  Cd Length: 436  Bit Score: 188.97  E-value: 3.58e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  36 SAVELEVSEISIVQTEINLALRNLRAWMRDEQVRRNLATQ-LDSAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGN 114
Cdd:cd07135    58 PPFETLLTEVSGVKNDILHMLKNLKKWAKDEKVKDGPLAFmFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGC 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 115 CVVLKPSEISKSTEKVLAEVLPRYLDQA------GGPPSglsgwgpsgalTVRLAEllcrgagrargdraaagaqvrlhl 188
Cdd:cd07135   138 TVVLKPSELTPHTAALLAELVPKYLDPDafqvvqGGVPE-----------TTALLE------------------------ 182

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1878746647 189 lHRPSHLVQVieghsgflprpGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDPQT 249
Cdd:cd07135   183 -QKFDKIFYT-----------GSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLEL 231
ALDH_YwdH-P39616 cd07136
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ...
 552-675 2.32e-52

Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.


Pssm-ID: 143454 [Multi-domain]  Cd Length: 449  Bit Score: 187.33  E-value: 2.32e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 552 DYLYRPK-MQERLLPALQSAITRFYGEDPRSSPDLGRIINEKHFQRLQGLLGCGRVAIGGQSDESDRYIAPTVLVDVQET 630
Cdd:cd07136   244 DYVLVHEsVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGKIVFGGNTDRETLYIEPTILDNVTWD 323

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1878746647 631 EPVMQEEIFGPILPIVNVRSLDEAIDFIKRREKPLALYAFSNSNQ 675
Cdd:cd07136   324 DPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKK 368
ALDH_AlkH-like cd07134
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ...
 5-254 3.65e-48

Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.


Pssm-ID: 143452 [Multi-domain]  Cd Length: 433  Bit Score: 175.11  E-value: 3.65e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647   5 RKLRAVVtKATQQQQLAALGTDAQPwaqdwmSAVELEVSEISIVQTEINLALRNLRAWMRDEQVRRNLATQLDSAFIRKE 84
Cdd:cd07134    27 KRLKKAI-LARREEIIAALAADFRK------PAAEVDLTEILPVLSEINHAIKHLKKWMKPKRVRTPLLLFGTKSKIRYE 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  85 PFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVlpryldqaggppsglsgwgpsgaltvrLAE 164
Cdd:cd07134   100 PKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKI---------------------------IRE 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 165 LLcrgagrargdraaagaqvrlhllhRPSHlVQVIEG--------------HSGFlprPGSPRVGKIVMAAAAKHLTPVT 230
Cdd:cd07134   153 AF------------------------DEDE-VAVFEGdaevaqallelpfdHIFF---TGSPAVGKIVMAAAAKHLASVT 204

                         250       260
                  ....*....|....*....|....
gi 1878746647 231 LELGGKNPCYVDDNCDPQTVVEQV 254
Cdd:cd07134   205 LELGGKSPTIVDETADLKKAAKKI 228
PTZ00381 PTZ00381
aldehyde dehydrogenase family protein; Provisional
 533-675 9.58e-46

aldehyde dehydrogenase family protein; Provisional


Pssm-ID: 240392  Cd Length: 493  Bit Score: 169.82  E-value: 9.58e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 533 KLLNNGDKWeaeitanIQADYLYRPK-MQERLLPALQSAITRFYGEDPRSSPDLGRIINEKHFQRLQGLLGC--GRVAIG 609
Cdd:PTZ00381  241 KFLNAGQTC-------VAPDYVLVHRsIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKDhgGKVVYG 313

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1878746647 610 GQSDESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLDEAIDFIKRREKPLALYAFSNSNQ 675
Cdd:PTZ00381  314 GEVDIENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKR 379
ALDH_F3FHI cd07137
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ...
 39-256 2.61e-45

Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.


Pssm-ID: 143455 [Multi-domain]  Cd Length: 432  Bit Score: 167.20  E-value: 2.61e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  39 ELEVSEISIVQTEINLALRNLRAWMRDEQVRRNLATQLDSAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVL 118
Cdd:cd07137    55 ESFRDEVSVLVSSCKLAIKELKKWMAPEKVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 119 KPSEISKSTEKVLAEVLPRYLDQA------GGPPSGlsgwgpsgaltvrlaellcrgagrargdraaagaqvrlhllhrp 192
Cdd:cd07137   135 KPSELAPATSALLAKLIPEYLDTKaikvieGGVPET-------------------------------------------- 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1878746647 193 SHLVQVIEGHSGFlprPGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDPQTVVEQVLA 256
Cdd:cd07137   171 TALLEQKWDKIFF---TGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAG 231
ALDH_AlkH-like cd07134
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ...
 533-673 6.48e-43

Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.


Pssm-ID: 143452 [Multi-domain]  Cd Length: 433  Bit Score: 160.47  E-value: 6.48e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 533 KLLNNGDkweaeitANIQADYLYRPK-MQERLLPALQSAITRFYGEDP--RSSPDLGRIINEKHFQRLQGLL-----GCG 604
Cdd:cd07134   232 KFLNAGQ-------TCIAPDYVFVHEsVKDAFVEHLKAEIEKFYGKDAarKASPDLARIVNDRHFDRLKGLLddavaKGA 304

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1878746647 605 RVAIGGQSDESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLDEAIDFIKRREKPLALYAFSNS 673
Cdd:cd07134   305 KVEFGGQFDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKD 373
ALDH_CALDH_CalB cd07133
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ...
 36-252 6.67e-43

Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.


Pssm-ID: 143451 [Multi-domain]  Cd Length: 434  Bit Score: 160.34  E-value: 6.67e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  36 SAVELEVSEISIVQTEINLALRNLRAWMRDEQVRRNLATQLDSAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNC 115
Cdd:cd07133    52 SRHETLLAEILPSIAGIKHARKHLKKWMKPSRRHVGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNR 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 116 VVLKPSEISKSTEKVLAEVLPRYLDQaggppsglsgwgpsgaltvrlaellcrgagrargdraaagaqvrlhllhrpsHL 195
Cdd:cd07133   132 VMIKPSEFTPRTSALLAELLAEYFDE----------------------------------------------------DE 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1878746647 196 VQVIEGH----SGFLPRP-------GSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDPQTVVE 252
Cdd:cd07133   160 VAVVTGGadvaAAFSSLPfdhllftGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAE 227
PLN02203 PLN02203
aldehyde dehydrogenase
 44-256 2.03e-40

aldehyde dehydrogenase


Pssm-ID: 165847 [Multi-domain]  Cd Length: 484  Bit Score: 154.50  E-value: 2.03e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  44 EISIVQTEINLALRNLRAWMRDEQVRRNLATQLDSAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEI 123
Cdd:PLN02203   67 EVGVLTKSANLALSNLKKWMAPKKAKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSEL 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 124 SKSTEKVLAEVLPRYLDQA------GGPpsglsgwgpsgaltvrlaellcrgagrargdraaagaQVRLHLLHRPSHLVQ 197
Cdd:PLN02203  147 APATSAFLAANIPKYLDSKavkvieGGP-------------------------------------AVGEQLLQHKWDKIF 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1878746647 198 VIeghsgflprpGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVD---DNCDPQTVVEQVLA 256
Cdd:PLN02203  190 FT----------GSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVG 241
ALDH_F14-YMR110C cd07135
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ...
 552-674 1.05e-36

Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.


Pssm-ID: 143453 [Multi-domain]  Cd Length: 436  Bit Score: 142.74  E-value: 1.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 552 DYLY-RPKMQERLLPALQSAITRFYGEDPRSSPDLGRIINEKHFQRLQGLLGC--GRVAIGGQSDESDRYIAPTVLVDVQ 628
Cdd:cd07135   252 DYVLvDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDTtkGKVVIGGEMDEATRFIPPTIVSDVS 331

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1878746647 629 ETEPVMQEEIFGPILPIVNVRSLDEAIDFIKRREKPLALYAFSNSN 674
Cdd:cd07135   332 WDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDK 377
ALDH_F3FHI cd07137
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ...
 547-672 1.39e-36

Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.


Pssm-ID: 143455 [Multi-domain]  Cd Length: 432  Bit Score: 142.55  E-value: 1.39e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 547 ANIQADYLYRPK-MQERLLPALQSAITRFYGEDPRSSPDLGRIINEKHFQRLQGLLGCGRVAI----GGQSDESDRYIAP 621
Cdd:cd07137   241 ACIAPDYVLVEEsFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADkivhGGERDEKNLYIEP 320

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1878746647 622 TVLVDVQETEPVMQEEIFGPILPIVNVRSLDEAIDFIKRREKPLALYAFSN 672
Cdd:cd07137   321 TILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTK 371
ALDH cd07078
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ...
 44-264 1.35e-35

NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.


Pssm-ID: 143397 [Multi-domain]  Cd Length: 432  Bit Score: 139.65  E-value: 1.35e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  44 EISIVQTEINLALRNLRAWMRDEQVRRNLATQldsAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEI 123
Cdd:cd07078    58 EVARAADTFRYYAGLARRLHGEVIPSPDPGEL---AIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSEL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 124 SKSTEKVLAEVLPryldQAGGPPsglsgwgpsGALTVrlaellcrgagrargdraaagaqvrlhLLHRPSHLVQVIEGHs 203
Cdd:cd07078   135 TPLTALLLAELLA----EAGLPP---------GVLNV---------------------------VTGDGDEVGAALASH- 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1878746647 204 gflPRP------GSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDPQTVVEQVLART--SSGGFC 264
Cdd:cd07078   174 ---PRVdkisftGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAfgNAGQVC 239
ALDH-SF cd06534
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
 39-264 1.97e-35

NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.


Pssm-ID: 143395 [Multi-domain]  Cd Length: 367  Bit Score: 137.75  E-value: 1.97e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  39 ELEVSE----ISIVQTEINLALRNLR---AWMRDEQVRRNLATQLDS-AFIRKEPFGLVLIVAPWNYPVNLTLLPLVGAL 110
Cdd:cd06534    38 ALETLEtgkpIEEALGEVARAIDTFRyaaGLADKLGGPELPSPDPGGeAYVRREPLGVVGVITPWNFPLLLAAWKLAPAL 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 111 AAGNCVVLKPSEISKSTEKVLAEVLPryldQAGGPPsglsgwgpsGALTVrlaellcrgagrargdraaagaqvrlhLLH 190
Cdd:cd06534   118 AAGNTVVLKPSELTPLTALALAELLQ----EAGLPP---------GVVNV---------------------------VPG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 191 RPSHLVQVIEGHsgflPRP------GSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDPQTVVEQVL--ARTSSGG 262
Cdd:cd06534   158 GGDEVGAALLSH----PRVdkisftGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVfgAFFNAGQ 233


                  ..
gi 1878746647 263 FC 264
Cdd:cd06534   234 IC 235
ALDH_CALDH_CalB cd07133
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ...
 552-675 7.73e-34

Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.


Pssm-ID: 143451 [Multi-domain]  Cd Length: 434  Bit Score: 134.53  E-value: 7.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 552 DYLYRPK-MQERLLPALQSAITRFYGeDPRSSPDLGRIINEKHFQRLQGLL------GCGRVAIG--GQSDESDRYIAPT 622
Cdd:cd07133   245 DYVLVPEdKLEEFVAAAKAAVAKMYP-TLADNPDYTSIINERHYARLQGLLedarakGARVIELNpaGEDFAATRKLPPT 323

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1878746647 623 VLVDVQETEPVMQEEIFGPILPIVNVRSLDEAIDFIKRREKPLALYAFSNSNQ 675
Cdd:cd07133   324 LVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKA 376
PLN02174 PLN02174
aldehyde dehydrogenase family 3 member H1
 8-256 1.01e-32

aldehyde dehydrogenase family 3 member H1


Pssm-ID: 177831  Cd Length: 484  Bit Score: 132.09  E-value: 1.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647   8 RAVVTKATQQQQLAALGTDAQP-WA---QDWMSAVELEVS--EISIVQTEINLALRNLRAWMRDEQVRRNLATQLDSAFI 81
Cdd:PLN02174   29 RGYEWRVTQLKKLMIICDNHEPeIVaalRDDLGKPELESSvyEVSLLRNSIKLALKQLKNWMAPEKAKTSLTTFPASAEI 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  82 RKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLPRYLDQAggppsglsgwgpsgalTVR 161
Cdd:PLN02174  109 VSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSS----------------AVR 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 162 LAEllcrgagrargdraaagaqvrlhllHRPSHLVQVIEGHSGFLPRPGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYV 241
Cdd:PLN02174  173 VVE-------------------------GAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVV 227

                         250
                  ....*....|....*
gi 1878746647 242 DDNCDPQTVVEQVLA 256
Cdd:PLN02174  228 DSDTDLKVTVRRIIA 242
PLN02203 PLN02203
aldehyde dehydrogenase
 538-672 2.56e-31

aldehyde dehydrogenase


Pssm-ID: 165847 [Multi-domain]  Cd Length: 484  Bit Score: 127.92  E-value: 2.56e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 538 GDKWEA-EITANIQADY-LYRPKMQERLLPALQSAITRFYGEDPRSSPDLGRIINEKHFQRLQGLLGCGRVAI----GGQ 611
Cdd:PLN02203  241 GGKWGScAGQACIAIDYvLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAAsivhGGS 320

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1878746647 612 SDESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLDEAIDFIKRREKPLALYAFSN 672
Cdd:PLN02203  321 IDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTN 381
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
 38-256 3.76e-29

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation


Pssm-ID: 440636 [Multi-domain]  Cd Length: 479  Bit Score: 121.39  E-value: 3.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  38 VELEVSE----ISIVQTEINLALRNLRAWMrdEQVRRNLATQLDS------AFIRKEPFGLVLIVAPWNYPVNLTLLPLV 107
Cdd:COG1012    86 AALLTLEtgkpLAEARGEVDRAADFLRYYA--GEARRLYGETIPSdapgtrAYVRREPLGVVGAITPWNFPLALAAWKLA 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 108 GALAAGNCVVLKPSEISKSTEKVLAEVlpryLDQAGGPPsglsgwgpsGALTVrlaellcrgagrargdraaagaqvrlh 187
Cdd:COG1012   164 PALAAGNTVVLKPAEQTPLSALLLAEL----LEEAGLPA---------GVLNV--------------------------- 203

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1878746647 188 LLHRPSHLVQVIEGHsgflPRP------GSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDPQTVVEQVLA 256
Cdd:COG1012   204 VTGDGSEVGAALVAH----PDVdkisftGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVR 274
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
 39-264 7.03e-29

Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.


Pssm-ID: 425500 [Multi-domain]  Cd Length: 459  Bit Score: 120.33  E-value: 7.03e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  39 ELEVSE----ISIVQTEINLALRNLR---AWMR--DEQVRRNLATQLdsAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGA 109
Cdd:pfam00171  73 ELETLEngkpLAEARGEVDRAIDVLRyyaGLARrlDGETLPSDPGRL--AYTRREPLGVVGAITPWNFPLLLPAWKIAPA 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 110 LAAGNCVVLKPSEISKSTEKVLAEVlpryLDQAGGPPsglsgwgpsGAltvrlaellcrgagrargdraaagaqvrLHLL 189
Cdd:pfam00171 151 LAAGNTVVLKPSELTPLTALLLAEL----FEEAGLPA---------GV----------------------------LNVV 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 190 HRPSHLV-QVIEGHsgflPRP------GSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDpqtvVEQVLARTSSGG 262
Cdd:pfam00171 190 TGSGAEVgEALVEH----PDVrkvsftGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDAD----LDAAVEAAVFGA 261


                  ..
gi 1878746647 263 FC 264
Cdd:pfam00171 262 FG 263
ALDH_DDALDH cd07099
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ...
 4-246 2.87e-26

Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.


Pssm-ID: 143417 [Multi-domain]  Cd Length: 453  Bit Score: 112.31  E-value: 2.87e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647   4 PRKLRAVVTKATQQQQ-LAALGTDA-----QPWAqDWMSAVELEVSEISIVQT---------EINLALRNLRAW------ 62
Cdd:cd07099    17 PAEVAAAVARARAAQRaWAALGVEGraqrlLRWK-RALADHADELAELLHAETgkpradaglEVLLALEAIDWAarnapr 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  63 -MRDEQVRRNLATQLDSAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLpryldQ 141
Cdd:cd07099    96 vLAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAW-----A 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 142 AGGPPSGL----SGWGPSGAltvrlaellcrgagrargdraaagaqvrlHLLHRPSHLVQvieghsgFlprPGSPRVGKI 217
Cdd:cd07099   171 AAGPPQGVlqvvTGDGATGA-----------------------------ALIDAGVDKVA-------F---TGSVATGRK 211

                         250       260
                  ....*....|....*....|....*....
gi 1878746647 218 VMAAAAKHLTPVTLELGGKNPCYVDDNCD 246
Cdd:cd07099   212 VMAAAAERLIPVVLELGGKDPMIVLADAD 240
ALDH_SaliADH cd07105
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ...
 77-264 3.58e-26

Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.


Pssm-ID: 143423 [Multi-domain]  Cd Length: 432  Bit Score: 111.90  E-value: 3.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  77 DSAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVlpryLDQAGGPPsglsgwgpsG 156
Cdd:cd07105    90 TLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRV----FHEAGLPK---------G 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 157 ALTVrlaellcrgagrargdraaagaqvrlhLLHRPSHLVQVIEghsGFLPRP--------GSPRVGKIVMAAAAKHLTP 228
Cdd:cd07105   157 VLNV---------------------------VTHSPEDAPEVVE---ALIAHPavrkvnftGSTRVGRIIAETAAKHLKP 206

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1878746647 229 VTLELGGKNPCYVDDNCDPQTVVEQVLArtssGGFC 264
Cdd:cd07105   207 VLLELGGKAPAIVLEDADLDAAANAALF----GAFL 238
ALDH cd07078
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ...
 551-672 1.59e-24

NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.


Pssm-ID: 143397 [Multi-domain]  Cd Length: 432  Bit Score: 106.91  E-value: 1.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 551 ADYLYRPK-MQERLLPALQSAITRFYGEDPRS-SPDLGRIINEKHFQRLQGLL-----GCGRVAIGGQSDESD--RYIAP 621
Cdd:cd07078   242 ASRLLVHEsIYDEFVERLVERVKALKVGNPLDpDTDMGPLISAAQLDRVLAYIedakaEGAKLLCGGKRLEGGkgYFVPP 321

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1878746647 622 TVLVDVQETEPVMQEEIFGPILPIVNVRSLDEAIDFIKRREKPLALYAFSN 672
Cdd:cd07078   322 TVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTR 372
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 454-526 2.52e-24

Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 96.35  E-value: 2.52e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEAEpradgsRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPnFEFSTETHEE 526
Cdd:COG1143     1 EDKCIGCGLCVRVCPVDAITIEDG------EPGKVYVIDPDKCIGCGLCVEVCPTGAISMTP-FELAVEDREE 66
ALDH_F15-22 cd07098
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ...
 44-264 2.69e-24

Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.


Pssm-ID: 143416 [Multi-domain]  Cd Length: 465  Bit Score: 106.62  E-value: 2.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  44 EISIVQTEINLALRNLRAWMRDEQVRRNLATQLDSAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSE- 122
Cdd:cd07098    79 EILVTCEKIRWTLKHGEKALRPESRPGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEq 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 123 ISKSTEKVLaEVLPRYLDQAGGPP---SGLSGWGPSG-ALTvrlaellcrgagrargdraaagaqvrlhllhrpSHlvqV 198
Cdd:cd07098   159 VAWSSGFFL-SIIRECLAACGHDPdlvQLVTCLPETAeALT---------------------------------SH---P 201

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1878746647 199 IEGHSGFLprpGSPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDPQTVVeQVLART---SSGGFC 264
Cdd:cd07098   202 VIDHITFI---GSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIA-SIIMRGtfqSSGQNC 266
ALDH_EDX86601 cd07102
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ...
 80-264 4.77e-23

Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.


Pssm-ID: 143420 [Multi-domain]  Cd Length: 452  Bit Score: 102.71  E-value: 4.77e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  80 FIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTekvlAEVLPRYLDQAGGPPSGLSGWGPSGALT 159
Cdd:cd07102   111 YIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLC----GERFAAAFAEAGLPEGVFQVLHLSHETS 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 160 VRLAEllcrgagrargdraaagaqvrlhllhrpshlvqviEGHSGFLPRPGSPRVGKIVMAAAAKHLTPVTLELGGKNPC 239
Cdd:cd07102   187 AALIA-----------------------------------DPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPA 231

                         170       180
                  ....*....|....*....|....*..
gi 1878746647 240 YVDDNCDPQTVVEQVL--ARTSSGGFC 264
Cdd:cd07102   232 YVRPDADLDAAAESLVdgAFFNSGQSC 258
PLN02174 PLN02174
aldehyde dehydrogenase family 3 member H1
 547-675 5.38e-22

aldehyde dehydrogenase family 3 member H1


Pssm-ID: 177831  Cd Length: 484  Bit Score: 99.74  E-value: 5.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 547 ANIQADYLYRPK-MQERLLPALQSAITRFYGEDPRSSPDLGRIINEKHFQRLQGLLG----CGRVAIGGQSDESDRYIAP 621
Cdd:PLN02174  252 ACISPDYILTTKeYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDekevSDKIVYGGEKDRENLKIAP 331

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1878746647 622 TVLVDVQETEPVMQEEIFGPILPIVNVRSLDEAIDFIKRREKPLALYAFSNSNQ 675
Cdd:PLN02174  332 TILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKK 385
PRK13473 PRK13473
aminobutyraldehyde dehydrogenase;
81-267 7.38e-21

aminobutyraldehyde dehydrogenase;


Pssm-ID: 237391  Cd Length: 475  Bit Score: 96.13  E-value: 7.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  81 IRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLPRYLdqaggpPSG----LSGWGPS- 155
Cdd:PRK13473  134 IRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADIL------PPGvlnvVTGRGATv 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 156 GAltvrlaellcrgagrargdraaagaqvrlhllhrpsHLVqvieGHsgflPRP------GSPRVGKIVMAAAAKHLTPV 229
Cdd:PRK13473  208 GD------------------------------------ALV----GH----PKVrmvsltGSIATGKHVLSAAADSVKRT 243

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1878746647 230 TLELGGKNPCYVDDNCDPQTVVEQvlARTssGGFC--GND 267
Cdd:PRK13473  244 HLELGGKAPVIVFDDADLDAVVEG--IRT--FGYYnaGQD 279
ALDH_F10_BADH cd07110
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ...
 66-256 1.27e-20

Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.


Pssm-ID: 143428 [Multi-domain]  Cd Length: 456  Bit Score: 95.11  E-value: 1.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  66 EQVRRNLATQLD------SAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVlpryL 139
Cdd:cd07110    95 EQLDAKAERAVPlpsedfKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEI----A 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 140 DQAGGPPSGL---SGWGP-SGAltvRLAEllcrgagrargdraaagaqvrlhllhrpshlvqviegHSGF--LPRPGSPR 213
Cdd:cd07110   171 AEAGLPPGVLnvvTGTGDeAGA---PLAA-------------------------------------HPGIdkISFTGSTA 210

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1878746647 214 VGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDPQTVVEQVLA 256
Cdd:cd07110   211 TGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMF 253
ALDH_VaniDH_like cd07150
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ...
 9-251 3.94e-20

Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.


Pssm-ID: 143468 [Multi-domain]  Cd Length: 451  Bit Score: 93.55  E-value: 3.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647   9 AVVTKATQQQQLAALGTDAQ---PWAQ--------------DWMSAVELEVSEISIVQT---------EINLALRNLRAW 62
Cdd:cd07150    13 ARVAVGSRQDAERAIAAAYDafpAWAAttpsererillkaaEIMERRADDLIDLLIDEGgstygkawfETTFTPELLRAA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  63 MrdEQVRRNLATQLDSAF------IRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVlp 136
Cdd:cd07150    93 A--GECRRVRGETLPSDSpgtvsmSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEI-- 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 137 ryLDQAGGPPsglsgwgpsGALTVrlaellcrgagrargdraaagaqvrlhLLHRPSHLVQVIEGHsgflPR------PG 210
Cdd:cd07150   169 --MEEAGLPK---------GVFNV---------------------------VTGGGAEVGDELVDD----PRvrmvtfTG 206

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1878746647 211 SPRVGKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDPQTVV 251
Cdd:cd07150   207 STAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAV 247
ALDH_ABALDH-YdcW cd07092
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ...
 78-268 1.15e-19

Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.


Pssm-ID: 143411 [Multi-domain]  Cd Length: 450  Bit Score: 92.39  E-value: 1.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  78 SAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLPRYLdqaggpPSG----LSGWG 153
Cdd:cd07092   111 TSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVL------PPGvvnvVCGGG 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 154 PS-GALTVRlaellcrgagrargdraaagaqvrlhllHRPSHLVQVIeghsgflprpGSPRVGKIVMAAAAKHLTPVTLE 232
Cdd:cd07092   185 ASaGDALVA----------------------------HPRVRMVSLT----------GSVRTGKKVARAAADTLKRVHLE 226

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1878746647 233 LGGKNPCYVDDNCDPQTVVEQVlartSSGGFCgNDG 268
Cdd:cd07092   227 LGGKAPVIVFDDADLDAAVAGI----ATAGYY-NAG 257
ALDH_F8_HMSADH cd07093
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ...
 84-246 1.57e-19

Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.


Pssm-ID: 143412 [Multi-domain]  Cd Length: 455  Bit Score: 91.86  E-value: 1.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  84 EPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVlpryLDQAGGPPSGLS---GWGPS-GALT 159
Cdd:cd07093   116 QPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAEL----ANEAGLPPGVVNvvhGFGPEaGAAL 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 160 VRlaellcrgagrargdraaagaqvrlHllhrpsHLVQVIEghsgFLprpGSPRVGKIVMAAAAKHLTPVTLELGGKNPC 239
Cdd:cd07093   192 VA-------------------------H------PDVDLIS----FT---GETATGRTIMRAAAPNLKPVSLELGGKNPN 233


                  ....*..
gi 1878746647 240 YVDDNCD 246
Cdd:cd07093   234 IVFADAD 240
ALDH_CddD_SSP0762 cd07138
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ...
 73-256 2.01e-19

Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.


Pssm-ID: 143456 [Multi-domain]  Cd Length: 466  Bit Score: 91.80  E-value: 2.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  73 ATQLDSAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVlpryLDQAGGPPsG---- 148
Cdd:cd07138   118 EERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEI----LDEAGLPA-Gvfnl 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 149 LSGWGPS-GALtvrLAellcrgagrargdraaagaqvrlhllhrpSH-LVQVIEghsgFlprPGSPRVGKIVMAAAAKHL 226
Cdd:cd07138   193 VNGDGPVvGEA---LS-----------------------------AHpDVDMVS----F---TGSTRAGKRVAEAAADTV 233

                         170       180       190
                  ....*....|....*....|....*....|
gi 1878746647 227 TPVTLELGGKNPCYVDDNCDPQTVVEQVLA 256
Cdd:cd07138   234 KRVALELGGKSANIILDDADLEKAVPRGVA 263
ALDH_AAS00426 cd07109
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ...
 79-255 2.40e-19

Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.


Pssm-ID: 143427 [Multi-domain]  Cd Length: 454  Bit Score: 91.53  E-value: 2.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  79 AFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLprylDQAGGPPSGLS---GWGP- 154
Cdd:cd07109   111 VYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELA----EEAGLPAGALNvvtGLGAe 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 155 SGAltvRLAEllcrgagrargdraaagaqvrlhllHRPSHlvqviegHSGFLprpGSPRVGKIVMAAAAKHLTPVTLELG 234
Cdd:cd07109   187 AGA---ALVA-------------------------HPGVD-------HISFT---GSVETGIAVMRAAAENVVPVTLELG 228

                         170       180
                  ....*....|....*....|.
gi 1878746647 235 GKNPCYVDDNCDPQTVVEQVL 255
Cdd:cd07109   229 GKSPQIVFADADLEAALPVVV 249
ALDH_F5_SSADH_GabD cd07103
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ...
 80-256 3.91e-19

Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.


Pssm-ID: 143421 [Multi-domain]  Cd Length: 451  Bit Score: 90.57  E-value: 3.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  80 FIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTekvlAEVLPRYLDQAGGPPsglsgwgpsGALT 159
Cdd:cd07103   112 LVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLS----ALALAELAEEAGLPA---------GVLN 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 160 V------RLAELLCrgagrargdraaagaqvrlhllhrPSHLVQVIeghsGFLprpGSPRVGKIVMAAAAKHLTPVTLEL 233
Cdd:cd07103   179 VvtgspaEIGEALC------------------------ASPRVRKI----SFT---GSTAVGKLLMAQAADTVKRVSLEL 227

                         170       180
                  ....*....|....*....|...
gi 1878746647 234 GGKNPCYVDDNCDPQTVVEQVLA 256
Cdd:cd07103   228 GGNAPFIVFDDADLDKAVDGAIA 250
PLN02467 PLN02467
betaine aldehyde dehydrogenase
 80-252 5.49e-19

betaine aldehyde dehydrogenase


Pssm-ID: 215260 [Multi-domain]  Cd Length: 503  Bit Score: 90.56  E-value: 5.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  80 FIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVlpryLDQAGGPPSGL---SGWGP-S 155
Cdd:PLN02467  146 YVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADI----CREVGLPPGVLnvvTGLGTeA 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 156 GAltvrlaeLLCrgagrargdraaagaqvrlhllhrpshlvqvieGHSGF--LPRPGSPRVGKIVMAAAAKHLTPVTLEL 233
Cdd:PLN02467  222 GA-------PLA---------------------------------SHPGVdkIAFTGSTATGRKIMTAAAQMVKPVSLEL 261

                         170
                  ....*....|....*....
gi 1878746647 234 GGKNPCYVDDNCDPQTVVE 252
Cdd:PLN02467  262 GGKSPIIVFDDVDLDKAVE 280
ALDH_MGR_2402 cd07108
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ...
 79-256 5.93e-19

Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.


Pssm-ID: 143426  Cd Length: 457  Bit Score: 90.11  E-value: 5.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  79 AFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLPRYLdqaggpPSG----LSGWGP 154
Cdd:cd07108   111 TYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQVL------PAGvlnvITGYGE 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 155 S-GALTVRlaellcrgagrargdraaagaqvrlhllHRPSHLVQVIeghsgflprpGSPRVGKIVMAAAAKHLTPVTLEL 233
Cdd:cd07108   185 EcGAALVD----------------------------HPDVDKVTFT----------GSTEVGKIIYRAAADRLIPVSLEL 226

                         170       180
                  ....*....|....*....|...
gi 1878746647 234 GGKNPCYVDDNCDPQTVVEQVLA 256
Cdd:cd07108   227 GGKSPMIVFPDADLDDAVDGAIA 249
ALDH_F1-2_Ald2-like cd07091
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...
 79-254 5.98e-19

ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.


Pssm-ID: 143410  Cd Length: 476  Bit Score: 90.35  E-value: 5.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  79 AFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLPryldQAGGPPsG----LSGWGP 154
Cdd:cd07091   135 AYTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIK----EAGFPP-GvvniVPGFGP 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 155 S--GALTvrlaellcrgagrargdraaagaqvrlhllhrpSHL-VQVIeghsGFlprPGSPRVGKIVMAAAAK-HLTPVT 230
Cdd:cd07091   210 TagAAIS---------------------------------SHMdVDKI----AF---TGSTAVGRTIMEAAAKsNLKKVT 249

                         170       180
                  ....*....|....*....|....
gi 1878746647 231 LELGGKNPCYVDDNCDPQTVVEQV 254
Cdd:cd07091   250 LELGGKSPNIVFDDADLDKAVEWA 273
ALDH_ALD2-YMR170C cd07144
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ...
 79-268 1.35e-18

Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.


Pssm-ID: 143462  Cd Length: 484  Bit Score: 89.39  E-value: 1.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  79 AFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAevlpRYLDQAGGPP---SGLSGWGPS 155
Cdd:cd07144   138 AYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFA----NLVKEAGFPPgvvNIIPGYGAV 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 156 GAltVRLAEllcrgagrargdraaagaqvrlhllhrpsHL-VQVIeghsGFlprPGSPRVGKIVMAAAAKHLTPVTLELG 234
Cdd:cd07144   214 AG--SALAE-----------------------------HPdVDKI----AF---TGSTATGRLVMKAAAQNLKAVTLECG 255

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1878746647 235 GKNPCYVDDNCDPQTVVEQVLArtssgGFCGNDG 268
Cdd:cd07144   256 GKSPALVFEDADLDQAVKWAAA-----GIMYNSG 284
ndhI CHL00014
NADH dehydrogenase subunit I
 412-531 1.40e-18

NADH dehydrogenase subunit I


Pssm-ID: 214334 [Multi-domain]  Cd Length: 167  Bit Score: 83.66  E-value: 1.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 412 RGLGMTLSYLFREPATINYPFEKGPLSPRFRGehalrRYPSGEERCIACKLCEAVCPAQAITIEAEPRAD-GSRRTTRYD 490
Cdd:CHL00014   21 QGFMITLSHANRLPVTIQYPYEKLITSERFRG-----RIHFEFDKCIACEVCVRVCPIDLPVVDWKLETDiRKKRLLNYS 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1878746647 491 IDMTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEELLYNK 531
Cdd:CHL00014   96 IDFGVCIFCGNCVEYCPTNCLSMTEEYELSTYDRHELNYNQ 136
ALDH_DhaS cd07114
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ...
 79-256 1.49e-18

Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.


Pssm-ID: 143432 [Multi-domain]  Cd Length: 457  Bit Score: 88.76  E-value: 1.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  79 AFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVlpryLDQAGGPP---SGLSGWGPS 155
Cdd:cd07114   113 NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKL----AEEAGFPPgvvNVVTGFGPE 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 156 -GALTVRlaellcrgagrargdraaagaqvrlHllhrpsHLVQVIeghsGFlprPGSPRVGKIVMAAAAKHLTPVTLELG 234
Cdd:cd07114   189 tGEALVE-------------------------H------PLVAKI----AF---TGGTETGRHIARAAAENLAPVTLELG 230

                         170       180
                  ....*....|....*....|..
gi 1878746647 235 GKNPCYVDDNCDPQTVVEQVLA 256
Cdd:cd07114   231 GKSPNIVFDDADLDAAVNGVVA 252
ALDH_AldA-AAD23400 cd07106
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ...
 81-264 1.64e-18

Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.


Pssm-ID: 143424 [Multi-domain]  Cd Length: 446  Bit Score: 88.74  E-value: 1.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  81 IRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLPRYLdqaggppsglsgwgPSGALTV 160
Cdd:cd07106   110 LRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEVL--------------PPGVLNV 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 161 -----RLAELLCrgagrargdraaagaqvrlhllhrpSH-LVQVIeghsGFlprPGSPRVGKIVMAAAAKHLTPVTLELG 234
Cdd:cd07106   176 vsggdELGPALT-------------------------SHpDIRKI----SF---TGSTATGKKVMASAAKTLKRVTLELG 223

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1878746647 235 GKNPCYVDDNCDPQTVVEQV--LARTSSGGFC 264
Cdd:cd07106   224 GNDAAIVLPDVDIDAVAPKLfwGAFINSGQVC 255
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
 576-673 1.81e-18

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation


Pssm-ID: 440636 [Multi-domain]  Cd Length: 479  Bit Score: 88.64  E-value: 1.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 576 GEDPrsSPDLGRIINEKHFQRLQGLLGCG-----RVAIGGQ--SDESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNV 648
Cdd:COG1012   316 PLDP--GTDMGPLISEAQLERVLAYIEDAvaegaELLTGGRrpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPF 393

                          90       100
                  ....*....|....*....|....*
gi 1878746647 649 RSLDEAIDFIKRREKPLALYAFSNS 673
Cdd:COG1012   394 DDEEEAIALANDTEYGLAASVFTRD 418
BADH TIGR01804
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...
 77-266 2.86e-18

betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 200131 [Multi-domain]  Cd Length: 467  Bit Score: 88.33  E-value: 2.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  77 DSAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLpryldQAGGPPSGLSG--WGP 154
Cdd:TIGR01804 125 SFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIM-----EEAGLPKGVFNvvQGD 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 155 SGALTVRLAEllcrgagrargdraaagaqvrlhllHRPSHLVQVIeghsgflprpGSPRVGKIVMAAAAKHLTPVTLELG 234
Cdd:TIGR01804 200 GAEVGPLLVN-------------------------HPDVAKVSFT----------GGVPTGKKIMAAAAGHLKHVTMELG 244

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1878746647 235 GKNPCYVDDNCDPQTVVEQVLART--SSGGFCGN 266
Cdd:TIGR01804 245 GKSPLIVFDDADLESAVDGAMLGNffSAGQVCSN 278
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 454-512 3.68e-18

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 80.90  E-value: 3.68e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEAEPRADgsrrttrydIDMTKCIYCGFCQEACPVDAIV 512
Cdd:cd10549    77 EEKCIGCGLCVKVCPVDAITLEDELEIV---------IDKEKCIGCGICAEVCPVNAIK 126
ALDH_BenzADH-like cd07104
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ...
 81-246 4.46e-18

ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.


Pssm-ID: 143422 [Multi-domain]  Cd Length: 431  Bit Score: 87.20  E-value: 4.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  81 IRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSE---ISKSTekVLAEVLpryldQAGGPPSGLsgwgpsga 157
Cdd:cd07104    94 VRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSrtpVTGGL--LIAEIF-----EEAGLPKGV-------- 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 158 ltvrlaellcrgagrargdraaagaqvrLHLL-HRPSHLVQVIEGHsgflPRP------GSPRVGKIVMAAAAKHLTPVT 230
Cdd:cd07104   159 ----------------------------LNVVpGGGSEIGDALVEH----PRVrmisftGSTAVGRHIGELAGRHLKKVA 206

                         170
                  ....*....|....*.
gi 1878746647 231 LELGGKNPCYVDDNCD 246
Cdd:cd07104   207 LELGGNNPLIVLDDAD 222
ALDH_LactADH-AldA cd07088
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ...
 78-265 4.52e-18

Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.


Pssm-ID: 143407 [Multi-domain]  Cd Length: 468  Bit Score: 87.71  E-value: 4.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  78 SAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTekvlAEVLPRYLDQAGGPP---SGLSGWGP 154
Cdd:cd07088   126 NIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLN----ALEFAELVDEAGLPAgvlNIVTGRGS 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 155 sgaltvRLAELLCRgagrargdraaagaqvrlhllHRPSHLVQVIeghsgflprpGSPRVGKIVMAAAAKHLTPVTLELG 234
Cdd:cd07088   202 ------VVGDALVA---------------------HPKVGMISLT----------GSTEAGQKIMEAAAENITKVSLELG 244

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1878746647 235 GKNPCYVDDNCDPQTVVEQVLArtSSGGFCG 265
Cdd:cd07088   245 GKAPAIVMKDADLDLAVKAIVD--SRIINCG 273
PRK12387 PRK12387
formate hydrogenlyase complex iron-sulfur subunit; Provisional
 425-532 9.22e-18

formate hydrogenlyase complex iron-sulfur subunit; Provisional


Pssm-ID: 183492 [Multi-domain]  Cd Length: 180  Bit Score: 81.62  E-value: 9.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 425 PATINYPFEKGPLSPRFRG--EHALrrypsgeERCIACKLCEAVCPAQAITIEAepraDGSRRTTRYDIDMTKCIYCGFC 502
Cdd:PRK12387   13 TATSSYPLEPIAVDKNFRGkpEYNP-------QQCIGCAACVNACPSNALTVET----DLATGELAWEFNLGRCIFCGRC 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 1878746647 503 QEACPVDAIVEGPNFEFSTETHEELLYNKE 532
Cdd:PRK12387   82 EEVCPTAAIKLSQEFELAVWKKEDLLQQSE 111
ALDH_PsfA-ACA09737 cd07120
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ...
 81-264 1.73e-17

Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.


Pssm-ID: 143438 [Multi-domain]  Cd Length: 455  Bit Score: 85.47  E-value: 1.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  81 IRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVlpryLDQAGGPPSG----LSGWGPSG 156
Cdd:cd07120   113 VLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRI----LAEIPSLPAGvvnlFTESGSEG 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 157 AltVRLAEllcrgagrargdraaagaqvrlhllhrpSHLVQVIEghsgFlprPGSPRVGKIVMAAAAKHLTPVTLELGGK 236
Cdd:cd07120   189 A--AHLVA----------------------------SPDVDVIS----F---TGSTATGRAIMAAAAPTLKRLGLELGGK 231

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1878746647 237 NPCYVDDNCDPQTVVEqVLAR---TSSGGFC 264
Cdd:cd07120   232 TPCIVFDDADLDAALP-KLERaltIFAGQFC 261
ALDH_CddD-AldA-like cd07089
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ...
 78-268 2.08e-17

Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.


Pssm-ID: 143408 [Multi-domain]  Cd Length: 459  Bit Score: 85.37  E-value: 2.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  78 SAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVlpryLDQAGGPPSGLSGWGPSGA 157
Cdd:cd07089   116 RRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEI----IAETDLPAGVVNVVTGSDN 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 158 LTvrlAELLCrgagrargdraaagaqvrlhllhrpSHlvqvieghsgflPR------PGSPRVGKIVMAAAAKHLTPVTL 231
Cdd:cd07089   192 AV---GEALT-------------------------TD------------PRvdmvsfTGSTAVGRRIMAQAAATLKRVLL 231

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1878746647 232 ELGGKNPCYVDDNCDPQTVVEQVLartssGGFCGNDG 268
Cdd:cd07089   232 ELGGKSANIVLDDADLAAAAPAAV-----GVCMHNAG 263
ALDH_BADH-GbsA cd07119
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ...
 81-255 4.85e-17

Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.


Pssm-ID: 143437  Cd Length: 482  Bit Score: 84.28  E-value: 4.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  81 IRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVlpryLDQAGGPPSGLS-GWGPSGALT 159
Cdd:cd07119   130 TVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFEL----IEEAGLPAGVVNlVTGSGATVG 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 160 VRLAEllcrgagrargdraaagaqvrlhllhrpSHLVQVIeghsGFlprPGSPRVGKIVMAAAAKHLTPVTLELGGKNPC 239
Cdd:cd07119   206 AELAE----------------------------SPDVDLV----SF---TGGTATGRSIMRAAAGNVKKVALELGGKNPN 250

                         170
                  ....*....|....*.
gi 1878746647 240 YVDDNCDPQTVVEQVL 255
Cdd:cd07119   251 IVFADADFETAVDQAL 266
ALDH_SNDH cd07118
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ...
 79-255 6.78e-17

Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.


Pssm-ID: 143436 [Multi-domain]  Cd Length: 454  Bit Score: 83.93  E-value: 6.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  79 AFIRKEPFGLVLIVAPWNYPVnLTL---LPLvgALAAGNCVVLKPSEISKSTEKVLAEVLPRyldqaGGPPSG----LSG 151
Cdd:cd07118   113 GLVLREPIGVVGIITPWNFPF-LILsqkLPF--ALAAGCTVVVKPSEFTSGTTLMLAELLIE-----AGLPAGvvniVTG 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 152 WG-PSGaltvrlaellcrgagrargdraaagaqvrlhllhrpshlvQVIEGHSG--FLPRPGSPRVGKIVMAAAAKHLTP 228
Cdd:cd07118   185 YGaTVG----------------------------------------QAMTEHPDvdMVSFTGSTRVGKAIAAAAARNLKK 224

                         170       180
                  ....*....|....*....|....*..
gi 1878746647 229 VTLELGGKNPCYVDDNCDPQTVVEQVL 255
Cdd:cd07118   225 VSLELGGKNPQIVFADADLDAAADAVV 251
ALDH_ACDHII_AcoD-like cd07559
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ...
 73-238 6.81e-17

Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.


Pssm-ID: 143471 [Multi-domain]  Cd Length: 480  Bit Score: 83.93  E-value: 6.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  73 ATQLDS---AFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLPRYLdqaggppsgl 149
Cdd:cd07559   121 LSEIDEdtlSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLL---------- 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 150 sgwgPSGALTVrlaellcrgagrargdraaagaqvrlhLLHRPSHLVQVIEGHSGF--LPRPGSPRVGKIVMAAAAKHLT 227
Cdd:cd07559   191 ----PKGVVNV---------------------------VTGFGSEAGKPLASHPRIakLAFTGSTTVGRLIMQYAAENLI 239

                         170
                  ....*....|.
gi 1878746647 228 PVTLELGGKNP 238
Cdd:cd07559   240 PVTLELGGKSP 250
ALDH_F9_TMBADH cd07090
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ...
 79-246 8.21e-17

NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.


Pssm-ID: 143409 [Multi-domain]  Cd Length: 457  Bit Score: 83.51  E-value: 8.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  79 AFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLpryldQAGGPPSGL----SGWGP 154
Cdd:cd07090   110 AYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEIL-----TEAGLPDGVfnvvQGGGE 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 155 SGAltvrlaellcrgagrargdraaagaqvrlHLLHRPShLVQVieghsGFlprPGSPRVGKIVMAAAAKHLTPVTLELG 234
Cdd:cd07090   185 TGQ-----------------------------LLCEHPD-VAKV-----SF---TGSVPTGKKVMSAAAKGIKHVTLELG 226

                         170
                  ....*....|..
gi 1878746647 235 GKNPCYVDDNCD 246
Cdd:cd07090   227 GKSPLIIFDDAD 238
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
445-518 1.11e-16

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 74.77  E-value: 1.11e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1878746647 445 HALRRYPSGEERCIACKLCEAVCPAQAITIEAEPradgsrrttrYDIDMTKCIYCGFCQEACPVDAIVEGPNFE 518
Cdd:COG2768     1 HSLGKPYVDEEKCIGCGACVKVCPVGAISIEDGK----------AVIDPEKCIGCGACIEVCPVGAIKIEWEED 64
ALDH_SSADH1_GabD1 cd07100
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ...
 61-262 1.27e-16

Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.


Pssm-ID: 143418 [Multi-domain]  Cd Length: 429  Bit Score: 82.51  E-value: 1.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  61 AWMRDEQVrrnlATQLDSAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVlpryLD 140
Cdd:cd07100    76 AFLADEPI----ETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEEL----FR 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 141 QAGGPPsglsgwgpsGALTvrlaellcrgagrargdraaagaqvrlHLLHRPSHLVQVIEGhsgflPR------PGSPRV 214
Cdd:cd07100   148 EAGFPE---------GVFQ---------------------------NLLIDSDQVEAIIAD-----PRvrgvtlTGSERA 186

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1878746647 215 GKIVMAAAAKHLTPVTLELGGKNPCYVDDNCDPQTVVEQ-VLARTSSGG 262
Cdd:cd07100   187 GRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTaVKGRLQNAG 235
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 454-533 1.98e-16

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 75.90  E-value: 1.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEaepraDGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEELLYNKEK 533
Cdd:cd10549     5 PEKCIGCGICVKACPTDAIELG-----PNGAIARGPEIDEDKCVFCGACVEVCPTGAIELTPEGKEYVPKEKEAEIDEEK 79
ABALDH TIGR03374
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1. ...
 78-254 2.43e-16

1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1.35), also called gamma-aminobutyraldehyde dehydrogenase. This enzyme can follow putrescine transaminase (EC 2.6.1.82) for a two-step conversion of putrescine to gamma-aminobutyric acid (GABA). The member from Escherichia coli is characterized as a homotetramer that binds one NADH per momomer. This enzyme belongs to the medium-chain aldehyde dehydrogenases, and is quite similar in sequence to the betaine aldehyde dehydrogenase (EC 1.2.1.8) family.


Pssm-ID: 132417  Cd Length: 472  Bit Score: 82.36  E-value: 2.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  78 SAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLPRYLdqaggppsglsgwgPSGA 157
Cdd:TIGR03374 130 TSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDIF--------------PAGV 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 158 LTVrlaellcrgagrargdraaagaqvrlhLLHRPSHLVQVIEGHS--GFLPRPGSPRVGKIVMAAAAKHLTPVTLELGG 235
Cdd:TIGR03374 196 VNI---------------------------LFGRGKTVGDPLTGHEkvRMVSLTGSIATGEHILSHTAPSIKRTHMELGG 248

                         170
                  ....*....|....*....
gi 1878746647 236 KNPCYVDDNCDPQTVVEQV 254
Cdd:TIGR03374 249 KAPVIVFDDADIDAVVEGV 267
ALDH_AldA-Rv0768 cd07139
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ...
 66-252 5.74e-16

Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.


Pssm-ID: 143457 [Multi-domain]  Cd Length: 471  Bit Score: 81.08  E-value: 5.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  66 EQVRRNLATqlDSAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVlpryLDQAGGP 145
Cdd:cd07139   120 EERRPGSGG--GHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEA----AEEAGLP 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 146 PsglsgwgpsGALTVRLAEllcrgagrargdraaagAQVRLHLLhrpshlvqvieGHSG-----FlprPGSPRVGKIVMA 220
Cdd:cd07139   194 P---------GVVNVVPAD-----------------REVGEYLV-----------RHPGvdkvsF---TGSTAAGRRIAA 233

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1878746647 221 AAAKHLTPVTLELGGKNPCYVDDNCDPQTVVE 252
Cdd:cd07139   234 VCGERLARVTLELGGKSAAIVLDDADLDAAVP 265
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 454-519 5.93e-16

Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 72.78  E-value: 5.93e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEAEpradgsrrttRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEF 519
Cdd:COG2221    14 EEKCIGCGLCVAVCPTGAISLDDG----------KLVIDEEKCIGCGACIRVCPTGAIKGEKPKKF 69
ALDH_KGSADH-YcbD cd07097
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ...
 80-263 5.97e-16

Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.


Pssm-ID: 143415 [Multi-domain]  Cd Length: 473  Bit Score: 80.76  E-value: 5.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  80 FIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVlpryLDQAGGPPSGLS-GWGPSGAL 158
Cdd:cd07097   130 ETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEI----LEEAGLPAGVFNlVMGSGSEV 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 159 TVRLAEllcrgagrargdraaagaqvrlhllHRPshlVQVIEghsgFlprPGSPRVGKIVMAAAAKHLTPVTLELGGKNP 238
Cdd:cd07097   206 GQALVE-------------------------HPD---VDAVS----F---TGSTAVGRRIAAAAAARGARVQLEMGGKNP 250

                         170       180
                  ....*....|....*....|....*
gi 1878746647 239 CYVDDNCDPQTVVEQVLArtssGGF 263
Cdd:cd07097   251 LVVLDDADLDLAVECAVQ----GAF 271
ALDH_PADH_NahF cd07113
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ...
 78-255 1.02e-15

Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.


Pssm-ID: 143431  Cd Length: 477  Bit Score: 80.18  E-value: 1.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  78 SAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVlpryLDQAGGPPsglsgwgpsGA 157
Cdd:cd07113   135 TAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAEL----AKEAGIPD---------GV 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 158 LTVrlaellcrgagrargdrAAAGAQVRLHLLHRPsHLVQVieghsGFlprPGSPRVGKIVMAAAAKHLTPVTLELGGKN 237
Cdd:cd07113   202 LNV-----------------VNGKGAVGAQLISHP-DVAKV-----SF---TGSVATGKKIGRQAASDLTRVTLELGGKN 255

                         170
                  ....*....|....*...
gi 1878746647 238 PCYVDDNCDPQTVVEQVL 255
Cdd:cd07113   256 AAAFLKDADIDWVVEGLL 273
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
 559-656 1.42e-15

Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.


Pssm-ID: 425500 [Multi-domain]  Cd Length: 459  Bit Score: 79.50  E-value: 1.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 559 MQERLLPALQSAITRFYGEDPR-SSPDLGRIINEKHFQRLQGLL-----GCGRVAIGGQSDESD-RYIAPTVLVDVQETE 631
Cdd:pfam00171 281 IYDEFVEKLVEAAKKLKVGDPLdPDTDMGPLISKAQLERVLKYVedakeEGAKLLTGGEAGLDNgYFVEPTVLANVTPDM 360

                          90       100
                  ....*....|....*....|....*
gi 1878746647 632 PVMQEEIFGPILPIVNVRSLDEAID 656
Cdd:pfam00171 361 RIAQEEIFGPVLSVIRFKDEEEAIE 385
ALDH_F1AB_F2_RALDH1 cd07141
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ...
 79-253 2.31e-15

NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.


Pssm-ID: 143459  Cd Length: 481  Bit Score: 79.31  E-value: 2.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  79 AFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVlpryLDQAGGPP---SGLSGWGPS 155
Cdd:cd07141   139 TYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASL----IKEAGFPPgvvNVVPGYGPT 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 156 --GALTvrlaellcrgagrargdraaagaqvrlhllhrpSHL-VQVIeghsGFlprPGSPRVGKIVMAAAAK-HLTPVTL 231
Cdd:cd07141   215 agAAIS---------------------------------SHPdIDKV----AF---TGSTEVGKLIQQAAGKsNLKRVTL 254

                         170       180
                  ....*....|....*....|..
gi 1878746647 232 ELGGKNPCYVDDNCDPQTVVEQ 253
Cdd:cd07141   255 ELGGKSPNIVFADADLDYAVEQ 276
ALDH_y4uC cd07149
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ...
 79-264 3.01e-15

Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.


Pssm-ID: 143467 [Multi-domain]  Cd Length: 453  Bit Score: 78.79  E-value: 3.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  79 AFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVlpryLDQAGGPPsglsgwgpsGAL 158
Cdd:cd07149   117 GFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAEL----LLEAGLPK---------GAL 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 159 TVrlaellcrgagrargdraaagaqvrlhlLHRPSHLV-QVIEGHsgflPRP------GSPRVGKIVMAAAAkhLTPVTL 231
Cdd:cd07149   184 NV----------------------------VTGSGETVgDALVTD----PRVrmisftGSPAVGEAIARKAG--LKKVTL 229

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1878746647 232 ELGGKNPCYVDDNCDpqtvVEQVLARTSSGGFC 264
Cdd:cd07149   230 ELGSNAAVIVDADAD----LEKAVERCVSGAFA 258
ALDH_PhdK-like cd07107
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ...
 80-271 3.34e-15

Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.


Pssm-ID: 143425 [Multi-domain]  Cd Length: 456  Bit Score: 78.57  E-value: 3.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  80 FIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLPRYLdqaggPP---SGLSGWGPS- 155
Cdd:cd07107   111 YTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREVL-----PPgvfNILPGDGATa 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 156 GALTVRlaellcrgagrargdraaagaqvrlhllHRPSHLVQVIeghsgflprpGSPRVGKIVMAAAAKHLTPVTLELGG 235
Cdd:cd07107   186 GAALVR----------------------------HPDVKRIALI----------GSVPTGRAIMRAAAEGIKHVTLELGG 227

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1878746647 236 KNPCYVDDNCDPQTVVEQVLAR---TSSGGFCGND--GFMH 271
Cdd:cd07107   228 KNALIVFPDADPEAAADAAVAGmnfTWCGQSCGSTsrLFVH 268
ALDH_SSADH2_GabD2 cd07101
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ...
 56-264 6.81e-15

Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).


Pssm-ID: 143419 [Multi-domain]  Cd Length: 454  Bit Score: 77.35  E-value: 6.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  56 LRNLRAWMRDEQvRRNLATQLDSAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSeiSKSTEKVLAEVl 135
Cdd:cd07101    90 ARRAERLLKPRR-RRGAIPVLTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPD--SQTALTALWAV- 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 136 pRYLDQAGGPpsglsgwgpsgaltvrlAELLcrgagrargdraaagaQVrlhLLHRPSHLVQVIEGHSGFLPRPGSPRVG 215
Cdd:cd07101   166 -ELLIEAGLP-----------------RDLW----------------QV---VTGPGSEVGGAIVDNADYVMFTGSTATG 208

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1878746647 216 KIVMAAAAKHLTPVTLELGGKNPCYVDDNCDPQTVVEQVLAR--TSSGGFC 264
Cdd:cd07101   209 RVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRAcfSNAGQLC 259
PRK08222 PRK08222
hydrogenase 4 subunit H; Validated
 426-531 7.85e-15

hydrogenase 4 subunit H; Validated


Pssm-ID: 181301 [Multi-domain]  Cd Length: 181  Bit Score: 73.25  E-value: 7.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 426 ATINYPFEKGPLSPRFRGEHALrrypsGEERCIACKLCEAVCPAQAITIEAepraDGSRRTTRYDIDMTKCIYCGFCQEA 505
Cdd:PRK08222   14 ATVKYPFAPLEVSPGFRGKPDL-----MPSQCIACGACTCACPANALTIQT----DDQQNSRTWQLYLGRCIYCGRCEEV 84

                          90       100
                  ....*....|....*....|....*.
gi 1878746647 506 CPVDAIVEGPNFEFsTETHEELLYNK 531
Cdd:PRK08222   85 CPTRAIQLTNNFEL-TVTNKADLYTR 109
ALDH_AldH-CAJ73105 cd07131
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ...
 79-255 8.15e-15

Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.


Pssm-ID: 143449 [Multi-domain]  Cd Length: 478  Bit Score: 77.39  E-value: 8.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  79 AFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEvlprYLDQAGGPPSGLS---GWGPS 155
Cdd:cd07131   129 AMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVE----LFAEAGLPPGVVNvvhGRGEE 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 156 -GALTVRlaellcrgagrargdraaagaqvrlhllhrpsHL-VQVIeghsGFlprPGSPRVGKIVMAAAAKHLTPVTLEL 233
Cdd:cd07131   205 vGEALVE--------------------------------HPdVDVV----SF---TGSTEVGERIGETCARPNKRVALEM 245

                         170       180
                  ....*....|....*....|..
gi 1878746647 234 GGKNPCYVDDNCDPQTVVEQVL 255
Cdd:cd07131   246 GGKNPIIVMDDADLDLALEGAL 267
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 457-510 1.03e-14

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 68.71  E-value: 1.03e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1878746647 457 CIACKLCEAVCPAQAITIEAEPRADGsrrTTRYDIDMTKCIYCGFCQEACPVDA 510
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKKG---TKTVVIDPERCVGCGACVAVCPTGA 51
PLN02278 PLN02278
succinic semialdehyde dehydrogenase
 80-256 1.04e-14

succinic semialdehyde dehydrogenase


Pssm-ID: 215157 [Multi-domain]  Cd Length: 498  Bit Score: 77.04  E-value: 1.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  80 FIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEvLPrylDQAGGPPsglsgwgpsGALT 159
Cdd:PLN02278  155 LVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAE-LA---LQAGIPP---------GVLN 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 160 VRLAEllcrgagrargdraaaGAQVRLHLLHrpSHLVQVIeghsGFlprPGSPRVGKIVMAAAAKHLTPVTLELGGKNPC 239
Cdd:PLN02278  222 VVMGD----------------APEIGDALLA--SPKVRKI----TF---TGSTAVGKKLMAGAAATVKRVSLELGGNAPF 276

                         170
                  ....*....|....*..
gi 1878746647 240 YVDDNCDPQTVVEQVLA 256
Cdd:PLN02278  277 IVFDDADLDVAVKGALA 293
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 454-511 1.34e-14

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 70.89  E-value: 1.34e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEaEPRADGSRRTTRYDIDMTKCIYCGFCQEACPVDAI 511
Cdd:cd10549    39 EDKCVFCGACVEVCPTGAIELT-PEGKEYVPKEKEAEIDEEKCIGCGLCVKVCPVDAI 95
ALDH_F11_NP-GAPDH cd07082
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ...
 79-256 1.69e-14

NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.


Pssm-ID: 143401 [Multi-domain]  Cd Length: 473  Bit Score: 76.46  E-value: 1.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  79 AFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSeiskSTEKVLAEVLPRYLDQAGGPPSGLSgwgpsgAL 158
Cdd:cd07082   135 AQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPA----TQGVLLGIPLAEAFHDAGFPKGVVN------VV 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 159 TVRLAELLcrgagrargdraaagaqvrlhllhrpSHLVQviEGHSGFLPRPGSPRVGKIVMAAAAKhlTPVTLELGGKNP 238
Cdd:cd07082   205 TGRGREIG--------------------------DPLVT--HGRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDP 254

                         170
                  ....*....|....*...
gi 1878746647 239 CYVDDNCDPQTVVEQVLA 256
Cdd:cd07082   255 AIVLPDADLELAAKEIVK 272
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 454-512 1.72e-14

TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 68.92  E-value: 1.72e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEAEPRAdgsrrttrydIDMTKCIYCGFCQEACPVDAIV 512
Cdd:COG4231    21 EDKCTGCGACVKVCPADAIEEGDGKAV----------IDPDLCIGCGSCVQVCPVDAIK 69
PRK03137 PRK03137
1-pyrroline-5-carboxylate dehydrogenase; Provisional
 578-656 1.93e-14

1-pyrroline-5-carboxylate dehydrogenase; Provisional


Pssm-ID: 179543  Cd Length: 514  Bit Score: 76.51  E-value: 1.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 578 DPRSSPDLGRIINEKHFQRLQGLL----GCGRVAIGGQSDESDRY-IAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLD 652
Cdd:PRK03137  351 NPEDNAYMGPVINQASFDKIMSYIeigkEEGRLVLGGEGDDSKGYfIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFD 430


                  ....
gi 1878746647 653 EAID 656
Cdd:PRK03137  431 HALE 434
ALDH_PutA-P5CDH-RocA cd07124
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ...
 84-265 2.28e-14

Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.


Pssm-ID: 143442  Cd Length: 512  Bit Score: 76.11  E-value: 2.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  84 EPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISksteKVLAEVLPRYLDQAGGPPsglsgwgpsGAltvrla 163
Cdd:cd07124   165 RPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDT----PVIAAKLVEILEEAGLPP---------GV------ 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 164 ellcrgagrargdraaagaqvrLHLLH-RPSHLVQVIEGHS--GFLPRPGSPRVGKIVMAAAAK------HLTPVTLELG 234
Cdd:cd07124   226 ----------------------VNFLPgPGEEVGDYLVEHPdvRFIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMG 283

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1878746647 235 GKNPCYVDDNCDPQTVVEQVLArtSSGGFCG 265
Cdd:cd07124   284 GKNAIIVDEDADLDEAAEGIVR--SAFGFQG 312
ALDH_GABALDH-PuuC cd07112
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ...
 79-256 2.55e-14

Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.


Pssm-ID: 143430 [Multi-domain]  Cd Length: 462  Bit Score: 75.72  E-value: 2.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  79 AFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEvlpryLDQAGGPPSG----LSGWGP 154
Cdd:cd07112   118 ALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAE-----LALEAGLPAGvlnvVPGFGH 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 155 SG--ALTvrlaellcrgagrargdraaagaqvrlhlLHRpshLVQVIeghsGFlprPGSPRVGKIVMAAAAK-HLTPVTL 231
Cdd:cd07112   193 TAgeALG-----------------------------LHM---DVDAL----AF---TGSTEVGRRFLEYSGQsNLKRVWL 233

                         170       180
                  ....*....|....*....|....*.
gi 1878746647 232 ELGGKNPCYVDDNC-DPQTVVEQVLA 256
Cdd:cd07112   234 ECGGKSPNIVFADApDLDAAAEAAAA 259
NapF COG1145
Ferredoxin [Energy production and conversion];
454-511 3.93e-14

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 72.45  E-value: 3.93e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEAEpradgsrrTTRYDIDMTKCIYCGFCQEACPVDAI 511
Cdd:COG1145   181 AEKCIGCGLCVKVCPTGAIRLKDG--------KPQIVVDPDKCIGCGACVKVCPVGAI 230
ALDH_F5_SSADH_GabD cd07103
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ...
 584-673 4.30e-14

Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.


Pssm-ID: 143421 [Multi-domain]  Cd Length: 451  Bit Score: 75.16  E-value: 4.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 584 DLGRIINEKHFQRLQGL----LGCG-RVAIGGQSDESD-RYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLDEAIDF 657
Cdd:cd07103   298 DMGPLINERAVEKVEALvedaVAKGaKVLTGGKRLGLGgYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIAR 377

                          90
                  ....*....|....*.
gi 1878746647 658 IKRREKPLALYAFSNS 673
Cdd:cd07103   378 ANDTPYGLAAYVFTRD 393
ALDH_HMSADH_HapE cd07115
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ...
 80-270 4.66e-14

Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.


Pssm-ID: 143433 [Multi-domain]  Cd Length: 453  Bit Score: 74.78  E-value: 4.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  80 FIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVlpryLDQAGGPPsglsgwgpsGALT 159
Cdd:cd07115   112 YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAEL----MAEAGFPA---------GVLN 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 160 VrlaellcrgagrargdraaagaqvrlhlLHRPSHLV-QVIEGHSGF--LPRPGSPRVGKIVMAAAAKHLTPVTLELGGK 236
Cdd:cd07115   179 V----------------------------VTGFGEVAgAALVEHPDVdkITFTGSTAVGRKIMQGAAGNLKRVSLELGGK 230

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1878746647 237 NPCYVDDNCDPQTVVeqvlaRTSSGGFCGNDGFM 270
Cdd:cd07115   231 SANIVFADADLDAAV-----RAAATGIFYNQGQM 259
ALDH_F7_AASADH-like cd07086
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ...
 85-255 4.81e-14

NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).


Pssm-ID: 143405 [Multi-domain]  Cd Length: 478  Bit Score: 74.91  E-value: 4.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  85 PFGLVLIVAPWNYPV-----NLTLlplvgALAAGNCVVLKPSE----ISKSTEKVLAEVlpryLDQAGGPPSGLS---GW 152
Cdd:cd07086   133 PLGVVGVITAFNFPVavpgwNAAI-----ALVCGNTVVWKPSEttplTAIAVTKILAEV----LEKNGLPPGVVNlvtGG 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 153 GPSGALTVRLAEllcrgagrargdraaagaqvrlhllhrpshlVQVIeghsGFlprPGSPRVGKIVMAAAAKHLTPVTLE 232
Cdd:cd07086   204 GDGGELLVHDPR-------------------------------VPLV----SF---TGSTEVGRRVGETVARRFGRVLLE 245

                         170       180
                  ....*....|....*....|...
gi 1878746647 233 LGGKNPCYVDDNCDPQTVVEQVL 255
Cdd:cd07086   246 LGGNNAIIVMDDADLDLAVRAVL 268
PRK10090 PRK10090
aldehyde dehydrogenase A; Provisional
 561-656 5.64e-14

aldehyde dehydrogenase A; Provisional


Pssm-ID: 182233 [Multi-domain]  Cd Length: 409  Bit Score: 74.39  E-value: 5.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 561 ERLLPALqSAITrfYGeDP--RSSPDLGRIINEKHFQRLQGLLG-----CGRVAIGGQSDESDRYI-APTVLVDVQETEP 632
Cdd:PRK10090  232 NRLGEAM-QAVQ--FG-NPaeRNDIAMGPLINAAALERVEQKVAraveeGARVALGGKAVEGKGYYyPPTLLLDVRQEMS 307

                          90       100
                  ....*....|....*....|....
gi 1878746647 633 VMQEEIFGPILPIVNVRSLDEAID 656
Cdd:PRK10090  308 IMHEETFGPVLPVVAFDTLEEAIA 331
ALDH_BenzADH cd07152
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ...
 3-246 1.00e-13

NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.


Pssm-ID: 143470 [Multi-domain]  Cd Length: 443  Bit Score: 73.87  E-value: 1.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647   3 PPRKLRAVVTKAtqqqqlAALGTDAQPWAQDW--------MSAVELEVSE-ISIVQTEINLALRNLRAWMRDEQVRRNLA 73
Cdd:cd07152    33 PPRERAAVLRRA------ADLLEEHADEIADWivresgsiRPKAGFEVGAaIGELHEAAGLPTQPQGEILPSAPGRLSLA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  74 tqldsafiRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVlaeVLPRYLDQAGGPPsGLSGWG 153
Cdd:cd07152   107 --------RRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGV---VIARLFEEAGLPA-GVLHVL 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 154 PSGALTvrlAELLCRGAGrargdraaagaqvrlhllhrpshlVQVIEghsgFlprPGSPRVGKIVMAAAAKHLTPVTLEL 233
Cdd:cd07152   175 PGGADA---GEALVEDPN------------------------VAMIS----F---TGSTAVGRKVGEAAGRHLKKVSLEL 220

                         250
                  ....*....|...
gi 1878746647 234 GGKNPCYVDDNCD 246
Cdd:cd07152   221 GGKNALIVLDDAD 233
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 454-512 1.14e-13

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 66.61  E-value: 1.14e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEAEpradgsrrtTRYDIDMTKCIYCGFCQEACPVDAIV 512
Cdd:COG1144    29 EDKCIGCGLCWIVCPDGAIRVDDG---------KYYGIDYDYCKGCGICAEVCPVKAIE 78
ALDH_StaphAldA1 cd07117
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ...
 73-254 1.57e-13

Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.


Pssm-ID: 143435  Cd Length: 475  Bit Score: 73.26  E-value: 1.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  73 ATQLDSAF---IRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLPRYLdqaggppsgl 149
Cdd:cd07117   121 ANMIDEDTlsiVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDVL---------- 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 150 sgwgPSGALTVrlaellcrgagrargdraaagaqvrlhLLHRPSHLVQVIEGHSGF--LPRPGSPRVGKIVMAAAAKHLT 227
Cdd:cd07117   191 ----PKGVVNI---------------------------VTGKGSKSGEYLLNHPGLdkLAFTGSTEVGRDVAIAAAKKLI 239

                         170       180
                  ....*....|....*....|....*..
gi 1878746647 228 PVTLELGGKNPCYVDDNCDPQTVVEQV 254
Cdd:cd07117   240 PATLELGGKSANIIFDDANWDKALEGA 266
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 454-515 1.82e-13

MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 65.52  E-value: 1.82e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEAEpradgsrrtTRYDIDMTKCIYCGFCQEACPVDAIVEGP 515
Cdd:COG1149    10 EEKCIGCGLCVEVCPEGAIKLDDG---------GAPVVDPDLCTGCGACVGVCPTGAITLEE 62
ALDH_LactADH-AldA cd07088
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ...
 583-673 1.84e-13

Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.


Pssm-ID: 143407 [Multi-domain]  Cd Length: 468  Bit Score: 73.07  E-value: 1.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 583 PDLGRIINEKHFQRLQGLL------GcGRVAIGGQSDESDR--YIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLDEA 654
Cdd:cd07088   313 TDMGPLVNEAALDKVEEMVeraveaG-ATLLTGGKRPEGEKgyFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEA 391

                          90
                  ....*....|....*....
gi 1878746647 655 IDFIKRREKPLALYAFSNS 673
Cdd:cd07088   392 IELANDSEYGLTSYIYTEN 410
ALDH_F21_LactADH-like cd07094
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ...
 79-263 2.07e-13

ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.


Pssm-ID: 143413 [Multi-domain]  Cd Length: 453  Bit Score: 72.85  E-value: 2.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  79 AFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVlpryLDQAGGPPsglsgwgpsGAL 158
Cdd:cd07094   117 AWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKI----LVEAGVPE---------GVL 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 159 TVRLAEllcrgagrargdraaagaqvrlhllhrPSHLVQVIEGHSGF--LPRPGSPRVGKIVMAAAAKhlTPVTLELGGK 236
Cdd:cd07094   184 QVVTGE---------------------------REVLGDAFAADERVamLSFTGSAAVGEALRANAGG--KRIALELGGN 234

                         170       180
                  ....*....|....*....|....*..
gi 1878746647 237 NPCYVDDNCDPQTVVEqvlaRTSSGGF 263
Cdd:cd07094   235 APVIVDRDADLDAAIE----ALAKGGF 257
ALDH_F1L_FTFDH cd07140
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ...
 80-253 2.26e-13

10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.


Pssm-ID: 143458 [Multi-domain]  Cd Length: 486  Bit Score: 72.91  E-value: 2.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  80 FIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLPRyldqAGGPPSGLSGWGPSGALt 159
Cdd:cd07140   142 LTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVK----AGFPKGVINILPGSGSL- 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 160 vrlaellcrgagrargdraaagaqVRLHLLHRPshLVQVIeghsGFlprPGSPRVGKIVMAAAAK-HLTPVTLELGGKNP 238
Cdd:cd07140   217 ------------------------VGQRLSDHP--DVRKL----GF---TGSTPIGKHIMKSCAVsNLKKVSLELGGKSP 263

                         170
                  ....*....|....*
gi 1878746647 239 CYVDDNCDPQTVVEQ 253
Cdd:cd07140   264 LIIFADCDMDKAVRM 278
ALDH_AldA_AN0554 cd07143
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ...
 79-263 2.29e-13

Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.


Pssm-ID: 143461  Cd Length: 481  Bit Score: 72.95  E-value: 2.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  79 AFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLPryldQAGGPP---SGLSGWGPS 155
Cdd:cd07143   138 TYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIP----EAGFPPgviNVVSGYGRT 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 156 GAltvrlaellcrgagrargdraaagaqvrlhllhrpshlvQVIEGHSGF--LPRPGSPRVGKIVMAAAAK-HLTPVTLE 232
Cdd:cd07143   214 CG---------------------------------------NAISSHMDIdkVAFTGSTLVGRKVMEAAAKsNLKKVTLE 254

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1878746647 233 LGGKNPCYVDDNCDpqtvVEQVLARTSSGGF 263
Cdd:cd07143   255 LGGKSPNIVFDDAD----LESAVVWTAYGIF 281
ALDH_ACDHII-AcoD cd07116
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ...
 73-238 3.13e-13

Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.


Pssm-ID: 143434 [Multi-domain]  Cd Length: 479  Bit Score: 72.48  E-value: 3.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  73 ATQLDS---AFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVlpryldqaggppsgl 149
Cdd:cd07116   121 ISEIDEntvAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMEL--------------- 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 150 sgwgpsgaltvrLAELLcrgagrargdraaagaqvrlhllhrPSHLVQVIEGHSGFLPRP--GSPRVGKI---------- 217
Cdd:cd07116   186 ------------IGDLL-------------------------PPGVVNVVNGFGLEAGKPlaSSKRIAKVaftgetttgr 228

                         170       180
                  ....*....|....*....|..
gi 1878746647 218 -VMAAAAKHLTPVTLELGGKNP 238
Cdd:cd07116   229 lIMQYASENIIPVTLELGGKSP 250
PRK13252 PRK13252
betaine aldehyde dehydrogenase; Provisional
 77-266 4.72e-13

betaine aldehyde dehydrogenase; Provisional


Pssm-ID: 183918  Cd Length: 488  Bit Score: 71.84  E-value: 4.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  77 DSAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVlpryLDQAGGPPsG----LSGW 152
Cdd:PRK13252  134 SFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEI----YTEAGLPD-GvfnvVQGD 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 153 GPSGALtvrlaellcrgagrargdraaagaqvrlhLLHRPshlvqVIEGHSgFlprPGSPRVGKIVMAAAAKHLTPVTLE 232
Cdd:PRK13252  209 GRVGAW-----------------------------LTEHP-----DIAKVS-F---TGGVPTGKKVMAAAAASLKEVTME 250

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1878746647 233 LGGKNPCYVDDNCDPQTVVE-QVLAR-TSSGGFCGN 266
Cdd:PRK13252  251 LGGKSPLIVFDDADLDRAADiAMLANfYSSGQVCTN 286
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 454-511 9.89e-13

NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 63.57  E-value: 9.89e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEAEpradgSRRTTRYDIDmtKCIYCGFCQEACPVDAI 511
Cdd:COG1146     7 TDKCIGCGACVEVCPVDVLELDEE-----GKKALVINPE--ECIGCGACELVCPVGAI 57
ALDH_F2BC cd07142
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ...
 83-252 9.93e-13

Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.


Pssm-ID: 143460  Cd Length: 476  Bit Score: 70.99  E-value: 9.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  83 KEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLPryldQAGGPPSGL---SGWGPS-GAl 158
Cdd:cd07142   139 HEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAA----EAGLPDGVLnivTGFGPTaGA- 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 159 tvrlaellcrgagrargdraaagaqvrlhllHRPSHL-VQVIeghsGFlprPGSPRVGKIVMAAAAK-HLTPVTLELGGK 236
Cdd:cd07142   214 -------------------------------AIASHMdVDKV----AF---TGSTEVGKIIMQLAAKsNLKPVTLELGGK 255

                         170
                  ....*....|....*.
gi 1878746647 237 NPCYVDDNCDPQTVVE 252
Cdd:cd07142   256 SPFIVCEDADVDKAVE 271
ALDH_AldA-AAD23400 cd07106
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ...
 576-656 1.23e-12

Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.


Pssm-ID: 143424 [Multi-domain]  Cd Length: 446  Bit Score: 70.25  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 576 GEDPRSspDLGRIINEKHFQRLQGLL-----GCGRVAIGGQSDESDRY-IAPTVLVDVQETEPVMQEEIFGPILPIVNVR 649
Cdd:cd07106   287 GLDPGT--TLGPVQNKMQYDKVKELVedakaKGAKVLAGGEPLDGPGYfIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYS 364


                  ....*..
gi 1878746647 650 SLDEAID 656
Cdd:cd07106   365 DEDEVIA 371
ALDH_BenzADH-like cd07104
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ...
 578-656 1.89e-12

ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.


Pssm-ID: 143422 [Multi-domain]  Cd Length: 431  Bit Score: 69.87  E-value: 1.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 578 DPRSsPD--LGRIINEKHFQRLQGLL------GcGRVAIGGQSDesDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVR 649
Cdd:cd07104   273 DPRD-PDtvIGPLINERQVDRVHAIVedavaaG-ARLLTGGTYE--GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFD 348


                  ....*..
gi 1878746647 650 SLDEAID 656
Cdd:cd07104   349 DDEEAVE 355
ALDH_DDALDH cd07099
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ...
 576-675 2.21e-12

Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.


Pssm-ID: 143417 [Multi-domain]  Cd Length: 453  Bit Score: 69.56  E-value: 2.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 576 GEDPRSSPDLGRIINEK-------HFQrlQGLLGCGRVAIGG-QSDESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVN 647
Cdd:cd07099   290 GADDIGDADIGPMTTARqldivrrHVD--DAVAKGAKALTGGaRSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMP 367

                          90       100
                  ....*....|....*....|....*...
gi 1878746647 648 VRSLDEAIDFIKRREKPLALYAFSNSNQ 675
Cdd:cd07099   368 VADEDEAIALANDSRYGLSASVFSRDLA 395
gabD2 PRK09407
succinic semialdehyde dehydrogenase; Reviewed
 85-264 2.64e-12

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236501 [Multi-domain]  Cd Length: 524  Bit Score: 69.52  E-value: 2.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  85 PFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSeiSKSTEKVLAEVlpRYLDQAGGPPSglsgwgpsgaltvrlae 164
Cdd:PRK09407  154 PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPD--SQTPLTALAAV--ELLYEAGLPRD----------------- 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 165 llcrgagrargdraaagaqvrlhllhrpshLVQVIEG-----------HSGFLPRPGSPRVGKIVMAAAAKHLTPVTLEL 233
Cdd:PRK09407  213 ------------------------------LWQVVTGpgpvvgtalvdNADYLMFTGSTATGRVLAEQAGRRLIGFSLEL 262

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1878746647 234 GGKNPCYVDDNCDPQTVVEQVL--ARTSSGGFC 264
Cdd:PRK09407  263 GGKNPMIVLDDADLDKAAAGAVraCFSNAGQLC 295
PLN02766 PLN02766
coniferyl-aldehyde dehydrogenase
 83-255 2.98e-12

coniferyl-aldehyde dehydrogenase


Pssm-ID: 215410 [Multi-domain]  Cd Length: 501  Bit Score: 69.46  E-value: 2.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  83 KEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEiskstEKVLAEVLPRYLDQAGGPPSG----LSGWGPSGAL 158
Cdd:PLN02766  156 KEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAE-----QTPLSALFYAHLAKLAGVPDGvinvVTGFGPTAGA 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 159 TVrlaellcrgagrargdraaagaqvrlhllhrPSHL-VQVIeghsGFlprPGSPRVGKIVMAAAAK-HLTPVTLELGGK 236
Cdd:PLN02766  231 AI-------------------------------ASHMdVDKV----SF---TGSTEVGRKIMQAAATsNLKQVSLELGGK 272

                         170
                  ....*....|....*....
gi 1878746647 237 NPCYVDDNCDPQTVVEQVL 255
Cdd:PLN02766  273 SPLLIFDDADVDMAVDLAL 291
ALDH_GABALDH-PuuC cd07112
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ...
 561-655 4.78e-12

Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.


Pssm-ID: 143430 [Multi-domain]  Cd Length: 462  Bit Score: 68.78  E-value: 4.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 561 ERLLPALQSAITRFYGEDPRS-SPDLGRIINEKHFQRLQGLLGCG-----RVAIGGQSDESDR---YIAPTVLVDVQETE 631
Cdd:cd07112   283 DEFLEKVVAAAREWKPGDPLDpATRMGALVSEAHFDKVLGYIESGkaegaRLVAGGKRVLTETggfFVEPTVFDGVTPDM 362

                          90       100
                  ....*....|....*....|....
gi 1878746647 632 PVMQEEIFGPILPIVNVRSLDEAI 655
Cdd:cd07112   363 RIAREEIFGPVLSVITFDSEEEAV 386
ALDH_F6_MMSDH cd07085
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ...
 561-662 4.83e-12

Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.


Pssm-ID: 143404 [Multi-domain]  Cd Length: 478  Bit Score: 68.70  E-value: 4.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 561 ERLLPALQSAITRF---YGEDPRSspDLGRIINEKHFQRLQGLLGCG-----RVAIGGQSDESDRY-----IAPTVLVDV 627
Cdd:cd07085   292 DEWIPKLVERAKKLkvgAGDDPGA--DMGPVISPAAKERIEGLIESGveegaKLVLDGRGVKVPGYengnfVGPTILDNV 369

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1878746647 628 QETEPVMQEEIFGPILPIVNVRSLDEAIDFIKRRE 662
Cdd:cd07085   370 TPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANP 404
ALDH_PutA-P5CDH-RocA cd07124
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ...
 578-657 4.90e-12

Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.


Pssm-ID: 143442  Cd Length: 512  Bit Score: 68.79  E-value: 4.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 578 DPRS-SPDLGRIINEKHFQRLQGLL----GCGRVAIGGQSDESDR---YIAPTVLVDVQETEPVMQEEIFGPILPIVNVR 649
Cdd:cd07124   346 DPEDpEVYMGPVIDKGARDRIRRYIeigkSEGRLLLGGEVLELAAegyFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAK 425


                  ....*...
gi 1878746647 650 SLDEAIDF 657
Cdd:cd07124   426 DFDEALEI 433
PLN02466 PLN02466
aldehyde dehydrogenase family 2 member
 84-252 5.00e-12

aldehyde dehydrogenase family 2 member


Pssm-ID: 215259 [Multi-domain]  Cd Length: 538  Bit Score: 68.68  E-value: 5.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  84 EPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTekvlAEVLPRYLDQAGGPPSGL---SGWGPS-GAlt 159
Cdd:PLN02466  194 EPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLS----ALYAAKLLHEAGLPPGVLnvvSGFGPTaGA-- 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 160 vRLAellcrgagrargdraaagaqvrlhllhrpSHLvqviegHSGFLPRPGSPRVGKIVMAAAAK-HLTPVTLELGGKNP 238
Cdd:PLN02466  268 -ALA-----------------------------SHM------DVDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSP 311

                         170
                  ....*....|....
gi 1878746647 239 CYVDDNCDPQTVVE 252
Cdd:PLN02466  312 FIVCEDADVDKAVE 325
ALDH_F16 cd07111
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ...
 73-254 7.66e-12

Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.


Pssm-ID: 143429 [Multi-domain]  Cd Length: 480  Bit Score: 68.19  E-value: 7.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  73 ATQLDSAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLpryldQAGGPPSGLsgw 152
Cdd:cd07111   135 AQLLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEIC-----AEAGLPPGV--- 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 153 gpsgaltvrlaellcrgagrargdraaagaqvrLHLLHRPSHLVQVIEGHSGF--LPRPGSPRVGKIVMAAAAKHLTPVT 230
Cdd:cd07111   207 ---------------------------------LNIVTGNGSFGSALANHPGVdkVAFTGSTEVGRALRRATAGTGKKLS 253

                         170       180
                  ....*....|....*....|....
gi 1878746647 231 LELGGKNPCYVDDNCDPQTVVEQV 254
Cdd:cd07111   254 LELGGKSPFIVFDDADLDSAVEGI 277
D1pyr5carbox2 TIGR01237
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ...
 85-265 9.61e-12

delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]


Pssm-ID: 200087 [Multi-domain]  Cd Length: 511  Bit Score: 67.97  E-value: 9.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  85 PFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLpryldQAGGPPSGLSGWGP-SGAltvrla 163
Cdd:TIGR01237 167 PTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEIL-----EEAGLPKGVVQFVPgSGS------ 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 164 ellcrgagrargdraaagaQVRLHLLHRPShlvqvieghSGFLPRPGSPRVGKIVMAAAAK------HLTPVTLELGGKN 237
Cdd:TIGR01237 236 -------------------EVGDYLVDHPK---------TSLITFTGSREVGTRIFERAAKvqpgqkHLKRVIAEMGGKD 287

                         170       180
                  ....*....|....*....|....*...
gi 1878746647 238 PCYVDDNCDPQTVVEQvlARTSSGGFCG 265
Cdd:TIGR01237 288 TVIVDEDADIELAAQS--AFTSAFGFAG 313
ALDH_BenzADH cd07152
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ...
 578-673 1.03e-11

NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.


Pssm-ID: 143470 [Multi-domain]  Cd Length: 443  Bit Score: 67.32  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 578 DPRSSP-DLGRIINEKHFQRLQGL------LGcGRVAIGGQSDesDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRS 650
Cdd:cd07152   284 DPATGQvALGPLINARQLDRVHAIvddsvaAG-ARLEAGGTYD--GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDS 360

                          90       100
                  ....*....|....*....|...
gi 1878746647 651 LDEAIDFIKRREKPLALYAFSNS 673
Cdd:cd07152   361 DEEAVALANDTEYGLSAGIISRD 383
PRK13984 PRK13984
putative oxidoreductase; Provisional
 420-506 1.21e-11

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 67.87  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 420 YLFREPATINYPFEKGPLSPRFRGEHAlrrypSGEERCIACKLCEAVCPAQAIT---IEAEPRADGSrRTTRYDIDMTKC 496
Cdd:PRK13984   15 FLFRKPVTIKVPNVKREAAERYRGFHI-----NDWEKCIGCGTCSKICPTDAITmveVPDLPQEYGK-KPQRPVIDYGRC 88

                          90
                  ....*....|
gi 1878746647 497 IYCGFCQEAC 506
Cdd:PRK13984   89 SFCALCVDIC 98
ALDH_F21_RNP123 cd07147
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ...
 66-263 2.02e-11

Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.


Pssm-ID: 143465 [Multi-domain]  Cd Length: 452  Bit Score: 66.50  E-value: 2.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  66 EQVRRNLATQLD----------SAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVL 135
Cdd:cd07147    94 EEATRIYGEVLPldisargegrQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVL 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 136 PRyldqaggppsglSGWgPSGALTVrlaeLLCrgagrargdraaagaqvrlhllHRPSHLVQVIEGHSGFLPRPGSPRVG 215
Cdd:cd07147   174 AE------------TGL-PKGAFSV----LPC----------------------SRDDADLLVTDERIKLLSFTGSPAVG 214

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1878746647 216 -KIVMAAAAKHltpVTLELGGKNPCYVDDNCDPQTVVEQVLArtssGGF 263
Cdd:cd07147   215 wDLKARAGKKK---VVLELGGNAAVIVDSDADLDFAAQRIIF----GAF 256
PRK10090 PRK10090
aldehyde dehydrogenase A; Provisional
 80-264 2.84e-11

aldehyde dehydrogenase A; Provisional


Pssm-ID: 182233 [Multi-domain]  Cd Length: 409  Bit Score: 65.91  E-value: 2.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  80 FIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLprylDQAGGPpsglsgwgpSGALT 159
Cdd:PRK10090   66 LLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIV----DEIGLP---------KGVFN 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 160 VrlaellcrgagrargdraaagaqvrlhLLHRPSHLVQVIEGHS--GFLPRPGSPRVGKIVMAAAAKHLTPVTLELGGKN 237
Cdd:PRK10090  133 L---------------------------VLGRGETVGQELAGNPkvAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKA 185

                         170       180
                  ....*....|....*....|....*....
gi 1878746647 238 PCYVDDNCDPQTVVEQVLAR--TSSGGFC 264
Cdd:PRK10090  186 PAIVMDDADLDLAVKAIVDSrvINSGQVC 214
ALDH_LactADH_F420-Bios cd07145
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ...
 578-672 3.98e-11

Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.


Pssm-ID: 143463 [Multi-domain]  Cd Length: 456  Bit Score: 65.83  E-value: 3.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 578 DP-RSSPDLGRIINEKHFQRLQGLL------GcGRVAIGGQSDESDrYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRS 650
Cdd:cd07145   297 DPlDESTDLGPLISPEAVERMENLVndavekG-GKILYGGKRDEGS-FFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKD 374

                          90       100
                  ....*....|....*....|..
gi 1878746647 651 LDEAIDFIKRREKPLALYAFSN 672
Cdd:cd07145   375 DEEAVEIANSTEYGLQASVFTN 396
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 414-522 4.62e-11

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 60.62  E-value: 4.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 414 LGMTLSYLFREPATINYP-FEKGPLSPRFRGEHALRRypsgeERCIACKLCEAVCPAQAITIEAEPRadgsrrttRYDID 492
Cdd:PRK08348    5 LPTVLRNLFKKPATNLFPaTEPVPVPEDFRGKILYDV-----DKCVGCRMCVTVCPAGVFVYLPEIR--------KVALW 71

                          90       100       110
                  ....*....|....*....|....*....|
gi 1878746647 493 MTKCIYCGFCQEACPVDAIVEGPNFEFSTE 522
Cdd:PRK08348   72 TGRCVFCGQCVDVCPTGALQMSDDFLLASY 101
ALDH_HBenzADH cd07151
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ...
 81-252 5.77e-11

NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.


Pssm-ID: 143469 [Multi-domain]  Cd Length: 465  Bit Score: 65.40  E-value: 5.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  81 IRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLaevLPRYLDQAGGPPsglsgwgpsGALTV 160
Cdd:cd07151   126 VYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGLL---LAKIFEEAGLPK---------GVLNV 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 161 rlaellcrgagrargdraaagaqvrlhLLHRPSHLVQVIEGHSgfLPR----PGSPRVGKIVMAAAAKHLTPVTLELGGK 236
Cdd:cd07151   194 ---------------------------VVGAGSEIGDAFVEHP--VPRlisfTGSTPVGRHIGELAGRHLKKVALELGGN 244

                         170
                  ....*....|....*.
gi 1878746647 237 NPCYVDDNCDPQTVVE 252
Cdd:cd07151   245 NPFVVLEDADIDAAVN 260
Fer4_9 pfam13187
4Fe-4S dicluster domain;
456-511 6.59e-11

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 57.95  E-value: 6.59e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1878746647 456 RCIACKLCEAVCPAQAITIeaepraDGSRRTTRYDIDMTKCIYCGFCQEACPVDAI 511
Cdd:pfam13187   1 KCTGCGACVAACPAGAIVP------DLVGQTIRGDIAGLACIGCGACVDACPRGAI 50
ALDH-SF cd06534
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
 622-672 9.74e-11

NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.


Pssm-ID: 143395 [Multi-domain]  Cd Length: 367  Bit Score: 63.79  E-value: 9.74e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1878746647 622 TVLVDVQETEPVMQEEIFGPILPIVNVRSLDEAIDFIKRREKPLALYAFSN 672
Cdd:cd06534   257 TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTR 307
ALDH_AAS00426 cd07109
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ...
 583-655 1.36e-10

Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.


Pssm-ID: 143427 [Multi-domain]  Cd Length: 454  Bit Score: 64.18  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 583 PDLGRIINEKHFQRLQGLL-----GCGRVAIGGQ----SDESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLDE 653
Cdd:cd07109   296 PDLGPLISAKQLDRVEGFVararaRGARIVAGGRiaegAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAE 375


                  ..
gi 1878746647 654 AI 655
Cdd:cd07109   376 AI 377
ALDH_MGR_2402 cd07108
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ...
 564-672 1.43e-10

Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.


Pssm-ID: 143426  Cd Length: 457  Bit Score: 63.92  E-value: 1.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 564 LPALQSAITRFYGEDPR-SSPDLGRIINEKHFQRLQGLLGCG------RVAIGGQSDESDR-----YIAPTVLVDVQETE 631
Cdd:cd07108   277 LEKLVAKLSKLKIGDPLdEATDIGAIISEKQFAKVCGYIDLGlstsgaTVLRGGPLPGEGPladgfFVQPTIFSGVDNEW 356

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1878746647 632 PVMQEEIFGPILPIVNVRSLDEAIDFIKRREKPLALYAFSN 672
Cdd:cd07108   357 RLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTR 397
ALDH_SNDH cd07118
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ...
 578-656 3.92e-10

Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.


Pssm-ID: 143436 [Multi-domain]  Cd Length: 454  Bit Score: 62.35  E-value: 3.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 578 DPRSspDLGRIINEKHFQRLQGLLGCGR-----VAIGGQSDESD--RYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRS 650
Cdd:cd07118   296 DPET--KVGAIINEAQLAKITDYVDAGRaegatLLLGGERLASAagLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDT 373


                  ....*.
gi 1878746647 651 LDEAID 656
Cdd:cd07118   374 VDEAIA 379
ALDH_CddD_SSP0762 cd07138
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ...
 578-656 5.61e-10

Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.


Pssm-ID: 143456 [Multi-domain]  Cd Length: 466  Bit Score: 62.14  E-value: 5.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 578 DPR-SSPDLGRIINEKHFQRLQGLLGCG-----RVAIGG----QSDESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVN 647
Cdd:cd07138   304 DPRdPATTLGPLASAAQFDRVQGYIQKGieegaRLVAGGpgrpEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIP 383


                  ....*....
gi 1878746647 648 VRSLDEAID 656
Cdd:cd07138   384 YDDEDEAIA 392
ALDH_F8_HMSADH cd07093
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ...
 578-655 6.06e-10

Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.


Pssm-ID: 143412 [Multi-domain]  Cd Length: 455  Bit Score: 61.81  E-value: 6.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 578 DPRS-SPDLGRIINEKHFQRLQGLLGCGR-----VAIGGQSDESDR-----YIAPTVLVDVQETEPVMQEEIFGPILPIV 646
Cdd:cd07093   291 DPLDpDTEVGPLISKEHLEKVLGYVELARaegatILTGGGRPELPDleggyFVEPTVITGLDNDSRVAQEEIFGPVVTVI 370


                  ....*....
gi 1878746647 647 NVRSLDEAI 655
Cdd:cd07093   371 PFDDEEEAI 379
ALDH_F6_MMSDH cd07085
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ...
 71-268 6.29e-10

Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.


Pssm-ID: 143404 [Multi-domain]  Cd Length: 478  Bit Score: 62.15  E-value: 6.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  71 NLATQLDSAFIRkEPFGLVLIVAPWNYP--VNLTLLPLvgALAAGNCVVLKPSEISKSTEKVLAEVlpryLDQAGGPPsg 148
Cdd:cd07085   123 NVARGIDTYSYR-QPLGVVAGITPFNFPamIPLWMFPM--AIACGNTFVLKPSERVPGAAMRLAEL----LQEAGLPD-- 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 149 lsgwgpsGALTVrlaellcrgagrargdraaagaqvrLH--------LLHRPshLVQVIeghsGFLprpGSPRVGKIVMA 220
Cdd:cd07085   194 -------GVLNV-------------------------VHggkeavnaLLDHP--DIKAV----SFV---GSTPVGEYIYE 232

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1878746647 221 AAAKHLTPVTLELGGKNPCYVDDNCDPQTVVEQVLartssGGFCGNDG 268
Cdd:cd07085   233 RAAANGKRVQALGGAKNHAVVMPDADLEQTANALV-----GAAFGAAG 275
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
457-513 8.32e-10

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 60.33  E-value: 8.32e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 457 CIACKLCEAVCPAQAITIE---AEpradgsrrttrydIDMTKCIYCGFCQEACPVDAIVE 513
Cdd:PRK07118  215 CIGCGKCVKACPAGAITMEnnlAV-------------IDQEKCTSCGKCVEKCPTKAIRI 261
ALDH_F15-22 cd07098
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ...
 583-656 8.33e-10

Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.


Pssm-ID: 143416 [Multi-domain]  Cd Length: 465  Bit Score: 61.55  E-value: 8.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 583 PDLGRIINEKHFQRLQGLLG----------CGRVAIGGQSDESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLD 652
Cdd:cd07098   303 VDVGAMISPARFDRLEELVAdavekgarllAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDE 382


                  ....
gi 1878746647 653 EAID 656
Cdd:cd07098   383 EAVE 386
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
454-533 8.70e-10

Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 61.58  E-value: 8.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEaepraDGSRRttrydIDMTKCIYCGFCQEACPVDAIVEgpnfefSTETHE--ELLYNK 531
Cdd:COG4624    90 KEKCKNCYPCVRACPVKAIKVD-----DGKAE-----IDEEKCISCGQCVAVCPFGAITE------KSDIEKvkKALKDP 153


                  ..
gi 1878746647 532 EK 533
Cdd:COG4624   154 EK 155
PRK03137 PRK03137
1-pyrroline-5-carboxylate dehydrogenase; Provisional
 84-265 1.13e-09

1-pyrroline-5-carboxylate dehydrogenase; Provisional


Pssm-ID: 179543  Cd Length: 514  Bit Score: 61.10  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  84 EPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVlpryLDQAGGPPSGLSGWGPSGAltvrla 163
Cdd:PRK03137  170 IPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEV----LEEAGLPAGVVNFVPGSGS------ 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 164 ellcrgagrargdraaagaQVRLHLLHRPshlvqviegHSGFLPRPGSPRVGKIVMAAAAK------HLTPVTLELGGKN 237
Cdd:PRK03137  240 -------------------EVGDYLVDHP---------KTRFITFTGSREVGLRIYERAAKvqpgqiWLKRVIAEMGGKD 291

                         170       180
                  ....*....|....*....|....*...
gi 1878746647 238 PCYVDDNCDPQTVVEQVLarTSSGGFCG 265
Cdd:PRK03137  292 AIVVDEDADLDLAAESIV--ASAFGFSG 317
ALDH_ABALDH-YdcW cd07092
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ...
 557-655 1.16e-09

Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.


Pssm-ID: 143411 [Multi-domain]  Cd Length: 450  Bit Score: 61.19  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 557 PKMQERLLPALQSAITRF-YGEDPRSSPDLGRIINEKHFQRLQGLL----GCGRVAIGGQSDESDRY-IAPTVLVDVQET 630
Cdd:cd07092   270 ESVYDEFVAALVEAVSAIrVGDPDDEDTEMGPLNSAAQRERVAGFVerapAHARVLTGGRRAEGPGYfYEPTVVAGVAQD 349

                          90       100
                  ....*....|....*....|....*
gi 1878746647 631 EPVMQEEIFGPILPIVNVRSLDEAI 655
Cdd:cd07092   350 DEIVQEEIFGPVVTVQPFDDEDEAI 374
ALDH_LactADH_F420-Bios cd07145
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ...
 79-264 1.38e-09

Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.


Pssm-ID: 143463 [Multi-domain]  Cd Length: 456  Bit Score: 60.82  E-value: 1.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  79 AFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVlpryLDQAGGPPSG---LSGWGps 155
Cdd:cd07145   117 AFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKI----LEEAGLPPGVinvVTGYG-- 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 156 galtvrlaellcrgagrargdraaagAQVRLHLLHRPshLVQVIEghsgFlprPGSPRVGKIVMAAAAKHLTPVTLELGG 235
Cdd:cd07145   191 --------------------------SEVGDEIVTNP--KVNMIS----F---TGSTAVGLLIASKAGGTGKKVALELGG 235

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1878746647 236 KNPCYVDDNCDPQTVVEQ-VLAR-TSSGGFC 264
Cdd:cd07145   236 SDPMIVLKDADLERAVSIaVRGRfENAGQVC 266
PRK09847 PRK09847
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
 79-153 1.39e-09

gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional


Pssm-ID: 182108 [Multi-domain]  Cd Length: 494  Bit Score: 61.07  E-value: 1.39e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1878746647  79 AFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEvlpryLDQAGGPPSG----LSGWG 153
Cdd:PRK09847  151 AMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAG-----LAKEAGLPDGvlnvVTGFG 224
ALDH_EDX86601 cd07102
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ...
 604-658 1.92e-09

Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.


Pssm-ID: 143420 [Multi-domain]  Cd Length: 452  Bit Score: 60.34  E-value: 1.92e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1878746647 604 GRVAIGGQ----SDESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLDEAIDFI 658
Cdd:cd07102   321 ARALIDGAlfpeDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALM 379
ALDH_PhpJ cd07146
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ...
 79-246 3.69e-09

Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.


Pssm-ID: 143464 [Multi-domain]  Cd Length: 451  Bit Score: 59.29  E-value: 3.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  79 AFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLPRyldqAGGPPSGLSgwgpsgAL 158
Cdd:cd07146   114 IFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYE----AGLPPDMLS------VV 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 159 TVRLAELLCRgagrargdraaagaqvrlhLLHRPShlVQVIEghsgFlprPGSPRVGKIVMAAAA-KHLtpvTLELGGKN 237
Cdd:cd07146   184 TGEPGEIGDE-------------------LITHPD--VDLVT----F---TGGVAVGKAIAATAGyKRQ---LLELGGND 232


                  ....*....
gi 1878746647 238 PCYVDDNCD 246
Cdd:cd07146   233 PLIVMDDAD 241
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
454-511 4.95e-09

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 59.49  E-value: 4.95e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEAEPRAdgsrrttryDIDMTKCIYCGFCQEACPVDAI 511
Cdd:COG1148   495 PEKCTGCGRCVEVCPYGAISIDEKGVA---------EVNPALCKGCGTCAAACPSGAI 543
ALDH_P5CDH cd07083
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ...
 75-265 4.96e-09

ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.


Pssm-ID: 143402 [Multi-domain]  Cd Length: 500  Bit Score: 59.13  E-value: 4.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  75 QLDSAFIRkePFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEisksTEKVLAEVLPRYLDQAGGPP---SGLSG 151
Cdd:cd07083   146 EDNESFYV--GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAE----DAVVVGYKVFEIFHEAGFPPgvvQFLPG 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 152 WGPSGALTVRLAELLCrgagrargdraaagaqvrlhllhrpshlvqvieghsgFLPRPGSPRVGKIVMAAAAKHLT---- 227
Cdd:cd07083   220 VGEEVGAYLTEHERIR-------------------------------------GINFTGSLETGKKIYEAAARLAPgqtw 262

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1878746647 228 --PVTLELGGKNPCYVDDNCDPQTVVEQVLarTSSGGFCG 265
Cdd:cd07083   263 fkRLYVETGGKNAIIVDETADFELVVEGVV--VSAFGFQG 300
ALDH_PhpJ cd07146
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ...
 562-658 6.57e-09

Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.


Pssm-ID: 143464 [Multi-domain]  Cd Length: 451  Bit Score: 58.52  E-value: 6.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 562 RLLPALQSAITrfYGEDPRSSPDLGRIINEK---HFQ-RLQGLLGCG-RVAIGGQSDESdrYIAPTVLVDVQETEPVMQE 636
Cdd:cd07146   279 DLLVEKSAALV--VGDPMDPATDMGTVIDEEaaiQIEnRVEEAIAQGaRVLLGNQRQGA--LYAPTVLDHVPPDAELVTE 354

                          90       100
                  ....*....|....*....|..
gi 1878746647 637 EIFGPILPIVNVRSLDEAIDFI 658
Cdd:cd07146   355 ETFGPVAPVIRVKDLDEAIAIS 376
ALDH_P5CDH cd07083
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ...
 561-658 7.09e-09

ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.


Pssm-ID: 143402 [Multi-domain]  Cd Length: 500  Bit Score: 58.74  E-value: 7.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 561 ERLLPALQSAITRFYGEDPRS-SPDLGRIINEKHFQRLQGLLGCGR----VAIGGQSDESDRY-IAPTVLVDVQETEPVM 634
Cdd:cd07083   317 EPVLERLLKRAERLSVGPPEEnGTDLGPVIDAEQEAKVLSYIEHGKnegqLVLGGKRLEGEGYfVAPTVVEEVPPKARIA 396

                          90       100
                  ....*....|....*....|....*.
gi 1878746647 635 QEEIFGPILPIVNVRSLD--EAIDFI 658
Cdd:cd07083   397 QEEIFGPVLSVIRYKDDDfaEALEVA 422
PLN02278 PLN02278
succinic semialdehyde dehydrogenase
 584-675 7.42e-09

succinic semialdehyde dehydrogenase


Pssm-ID: 215157 [Multi-domain]  Cd Length: 498  Bit Score: 58.55  E-value: 7.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 584 DLGRIINEKHFQRLQG------------LLGCGRVAIGGQsdesdrYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSL 651
Cdd:PLN02278  341 TQGPLINEAAVQKVEShvqdavskgakvLLGGKRHSLGGT------FYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTE 414

                          90       100
                  ....*....|....*....|....
gi 1878746647 652 DEAIDFIKRREKPLALYAFSNSNQ 675
Cdd:PLN02278  415 EEAIAIANDTEAGLAAYIFTRDLQ 438
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 444-512 7.71e-09

Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319870 [Multi-domain]  Cd Length: 136  Bit Score: 54.70  E-value: 7.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 444 EHALRRYPSG-----EERCIACKLCEAVCPAQAITIEAEPRadgsrrttrydiDMTKCIYCGF---------CQEACPVD 509
Cdd:cd04410    64 TGAIYKDEDGivlidEDKCIGCGSCVEACPYGAIVFDPEPG------------KAVKCDLCGDrldeglepaCVKACPTG 131


                  ...
gi 1878746647 510 AIV 512
Cdd:cd04410   132 ALT 134
ALDH_y4uC cd07149
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ...
 584-656 1.23e-08

Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.


Pssm-ID: 143467 [Multi-domain]  Cd Length: 453  Bit Score: 57.61  E-value: 1.23e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1878746647 584 DLGRIINEKHFQRLQGLL-----GCGRVAIGGQSDEsdRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLDEAID 656
Cdd:cd07149   302 DVGPMISEAEAERIEEWVeeaveGGARLLTGGKRDG--AILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIA 377
ALDH_HBenzADH cd07151
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ...
 575-656 1.24e-08

NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.


Pssm-ID: 143469 [Multi-domain]  Cd Length: 465  Bit Score: 57.70  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 575 YGeDPrSSPD--LGRIINEKHFQRLQGLL------GcGRVAIGGQSDesDRYIAPTVLVDVQETEPVMQEEIFGPILPIV 646
Cdd:cd07151   303 YG-DP-SDPDtvVGPLINESQVDGLLDKIeqaveeG-ATLLVGGEAE--GNVLEPTVLSDVTNDMEIAREEIFGPVAPII 377

                          90
                  ....*....|
gi 1878746647 647 NVRSLDEAID 656
Cdd:cd07151   378 KADDEEEALE 387
ALDH_F11_NP-GAPDH cd07082
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ...
 561-662 1.38e-08

NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.


Pssm-ID: 143401 [Multi-domain]  Cd Length: 473  Bit Score: 57.58  E-value: 1.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 561 ERLLPALQSAITRFYGEDPRS-SPDLGRIINEKHFQRLQGLL------GcGRVAIGGQSdESDRYIAPTVLVDVQETEPV 633
Cdd:cd07082   296 DELVELLKEEVAKLKVGMPWDnGVDITPLIDPKSADFVEGLIddavakG-ATVLNGGGR-EGGNLIYPTLLDPVTPDMRL 373

                          90       100
                  ....*....|....*....|....*....
gi 1878746647 634 MQEEIFGPILPIVNVRSLDEAIDFIKRRE 662
Cdd:cd07082   374 AWEEPFGPVLPIIRVNDIEEAIELANKSN 402
ALDH_CddD-AldA-like cd07089
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ...
 578-655 1.67e-08

Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.


Pssm-ID: 143408 [Multi-domain]  Cd Length: 459  Bit Score: 57.25  E-value: 1.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 578 DPRSsPD--LGRIINEKHFQRLQGLLGCGR------VAIGGQSDESDR--YIAPTVLVDVQETEPVMQEEIFGPILPIVN 647
Cdd:cd07089   297 DPAD-PGtvMGPLISAAQRDRVEGYIARGRdegarlVTGGGRPAGLDKgfYVEPTLFADVDNDMRIAQEEIFGPVLVVIP 375


                  ....*...
gi 1878746647 648 VRSLDEAI 655
Cdd:cd07089   376 YDDDDEAV 383
FeFe_hydrog_B1 TIGR04105
[FeFe] hydrogenase, group B1/B3; See for descriptions of different groups.
 455-513 2.11e-08

[FeFe] hydrogenase, group B1/B3; See for descriptions of different groups.


Pssm-ID: 274983 [Multi-domain]  Cd Length: 462  Bit Score: 57.22  E-value: 2.11e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1878746647 455 ERCIACKLCEAVCPAQAIT------IEAEP-RADGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVE 513
Cdd:TIGR04105 142 EKCIECGKCKKACPYNAIVeierpcEKACPvGAISSDEDGRAVIDYDKCISCGACMVACPFGAISD 207
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 454-511 2.62e-08

HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.


Pssm-ID: 319876 [Multi-domain]  Cd Length: 149  Bit Score: 53.42  E-value: 2.62e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEAEPRADGSRRTTRYDIdMTKCIYCGF------CQEACPVDAI 511
Cdd:cd10554    84 EERCIGCKLCVLACPFGAIEMAPTTVPGVDWERGPRAV-AVKCDLCAGreggpaCVEACPTKAL 146
ALDH_DhaS cd07114
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ...
 578-655 2.79e-08

Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.


Pssm-ID: 143432 [Multi-domain]  Cd Length: 457  Bit Score: 56.79  E-value: 2.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 578 DPRSspDLGRIINEKHFQRLQGLLGC-----GRVAIGGQ---SDESDR--YIAPTVLVDVQETEPVMQEEIFGPILPIVN 647
Cdd:cd07114   296 DPET--QMGPLATERQLEKVERYVARareegARVLTGGErpsGADLGAgyFFEPTILADVTNDMRIAQEEVFGPVLSVIP 373


                  ....*...
gi 1878746647 648 VRSLDEAI 655
Cdd:cd07114   374 FDDEEEAI 381
PRK06273 PRK06273
ferredoxin; Provisional
 454-508 3.15e-08

ferredoxin; Provisional


Pssm-ID: 235764 [Multi-domain]  Cd Length: 165  Bit Score: 53.56  E-value: 3.15e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1878746647 454 EERCIACKLCEAVCPAQAIT-IEAEPR--ADGSRRTTRYDIDMTKCIYCGFCQEACPV 508
Cdd:PRK06273   48 EELCIGCGGCANVCPTKAIEmIPVEPVkiTEGYVKTKIPKIDYEKCVYCLYCHDFCPV 105
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 454-507 3.61e-08

4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 50.33  E-value: 3.61e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEAEPRADGSRRTtryDIDMTKCIYCGFCQEACP 507
Cdd:pfam13237   6 PDKCIGCGRCTAACPAGLTRVGAIVERLEGEAV---RIGVWKCIGCGACVEACP 56
ALDH_AldH-CAJ73105 cd07131
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ...
 584-655 3.72e-08

Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.


Pssm-ID: 143449 [Multi-domain]  Cd Length: 478  Bit Score: 56.20  E-value: 3.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 584 DLGRIINEKHFQRLQG-----------LLGCGRVAIGGQSDESdRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLD 652
Cdd:cd07131   316 DMGPLINEAQLEKVLNyneigkeegatLLLGGERLTGGGYEKG-YFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLE 394


                  ...
gi 1878746647 653 EAI 655
Cdd:cd07131   395 EAI 397
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 455-520 4.09e-08

polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial polysulfide reductase (PsrABC), an integral membrane-bound enzyme responsible for quinone-coupled reduction of polysulfides, a process important in extreme environments such as deep-sea vents and hot springs. Polysulfide reductase contains three subunits: a catalytic subunit PsrA, an electron transfer PsrB subunit and the hydrophobic transmembrane PsrC subunit. PsrB belongs to the DMSO reductase superfamily that contains [4Fe-4S] clusters which transfer the electrons from the A subunit to the hydrophobic integral membrane C subunit via the B subunit. In Shewanella oneidensis, which has highly diverse anaerobic respiratory pathways, PsrABC is responsible for H2S generation as well as its regulation via respiration of sulfur species. PsrB transfers electrons from PsrC (serving as quinol oxidase) to the catalytic subunit PsrA for reduction of corresponding electron acceptors. It has been shown that T. thermophilus polysulfide reductase could be a key energy-conserving enzyme of the respiratory chain, using polysulfide as the terminal electron acceptor and pumping protons across the membrane.


Pssm-ID: 319873 [Multi-domain]  Cd Length: 185  Bit Score: 53.69  E-value: 4.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 455 ERCIACKLCEAVCPAQAITI-EAEPRADGSRRTTRYDIdMTKCIYC------G---FCQEACPVDAIVEG----PNFEFS 520
Cdd:cd10551    83 DKCIGCRYCMAACPYGARYFnPEEPHEFGEVPVRPKGV-VEKCTFCyhrldeGllpACVEACPTGARIFGdlddPNSEVS 161
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 448-512 5.39e-08

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 51.81  E-value: 5.39e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 448 RRYPSGEERCIACKLCE-----AVCPAQAITIEAEpradgsrrTTRYDIDMTKCIYCGFCQEACPVDAIV 512
Cdd:cd10550    37 RFEPEGLDVPVVCRQCEdapcvEACPVGAISRDEE--------TGAVVVDEDKCIGCGMCVEACPFGAIR 98
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
457-507 5.50e-08

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 49.80  E-value: 5.50e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1878746647 457 CIACKLCEAVCPAQAITiEAEPRADgSRRTTRYDIDMTK--------------CIYCGFCQEACP 507
Cdd:pfam13484   1 CGSCGKCIDACPTGAIV-GPEGVLD-ARRCISYLTIEKKglipdelrcllgnrCYGCDICQDVCP 63
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 445-512 5.56e-08

Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 53.41  E-value: 5.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 445 HALRRYPSG-----EERCIACKLCEAVCPAQAITIEAEPRAdgsrrttrydidMTKCIYCGF---------CQEACPVDA 510
Cdd:COG0437    75 GATYKREDGivlvdYDKCIGCRYCVAACPYGAPRFNPETGV------------VEKCTFCADrldegllpaCVEACPTGA 142


                  ..
gi 1878746647 511 IV 512
Cdd:COG0437   143 LV 144
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
454-511 9.56e-08

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 53.91  E-value: 9.56e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1878746647 454 EERCIACKLCEAVCPAQAItieaePRaDGSrrttrydIDMTKCIYCGFCQEACPVDAI 511
Cdd:COG0348   209 RGDCIDCGLCVKVCPMGID-----IR-KGE-------INQSECINCGRCIDACPKDAI 253
ALDH_KGSADH-YcbD cd07097
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ...
 584-656 9.67e-08

Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.


Pssm-ID: 143415 [Multi-domain]  Cd Length: 473  Bit Score: 54.95  E-value: 9.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 584 DLGRIINEKHFQRL-----QGLLGCGRVAIGGQ---SDESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLDEAI 655
Cdd:cd07097   316 DIGPVVSERQLEKDlryieIARSEGAKLVYGGErlkRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEAL 395


                  .
gi 1878746647 656 D 656
Cdd:cd07097   396 A 396
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
454-512 1.03e-07

Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 51.20  E-value: 1.03e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEAEPRADGSrrttrydidmTKCIYCGF------CQEACPVDAIV 512
Cdd:COG1142    80 EEKCIGCGLCVLACPFGAITMVGEKSRAVA----------VKCDLCGGreggpaCVEACPTGALR 134
ALDH_F10_BADH cd07110
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ...
 561-656 1.13e-07

Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.


Pssm-ID: 143428 [Multi-domain]  Cd Length: 456  Bit Score: 54.66  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 561 ERLLPALQSAITRFYGEDPRSSP-DLGRIINEKHFQRLQGLLGCG-----RVAIGGQSDESDR---YIAPTVLVDVQETE 631
Cdd:cd07110   277 DAFLERLATAAEAIRVGDPLEEGvRLGPLVSQAQYEKVLSFIARGkeegaRLLCGGRRPAHLEkgyFIAPTVFADVPTDS 356

                          90       100
                  ....*....|....*....|....*
gi 1878746647 632 PVMQEEIFGPILPIVNVRSLDEAID 656
Cdd:cd07110   357 RIWREEIFGPVLCVRSFATEDEAIA 381
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
457-511 1.14e-07

Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 51.20  E-value: 1.14e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1878746647 457 CIACKL--CEAVCPAQAITieaepradgsRRTTRYDIDMTKCIYCGFCQEACPVDAI 511
Cdd:COG1142    52 CRHCEDapCAEVCPVGAIT----------RDDGAVVVDEEKCIGCGLCVLACPFGAI 98
ALDH_VaniDH_like cd07150
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ...
 578-655 1.33e-07

Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.


Pssm-ID: 143468 [Multi-domain]  Cd Length: 451  Bit Score: 54.64  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 578 DPRSsPD--LGRIINEKHFQRLQGLL------GcGRVAIGGQSDesDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVR 649
Cdd:cd07150   293 DPRD-PDtvIGPLISPRQVERIKRQVedavakG-AKLLTGGKYD--GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAK 368


                  ....*.
gi 1878746647 650 SLDEAI 655
Cdd:cd07150   369 DAEEAL 374
gabD PRK11241
NADP-dependent succinate-semialdehyde dehydrogenase I;
83-256 1.65e-07

NADP-dependent succinate-semialdehyde dehydrogenase I;


Pssm-ID: 183050 [Multi-domain]  Cd Length: 482  Bit Score: 54.14  E-value: 1.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  83 KEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEvlpryLDQAGGPPSGLSG--WGPSGALTV 160
Cdd:PRK11241  144 KQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAE-----LAIRAGIPAGVFNvvTGSAGAVGG 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 161 RLAEllcrgagrargdraaagaqvrlhllhrpSHLVQVieghsgfLPRPGSPRVGKIVMAAAAKHLTPVTLELGGKNPCY 240
Cdd:PRK11241  219 ELTS----------------------------NPLVRK-------LSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFI 263

                         170
                  ....*....|....*.
gi 1878746647 241 VDDNCDPQTVVEQVLA 256
Cdd:PRK11241  264 VFDDADLDKAVEGALA 279
ALDH_HMSADH_HapE cd07115
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ...
 558-655 2.04e-07

Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.


Pssm-ID: 143433 [Multi-domain]  Cd Length: 453  Bit Score: 53.98  E-value: 2.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 558 KMQERLLPALQSAITRFYGEDP-RSSPDLGRIINEKHFQRLQGLLGCGR------VAIGGQSDESDRYIAPTVLVDVQET 630
Cdd:cd07115   271 SIYDEFLERFTSLARSLRPGDPlDPKTQMGPLVSQAQFDRVLDYVDVGReegarlLTGGKRPGARGFFVEPTIFAAVPPE 350

                          90       100
                  ....*....|....*....|....*
gi 1878746647 631 EPVMQEEIFGPILPIVNVRSLDEAI 655
Cdd:cd07115   351 MRIAQEEIFGPVVSVMRFRDEEEAL 375
ALDH_F1-2_Ald2-like cd07091
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...
 586-673 2.55e-07

ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.


Pssm-ID: 143410  Cd Length: 476  Bit Score: 53.75  E-value: 2.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 586 GRIINEKHFQRLQGLLGCG-----RVAIGGQSDESDRY-IAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLDEAIDFIK 659
Cdd:cd07091   325 GPQVSKAQFDKILSYIESGkkegaTLLTGGERHGSKGYfIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERAN 404

                          90
                  ....*....|....
gi 1878746647 660 RREKPLALYAFSNS 673
Cdd:cd07091   405 DTEYGLAAGVFTKD 418
ALDH_AldA-Rv0768 cd07139
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ...
 584-655 2.61e-07

Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.


Pssm-ID: 143457 [Multi-domain]  Cd Length: 471  Bit Score: 53.73  E-value: 2.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 584 DLGRIINEKHFQRLQGLLGCGR------VAIGGQSDESDR--YIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLDEAI 655
Cdd:cd07139   317 QIGPLASARQRERVEGYIAKGRaegarlVTGGGRPAGLDRgwFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAV 396
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 458-511 2.98e-07

NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 49.93  E-value: 2.98e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1878746647 458 IACKLCEAVCPAQAITIEaePRADGSRRTTrydIDMTKCIYCGFCQEACPVDAI 511
Cdd:cd10564    86 VECRSCQDACPTQAIRFR--PRLGGIALPE---LDADACTGCGACVSVCPVGAI 134
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 454-512 3.18e-07

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 50.33  E-value: 3.18e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1878746647 454 EERCIA------CKLCEAVCPAQAITIEAEpraDGSRRTTrydIDMTKCIYCGFCQEACPVD---AIV 512
Cdd:cd16373    90 KDRCLAwqggtdCGVCVEACPTEAIAIVLE---DDVLRPV---VDEDKCVGCGLCEYVCPVEppkAIV 151
ALDH_F1AB_F2_RALDH1 cd07141
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ...
 589-656 3.55e-07

NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.


Pssm-ID: 143459  Cd Length: 481  Bit Score: 53.12  E-value: 3.55e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1878746647 589 INEKHFQRLQGLLGCGR------VAIGGQSDESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLDEAID 656
Cdd:cd07141   332 IDEEQFKKILELIESGKkegaklECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIE 405
ALDH_BADH-GbsA cd07119
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ...
 576-655 3.94e-07

Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.


Pssm-ID: 143437  Cd Length: 482  Bit Score: 53.08  E-value: 3.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 576 GEDPRSspDLGRIINEKHFQRLQGLLGCG-----RVAIGGQSDESDR-----YIAPTVLVDVQETEPVMQEEIFGPILPI 645
Cdd:cd07119   309 GLDADT--EMGPLVSAEHREKVLSYIQLGkeegaRLVCGGKRPTGDElakgyFVEPTIFDDVDRTMRIVQEEIFGPVLTV 386

                          90
                  ....*....|
gi 1878746647 646 VNVRSLDEAI 655
Cdd:cd07119   387 ERFDTEEEAI 396
ALDH_PutA-P5CDH cd07125
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ...
 81-149 4.05e-07

Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.


Pssm-ID: 143443 [Multi-domain]  Cd Length: 518  Bit Score: 52.97  E-value: 4.05e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1878746647  81 IRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISksteKVLAEVLPRYLDQAGGPPSGL 149
Cdd:cd07125   163 LELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQT----PLIAARAVELLHEAGVPRDVL 227
ALDH_F7_AASADH-like cd07086
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ...
 584-655 4.85e-07

NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).


Pssm-ID: 143405 [Multi-domain]  Cd Length: 478  Bit Score: 52.95  E-value: 4.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 584 DLGRIINEKHFQRLQGLL------GcGRVAIGG---QSDESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLDEA 654
Cdd:cd07086   317 LVGPLINQAAVEKYLNAIeiaksqG-GTVLTGGkriDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEA 395


                  .
gi 1878746647 655 I 655
Cdd:cd07086   396 I 396
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 463-511 5.96e-07

Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 50.33  E-value: 5.96e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1878746647 463 CEAVCPAQAITIeaepRADGSRRttrydIDMTKCIYCGFCQEACPVDAI 511
Cdd:COG0437    68 CVKVCPTGATYK----REDGIVL-----VDYDKCIGCRYCVAACPYGAP 107
astD PRK09457
succinylglutamic semialdehyde dehydrogenase; Reviewed
 79-146 7.32e-07

succinylglutamic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181873  Cd Length: 487  Bit Score: 52.27  E-value: 7.32e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1878746647  79 AFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEIsksTEKVlAEVLPRYLDQAGGPP 146
Cdd:PRK09457  128 AVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSEL---TPWV-AELTVKLWQQAGLPA 191
PRK13795 PRK13795
hypothetical protein; Provisional
 456-508 9.40e-07

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 51.92  E-value: 9.40e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1878746647 456 RCIACKLCEAVCPAQAITIEAEPRadgsrrttRYDIDMTKCIYCGFCQEACPV 508
Cdd:PRK13795  582 ECVGCGVCVGACPTGAIRIEEGKR--------KISVDEEKCIHCGKCTEVCPV 626
PRK14028 PRK14028
pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional
 456-511 9.77e-07

pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional


Pssm-ID: 172522 [Multi-domain]  Cd Length: 312  Bit Score: 51.15  E-value: 9.77e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 456 RCIACKLCEAVCPAQAItIEAEPRADGSR----RTTRYDIDMTKCIYCGFCQEACPVDAI 511
Cdd:PRK14028  248 KCIMCRKCWLYCPDDAI-IEAWREAEGPRgrkfRMKMIDFDYQYCKGCGVCAEVCPTGAI 306
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 457-511 9.80e-07

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 48.42  E-value: 9.80e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1878746647 457 CIACKL--CEAVCPAQAItieaEPRADGSrrtTRYDIDmtKCIYCGFCQEACPVDAI 511
Cdd:cd16370    53 CRACEDppCAEACPTGAL----EPRKGGG---VVLDKE--KCIGCGNCVKACIVGAI 100
ALDH_F21_LactADH-like cd07094
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ...
 578-656 1.10e-06

ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.


Pssm-ID: 143413 [Multi-domain]  Cd Length: 453  Bit Score: 51.66  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 578 DP-RSSPDLGRIINEKHFQRLQ-----GLLGCGRVAIGGQSDesDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSL 651
Cdd:cd07094   295 DPlDEDTDVGPLISEEAAERVErwveeAVEAGARLLCGGERD--GALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDF 372


                  ....*
gi 1878746647 652 DEAID 656
Cdd:cd07094   373 EEAIR 377
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 489-511 1.25e-06

4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 459642 [Multi-domain]  Cd Length: 24  Bit Score: 44.93  E-value: 1.25e-06
                          10        20
                  ....*....|....*....|...
gi 1878746647 489 YDIDMTKCIYCGFCQEACPVDAI 511
Cdd:pfam00037   1 VVIDEEKCIGCGACVEVCPVGAI 23
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
456-511 1.26e-06

Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 51.57  E-value: 1.26e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1878746647 456 RCIACKLCEAVCPAQAITIEAEPRADGSRRTTRYDIDMTKCIYCGFCQEACPVDAI 511
Cdd:COG4624    53 RCCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSIIRDKEKCKNCYPCVRACPVKAI 108
PRK13473 PRK13473
aminobutyraldehyde dehydrogenase;
584-655 1.38e-06

aminobutyraldehyde dehydrogenase;


Pssm-ID: 237391  Cd Length: 475  Bit Score: 51.45  E-value: 1.38e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1878746647 584 DLGRIINEKHFQRLQGL------LGCGRVAIGGQ-SDESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLDEAI 655
Cdd:PRK13473  318 ELGPLISAAHRDRVAGFverakaLGHIRVVTGGEaPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAV 396
PLN00412 PLN00412
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
 83-120 1.51e-06

NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 215110 [Multi-domain]  Cd Length: 496  Bit Score: 51.30  E-value: 1.51e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1878746647  83 KEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKP 120
Cdd:PLN00412  156 KIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKP 193
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 421-511 1.56e-06

EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 49.86  E-value: 1.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 421 LFREPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAVCPAQAITIEAE-PRADGsrrttrydidmtKCIYC 499
Cdd:NF038196  151 GPEKKKGFIPRLLSKLVNPLFYKFKVKDKKFHVTDKCIGCGICAKVCPVNNIEMEDGkPVWGH------------NCTHC 218

                          90
                  ....*....|..
gi 1878746647 500 GFCQEACPVDAI 511
Cdd:NF038196  219 LACIHRCPKEAI 230
PFLE_PFLC TIGR02494
glycyl-radical enzyme activating protein; This subset of the radical-SAM family (pfam04055) ...
 454-511 2.02e-06

glycyl-radical enzyme activating protein; This subset of the radical-SAM family (pfam04055) includes a number of probable activating proteins acting on different enzymes all requiring an amino-acid-centered radical. The closest relatives to this family are the pyruvate-formate lyase activating enzyme (PflA, 1.97.1.4, TIGR02493) and the anaerobic ribonucleotide reductase activating enzyme (TIGR02491). Included within this subfamily are activators of hydroxyphenyl acetate decarboxylase (HdpA), benzylsuccinate synthase (BssD), gycerol dehydratase (DhaB2) as well as enzymes annotated in E. coli as activators of different isozymes of pyruvate-formate lyase (PFLC and PFLE) however, these appear to lack characterization and may activate enzymes with distinctive functions. Most of the sequence-level variability between these forms is concentrated within an N-terminal domain which follows a conserved group of three cysteines and contains a variable pattern of 0 to 8 additional cysteines.


Pssm-ID: 274163 [Multi-domain]  Cd Length: 295  Bit Score: 50.02  E-value: 2.02e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1878746647 454 EERCIACKLCEAVCPAQaiTIEAEPRADGSrrtTRYDIDMTKCIYCGFCQEACPVDAI 511
Cdd:TIGR02494  47 ENRCLGCGKCVEVCPAG--TARLSELADGR---NRIIIRREKCTHCGKCTEACPSGAL 99
ALDH_SGSD_AstD cd07095
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ...
 44-264 2.04e-06

N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.


Pssm-ID: 143414 [Multi-domain]  Cd Length: 431  Bit Score: 50.73  E-value: 2.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  44 EISIVQTEINLALRNL--RAWmrdeqvRRNLATQLDSAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPS 121
Cdd:cd07095    60 EVAAMAGKIDISIKAYheRTG------ERATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPS 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 122 EISKSTekvlAEVLPRYLDQAGGPPSGLS---GWGPSGALTVRLAEllcrgagrargdraaagaqvrlhllhrpshlvqv 198
Cdd:cd07095   134 ELTPAV----AELMVELWEEAGLPPGVLNlvqGGRETGEALAAHEG---------------------------------- 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1878746647 199 IEGhsgfLPRPGSPRVGKIVMAAAAKHltP---VTLELGGKNPCYVDDNCDPQTVVEQVL--ARTSSGGFC 264
Cdd:cd07095   176 IDG----LLFTGSAATGLLLHRQFAGR--PgkiLALEMGGNNPLVVWDVADIDAAAYLIVqsAFLTAGQRC 240
PLN02766 PLN02766
coniferyl-aldehyde dehydrogenase
 578-655 2.41e-06

coniferyl-aldehyde dehydrogenase


Pssm-ID: 215410 [Multi-domain]  Cd Length: 501  Bit Score: 50.59  E-value: 2.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 578 DPRSspDLGRIINEKHFQRLQGLLGCGR-----VAIGGQS-DESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSL 651
Cdd:PLN02766  336 DPRA--RQGPQVDKQQFEKILSYIEHGKregatLLTGGKPcGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTV 413


                  ....
gi 1878746647 652 DEAI 655
Cdd:PLN02766  414 EEAI 417
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 454-515 2.45e-06

Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319870 [Multi-domain]  Cd Length: 136  Bit Score: 47.38  E-value: 2.45e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1878746647 454 EERCIACKLCEAVCPaQAITIEAEPRADGSRRTTRYDIDM----TKCIYCGF--CQEACPVDAIVEGP 515
Cdd:cd04410     5 LDRCIGCGTCEVACK-QEHGLRPGPDWSRIKVIEGGGLERaflpVSCMHCEDppCVKACPTGAIYKDE 71
ALDH_SSADH1_GabD1 cd07100
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ...
 605-656 2.47e-06

Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.


Pssm-ID: 143418 [Multi-domain]  Cd Length: 429  Bit Score: 50.54  E-value: 2.47e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1878746647 605 RVAIGGQSDESDR-YIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLDEAID 656
Cdd:cd07100   302 TLLLGGKRPDGPGaFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIA 354
NapF COG1145
Ferredoxin [Energy production and conversion];
453-516 2.78e-06

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 49.34  E-value: 2.78e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1878746647 453 GEERCIACKLCEAVCPAQAITIEAEPRADGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPN 516
Cdd:COG1145   141 EAGLAILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGLCVKVCPTGAIRLKDG 204
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 454-511 3.02e-06

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 46.80  E-value: 3.02e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEAEpradgsrrtTRYdidMTKCIYCG---FCQEACPVDAI 511
Cdd:cd10550    79 EDKCIGCGMCVEACPFGAIRVDPE---------TGK---AIKCDLCGgdpACVKVCPTGAL 127
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 457-515 3.13e-06

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 50.26  E-value: 3.13e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1878746647 457 CIACKLCEAVCPAQAITIEAEPRadgsrrttRYDIDMTKCIYCGFCQEACPVDAIVEGP 515
Cdd:PRK12771  512 CFECDNCYGACPQDAIIKLGPGR--------RYHFDYDKCTGCHICADVCPCGAIEMGP 562
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 456-511 3.15e-06

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 47.64  E-value: 3.15e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1878746647 456 RCIACKLCEAVCPAQAITIeaEPRADGSR--RTTRYDIDMTKCIYCG-FCQEACPVDAI 511
Cdd:cd16373    15 LCIRCGLCVEACPTGVIQP--AGLEDGLEggRTPYLDPREGPCDLCCdACVEVCPTGAL 71
ALDH_F7_AASADH cd07130
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ...
 85-255 3.15e-06

NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.


Pssm-ID: 143448  Cd Length: 474  Bit Score: 50.28  E-value: 3.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  85 PFGLVLIVAPWNYPV-----NLTLlplvgALAAGNCVVLKPSE----ISKSTEKVLAEVlpryLDQAGGPPSGLS---GW 152
Cdd:cd07130   132 PLGVVGVITAFNFPVavwgwNAAI-----ALVCGNVVVWKPSPttplTAIAVTKIVARV----LEKNGLPGAIASlvcGG 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 153 GPSGALTVRLAellcrgagrargdraaagaqvRLHLLhrpshlvqvieghsGFlprPGSPRVGKIVMAAAAKHLTPVTLE 232
Cdd:cd07130   203 ADVGEALVKDP---------------------RVPLV--------------SF---TGSTAVGRQVGQAVAARFGRSLLE 244

                         170       180
                  ....*....|....*....|...
gi 1878746647 233 LGGKNPCYVDDNCDPQTVVEQVL 255
Cdd:cd07130   245 LGGNNAIIVMEDADLDLAVRAVL 267
ALDH_F21_RNP123 cd07147
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ...
 578-672 3.21e-06

Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.


Pssm-ID: 143465 [Multi-domain]  Cd Length: 452  Bit Score: 49.94  E-value: 3.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 578 DPRS-SPDLGRIINEKHFQRLQGLL-----GCGRVAIGGQSDESdrYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSL 651
Cdd:cd07147   294 DPKDdATDVGPMISESEAERVEGWVneavdAGAKLLTGGKRDGA--LLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDF 371

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1878746647 652 DEAIDFIKR-----------REKPLALYAFSN 672
Cdd:cd07147   372 DEALAAVNDskfglqagvftRDLEKALRAWDE 403
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
455-517 3.57e-06

Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 46.96  E-value: 3.57e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1878746647 455 ERCIACKLCEAVCPAQAITIEAE---PRADGSRRTTRYDIDMtkCIYC--GFCQEACPVDAIVEGPNF 517
Cdd:COG1142    10 EKCIGCRTCEAACAVAHEGEEGEpflPRIRVVRKAGVSAPVQ--CRHCedAPCAEVCPVGAITRDDGA 75
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 458-512 3.59e-06

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319893 [Multi-domain]  Cd Length: 140  Bit Score: 46.79  E-value: 3.59e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 458 IACKLCE-----AVCPAQAITIeaepRADGsrrTTRYDIDmtKCIYCGFCQEACPVDAIV 512
Cdd:cd16371    52 MSCNHCEnpacvKVCPTGAITK----REDG---IVVVDQD--KCIGCGYCVWACPYGAPQ 102
ALDH_StaphAldA1 cd07117
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ...
 561-671 5.46e-06

Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.


Pssm-ID: 143435  Cd Length: 475  Bit Score: 49.38  E-value: 5.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 561 ERLLPALQSAITRFYGEDPRSsPD--LGRIINEKHFQRLQGLLGCG-----RVAIGGQ---SDESDR--YIAPTVLVDVQ 628
Cdd:cd07117   292 DEFVAKLKEKFENVKVGNPLD-PDtqMGAQVNKDQLDKILSYVDIAkeegaKILTGGHrltENGLDKgfFIEPTLIVNVT 370

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1878746647 629 ETEPVMQEEIFGPILPIVNVRSLDEAIDFIKRREKPLALYAFS 671
Cdd:cd07117   371 NDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFT 413
ALDH_F9_TMBADH cd07090
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ...
 586-656 5.75e-06

NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.


Pssm-ID: 143409 [Multi-domain]  Cd Length: 457  Bit Score: 49.22  E-value: 5.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 586 GRIINEKHFQRLQGLLGCG-----RVAIGGQSDESDR------YIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLDEA 654
Cdd:cd07090   298 GALISEEHLEKVLGYIESAkqegaKVLCGGERVVPEDglengfYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEV 377


                  ..
gi 1878746647 655 ID 656
Cdd:cd07090   378 IR 379
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 485-516 6.17e-06

TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 44.65  E-value: 6.17e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1878746647 485 RTT--RYDIDMTKCIYCGFCQEACPVDAIVEGPN 516
Cdd:COG4231    11 RTTamRYVIDEDKCTGCGACVKVCPADAIEEGDG 44
ALDH_RL0313 cd07148
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ...
 79-263 6.58e-06

Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.


Pssm-ID: 143466 [Multi-domain]  Cd Length: 455  Bit Score: 48.95  E-value: 6.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  79 AFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSeiskSTEKVLAEVLPRYLDQAGGPPsglsGWGPSGAL 158
Cdd:cd07148   118 AFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA----LATPLSCLAFVDLLHEAGLPE----GWCQAVPC 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 159 TVRLAELLcrgagrargdraaagaqvrlhllhrpshlvqVIEGHSGFLPRPGSPRVGKIVMAAAAKHlTPVTLELGGKNP 238
Cdd:cd07148   190 ENAVAEKL-------------------------------VTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAP 237

                         170       180
                  ....*....|....*....|....*
gi 1878746647 239 CYVDDNCDpqtvVEQVLARTSSGGF 263
Cdd:cd07148   238 VIVDRSAD----LDAMIPPLVKGGF 258
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 463-511 6.92e-06

polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial polysulfide reductase (PsrABC), an integral membrane-bound enzyme responsible for quinone-coupled reduction of polysulfides, a process important in extreme environments such as deep-sea vents and hot springs. Polysulfide reductase contains three subunits: a catalytic subunit PsrA, an electron transfer PsrB subunit and the hydrophobic transmembrane PsrC subunit. PsrB belongs to the DMSO reductase superfamily that contains [4Fe-4S] clusters which transfer the electrons from the A subunit to the hydrophobic integral membrane C subunit via the B subunit. In Shewanella oneidensis, which has highly diverse anaerobic respiratory pathways, PsrABC is responsible for H2S generation as well as its regulation via respiration of sulfur species. PsrB transfers electrons from PsrC (serving as quinol oxidase) to the catalytic subunit PsrA for reduction of corresponding electron acceptors. It has been shown that T. thermophilus polysulfide reductase could be a key energy-conserving enzyme of the respiratory chain, using polysulfide as the terminal electron acceptor and pumping protons across the membrane.


Pssm-ID: 319873 [Multi-domain]  Cd Length: 185  Bit Score: 47.14  E-value: 6.92e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1878746647 463 CEAVCPAQAITIeaepRADGsrrttRYDIDMTKCIYCGFCQEACPVDAI 511
Cdd:cd10551    61 CVKVCPTGATYK----REDG-----IVLVDYDKCIGCRYCMAACPYGAR 100
ALDH_ALD2-YMR170C cd07144
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ...
 585-655 7.80e-06

Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.


Pssm-ID: 143462  Cd Length: 484  Bit Score: 48.94  E-value: 7.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 585 LGRIINEKHFQRLQGLLGCGR------VAIG---GQSDESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLDEAI 655
Cdd:cd07144   327 VGPQVSKTQYDRVLSYIEKGKkegaklVYGGekaPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAI 406
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 443-482 8.19e-06

NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 43.93  E-value: 8.19e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1878746647 443 GEHALRRYPsgeERCIACKLCEAVCPAQAITIEAEPRADG 482
Cdd:COG1146    31 GKKALVINP---EECIGCGACELVCPVGAITVEDDEPEEQ 67
ALDH_F2BC cd07142
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ...
 566-672 8.64e-06

Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.


Pssm-ID: 143460  Cd Length: 476  Bit Score: 48.64  E-value: 8.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 566 ALQSAITRFYGEDPRSSPDLGRIINEKHFQRLQGLLGCGR------VAIGGQSDESDRYIAPTVLVDVQETEPVMQEEIF 639
Cdd:cd07142   305 AKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGKeegatlITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIF 384

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1878746647 640 GPILPIVNVRSLDEAIDFIKRREKPLALYAFSN 672
Cdd:cd07142   385 GPVQSILKFKTVDEVIKRANNSKYGLAAGVFSK 417
PLN02466 PLN02466
aldehyde dehydrogenase family 2 member
 570-655 9.90e-06

aldehyde dehydrogenase family 2 member


Pssm-ID: 215259 [Multi-domain]  Cd Length: 538  Bit Score: 48.65  E-value: 9.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 570 AITRFYGEDPRSSPDLGRIINEKHFQRLQGLL------GCGRVAIGGQSDESDRYIAPTVLVDVQETEPVMQEEIFGPIL 643
Cdd:PLN02466  363 ALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIksgvesGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQ 442

                          90
                  ....*....|..
gi 1878746647 644 PIVNVRSLDEAI 655
Cdd:PLN02466  443 SILKFKDLDEVI 454
ALDH_PADH_NahF cd07113
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ...
 553-658 1.03e-05

Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.


Pssm-ID: 143431  Cd Length: 477  Bit Score: 48.59  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 553 YLYRPKMQErLLPALQSAITRFYGEDPRS-SPDLGRIINEKHFQRLQGLLGCGR------VAIGGQSDESDRYIAPTVLV 625
Cdd:cd07113   291 YVHRSKFDE-LVTKLKQALSSFQVGSPMDeSVMFGPLANQPHFDKVCSYLDDARaegdeiVRGGEALAGEGYFVQPTLVL 369

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1878746647 626 DVQETEPVMQEEIFGPILPIVNVRSLDEAIDFI 658
Cdd:cd07113   370 ARSADSRLMREETFGPVVSFVPYEDEEELIQLI 402
ALDH_SSADH2_GabD2 cd07101
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ...
 582-656 1.05e-05

Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).


Pssm-ID: 143419 [Multi-domain]  Cd Length: 454  Bit Score: 48.46  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 582 SPDLGRIINEKHFQRLQGLLGCGR-----VAIGGQS--DESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLDEA 654
Cdd:cd07101   295 GPDMGSLISQAQLDRVTAHVDDAVakgatVLAGGRArpDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEA 374


                  ..
gi 1878746647 655 ID 656
Cdd:cd07101   375 IE 376
ALDH_PhdK-like cd07107
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ...
 584-656 1.26e-05

Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.


Pssm-ID: 143425 [Multi-domain]  Cd Length: 456  Bit Score: 48.14  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 584 DLGRIINEKHFQRLQGLLGCGR------VAIGGQSD----ESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLDE 653
Cdd:cd07107   297 TMGPLVSRQQYDRVMHYIDSAKregarlVTGGGRPEgpalEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAE 376


                  ...
gi 1878746647 654 AID 656
Cdd:cd07107   377 MVA 379
ALDH_F12_P5CDH cd07126
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ...
 85-149 1.42e-05

Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.


Pssm-ID: 143444  Cd Length: 489  Bit Score: 48.26  E-value: 1.42e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1878746647  85 PFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKpseiSKSTEKVLAEVLPRYLDQAGGPPSGL 149
Cdd:cd07126   142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLK----VDSKVSVVMEQFLRLLHLCGMPATDV 202
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 454-511 1.44e-05

Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 46.91  E-value: 1.44e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEAE--PRadgsrrttrydIDMTKCIYCGFCQEACPVDAI 511
Cdd:COG2878   136 EYGCIGCGDCIKACPFDAIVGAAKgmHT-----------VDEDKCTGCGLCVEACPVDCI 184
ALDH_SaliADH cd07105
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ...
 581-655 1.47e-05

Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.


Pssm-ID: 143423 [Multi-domain]  Cd Length: 432  Bit Score: 47.96  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 581 SSPDLGRIINEKHFQRLQGL----LGCG-RVAIGGQSDESDR--YIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLDE 653
Cdd:cd07105   274 GPVVLGSLVSAAAADRVKELvddaLSKGaKLVVGGLADESPSgtSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEE 353


                  ..
gi 1878746647 654 AI 655
Cdd:cd07105   354 AV 355
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 454-511 1.56e-05

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319893 [Multi-domain]  Cd Length: 140  Bit Score: 45.25  E-value: 1.56e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEAEpraDGSrrttrydidMTKCIYC------G---FCQEACPVDAI 511
Cdd:cd16371    83 QDKCIGCGYCVWACPYGAPQYNPE---TGK---------MDKCDMCvdrldeGekpACVAACPTRAL 137
vorD PRK09623
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
454-511 1.60e-05

3-methyl-2-oxobutanoate dehydrogenase subunit delta;


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 44.17  E-value: 1.60e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1878746647 454 EERCIACKLCEAVCPAQAITIeaepRADGSrrttrYDIDMTKCIYCGFCQEACPVDAI 511
Cdd:PRK09623   50 ESKCVKCYICWKFCPEPAIYI----KEDGY-----VAIDYDYCKGCGICANECPTKAI 98
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 454-516 1.68e-05

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 44.63  E-value: 1.68e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1878746647 454 EERCIACKLCEAVCpaqAITIEAEPRADGSR-RTTRYD--IDMTKCIYCGFCQEACPVDAIVEGPN 516
Cdd:cd16372     7 PEKCIGCLQCEEAC---SKTFFKEEDREKSCiRITETEggYAINVCNQCGECIDVCPTGAITRDAN 69
gabD1 PRK09406
succinic semialdehyde dehydrogenase; Reviewed
 79-262 1.77e-05

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181826 [Multi-domain]  Cd Length: 457  Bit Score: 47.81  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  79 AFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLPRyldqaGGPPSG-----LSGwg 153
Cdd:PRK09406  117 AYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRR-----AGFPDGcfqtlLVG-- 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 154 pSGALTVRLAEllcrgagrargdraaagAQVRLHLLhrpshlvqvieghsgflprPGSPRVGKIVMAAAAKHLTPVTLEL 233
Cdd:PRK09406  190 -SGAVEAILRD-----------------PRVAAATL-------------------TGSEPAGRAVAAIAGDEIKKTVLEL 232

                         170       180       190
                  ....*....|....*....|....*....|
gi 1878746647 234 GGKNPCYVDDNCDPQTVVE-QVLARTSSGG 262
Cdd:PRK09406  233 GGSDPFIVMPSADLDRAAEtAVTARVQNNG 262
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 448-511 1.91e-05

NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 44.93  E-value: 1.91e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1878746647 448 RRYPSGEE-----RCIACKLCEAVCPAQAITIeaepradGSRRTTRYDIDMTKCIYCGFCQEACPVDAI 511
Cdd:cd10564     1 RPPWAVDEalfldLCTRCGDCVEACPEGIIVR-------GDGGFPELDFSRGECTFCGACAEACPEGAL 62
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 491-526 2.14e-05

NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 42.77  E-value: 2.14e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1878746647 491 IDMTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEE 526
Cdd:COG1146     5 IDTDKCIGCGACVEVCPVDVLELDEEGKKALVINPE 40
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 446-511 2.55e-05

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 44.19  E-value: 2.55e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1878746647 446 ALRRYPSG-----EERCIACKLCEAVCPAQAITIEAEpradgsrrtTRYDIdmtKCIYCGFCQEACPVDAI 511
Cdd:cd16370    69 ALEPRKGGgvvldKEKCIGCGNCVKACIVGAIFWDEE---------TNKPI---ICIHCGYCARYCPHDVL 127
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 457-512 2.70e-05

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 44.25  E-value: 2.70e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1878746647 457 CIACKLCEAVCPAQAITieaepradgsrRTTR--YDIDMTKCIYCGFCQEACPVDAIV 512
Cdd:cd16372    49 CNQCGECIDVCPTGAIT-----------RDANgvVMINKKLCVGCLMCVGFCPEGAMF 95
ALDH_F4-17_P5CDH cd07123
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ...
 557-643 2.82e-05

Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.


Pssm-ID: 143441 [Multi-domain]  Cd Length: 522  Bit Score: 47.20  E-value: 2.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 557 PKMQERLLPALQSaITrfYGeDPR--SSPdLGRIINEKHFQRLQGLLGCGR------VAIGGQSDESDRY-IAPTVLVDV 627
Cdd:cd07123   332 PEVKERLLEELKE-IK--MG-DPDdfSNF-MGAVIDEKAFDRIKGYIDHAKsdpeaeIIAGGKCDDSVGYfVEPTVIETT 406

                          90
                  ....*....|....*.
gi 1878746647 628 QETEPVMQEEIFGPIL 643
Cdd:cd07123   407 DPKHKLMTEEIFGPVL 422
PLN02467 PLN02467
betaine aldehyde dehydrogenase
 585-672 3.25e-05

betaine aldehyde dehydrogenase


Pssm-ID: 215260 [Multi-domain]  Cd Length: 503  Bit Score: 47.03  E-value: 3.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 585 LGRIINEKHFQRLQGLLGCGR-----VAIGGQSDESDR---YIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLDEAID 656
Cdd:PLN02467  333 LGPVVSEGQYEKVLKFISTAKsegatILCGGKRPEHLKkgfFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIE 412

                          90
                  ....*....|....*.
gi 1878746647 657 FIKRREKPLALYAFSN 672
Cdd:PLN02467  413 LANDSHYGLAGAVISN 428
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 456-511 3.26e-05

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 44.19  E-value: 3.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1878746647 456 RCIACK--LCEAVCPAQAITIEAepraDGSRRttrydIDMTKCIYCGFCQEACPVDAI 511
Cdd:cd16374    42 RCRHCEdaPCMEVCPTGAIYRDE----DGAVL-----VDPDKCIGCGMCAMACPFGVP 90
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 491-512 4.27e-05

MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 42.02  E-value: 4.27e-05
                          10        20
                  ....*....|....*....|..
gi 1878746647 491 IDMTKCIYCGFCQEACPVDAIV 512
Cdd:COG1149     8 IDEEKCIGCGLCVEVCPEGAIK 29
ALDH_F16 cd07111
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ...
 561-655 4.45e-05

Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.


Pssm-ID: 143429 [Multi-domain]  Cd Length: 480  Bit Score: 46.62  E-value: 4.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 561 ERLLPALQSAITRFYGEDP-RSSPDLGRIINEKHFQRLQGLLGCGRvAIGGQSDESDR-------YIAPTVLVDVQETEP 632
Cdd:cd07111   303 EELIRKLKERMSHLRVGDPlDKAIDMGAIVDPAQLKRIRELVEEGR-AEGADVFQPGAdlpskgpFYPPTLFTNVPPASR 381

                          90       100
                  ....*....|....*....|...
gi 1878746647 633 VMQEEIFGPILPIVNVRSLDEAI 655
Cdd:cd07111   382 IAQEEIFGPVLVVLTFRTAKEAV 404
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 455-511 4.89e-05

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 43.33  E-value: 4.89e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1878746647 455 ERCIACKLCEAVC---------PAQA-ITIEAEPRADgsrrttrYDIDMTkCIYCG--FCQEACPVDAI 511
Cdd:cd10550     6 EKCTGCRTCELACslkhegvfnPSLSrIRVVRFEPEG-------LDVPVV-CRQCEdaPCVEACPVGAI 66
PRK09898 PRK09898
ferredoxin-like protein;
454-511 5.03e-05

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 44.83  E-value: 5.03e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEAEPRADgsrrttrydidmTKCIYCGFCQEACPVDAI 511
Cdd:PRK09898  153 HKRCIGCSACTTACPWMMATVNTESKKS------------SKCVLCGECANACPTGAL 198
ALDH_RL0313 cd07148
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ...
 602-656 5.09e-05

Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.


Pssm-ID: 143466 [Multi-domain]  Cd Length: 455  Bit Score: 46.26  E-value: 5.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1878746647 602 GCGRVAIGGQSdESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLDEAID 656
Cdd:cd07148   326 AGARLLCGGKR-LSDTTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIA 379
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 446-522 5.16e-05

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 43.42  E-value: 5.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 446 ALRRYPSG-----EERCIACKLCEAVCPAQAITIEAEPRAdgsrrttrydidMTKCIYCG---------FCQEACPVDAI 511
Cdd:cd16374    59 AIYRDEDGavlvdPDKCIGCGMCAMACPFGVPRFDPSLKV------------AVKCDLCIdrrregklpACVEACPTGAL 126

                          90
                  ....*....|.
gi 1878746647 512 VEGPNFEFSTE 522
Cdd:cd16374   127 KFGDIEELLKE 137
ALDH_AldA_AN0554 cd07143
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ...
 575-672 5.50e-05

Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.


Pssm-ID: 143461  Cd Length: 481  Bit Score: 46.37  E-value: 5.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 575 YGEDPRSSPDLGRIinekHFQRLQGLLGCGR-----VAIGGQSDESDRY-IAPTVLVDVQETEPVMQEEIFGPILPIVNV 648
Cdd:cd07143   321 FAEDTFQGPQVSQI----QYERIMSYIESGKaegatVETGGKRHGNEGYfIEPTIFTDVTEDMKIVKEEIFGPVVAVIKF 396

                          90       100
                  ....*....|....*....|....
gi 1878746647 649 RSLDEAIDFIKRREKPLALYAFSN 672
Cdd:cd07143   397 KTEEEAIKRANDSTYGLAAAVFTN 420
PRK13968 PRK13968
putative succinate semialdehyde dehydrogenase; Provisional
 79-256 5.71e-05

putative succinate semialdehyde dehydrogenase; Provisional


Pssm-ID: 184426 [Multi-domain]  Cd Length: 462  Bit Score: 46.01  E-value: 5.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  79 AFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEVLpryldQAGGPPSGLSGW------ 152
Cdd:PRK13968  120 AVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVF-----KDAGIPQGVYGWlnadnd 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 153 GPSGALT-VRLAEllcrgagrargdraaagaqvrlhllhrpshlVQVIeghsgflprpGSPRVGKIVMAAAAKHLTPVTL 231
Cdd:PRK13968  195 GVSQMINdSRIAA-------------------------------VTVT----------GSVRAGAAIGAQAGAALKKCVL 233

                         170       180
                  ....*....|....*....|....*
gi 1878746647 232 ELGGKNPCYVDDNCDPQTVVEQVLA 256
Cdd:PRK13968  234 ELGGSDPFIVLNDADLELAVKAAVA 258
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 482-522 7.19e-05

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 41.58  E-value: 7.19e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1878746647 482 GSRRTTRYDIDMTKCIYCGFCQEACPVDAI--VEGPNFEFSTE 522
Cdd:COG1144    18 GGWRVERPVVDEDKCIGCGLCWIVCPDGAIrvDDGKYYGIDYD 60
porD PRK09624
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
 454-512 7.29e-05

pyruvate ferredoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 170017 [Multi-domain]  Cd Length: 105  Bit Score: 42.32  E-value: 7.29e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEAE--PRADgsrrttrYDIdmtkCIYCGFCQEACPVDAIV 512
Cdd:PRK09624   50 RDKCVRCYLCYIYCPEPAIYLDEEgyPVFD-------YDY----CKGCGICANECPTKAIE 99
PRK09847 PRK09847
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
 554-655 7.90e-05

gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional


Pssm-ID: 182108 [Multi-domain]  Cd Length: 494  Bit Score: 45.66  E-value: 7.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 554 LYRPKMQERLLPALQSAITRFYGEDPRSsPD--LGRIINEKHFQR----LQGLLGCGRVAIGGQSDESDRYIAPTVLVDV 627
Cdd:PRK09847  309 LLEESIADEFLALLKQQAQNWQPGHPLD-PAttMGTLIDCAHADSvhsfIREGESKGQLLLDGRNAGLAAAIGPTIFVDV 387

                          90       100
                  ....*....|....*....|....*...
gi 1878746647 628 QETEPVMQEEIFGPILPIVNVRSLDEAI 655
Cdd:PRK09847  388 DPNASLSREEIFGPVLVVTRFTSEEQAL 415
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 446-512 8.04e-05

CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the iron-sulfur subunit of carbon monoxide dehydrogenase (CODH), found in anaerobic bacteria and archaea. Carbon monoxide dehydrogenase is a key enzyme for carbon monoxide (CO) metabolism, where CooF is the proposed mediator of electron transfer between CODH and the CO-induced hydrogenase, catalyzing the reaction that uses CO as a single carbon and energy source, and producing only H2 and CO2. The ion-sulfur subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons in the protein complex during reaction.


Pssm-ID: 319885 [Multi-domain]  Cd Length: 140  Bit Score: 43.01  E-value: 8.04e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1878746647 446 ALRRYP-SG-----EERCIACKLCEAVCPAQAITIEAEPRAdgsrrttrydidMTKCIYCGF-----CQEACPVDAIV 512
Cdd:cd10563    73 AMHKDPeTGivihdEEKCVGCWMCVMVCPYGAIRPDKERKV------------ALKCDLCPDretpaCVEACPTGALV 138
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 454-512 8.92e-05

electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 43.63  E-value: 8.92e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1878746647 454 EERCIACKLCEAVCPAQAITieAEPRAdgsrrttRYDIDMTKCIYCGFCQEACPVDAIV 512
Cdd:TIGR01944 112 EDNCIGCTKCIQACPVDAIV--GAAKA-------MHTVIADECTGCDLCVEPCPTDCIE 161
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 446-511 8.93e-05

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 42.71  E-value: 8.93e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1878746647 446 ALRRYPSG-----EERCIACKLCEAVCPAQAItIEAEPRadgsrrttrydIDMTKCIYCGFCQEACPVDAI 511
Cdd:cd16372    63 AITRDANGvvminKKLCVGCLMCVGFCPEGAM-FKHEDY-----------PEPFKCIACGICVKACPTGAL 121
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 454-511 9.65e-05

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 45.51  E-value: 9.65e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEAEPRADGSRRTTRYdidmtKCIYCG------FCQEACPVDAI 511
Cdd:PRK12769   84 QQKCIGCKSCVVACPFGTMQIVLTPVAAGKVKATAH-----KCDLCAgrengpACVENCPADAL 142
oorD PRK09626
2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed
 454-525 9.90e-05

2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed


Pssm-ID: 236597 [Multi-domain]  Cd Length: 103  Bit Score: 42.01  E-value: 9.90e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEAEPRAD-GSRRTTRYDidmTKCIYCGFCQEACPVDAI--VEGPNFEFSTETHE 525
Cdd:PRK09626   15 ESRCKACDICVSVCPAGVLAMRIDPHAVlGKMIKVVHP---ESCIGCRECELHCPDFAIyvADRKEFKFAKLSKE 86
ALDH_KGSADH-like cd07084
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ...
 85-149 9.97e-05

ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.


Pssm-ID: 143403 [Multi-domain]  Cd Length: 442  Bit Score: 45.31  E-value: 9.97e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1878746647  85 PFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSeiskSTEKVLAEVLPRYLDQAGGPPSGL 149
Cdd:cd07084   100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPH----TAVSIVMQIMVRLLHYAGLLPPED 160
ALDH_ACDHII_AcoD-like cd07559
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ...
 585-656 1.02e-04

Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.


Pssm-ID: 143471 [Multi-domain]  Cd Length: 480  Bit Score: 45.41  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 585 LGRIINEKHFQRLQGLLGCGR-----VAIGGQSDESDR-----YIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLDEA 654
Cdd:cd07559   322 MGAQVSKDQLEKILSYVDIGKeegaeVLTGGERLTLGGldkgyFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEA 401


                  ..
gi 1878746647 655 ID 656
Cdd:cd07559   402 IA 403
D1pyr5carbox3 TIGR01238
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ...
 84-149 1.04e-04

delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273518 [Multi-domain]  Cd Length: 500  Bit Score: 45.29  E-value: 1.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1878746647  84 EPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISksteKVLAEVLPRYLDQAGGPPSGL 149
Cdd:TIGR01238 159 ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQT----SLIAYRAVELMQEAGFPAGTI 220
gabD PRK11241
NADP-dependent succinate-semialdehyde dehydrogenase I;
561-671 1.04e-04

NADP-dependent succinate-semialdehyde dehydrogenase I;


Pssm-ID: 183050 [Multi-domain]  Cd Length: 482  Bit Score: 45.28  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 561 ERLLPALQSAITRFY-GEDPRSSPDLGRIINEKHFQRLQ-----GLLGCGRVAIGGQSDE-SDRYIAPTVLVDVQETEPV 633
Cdd:PRK11241  303 DRFAEKLQQAVSKLHiGDGLEKGVTIGPLIDEKAVAKVEehiadALEKGARVVCGGKAHElGGNFFQPTILVDVPANAKV 382

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1878746647 634 MQEEIFGPILPIVNVRSLDEAIDFIKRREKPLALYAFS 671
Cdd:PRK11241  383 AKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYA 420
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 456-509 1.10e-04

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 433017 [Multi-domain]  Cd Length: 64  Bit Score: 40.76  E-value: 1.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1878746647 456 RCIACKLCEAVCPA---------QAITIEAEPRADGSRRTTRYDIDMTKCIYCGFCQEACPVD 509
Cdd:pfam13183   1 RCIRCGACLAACPVylvtggrfpGDPRGGAAALLGRLEALEGLAEGLWLCTLCGACTEVCPVG 63
PRK11904 PRK11904
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
81-149 1.20e-04

bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;


Pssm-ID: 237017 [Multi-domain]  Cd Length: 1038  Bit Score: 45.57  E-value: 1.20e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1878746647   81 IRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEiskSTEKVLAEVLpRYLDQAGGPPSGL 149
Cdd:PRK11904   680 LRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAE---QTPLIAAEAV-KLLHEAGIPKDVL 744
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 454-473 1.24e-04

4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 459642 [Multi-domain]  Cd Length: 24  Bit Score: 39.54  E-value: 1.24e-04
                          10        20
                  ....*....|....*....|
gi 1878746647 454 EERCIACKLCEAVCPAQAIT 473
Cdd:pfam00037   5 EEKCIGCGACVEVCPVGAIT 24
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
454-489 1.40e-04

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 40.48  E-value: 1.40e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEAEPRADGSRRTTRY 489
Cdd:COG2768    39 PEKCIGCGACIEVCPVGAIKIEWEEDEEFQEKMAEY 74
putA PRK11809
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ...
 85-146 1.58e-04

trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed


Pssm-ID: 236989 [Multi-domain]  Cd Length: 1318  Bit Score: 44.96  E-value: 1.58e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1878746647   85 PFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEiskSTEKVLAEVLpRYLDQAGGPP 146
Cdd:PRK11809   768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAE---QTPLIAAQAV-RILLEAGVPA 825
PRK09898 PRK09898
ferredoxin-like protein;
455-507 1.64e-04

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 43.29  E-value: 1.64e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1878746647 455 ERCIACK--LCEAVCPAQAITIEAEPRAdgsrrttrYDIDMTKCIYCGFCQEACP 507
Cdd:PRK09898  121 DTCRQCKepQCMNVCPIGAITWQQKEGC--------ITVDHKRCIGCSACTTACP 167
PRK13252 PRK13252
betaine aldehyde dehydrogenase; Provisional
 584-655 1.67e-04

betaine aldehyde dehydrogenase; Provisional


Pssm-ID: 183918  Cd Length: 488  Bit Score: 44.49  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 584 DLGRIINEKHFQRLQGLLGCG-----RVAIGGQS---DESDR--YIAPTVLVDVQETEPVMQEEIFGPILPIVNVRSLDE 653
Cdd:PRK13252  322 NFGPLVSFAHRDKVLGYIEKGkaegaRLLCGGERlteGGFANgaFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDE 401


                  ..
gi 1878746647 654 AI 655
Cdd:PRK13252  402 VI 403
PLN02419 PLN02419
methylmalonate-semialdehyde dehydrogenase [acylating]
 576-673 1.84e-04

methylmalonate-semialdehyde dehydrogenase [acylating]


Pssm-ID: 166060 [Multi-domain]  Cd Length: 604  Bit Score: 44.74  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 576 GEDPRSspDLGRIINEKHFQRLQGLLGCG-----RVAIGGQS-----DESDRYIAPTVLVDVQETEPVMQEEIFGPILPI 645
Cdd:PLN02419  422 GSEPDA--DLGPVISKQAKERICRLIQSGvddgaKLLLDGRDivvpgYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVC 499

                          90       100
                  ....*....|....*....|....*...
gi 1878746647 646 VNVRSLDEAIDFIKRREKPLALYAFSNS 673
Cdd:PLN02419  500 MQANSFDEAISIINKNKYGNGAAIFTSS 527
PLN02315 PLN02315
aldehyde dehydrogenase family 7 member
 604-656 1.92e-04

aldehyde dehydrogenase family 7 member


Pssm-ID: 177949  Cd Length: 508  Bit Score: 44.44  E-value: 1.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1878746647 604 GRVAIGGQSDESD-RYIAPTVlVDVQETEPVMQEEIFGPILPIVNVRSLDEAID 656
Cdd:PLN02315  363 GKILTGGSAIESEgNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLEEAIE 415
Fer4_21 pfam14697
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 454-511 1.99e-04

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 434137 [Multi-domain]  Cd Length: 59  Bit Score: 39.57  E-value: 1.99e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1878746647 454 EERCIACKLCEAVCPA---QAITIEAEpradgsrrtTRYDIDMTKCIYCGFCQEACPV-DAI 511
Cdd:pfam14697   5 EDTCIGCGKCYIACPDtshQAIVGDGK---------RHHTVIEDECTGCNLCVSVCPVdDCI 57
PutA2 COG4230
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
71-122 2.74e-04

Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];


Pssm-ID: 443374 [Multi-domain]  Cd Length: 1156  Bit Score: 44.16  E-value: 2.74e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1878746647   71 NLATQLDSAFIRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSE 122
Cdd:COG4230    666 AQARRLFAAPTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAE 717
PRK11905 PRK11905
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
 66-122 3.19e-04

bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed


Pssm-ID: 237018 [Multi-domain]  Cd Length: 1208  Bit Score: 44.09  E-value: 3.19e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1878746647   66 EQVRRNLATQldsafiRKEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSE 122
Cdd:PRK11905   663 AQARRLLNGP------GHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAE 713
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 454-475 3.52e-04

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 40.84  E-value: 3.52e-04
                          10        20
                  ....*....|....*....|..
gi 1878746647 454 EERCIACKLCEAVCPAQAITIE 475
Cdd:cd10549   107 KEKCIGCGICAEVCPVNAIKLV 128
PLN02419 PLN02419
methylmalonate-semialdehyde dehydrogenase [acylating]
 71-149 3.76e-04

methylmalonate-semialdehyde dehydrogenase [acylating]


Pssm-ID: 166060 [Multi-domain]  Cd Length: 604  Bit Score: 43.58  E-value: 3.76e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1878746647  71 NLATQLDSAFIRkEPFGLVLIVAPWNYPVNLTLLPLVGALAAGNCVVLKPSEISKSTEKVLAEvlpryLDQAGGPPSGL 149
Cdd:PLN02419  236 NVSNGVDTYSIR-EPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAE-----LAMEAGLPDGV 308
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 454-480 3.98e-04

TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 39.26  E-value: 3.98e-04
                          10        20
                  ....*....|....*....|....*..
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEAEPRA 480
Cdd:COG4231    50 PDLCIGCGSCVQVCPVDAIKLEKRVPE 76
PRK08318 PRK08318
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
454-513 3.99e-04

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 43.39  E-value: 3.99e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1878746647 454 EERCIACKLCEAVC---PAQAITIEAepraDGSRRttrYDIDMTKCIYCGFCQEACPVDAIVE 513
Cdd:PRK08318  341 QDKCIGCGRCYIACedtSHQAIEWDE----DGTRT---PEVIEEECVGCNLCAHVCPVEGCIT 396
RDH TIGR02486
reductive dehalogenase; This model represents a family of corrin and 8-iron Fe-S ...
 457-507 4.71e-04

reductive dehalogenase; This model represents a family of corrin and 8-iron Fe-S cluster-containing reductive dehalogenases found primarily in halorespiring microorganisms such as dehalococcoides ethenogenes which contains as many as 17 enzymes of this type with varying substrate ranges. One example of a characterized species is the tetrachloroethene reductive dehalogenase (1.97.1.8) which also acts on trichloroethene converting it to dichloroethene.


Pssm-ID: 274158  Cd Length: 314  Bit Score: 42.81  E-value: 4.71e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1878746647 457 CIACKLCEAVCPAQAITIEAEPRADGSRRTTRYD----------IDMTKCI----------YCGFCQEACP 507
Cdd:TIGR02486 207 CETCGKCADECPSGAISKGGEPTWDPEDSNGDPPgennpglkwqYDGWRCLlfrcynegggGCGVCQAVCP 277
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 490-516 4.75e-04

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 40.46  E-value: 4.75e-04
                          10        20
                  ....*....|....*....|....*..
gi 1878746647 490 DIDMTKCIYCGFCQEACPVDAIVEGPN 516
Cdd:cd10549     2 KYDPEKCIGCGICVKACPTDAIELGPN 28
NapF COG1145
Ferredoxin [Energy production and conversion];
454-478 4.91e-04

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 42.40  E-value: 4.91e-04
                          10        20
                  ....*....|....*....|....*
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEAEP 478
Cdd:COG1145   212 PDKCIGCGACVKVCPVGAISLEPKE 236
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 463-511 7.10e-04

uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes the beta-subunit of formate dehydrogenases that are as yet uncharacterized. Members of the DMSO reductase family include formate dehydrogenase N and O (FDH-N, FDH-O) and tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N, a major component of nitrate respiration of Escherichia coli, is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. It forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons.


Pssm-ID: 319884 [Multi-domain]  Cd Length: 161  Bit Score: 40.75  E-value: 7.10e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1878746647 463 CEAVCPAQAITIEAepraDGSrrttrYDIDMTKCIYCGFCQEACPVDAI 511
Cdd:cd10562    78 CVKVCPTGALYKTE----NGA-----VVVDEDKCIGCGYCVAACPFDVP 117
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 486-511 7.52e-04

Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 38.49  E-value: 7.52e-04
                          10        20
                  ....*....|....*....|....*.
gi 1878746647 486 TTRYDIDMTKCIYCGFCQEACPVDAI 511
Cdd:COG2221     7 TWPPKIDEEKCIGCGLCVAVCPTGAI 32
ALDH_EutE cd07121
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ...
 607-663 7.90e-04

Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.


Pssm-ID: 143439 [Multi-domain]  Cd Length: 429  Bit Score: 42.22  E-value: 7.90e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1878746647 607 AIGGQSDESDRYIaptvLVDVQETEPVMQEEIFGPILPIVNVRSLDEAIDFIKRREK 663
Cdd:cd07121   304 AAGIEVPADIRLI----IVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEH 356
PRK10330 PRK10330
electron transport protein HydN;
454-512 8.00e-04

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 41.03  E-value: 8.00e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEAEP--RADGSRRTTR-YDIDMTKCIYCGF------CQEACPVDAIV 512
Cdd:PRK10330   86 QERCIGCKTCVVACPYGAMEVVVRPviRNSGAGLNVRaEKAEANKCDLCNHredgpaCMAACPTHALI 153
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 435-507 8.42e-04

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 42.30  E-value: 8.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 435 GPLSPRFRGEHALRRYPSGEER------CIACKLCEAVCPAQAIT-------------IEAEPRADGSRRTTRYDIDMTK 495
Cdd:PRK06259  107 KSLRNYLQRKNEKITYPEDIEDikklrgCIECLSCVSTCPARKVSdypgptfmrqlarFAFDPRDEGDREKEAFDEGLYN 186

                          90
                  ....*....|..
gi 1878746647 496 CIYCGFCQEACP 507
Cdd:PRK06259  187 CTTCGKCVEVCP 198
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
377-509 8.51e-04

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 41.66  E-value: 8.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 377 AVAATYKYVNVREPTMDMKSVTDraaqtLL--WTELIRGLGMTLSYLFRepatiNYPFEKGPLSPRFRGEHALRRYPSGE 454
Cdd:PRK12576   84 DVAKKYNSVITIEPMDYFKVVKD-----LIvdFDEFYERMFKVKPRLYR-----AKEVLEGKAEHRLKPEDQKELWKFAQ 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 455 erCIACKLCEAVCPAQAITIE--------------AEPRADGSRRTTRYDIDMT-KCIYCGFCQEACPVD 509
Cdd:PRK12576  154 --CIWCGLCVSACPVVAIDPEflgpaahakgyrflADPRDTITEERMKILIDSSwRCTYCYSCSNVCPRD 221
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 445-527 9.04e-04

the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 (Hyd-2), an enzyme that catalyzes the reversible oxidation of H2 to protons and electrons. Hyd-2 is membrane-associated and forms an unusual heterotetrameric [NiFe]-hydrogenase in that it lacks the typical cytochrome b membrane anchor subunit that transfers electrons to the quinone pool. The electron transfer subunit of Hyd-2 (HybA) which is predicted to contain four iron-sulfur clusters, is essential for electron transfer from Hyd-2 to menaquinone/demethylmenaquinone (MQ/DMQ) to couple hydrogen oxidation to fumarate reduction.


Pssm-ID: 319883 [Multi-domain]  Cd Length: 196  Bit Score: 41.04  E-value: 9.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 445 HALRRYPSG-----EERCIACKLCEAVCPAQAITIE---AEPRadgsrrttrydidMTKCIYCgF----------CQEAC 506
Cdd:cd10561    84 GALRKTPEGpvtydEDKCIGCRYCMVACPFNIPKYEwdsANPK-------------IRKCTMC-YdrlkegkqpaCVEAC 149

                          90       100
                  ....*....|....*....|.
gi 1878746647 507 PVDAIVEGPNFEFSTETHEEL 527
Cdd:cd10561   150 PTGALLFGKREELLAEAKRRI 170
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 491-517 1.11e-03

electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 40.17  E-value: 1.11e-03
                          10        20
                  ....*....|....*....|....*..
gi 1878746647 491 IDMTKCIYCGFCQEACPVDAIVEGPNF 517
Cdd:TIGR01944 110 IDEDNCIGCTKCIQACPVDAIVGAAKA 136
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 458-511 1.16e-03

HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.


Pssm-ID: 319876 [Multi-domain]  Cd Length: 149  Bit Score: 39.94  E-value: 1.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1878746647 458 IACKLCE-----AVCPAQAITieaepRADGSRRttrydIDMTKCIYCGFCQEACPVDAI 511
Cdd:cd10554    54 VQCRQCEdapcaNVCPVGAIS-----QEDGVVQ-----VDEERCIGCKLCVLACPFGAI 102
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 456-509 1.34e-03

4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 433287 [Multi-domain]  Cd Length: 61  Bit Score: 37.44  E-value: 1.34e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1878746647 456 RCIACKLCEAVCPAQAITieaepraDGSRRTTRYDIDMTK------------CIYCGFCQEACPVD 509
Cdd:pfam13534   1 RCIQCGCCVDECPRYLLN-------GDEPKKLMRAAYLGDleelqankvanlCSECGLCEYACPMG 59
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 457-507 1.52e-03

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319891 [Multi-domain]  Cd Length: 172  Bit Score: 40.06  E-value: 1.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1878746647 457 CIACKL--CEAVCPAQAITIEaeprADGSRRTTrydiDMTKCIYCGFCQEACP 507
Cdd:cd16369    51 CMHCEDptCAEVCPADAIKVT----EDGVVQSA----LKPRCIGCSNCVNACP 95
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 454-515 1.82e-03

uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes the beta-subunit of formate dehydrogenases that are as yet uncharacterized. Members of the DMSO reductase family include formate dehydrogenase N and O (FDH-N, FDH-O) and tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N, a major component of nitrate respiration of Escherichia coli, is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. It forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons.


Pssm-ID: 319884 [Multi-domain]  Cd Length: 161  Bit Score: 39.59  E-value: 1.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1878746647 454 EERCIACKLCEAVCPAQAitieaePRADgsrrttRYDIDMTKCIYC------GF---CQEACPVDAIVEGP 515
Cdd:cd10562    99 EDKCIGCGYCVAACPFDV------PRYD------ETTNKITKCTLCfdrienGMqpaCVKTCPTGALTFGD 157
gabD2 PRK09407
succinic semialdehyde dehydrogenase; Reviewed
 621-656 2.12e-03

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236501 [Multi-domain]  Cd Length: 524  Bit Score: 41.02  E-value: 2.12e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1878746647 621 PTVLVDVQETEPVMQEEIFGPILPIVNVRSLDEAID 656
Cdd:PRK09407  377 PTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVE 412
Fer4_6 pfam12837
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
 454-472 2.47e-03

4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 432822 [Multi-domain]  Cd Length: 24  Bit Score: 35.67  E-value: 2.47e-03
                          10
                  ....*....|....*....
gi 1878746647 454 EERCIACKLCEAVCPAQAI 472
Cdd:pfam12837   6 PDKCIGCGRCVVVCPYGAI 24
ALDH_F7_AASADH cd07130
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ...
 604-657 2.85e-03

NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.


Pssm-ID: 143448  Cd Length: 474  Bit Score: 40.65  E-value: 2.85e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1878746647 604 GRVAIGGQS-DESDRYIAPTVlVDVQETEPVMQEEIFGPILPIVNVRSLDEAIDF 657
Cdd:cd07130   341 GTVLFGGKViDGPGNYVEPTI-VEGLSDAPIVKEETFAPILYVLKFDTLEEAIAW 394
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 454-518 2.89e-03

Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 39.98  E-value: 2.89e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEAEPrADGSRRTTRYDIDMTKCIYC-GFCQEACPVDAIVEGPNFE 518
Cdd:COG2878   166 EDKCTGCGLCVEACPVDCIEMVPVS-PTVVVSSWDKGKAVRKVVGCiGLCCKKCCPAAAITVNNLA 230
ALDH_SGSD_AstD cd07095
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ...
 561-656 3.01e-03

N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.


Pssm-ID: 143414 [Multi-domain]  Cd Length: 431  Bit Score: 40.72  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 561 ERLLPALQSAITRFYGEDPRSSPD-LGRIINEKHFQRL----QGLLGCGRVAIGGQS--DESDRYIAPTvLVDVQETEPV 633
Cdd:cd07095   255 DAFLERLVEAAKRLRIGAPDAEPPfMGPLIIAAAAARYllaqQDLLALGGEPLLAMErlVAGTAFLSPG-IIDVTDAADV 333

                          90       100
                  ....*....|....*....|...
gi 1878746647 634 MQEEIFGPILPIVNVRSLDEAID 656
Cdd:cd07095   334 PDEEIFGPLLQVYRYDDFDEAIA 356
ALDH_KGSADH cd07129
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ...
 595-662 3.21e-03

Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.


Pssm-ID: 143447 [Multi-domain]  Cd Length: 454  Bit Score: 40.60  E-value: 3.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1878746647 595 QRLQGLLGcGRVAIGGQSDESDRYIAPTVL-VDVQE--TEPVMQEEIFGPILPIVNVRSLDEAIDFIKRRE 662
Cdd:cd07129   306 EALAAAPG-VRVLAGGAAAEGGNQAAPTLFkVDAAAflADPALQEEVFGPASLVVRYDDAAELLAVAEALE 375
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 455-477 4.14e-03

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 36.57  E-value: 4.14e-03
                          10        20
                  ....*....|....*....|...
gi 1878746647 455 ERCIACKLCEAVCPAQAITIEAE 477
Cdd:COG1144    60 DYCKGCGICAEVCPVKAIEMVPE 82
PRK00783 PRK00783
DNA-directed RNA polymerase subunit D; Provisional
 454-523 4.25e-03

DNA-directed RNA polymerase subunit D; Provisional


Pssm-ID: 234837 [Multi-domain]  Cd Length: 263  Bit Score: 39.48  E-value: 4.25e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1878746647 454 EERCIACKLCEAVCPAQAITIEaepraDGSRRTTrydiDMTKCIYCGFCQEACPVDAIVEG--PN-FEFSTET 523
Cdd:PRK00783  168 SEDCDECEKCVEACPRGVLELK-----EGKLVVT----DLLNCSLCKLCERACPGKAIRVSddENkFIFTVES 231
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 446-514 4.41e-03

beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family contains beta FeS subunits of several dehydrogenases in the DMSO reductase superfamily, including formate dehydrogenase N (FDH-N), tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N is a major component of nitrate respiration of Escherichia coli; it catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate to a cytochrome. W-FDH contains a tungsten instead of molybdenum at the catalytic center and seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate.


Pssm-ID: 319888 [Multi-domain]  Cd Length: 156  Bit Score: 38.15  E-value: 4.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 446 ALRRYPSG-----EERCIACKLCEAVCPAQAITIEAEpradgsrrttryDIDMTKCIYC------GF---CQEACPVDAI 511
Cdd:cd16366    86 AIIRTETGtvvvdPETCIGCGYCVNACPFDIPRFDEE------------TGRVAKCTLCydrisnGLqpaCVKTCPTGAL 153


                  ...
gi 1878746647 512 VEG 514
Cdd:cd16366   154 TFG 156
ALDH-like cd07077
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ...
 8-167 4.60e-03

NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.


Pssm-ID: 143396 [Multi-domain]  Cd Length: 397  Bit Score: 39.90  E-value: 4.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647   8 RAVVTKATQQQQLA------ALGTDAQPWAQdwMSAVELEVSE----------ISIVQTEIN-LALRNLRAWMRDEQVRR 70
Cdd:cd07077     8 RTLAVNHDEQRDLIinaianALYDTRQRLAS--EAVSERGAYIrslianwiamMGCSESKLYkNIDTERGITASVGHIQD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647  71 NLATQLDSAFIRKEPFGLVLIVAPWNYP---VNLTLLplvgALAAGNCVVLKPSEISKSTEKVLAEVLPRYLdqAGGPPS 147
Cdd:cd07077    86 VLLPDNGETYVRAFPIGVTMHILPSTNPlsgITSALR----GIATRNQCIFRPHPSAPFTNRALALLFQAAD--AAHGPK 159

                         170       180
                  ....*....|....*....|
gi 1878746647 148 GLSGWGPSGALTvrLAELLC 167
Cdd:cd07077   160 ILVLYVPHPSDE--LAEELL 177
Fer4_6 pfam12837
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
 491-511 4.72e-03

4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 432822 [Multi-domain]  Cd Length: 24  Bit Score: 34.90  E-value: 4.72e-03
                          10        20
                  ....*....|....*....|.
gi 1878746647 491 IDMTKCIYCGFCQEACPVDAI 511
Cdd:pfam12837   4 VDPDKCIGCGRCVVVCPYGAI 24
PRK15398 PRK15398
aldehyde dehydrogenase;
607-663 4.73e-03

aldehyde dehydrogenase;


Pssm-ID: 237956  Cd Length: 465  Bit Score: 39.89  E-value: 4.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1878746647 607 AIGGQSDESDRYIaptvLVDVQETEPVMQEEIFGPILPIVNVRSLDEAIDFIKRREK 663
Cdd:PRK15398  334 AAGINVPKDTRLL----IVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEH 386
ALDH_PutA-P5CDH cd07125
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ...
 584-658 5.05e-03

Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.


Pssm-ID: 143443 [Multi-domain]  Cd Length: 518  Bit Score: 39.87  E-value: 5.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 584 DLGRIINEKHFQRLQGLL----GCGRVAIGGQSDESD-RYIAPTVLVDVqeTEPVMQEEIFGPILPIV--NVRSLDEAID 656
Cdd:cd07125   351 DVGPLIDKPAGKLLRAHTelmrGEAWLIAPAPLDDGNgYFVAPGIIEIV--GIFDLTTEVFGPILHVIrfKAEDLDEAIE 428


                  ..
gi 1878746647 657 FI 658
Cdd:cd07125   429 DI 430
Fer4_18 pfam13746
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 449-506 5.21e-03

4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 404610 [Multi-domain]  Cd Length: 114  Bit Score: 37.38  E-value: 5.21e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1878746647 449 RYPSGEERCIACKLCEAVCPAqAITIeaepradgsRRTTRYDidmtkCIYCGFCQEAC 506
Cdd:pfam13746  53 RQQKGVGDCIDCESCVQVCPT-GIDI---------RKGLQLE-----CINCGLCIDAC 95
ALDH_PAD-PaaZ cd07127
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ...
 566-673 5.73e-03

Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.


Pssm-ID: 143445  Cd Length: 549  Bit Score: 39.77  E-value: 5.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 566 ALQSAITRFYGEDPRSSPDLGRIINEKHFQRLQGLLGCGRVAIGGQSDESDRYI-----APTVLVDVQETEPVMQEEIFG 640
Cdd:cd07127   367 DLAAAIDGLLADPARAAALLGAIQSPDTLARIAEARQLGEVLLASEAVAHPEFPdarvrTPLLLKLDASDEAAYAEERFG 446

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1878746647 641 PILPIVNVRSLDEAIDFIKR--REK-PLALYAFSNS 673
Cdd:cd07127   447 PIAFVVATDSTDHSIELAREsvREHgAMTVGVYSTD 482
PRK06991 PRK06991
electron transport complex subunit RsxB;
491-515 5.82e-03

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 39.01  E-value: 5.82e-03
                          10        20
                  ....*....|....*....|....*
gi 1878746647 491 IDMTKCIYCGFCQEACPVDAIVEGP 515
Cdd:PRK06991   82 IDEQLCIGCTLCMQACPVDAIVGAP 106
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 441-516 7.03e-03

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319889 [Multi-domain]  Cd Length: 138  Bit Score: 37.29  E-value: 7.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 441 FRGEHALRRypsGEERCIACKLCEAVCpaqAITIEAEPRADgsRRTTRYD-IDM-TKCIYC--GFCQEACPVDAIVEGPN 516
Cdd:cd16367     8 IQGTNLLVI---DLDRCIRCDNCEKAC---ADTHDGHSRLD--RNGLRFGnLLVpTACRHCvdPVCMIGCPTGAIHRDDG 79
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 456-511 8.06e-03

beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family contains beta FeS subunits of several dehydrogenases in the DMSO reductase superfamily, including formate dehydrogenase N (FDH-N), tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N is a major component of nitrate respiration of Escherichia coli; it catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate to a cytochrome. W-FDH contains a tungsten instead of molybdenum at the catalytic center and seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate.


Pssm-ID: 319888 [Multi-domain]  Cd Length: 156  Bit Score: 37.38  E-value: 8.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1878746647 456 RCIACKLCE-----AVCPAQAItieaepradgSRRTT-RYDIDMTKCIYCGFCQEACPVDAI 511
Cdd:cd16366    66 RKDQCMHCTdagclAACPTGAI----------IRTETgTVVVDPETCIGCGYCVNACPFDIP 117
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 455-515 8.58e-03

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319891 [Multi-domain]  Cd Length: 172  Bit Score: 37.75  E-value: 8.58e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1878746647 455 ERCIACKLCEAVCPaqaitiEAEPRaDGSRRTTRYDID--------MTKCIYC--GFCQEACPVDAIVEGP 515
Cdd:cd16369     9 SRCIGCRACVAACR------ECGTH-RGKSMIHVDYIDrgestqtaPTVCMHCedPTCAEVCPADAIKVTE 72
RNAP_D cd07030
D subunit of Archaeal RNA polymerase; The D subunit of archaeal RNA polymerase (RNAP) is ...
 444-523 8.76e-03

D subunit of Archaeal RNA polymerase; The D subunit of archaeal RNA polymerase (RNAP) is involved in the assembly of RNAP subunits. RNAP is a large multi-subunit complex responsible for the synthesis of RNA. It is the principal enzyme of the transcription process, and is a final target in many regulatory pathways that control gene expression in all living cells. A single distinct RNAP complex is found in archaea, which may be responsible for the synthesis of all RNAs. The archaeal RNAP harbors homologues of all eukaryotic RNAP II subunits with two exceptions (RPB8 and RPB9). The 12 archaeal subunits are designated by letters and can be divided into three functional groups that are engaged in: (I) catalysis (A'/A", B'/B" or B); (II) assembly (L, N, D and P); and (III) auxiliary functions (F, E, H and K). The D subunit is equivalent to the RPB3 subunit of eukaryotic RNAP II. It contains two subdomains: one subdomain is similar the eukaryotic Rpb11/AC19/archaeal L subunit which is involved in dimerization, and the other is an inserted beta sheet subdomain. The assembly of the two largest archaeal RNAP subunits that provide most of the enzyme's catalytic functions depends on the presence of the archaeal D/L heterodimer.


Pssm-ID: 132908 [Multi-domain]  Cd Length: 259  Bit Score: 38.40  E-value: 8.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 444 EHA---------LRRYPSGE--ERCIACKLCEAVCPAQAITIEAEPRADGsrrttrydiDMTKCIYCGFCQEACPVDAIV 512
Cdd:cd07030   147 EHAkwqpttacgYKYYPVIEidEDCDGCGKCVEECPRGVLELEEGKVVVE---------DLEDCSLCKLCERACDAGAIR 217

                          90
                  ....*....|....
gi 1878746647 513 EGP---NFEFSTET 523
Cdd:cd07030   218 VGWdedRFIFEVES 231
ALDH_PsfA-ACA09737 cd07120
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ...
 576-655 8.97e-03

Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.


Pssm-ID: 143438 [Multi-domain]  Cd Length: 455  Bit Score: 39.25  E-value: 8.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1878746647 576 GEDPRSspDLGRIINEKHFQRLQGLLG-----CGRVAI-GGQSDESDR---YIAPTVLVDVQETEPVMQEEIFGPILPIV 646
Cdd:cd07120   293 GLDPAS--DMGPLIDRANVDRVDRMVEraiaaGAEVVLrGGPVTEGLAkgaFLRPTLLEVDDPDADIVQEEIFGPVLTLE 370


                  ....*....
gi 1878746647 647 NVRSLDEAI 655
Cdd:cd07120   371 TFDDEAEAV 379
napF TIGR00402
ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of ...
 452-521 9.34e-03

ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of the periplasmic nitrate reductase system, as in Escherichia coli. NapF interacts with the catalytic subunit, NapA, and may be an accessory protein for NapA maturation. [Energy metabolism, Electron transport]


Pssm-ID: 273060 [Multi-domain]  Cd Length: 101  Bit Score: 36.08  E-value: 9.34e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1878746647 452 SGEE-----RCIACKLCEAVCPAQAITieaepRADGSRRTTRydIDMTKCIYCGFCQEACPVDAIveGPNFEFST 521
Cdd:TIGR00402  26 SAREslfsaVCTRCGECASACENNILQ-----LGQQGQPTVE--FDNAECDFCGKCAEACPTNAF--HPRFPGDW 91
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 455-509 9.56e-03

Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 38.90  E-value: 9.56e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1878746647 455 ERCIACKLCEAVCPAQAIT-----------------IEAEPRADGSRRTTRYdidMTKCIYCGFCQEACPVD 509
Cdd:COG0247    78 DACVGCGFCRAMCPSYKATgdekdsprgrinllrevLEGELPLDLSEEVYEV---LDLCLTCKACETACPSG 146
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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