NCBI Conserved Domain Search

Conserved domains on [gi|393195303|ref|NP_001257294|]

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cytosolic 10-formyltetrahydrofolate dehydrogenase isoform 3 [Homo sapiens]

Protein Classification

bifunctional UDP-glucuronic acid decarboxylase/UDP-4-amino-4-deoxy-L-arabinose formyltransferase; acyl carrier protein( domain architecture ID 10222379)

bifunctional UDP-glucuronic acid decarboxylase/UDP-4-amino-4-deoxy-L-arabinose formyltransferase is specific to the lipid A-Ara4N pathway; it catalyzes the NAD+-dependent oxidative decarboxylation of UDP-glucuronic acid and formylates UDP-Ara4N| acyl carrier protein may function as a carrier of the growing fatty acid chain in fatty acid biosynthesis or as the carrier of activated (amino) acid groups in polyketide synthases and non-ribosomal peptide synthases

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

ALDH_F1L_FTFDH

cd07140

10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ...

316-801

0e+00

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: 1009.72 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 316 TVRMPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLM 395
Cdd:cd07140    1 TLKMPHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 396 EQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQARPNRNLTLTRKEPVGVCGIIIPWNYP 475
Cdd:cd07140   81 EEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQARPNRNLTLTKREPIGVCGIVIPWNYP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 476 LMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGK 555
Cdd:cd07140  161 LMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 556 HIMKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKV 635
Cdd:cd07140  241 HIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKI 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 636 GNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFA 715
Cdd:cd07140  321 GDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFD 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 716 DGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVK 795
Cdd:cd07140  401 DGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTK 480


                 ....*.
gi 393195303 796 TVTFEY 801
Cdd:cd07140  481 TVTIEY 486

FMT_core super family

cl00395

Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...

1-128

2.22e-85

Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The proteins of this superfamily contain a formyltransferase domain that hydrolyzes the removal of a formyl group from its substrate as part of a multistep transfer mechanism, and this alignment model represents the catalytic core of the formyltransferase domain. This family includes the following known members; Glycinamide Ribonucleotide Transformylase (GART), Formyl-FH4 Hydrolase, Methionyl-tRNA Formyltransferase, ArnA, and 10-Formyltetrahydrofolate Dehydrogenase (FDH). Glycinamide Ribonucleotide Transformylase (GART) catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Methionyl-tRNA Formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA, which plays important role in translation initiation. ArnA is required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. 10-formyltetrahydrofolate dehydrogenase (FDH) catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. Members of this family are multidomain proteins. The formyltransferase domain is located at the N-terminus of FDH, Methionyl-tRNA Formyltransferase and ArnA, and at the C-terminus of Formyl-FH4 Hydrolase. Prokaryotic Glycinamide Ribonucleotide Transformylase (GART) is a single domain protein while eukaryotic GART is a trifunctional protein that catalyzes the second, third and fifth steps in de novo purine biosynthesis.

The actual alignment was detected with superfamily member cd08647:

Pssm-ID: 444886 [Multi-domain] Cd Length: 203 Bit Score: 269.70 E-value: 2.22e-85

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303   1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADPLGLEAEKDGVPVFKYSRWRAKGQALPDVVAKYQALGAEL 80
Cdd:cd08647    1 MKIAVIGQSLFGQEVYKELRKEGHEVVGVFTIPDKDGKADPLALEAEKDGVPVFKFPRWRAKGQAIPEVVAKYKALGAEL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 393195303  81 NVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAIhNW--IRGNDK 128
Cdd:cd08647   81 NVLPFCSQFIPMEVIDAPKHGSIIYHPSILPRHRGASAI-NWtlIHGDKK 129

FDH_Hydrolase_C

cd08703

The C-terminal subdomain of the hydrolase domain on the bi-functional protein ...

116-205

6.67e-42

The C-terminal subdomain of the hydrolase domain on the bi-functional protein 10-formyltetrahydrofolate dehydrogenase; The family represents the C-terminal subdomain of the hydrolase domain on the bi-functional protein, 10-formyltetrahydrofolate dehydrogenase (FDH). FDH catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. The protein comprises two functional domains: the N-terminal hydrolase domain that removes a formyl group from 10-formyltetrahydrofolate and the C-terminal NADP-dependent dehydrogenase domain that reduces the formyl group to carbon dioxide. The hydrolase domain contains an N-terminal formyl transferase catalytic core subdomain and this C-terminal subdomain, which may be involved in substrate binding.

Pssm-ID: 187731 [Multi-domain] Cd Length: 100 Bit Score: 147.88 E-value: 6.67e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 116 ASAIHNWIRGNDKVPGAWTEACEQKLTFFNSTLNTSGLVPEGdALPIPGAHRPGVVTKAGLILFGNDDKMLLVKNIQLED 195
Cdd:cd08703   12 AEALHNFIRGNDKVPGAWATIDGEQVTLFGSSLWKGGKPPGG-EVEVEGLERPGIVHKNGLLITGSDGKMVNVKRLQFED 90

                         90
                 ....*....|
gi 393195303 196 GKMILASNFF 205
Cdd:cd08703   91 GKMIPASKYG 100

Name

Accession

Description

Interval

E-value

ALDH_F1L_FTFDH

cd07140

10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ...

316-801

0e+00

Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 1009.72 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 316 TVRMPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLM 395
Cdd:cd07140    1 TLKMPHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 396 EQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQARPNRNLTLTRKEPVGVCGIIIPWNYP 475
Cdd:cd07140   81 EEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQARPNRNLTLTKREPIGVCGIVIPWNYP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 476 LMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGK 555
Cdd:cd07140  161 LMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 556 HIMKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKV 635
Cdd:cd07140  241 HIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKI 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 636 GNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFA 715
Cdd:cd07140  321 GDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFD 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 716 DGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVK 795
Cdd:cd07140  401 DGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTK 480


                 ....*.
gi 393195303 796 TVTFEY 801
Cdd:cd07140  481 TVTIEY 486

Aldedh

pfam00171

Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...

329-797

0e+00

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: 620.70 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  329 FVDAEGaKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEAL 408
Cdd:pfam00171   1 WVDSES-ETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP--AWRKTPAAERAAILRKAADLLEERKDELAELETL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  409 DAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPINQARpnrnLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLA 488
Cdd:pfam00171  78 ENGKPLAEA-RGEVDRAIDVLRYYAGLARRLDGETLPSDPGR----LAYTRREPLGVVGAITPWNFPLLLPAWKIAPALA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  489 AGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKK 568
Cdd:pfam00171 153 AGNTVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAA-QNLKR 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  569 VSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQ 648
Cdd:pfam00171 232 VTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPL 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  649 NHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANA 728
Cdd:pfam00171 312 ISKAQLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFK--DEEEAIEIAND 389

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  729 TEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDV-AAPFGGFKQSGFGKDLGEAALNEYLRVKTV 797
Cdd:pfam00171 390 TEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459

AdhE

COG1012

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...

320-801

0e+00

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: 604.04 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 320 PHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRLADLMEQHQ 399
Cdd:COG1012    5 EYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAF--PAWAATPPAERAAILLRAADLLEERR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 400 EELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPInqARPNRnLTLTRKEPVGVCGIIIPWNYPLMML 479
Cdd:COG1012   83 EELAALLTLETGKPLAEA-RGEVDRAADFLRYYAGEARRLYGETIPS--DAPGT-RAYVRREPLGVVGAITPWNFPLALA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 480 SWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMK 559
Cdd:COG1012  159 AWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 560 SCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPL 639
Cdd:COG1012  239 AAA-ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPL 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 640 DRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPR-PGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgD 718
Cdd:COG1012  318 DPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFD--D 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 719 LDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVA-APFGGFKQSGFGKDLGEAALNEYLRVKTV 797
Cdd:COG1012  396 EEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPqAPFGGVKQSGIGREGGREGLEEYTETKTV 475


                 ....
gi 393195303 798 TFEY 801
Cdd:COG1012  476 TIRL 479

PLN02766

coniferyl-aldehyde dehydrogenase

313-797

1.17e-176

coniferyl-aldehyde dehydrogenase

Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 517.07 E-value: 1.17e-176

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 313 NKRTVRMPH----QLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLM 388
Cdd:PLN02766   9 GASGVKVPEikftKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFERGRIM 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 389 YRLADLMEQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPInqARPNRNLTLtrKEPVGVCGI 468
Cdd:PLN02766  89 MKFADLIEEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKM--SRQLQGYTL--KEPIGVVGH 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 469 IIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFT 548
Cdd:PLN02766 165 IIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFT 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 549 GSTEVGKHIMKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVE 628
Cdd:PLN02766 245 GSTEVGRKIMQAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVE 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 629 EVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPV 708
Cdd:PLN02766 325 KAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPV 404

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 709 MIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAAL 788
Cdd:PLN02766 405 MSLMKFK--TVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDAL 482


                 ....*....
gi 393195303 789 NEYLRVKTV 797
Cdd:PLN02766 483 DKYLQVKSV 491

BADH

TIGR01804

betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...

324-795

1.87e-162

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: 479.31 E-value: 1.87e-162

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  324 FIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRLADLMEQHQEELA 403
Cdd:TIGR01804   1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ--GEWAAMSPMERGRILRRAADLIRERNEELA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  404 TIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPInqarPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKT 483
Cdd:TIGR01804  79 KLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPL----GGPSFAYTIREPLGVCVGIGAWNYPLQIASWKI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  484 AACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAi 563
Cdd:TIGR01804 155 APALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAA- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  564 SNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDT 643
Cdd:TIGR01804 234 GHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEAT 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  644 DHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGdl 719
Cdd:TIGR01804 314 EMGPLISAAHRDKVLSYIEKGKAEGATLATGGGRPENVglqnGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDE-- 391

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 393195303  720 DAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVK 795
Cdd:TIGR01804 392 DEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467

FMT_core_FDH_N

cd08647

10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...

1-128

2.22e-85

10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family represents the N-terminal hydrolase domain of the bifunctional protein 10-formyltetrahydrofolate dehydrogenase (FDH). This domain contains a 10-formyl-tetrahydrofolate (10-formyl-THF) binding site and shares sequence homology and structural topology with other enzymes utilizing this substrate. This domain functions as a hydrolase, catalyzing the conversion of 10-formyl-THF, a precursor for nucleotide biosynthesis, to tetrahydrofolate (THF). The overall FDH reaction mechanism is a coupling of two sequential reactions, a hydrolase and a formyl dehydrogenase, bridged by a substrate transfer step. The N-terminal hydrolase domain removes the formyl group from 10-formyl-THF and the C-terminal NADP-dependent dehydrogenase domain then reduces the formyl group to carbon dioxide. The two catalytic domains are connected by a third intermediate linker domain that transfers the formyl group, covalently attached to the sulfhydryl group of the phosphopantetheine arm, from the N-terminal domain to the C-terminal domain.

Pssm-ID: 187716 [Multi-domain] Cd Length: 203 Bit Score: 269.70 E-value: 2.22e-85

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303   1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADPLGLEAEKDGVPVFKYSRWRAKGQALPDVVAKYQALGAEL 80
Cdd:cd08647    1 MKIAVIGQSLFGQEVYKELRKEGHEVVGVFTIPDKDGKADPLALEAEKDGVPVFKFPRWRAKGQAIPEVVAKYKALGAEL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 393195303  81 NVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAIhNW--IRGNDK 128
Cdd:cd08647   81 NVLPFCSQFIPMEVIDAPKHGSIIYHPSILPRHRGASAI-NWtlIHGDKK 129

FDH_Hydrolase_C

cd08703

The C-terminal subdomain of the hydrolase domain on the bi-functional protein ...

116-205

6.67e-42

Pssm-ID: 187731 [Multi-domain] Cd Length: 100 Bit Score: 147.88 E-value: 6.67e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 116 ASAIHNWIRGNDKVPGAWTEACEQKLTFFNSTLNTSGLVPEGdALPIPGAHRPGVVTKAGLILFGNDDKMLLVKNIQLED 195
Cdd:cd08703   12 AEALHNFIRGNDKVPGAWATIDGEQVTLFGSSLWKGGKPPGG-EVEVEGLERPGIVHKNGLLITGSDGKMVNVKRLQFED 90

                         90
                 ....*....|
gi 393195303 196 GKMILASNFF 205
Cdd:cd08703   91 GKMIPASKYG 100

Formyl_trans_N

pfam00551

Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...

1-132

2.71e-38

Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function.

Pssm-ID: 395436 [Multi-domain] Cd Length: 181 Bit Score: 140.50 E-value: 2.71e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303    1 MKIAVI--GQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADPLGLEAEKDGVPVFKYSRWRAKGQALPDVVAKYQALGA 78
Cdd:pfam00551   1 MKIAVLisGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 393195303   79 ELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAIHNWIRGNDKVPGA 132
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGV 134

Fmt

COG0223

Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];

1-120

1.37e-21

Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];

Pssm-ID: 439993 [Multi-domain] Cd Length: 308 Bit Score: 96.33 E-value: 1.37e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303   1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKD---GK---ADPLGLEAEKDGVPVFKYSRWRAkgqalPDVVAKYQ 74
Cdd:COG0223    1 MRIVFMGTPDFAVPSLEALLAAGHEVVAVVTQPDRPagrGRkltPSPVKELALEHGIPVLQPESLKD-----PEFLEELR 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 393195303  75 ALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAIH 120
Cdd:COG0223   76 ALNPDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQ 121

fmt

TIGR00460

methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...

1-131

1.88e-16

methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than methionyl-tRNA formyltransferase (fmt) itself are formyltetrahydrofolate dehydrogenases. The mitochondrial methionyl-tRNA formyltransferases are so divergent that, in a multiple alignment of bacterial fmt, mitochondrial fmt, and formyltetrahydrofolate dehydrogenases, the mitochondrial fmt appears the most different. However, because both bacterial and mitochondrial fmt are included in the seed alignment, all credible fmt sequences score higher than any non-fmt sequence. This enzyme modifies Met on initiator tRNA to f-Met. [Protein synthesis, tRNA aminoacylation]

Pssm-ID: 273088 [Multi-domain] Cd Length: 313 Bit Score: 80.91 E-value: 1.88e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303    1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDG------KADPLGLEAEKDGVPVFKYsrwraKGQALPDVVAKYQ 74
Cdd:TIGR00460   1 LRIVFFGTPTFSLPVLEELREDNFEVVGVVTQPDKPAgrgkklTPPPVKVLAEEKGIPVFQP-----EKQRQLEELPLVR 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 393195303   75 ALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAIHNWIRGNDKVPG 131
Cdd:TIGR00460  76 ELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTG 132

Formyl_trans_C

pfam02911

Formyl transferase, C-terminal domain;

116-208

6.20e-10

Formyl transferase, C-terminal domain;

Pssm-ID: 460744 [Multi-domain] Cd Length: 99 Bit Score: 56.90 E-value: 6.20e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  116 ASAIHNWIRGNDKVPGAWTEACEQKLTFFNSTLntsglvpegdaLPIPGAHRPG--VVTKAGLILFGNDDKMLLVKNIQL 193
Cdd:pfam02911  15 AEEIHRLIRALDPWPGAYTFLNGKRVKLLKASV-----------LDQESGAAPGtiVTVDKGGLLVACGDGALLILELQL 83

                          90
                  ....*....|....*
gi 393195303  194 EDGKMILASNFFKGA 208
Cdd:pfam02911  84 EGKKPMSAEDFLNGF 98

PLN02285

methionyl-tRNA formyltransferase

25-131

7.68e-06

methionyl-tRNA formyltransferase

Pssm-ID: 215159 [Multi-domain] Cd Length: 334 Bit Score: 48.92 E-value: 7.68e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  25 EVVGVFTVPDKDGK------ADPLGLEAEKDGVP---VFKYSRWRAkgqalPDVVAKYQALGAELNVLPFCSQFIPMEII 95
Cdd:PLN02285  37 EVAAVVTQPPARRGrgrklmPSPVAQLALDRGFPpdlIFTPEKAGE-----EDFLSALRELQPDLCITAAYGNILPQKFL 111

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 393195303  96 SAPRHGSIIYHPSLLPRHRGASAIHNWIRGNDKVPG 131
Cdd:PLN02285 112 DIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETG 147

Name

Accession

Description

Interval

E-value

ALDH_F1L_FTFDH

cd07140

10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ...

316-801

0e+00

Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 1009.72 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 316 TVRMPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLM 395
Cdd:cd07140    1 TLKMPHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 396 EQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQARPNRNLTLTRKEPVGVCGIIIPWNYP 475
Cdd:cd07140   81 EEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQARPNRNLTLTKREPIGVCGIVIPWNYP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 476 LMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGK 555
Cdd:cd07140  161 LMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 556 HIMKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKV 635
Cdd:cd07140  241 HIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKI 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 636 GNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFA 715
Cdd:cd07140  321 GDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFD 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 716 DGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVK 795
Cdd:cd07140  401 DGDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTK 480


                 ....*.
gi 393195303 796 TVTFEY 801
Cdd:cd07140  481 TVTIEY 486

ALDH_F1-2_Ald2-like

cd07091

ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...

319-799

0e+00

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: 779.08 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 319 MPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQH 398
Cdd:cd07091    2 QPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIERD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 399 QEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINqarpNRNLTLTRKEPVGVCGIIIPWNYPLMM 478
Cdd:cd07091   82 RDELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPID----GNFLAYTRREPIGVCGQIIPWNFPLLM 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 479 LSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIM 558
Cdd:cd07091  158 LAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIM 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 559 KSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNP 638
Cdd:cd07091  238 EAAAKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDP 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 639 LDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgD 718
Cdd:cd07091  318 FDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFK--T 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 719 LDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 798
Cdd:cd07091  396 EDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVT 475


                 .
gi 393195303 799 F 799
Cdd:cd07091  476 I 476

ALDH_F1AB_F2_RALDH1

cd07141

NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ...

321-798

0e+00

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: 620.90 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 321 HQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGR-WGKISARDRGRLMYRLADLMEQHQ 399
Cdd:cd07141    7 TKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSpWRTMDASERGRLLNKLADLIERDR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 400 EELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINqarpNRNLTLTRKEPVGVCGIIIPWNYPLMML 479
Cdd:cd07141   87 AYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMD----GDFFTYTRHEPVGVCGQIIPWNFPLLMA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 480 SWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMK 559
Cdd:cd07141  163 AWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQ 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 560 SCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPL 639
Cdd:cd07141  243 AAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPF 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 640 DRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDL 719
Cdd:cd07141  323 DPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFK--TI 400

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 393195303 720 DAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 798
Cdd:cd07141  401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVT 479

Aldedh

pfam00171

Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...

329-797

0e+00

Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 620.70 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  329 FVDAEGaKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEAL 408
Cdd:pfam00171   1 WVDSES-ETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP--AWRKTPAAERAAILRKAADLLEERKDELAELETL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  409 DAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPINQARpnrnLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLA 488
Cdd:pfam00171  78 ENGKPLAEA-RGEVDRAIDVLRYYAGLARRLDGETLPSDPGR----LAYTRREPLGVVGAITPWNFPLLLPAWKIAPALA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  489 AGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKK 568
Cdd:pfam00171 153 AGNTVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAA-QNLKR 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  569 VSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQ 648
Cdd:pfam00171 232 VTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPL 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  649 NHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANA 728
Cdd:pfam00171 312 ISKAQLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFK--DEEEAIEIAND 389

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  729 TEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDV-AAPFGGFKQSGFGKDLGEAALNEYLRVKTV 797
Cdd:pfam00171 390 TEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459

AdhE

COG1012

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...

320-801

0e+00

Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 604.04 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 320 PHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRLADLMEQHQ 399
Cdd:COG1012    5 EYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAF--PAWAATPPAERAAILLRAADLLEERR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 400 EELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPInqARPNRnLTLTRKEPVGVCGIIIPWNYPLMML 479
Cdd:COG1012   83 EELAALLTLETGKPLAEA-RGEVDRAADFLRYYAGEARRLYGETIPS--DAPGT-RAYVRREPLGVVGAITPWNFPLALA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 480 SWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMK 559
Cdd:COG1012  159 AWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 560 SCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPL 639
Cdd:COG1012  239 AAA-ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPL 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 640 DRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPR-PGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgD 718
Cdd:COG1012  318 DPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFD--D 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 719 LDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVA-APFGGFKQSGFGKDLGEAALNEYLRVKTV 797
Cdd:COG1012  396 EEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPqAPFGGVKQSGIGREGGREGLEEYTETKTV 475


                 ....
gi 393195303 798 TFEY 801
Cdd:COG1012  476 TIRL 479

ALDH

cd07078

NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ...

376-799

0e+00

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: 565.30 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 376 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTlALKTHVGMSIQTFRYFAGWCDKIQGSTIPINqarPNRNL 455
Cdd:cd07078   14 WAALPPAERAAILRKLADLLEERREELAALETLETGKPIE-EALGEVARAADTFRYYAGLARRLHGEVIPSP---DPGEL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 456 TLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQR 535
Cdd:cd07078   90 AIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAA 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 536 LSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVE 615
Cdd:cd07078  170 LASHPRVDKISFTGSTAVGKAIMRAAA-ENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVH 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 616 DSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPR-PGFFFEPTVFTDVE 694
Cdd:cd07078  249 ESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGgKGYFVPPTVLTDVD 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 695 DHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNK-TDVAAPFGG 773
Cdd:cd07078  329 PDMPIAQEEIFGPVLPVIPFK--DEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVgAEPSAPFGG 406

                        410       420
                 ....*....|....*....|....*.
gi 393195303 774 FKQSGFGKDLGEAALNEYLRVKTVTF 799
Cdd:cd07078  407 VKQSGIGREGGPYGLEEYTEPKTVTI 432

ALDH_ALD2-YMR170C

cd07144

Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ...

314-797

0e+00

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: 547.01 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 314 KRTVRMPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgRWGKISARDRGRLMYRLAD 393
Cdd:cd07144    1 GKSYDQPTGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFES-WWSKVTGEERGELLDKLAD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 394 LMEQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINqarpNRNLTLTRKEPVGVCGIIIPWN 473
Cdd:cd07144   80 LVEKNRDLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTS----PNKLAYTLHEPYGVCGQIIPWN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 474 YPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEV 553
Cdd:cd07144  156 YPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTAT 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 554 GKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRK- 632
Cdd:cd07144  236 GRLVMKAAA-QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQn 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 633 MKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGN---QVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVM 709
Cdd:cd07144  315 YKVGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEkapEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVV 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 710 IISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALN 789
Cdd:cd07144  395 VISKFK--TYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLE 472


                 ....*...
gi 393195303 790 EYLRVKTV 797
Cdd:cd07144  473 TYTQTKAV 480

ALDH_DhaS

cd07114

Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ...

340-799

0e+00

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: 544.07 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 340 TINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTlALK 419
Cdd:cd07114    1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIR-ETR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 420 THVGMSIQTFRYFAGWCDKIQGSTIPINqaRPNRnLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 499
Cdd:cd07114   80 AQVRYLAEWYRYYAGLADKIEGAVIPVD--KGDY-LNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 500 VTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKScAISNVKKVSLELGGKSPL 579
Cdd:cd07114  157 HTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARA-AAENLAPVTLELGGKSPN 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 580 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLME 659
Cdd:cd07114  236 IVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVER 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 660 YCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDlDAVlSRANATEFGLAS 735
Cdd:cd07114  316 YVARAREEGARVLTGGERPSGAdlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEE-EAI-ALANDSEYGLAA 393

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 393195303 736 GVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 799
Cdd:cd07114  394 GIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457

ALDH_BADH-GbsA

cd07119

Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ...

324-797

0e+00

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: 541.52 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 324 FIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEELA 403
Cdd:cd07119    1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 404 TIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPinqaRPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKT 483
Cdd:cd07119   81 RLETLNTGKTLRES-EIDIDDVANCFRYYAGLATKETGEVYD----VPPHVISRTVREPVGVCGLITPWNYPLLQAAWKL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 484 AACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAi 563
Cdd:cd07119  156 APALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAA- 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 564 SNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDT 643
Cdd:cd07119  235 GNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADT 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 644 DHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDl 719
Cdd:cd07119  315 EMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEE- 393

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 393195303 720 DAVlSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 797
Cdd:cd07119  394 EAI-RLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470

ALDH_GABALDH-PuuC

cd07112

Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ...

336-797

0e+00

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: 537.57 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 336 KTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYT 415
Cdd:cd07112    2 ETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPIS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 416 LALKTHVGMSIQTFRYFAGWCDKIQGSTIPInqarPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVI 495
Cdd:cd07112   82 DALAVDVPSAANTFRWYAEAIDKVYGEVAPT----GPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 496 KPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAISNVKKVSLELGG 575
Cdd:cd07112  158 KPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 576 KSPLIIFADC-DLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHL 654
Cdd:cd07112  238 KSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHF 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 655 VKLMEYCQHGVKEGATLVCGGNQV--PRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDlDAVlSRANATEFG 732
Cdd:cd07112  318 DKVLGYIESGKAEGARLVAGGKRVltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEE-EAV-ALANDSVYG 395

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 393195303 733 LASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 797
Cdd:cd07112  396 LAASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460

ALDH_F2BC

cd07142

Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ...

320-797

0e+00

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: 536.31 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 320 PHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQ 399
Cdd:cd07142    3 HTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYERSRILLRFADLLEKHA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 400 EELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQarPNRNLTLtrKEPVGVCGIIIPWNYPLMML 479
Cdd:cd07142   83 DELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADG--PHHVYTL--HEPIGVVGQIIPWNFPLLMF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 480 SWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMK 559
Cdd:cd07142  159 AWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQ 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 560 SCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPL 639
Cdd:cd07142  239 LAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPF 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 640 DRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDL 719
Cdd:cd07142  319 RKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFK--TV 396

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 393195303 720 DAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 797
Cdd:cd07142  397 DEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474

ALDH_AldA_AN0554

cd07143

Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ...

316-797

0e+00

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: 533.26 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 316 TVRMPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGrWG-KISARDRGRLMYRLADL 394
Cdd:cd07143    2 KYEQPTGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETD-WGlKVSGSKRGRCLSKLADL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 395 MEQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQARpnrnLTLTRKEPVGVCGIIIPWNY 474
Cdd:cd07143   81 MERNLDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKK----LTYTRHEPIGVCGQIIPWNF 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 475 PLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVG 554
Cdd:cd07143  157 PLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVG 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 555 KHIMKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMK 634
Cdd:cd07143  237 RKVMEAAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLK 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 635 VGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRF 714
Cdd:cd07143  317 VGDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKF 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 715 ADGdlDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRV 794
Cdd:cd07143  397 KTE--EEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQI 474


                 ...
gi 393195303 795 KTV 797
Cdd:cd07143  475 KAV 477

ALDH_HMSADH_HapE

cd07115

Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ...

340-797

0e+00

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: 527.78 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 340 TINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALK 419
Cdd:cd07115    1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEA--WSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 420 THVGMSIQTFRYFAGWCDKIQGSTIPInqaRPnRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 499
Cdd:cd07115   79 LDVPRAADTFRYYAGWADKIEGEVIPV---RG-PFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 500 VTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPL 579
Cdd:cd07115  155 LTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA-GNLKRVSLELGGKSAN 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 580 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLME 659
Cdd:cd07115  234 IVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLD 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 660 YCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFadGDLDAVLSRANATEFGLASGVFT 739
Cdd:cd07115  314 YVDVGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRF--RDEEEALRIANGTEYGLAAGVWT 391

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 393195303 740 RDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 797
Cdd:cd07115  392 RDLGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSV 449

ALDH_F5_SSADH_GabD

cd07103

Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ...

341-799

8.41e-178

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: 518.14 E-value: 8.41e-178

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 341 INPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlKT 420
Cdd:cd07103    2 INPATGEVIGEVPDAGAADADAAIDAAAAAFK--TWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA-RG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 421 HVGMSIQTFRYFAGWCDKIQGSTIPinQARPNRNLtLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQV 500
Cdd:cd07103   79 EVDYAASFLEWFAEEARRIYGRTIP--SPAPGKRI-LVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 501 TPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLI 580
Cdd:cd07103  156 TPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAA-DTVKRVSLELGGNAPFI 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 581 IFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEY 660
Cdd:cd07103  235 VFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEAL 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 661 CQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTR 740
Cdd:cd07103  315 VEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFD--TEDEVIARANDTPYGLAAYVFTR 392

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 393195303 741 DINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 799
Cdd:cd07103  393 DLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451

PLN02766

coniferyl-aldehyde dehydrogenase

313-797

1.17e-176

coniferyl-aldehyde dehydrogenase

Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 517.07 E-value: 1.17e-176

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 313 NKRTVRMPH----QLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLM 388
Cdd:PLN02766   9 GASGVKVPEikftKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFERGRIM 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 389 YRLADLMEQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPInqARPNRNLTLtrKEPVGVCGI 468
Cdd:PLN02766  89 MKFADLIEEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKM--SRQLQGYTL--KEPIGVVGH 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 469 IIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFT 548
Cdd:PLN02766 165 IIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFT 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 549 GSTEVGKHIMKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVE 628
Cdd:PLN02766 245 GSTEVGRKIMQAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVE 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 629 EVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPV 708
Cdd:PLN02766 325 KAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPV 404

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 709 MIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAAL 788
Cdd:PLN02766 405 MSLMKFK--TVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDAL 482


                 ....*....
gi 393195303 789 NEYLRVKTV 797
Cdd:PLN02766 483 DKYLQVKSV 491

ALDH_F8_HMSADH

cd07093

Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ...

340-798

2.87e-172

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: 504.02 E-value: 2.87e-172

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 340 TINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALK 419
Cdd:cd07093    1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFP--GWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLART 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 420 THVGMSIQTFRYFAGWCDKIQGSTIPinqaRPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 499
Cdd:cd07093   79 RDIPRAAANFRFFADYILQLDGESYP----QDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 500 VTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPL 579
Cdd:cd07093  155 WTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAA-PNLKPVSLELGGKNPN 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 580 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLME 659
Cdd:cd07093  234 IVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLG 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 660 YCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGdlDAVLSRANATEFGLAS 735
Cdd:cd07093  314 YVELARAEGATILTGGGRPELPdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDE--EEAIELANDTPYGLAA 391

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 393195303 736 GVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 798
Cdd:cd07093  392 YVWTRDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVC 454

ALDH_F9_TMBADH

cd07090

NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ...

340-797

4.99e-169

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: 495.67 E-value: 4.99e-169

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 340 TINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlK 419
Cdd:cd07090    1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQK--EWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEA-R 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 420 THVGMSIQTFRYFAGWCDKIQGSTIPInqarPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 499
Cdd:cd07090   78 VDIDSSADCLEYYAGLAPTLSGEHVPL----PGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSP 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 500 VTPLTALKFAELTLKAGIPKGVVNVLPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPL 579
Cdd:cd07090  154 FTPLTALLLAEILTEAGLPDGVFNVVQGGGE-TGQLLCEHPDVAKVSFTGSVPTGKKVMSAAA-KGIKHVTLELGGKSPL 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 580 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLME 659
Cdd:cd07090  232 IIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLG 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 660 YCQHGVKEGATLVCGGNQVP-----RPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLA 734
Cdd:cd07090  312 YIESAKQEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFD--TEEEVIRRANDTTYGLA 389

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 393195303 735 SGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 797
Cdd:cd07090  390 AGVFTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452

PLN02466

aldehyde dehydrogenase family 2 member

322-797

4.23e-168

aldehyde dehydrogenase family 2 member

Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 496.64 E-value: 4.23e-168

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 322 QLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEE 401
Cdd:PLN02466  59 QLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRILLRFADLLEKHNDE 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 402 LATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQarPNRNLTLtrKEPVGVCGIIIPWNYPLMMLSW 481
Cdd:PLN02466 139 LAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADG--PHHVQTL--HEPIGVAGQIIPWNFPLLMFAW 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 482 KTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSC 561
Cdd:PLN02466 215 KVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELA 294

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 562 AISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDR 641
Cdd:PLN02466 295 AKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKK 374

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 642 DTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDA 721
Cdd:PLN02466 375 GVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFK--DLDE 452

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 393195303 722 VLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 797
Cdd:PLN02466 453 VIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAV 528

BADH

TIGR01804

betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...

324-795

1.87e-162

Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 479.31 E-value: 1.87e-162

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  324 FIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRLADLMEQHQEELA 403
Cdd:TIGR01804   1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ--GEWAAMSPMERGRILRRAADLIRERNEELA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  404 TIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPInqarPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKT 483
Cdd:TIGR01804  79 KLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPL----GGPSFAYTIREPLGVCVGIGAWNYPLQIASWKI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  484 AACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAi 563
Cdd:TIGR01804 155 APALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAA- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  564 SNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDT 643
Cdd:TIGR01804 234 GHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEAT 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  644 DHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGdl 719
Cdd:TIGR01804 314 EMGPLISAAHRDKVLSYIEKGKAEGATLATGGGRPENVglqnGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDE-- 391

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 393195303  720 DAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVK 795
Cdd:TIGR01804 392 DEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467

PRK13252

betaine aldehyde dehydrogenase; Provisional

318-797

1.16e-158

betaine aldehyde dehydrogenase; Provisional

Pssm-ID: 183918 Cd Length: 488 Bit Score: 470.52 E-value: 1.16e-158

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 318 RMP-HQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLME 396
Cdd:PRK13252   3 RQPlQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQK--IWAAMTAMERSRILRRAVDILR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 397 QHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQArpnrNLTLTRKEPVGVCGIIIPWNYPL 476
Cdd:PRK13252  81 ERNDELAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGG----SFVYTRREPLGVCAGIGAWNYPI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 477 MMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKH 556
Cdd:PRK13252 157 QIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKK 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 557 IMKSCAISnVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVG 636
Cdd:PRK13252 236 VMAAAAAS-LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIG 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 637 NPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPR----PGFFFEPTVFTDVEDHMFIAKEESFGPVMIIS 712
Cdd:PRK13252 315 DPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVL 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 713 RFADGdlDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYL 792
Cdd:PRK13252 395 TFDDE--DEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYT 472


                 ....*
gi 393195303 793 RVKTV 797
Cdd:PRK13252 473 QIKSV 477

ALDH_CddD_SSP0762

cd07138

Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ...

323-799

4.36e-156

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: 462.74 E-value: 4.36e-156

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 323 LFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEEL 402
Cdd:cd07138    1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFP--AWSATSVEERAALLERIAEAYEARADEL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 403 ATIEALDAGAVYTLALKTHVGMSIQTFRYFAGwcdkiQGSTIPINQARPNrnlTLTRKEPVGVCGIIIPWNYPLMMLSWK 482
Cdd:cd07138   79 AQAITLEMGAPITLARAAQVGLGIGHLRAAAD-----ALKDFEFEERRGN---SLVVREPIGVCGLITPWNWPLNQIVLK 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 483 TAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKScA 562
Cdd:cd07138  151 VAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEA-A 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 563 ISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRD 642
Cdd:cd07138  230 ADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPA 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 643 TDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPR---PGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDl 719
Cdd:cd07138  310 TTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPGRPEgleRGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDED- 388

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 720 DAVlSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNtYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 799
Cdd:cd07138  389 EAI-AIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQG 466

ALDH_SNDH

cd07118

Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ...

371-799

1.03e-155

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: 461.42 E-value: 1.03e-155

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 371 FENGRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIpiNQAR 450
Cdd:cd07118   32 FDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQA-RGEIEGAADLWRYAASLARTLHGDSY--NNLG 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 451 PNRnLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGS 530
Cdd:cd07118  109 DDM-LGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGA 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 531 LVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAG 610
Cdd:cd07118  188 TVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAA-RNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGS 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 611 RLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVP-RPGFFFEPTV 689
Cdd:cd07118  267 RLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLAsAAGLFYQPTI 346

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 690 FTDVEDHMFIAKEESFGPVMIISRFadGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAA 769
Cdd:cd07118  347 FTDVTPDMAIAREEIFGPVLSVLTF--DTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSPEL 424

                        410       420       430
                 ....*....|....*....|....*....|
gi 393195303 770 PFGGFKQSGFGKDLGEAALNEYLRVKTVTF 799
Cdd:cd07118  425 PFGGFKQSGIGRELGRYGVEEYTELKTVHL 454

ALDH_AAS00426

cd07109

Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ...

341-799

1.26e-152

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: 453.61 E-value: 1.26e-152

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 341 INPTDGSVICQVSLAQVTDVDKAVAAAKDAFEnGRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlKT 420
Cdd:cd07109    2 FDPSTGEVFARIARGGAADVDRAVQAARRAFE-SGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQA-RA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 421 HVGMSIQTFRYFAGWCDKIQGSTIPINQArpnrNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQV 500
Cdd:cd07109   80 DVEAAARYFEYYGGAADKLHGETIPLGPG----YFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAED 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 501 TPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLI 580
Cdd:cd07109  156 APLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAA-ENVVPVTLELGGKSPQI 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 581 IFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDrDTDHGPQNHHAHLVKLMEY 660
Cdd:cd07109  235 VFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGF 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 661 CQHGVKEGATLVCGGNQV---PRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFadGDLDAVLSRANATEFGLASGV 737
Cdd:cd07109  314 VARARARGARIVAGGRIAegaPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPF--DDEAEAIALANGTDYGLVAGV 391

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 393195303 738 FTRDINKALYVSDKLQAGTVFVNTYNKT-DVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 799
Cdd:cd07109  392 WTRDGDRALRVARRLRAGQVFVNNYGAGgGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454

ALDH-SF

cd06534

NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...

376-799

3.22e-152

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: 449.37 E-value: 3.22e-152

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 376 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALkTHVGMSIQTFRYFAGWCDKIQGSTIPINqarPNRNL 455
Cdd:cd06534   10 WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEAL-GEVARAIDTFRYAAGLADKLGGPELPSP---DPGGE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 456 TLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQR 535
Cdd:cd06534   86 AYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 536 LSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVE 615
Cdd:cd06534  166 LLSHPRVDKISFTGSTAVGKAIMKAAA-ENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVH 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 616 DSIHDEFVRRVVeevrkmkvgnpldrdtdhgpqnhhahlvklmeycqhgvkegatlvcggnqvprpgfffepTVFTDVED 695
Cdd:cd06534  245 ESIYDEFVEKLV------------------------------------------------------------TVLVDVDP 264

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 696 HMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNK-TDVAAPFGGF 774
Cdd:cd06534  265 DMPIAQEEIFGPVLPVIRFK--DEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGPEAPFGGV 342

                        410       420
                 ....*....|....*....|....*
gi 393195303 775 KQSGFGKDLGEAALNEYLRVKTVTF 799
Cdd:cd06534  343 KNSGIGREGGPYGLEEYTRTKTVVI 367

PRK13473

aminobutyraldehyde dehydrogenase;

319-799

9.29e-151

aminobutyraldehyde dehydrogenase;

Pssm-ID: 237391 Cd Length: 475 Bit Score: 449.75 E-value: 9.29e-151

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 319 MPHQLFIGGEFVDAEGAkTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQH 398
Cdd:PRK13473   1 MQTKLLINGELVAGEGE-KQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFP--EWSQTTPKERAEALLKLADAIEEN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 399 QEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQG-----------STIpinqarpnrnltltRKEPVGVCG 467
Cdd:PRK13473  78 ADEFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGkaageyleghtSMI--------------RRDPVGVVA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 468 IIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAgIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGF 547
Cdd:PRK13473 144 SIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSL 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 548 TGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVV 627
Cdd:PRK13473 223 TGSIATGKHVLSAAA-DSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLA 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 628 EEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEG-ATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFG 706
Cdd:PRK13473 302 AAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFG 381

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 707 PVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEA 786
Cdd:PRK13473 382 PVVSVTPFD--DEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLY 459

                        490
                 ....*....|...
gi 393195303 787 ALNEYLRVKTVTF 799
Cdd:PRK13473 460 GLEDYTVVRHVMV 472

ALDH_KGSADH-YcbD

cd07097

Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ...

324-797

4.92e-150

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: 447.85 E-value: 4.92e-150

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 324 FIGGEFVdaEGAKTSETINPTDGS-VICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEEL 402
Cdd:cd07097    4 YIDGEWV--AGGDGEENRNPSDTSdVVGKYARASAEDADAAIAAAAAAFPA--WRRTSPEARADILDKAGDELEARKEEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 403 ATIEALDAGAvyTLAL-KTHVGMSIQTFRYFAGWCDKIQGSTIPinQARPNRNLTlTRKEPVGVCGIIIPWNYPLMMLSW 481
Cdd:cd07097   80 ARLLTREEGK--TLPEaRGEVTRAGQIFRYYAGEALRLSGETLP--STRPGVEVE-TTREPLGVVGLITPWNFPIAIPAW 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 482 KTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSc 561
Cdd:cd07097  155 KIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAA- 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 562 AISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDR 641
Cdd:cd07097  234 AAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDE 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 642 DTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP--GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDL 719
Cdd:cd07097  314 GVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVR--DY 391

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 720 DAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN-TYNKTDVAAPFGGFKQSGFG-KDLGEAALNEYLRVKTV 797
Cdd:cd07097  392 DEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlPTAGVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471

ALDH_AldA-Rv0768

cd07139

Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ...

323-799

5.40e-150

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: 447.41 E-value: 5.40e-150

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 323 LFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEEL 402
Cdd:cd07139    1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSPAERAAVLRRLADALEARADEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 403 ATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWcdkiqGSTIPINQARP--NRNLTLTRKEPVGVCGIIIPWNYPLMMLS 480
Cdd:cd07139   81 ARLWTAENGMPISWSRRAQGPGPAALLRYYAAL-----ARDFPFEERRPgsGGGHVLVRREPVGVVAAIVPWNAPLFLAA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 481 WKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGsGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKS 560
Cdd:cd07139  156 LKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAV 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 561 CAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLD 640
Cdd:cd07139  235 CG-ERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLD 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 641 RDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP--GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGD 718
Cdd:cd07139  314 PATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGLdrGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDED 393

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 719 lDAVlSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYnKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 798
Cdd:cd07139  394 -DAV-RIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIY 470


                 .
gi 393195303 799 F 799
Cdd:cd07139  471 L 471

ALDH_ABALDH-YdcW

cd07092

Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ...

341-799

6.76e-149

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: 444.08 E-value: 6.76e-149

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 341 INPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWgkISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALKT 420
Cdd:cd07092    2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRR--TTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 421 HVGMSIQTFRYFAGWCDKIQGSTIpiNQARPNRnLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQV 500
Cdd:cd07092   80 ELPGAVDNFRFFAGAARTLEGPAA--GEYLPGH-TSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSET 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 501 TPLTALKFAELtLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKScAISNVKKVSLELGGKSPLI 580
Cdd:cd07092  157 TPLTTLLLAEL-AAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARA-AADTLKRVHLELGGKAPVI 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 581 IFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEY 660
Cdd:cd07092  235 VFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGF 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 661 CQhGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTR 740
Cdd:cd07092  315 VE-RAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFD--DEDEAIELANDVEYGLASSVWTR 391

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 393195303 741 DINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 799
Cdd:cd07092  392 DVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450

ALDH_LactADH-AldA

cd07088

Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ...

324-797

3.94e-146

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: 437.47 E-value: 3.94e-146

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 324 FIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEELA 403
Cdd:cd07088    1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKA--WERLPAIERAAYLRKLADLIRENADELA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 404 TIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPinQARPNRNLTLtRKEPVGVCGIIIPWNYPLMMLSWKT 483
Cdd:cd07088   79 KLIVEEQGKTLSLA-RVEVEFTADYIDYMAEWARRIEGEIIP--SDRPNENIFI-FKVPIGVVAGILPWNFPFFLIARKL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 484 AACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAi 563
Cdd:cd07088  155 APALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAA- 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 564 SNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDT 643
Cdd:cd07088  234 ENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAAT 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 644 DHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVP-RPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAV 722
Cdd:cd07088  314 DMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFS--SLDEA 391

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 393195303 723 LSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 797
Cdd:cd07088  392 IELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVV 466

ALDH_ACDHII_AcoD-like

cd07559

Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ...

321-801

4.54e-146

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: 437.93 E-value: 4.54e-146

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 321 HQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQE 400
Cdd:cd07559    1 YDNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFK--TWGKTSVAERANILNKIADRIEENLE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 401 ELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQarpnRNLTLTRKEPVGVCGIIIPWNYPLMMLS 480
Cdd:cd07559   79 LLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDE----DTLSYHFHEPLGVVGQIIPWNFPLLMAA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 481 WKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAgIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKS 560
Cdd:cd07559  155 WKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQY 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 561 cAISNVKKVSLELGGKSPLIIFAD-----CDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKV 635
Cdd:cd07559  234 -AAENLIPVTLELGGKSPNIFFDDamdadDDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKV 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 636 GNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMII 711
Cdd:cd07559  313 GNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLAV 392

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 712 SRFADgdLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEY 791
Cdd:cd07559  393 ITFKD--EEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHY 470

                        490
                 ....*....|
gi 393195303 792 LRVKTVTFEY 801
Cdd:cd07559  471 QQTKNILVSY 480

ALDH_F16

cd07111

Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ...

323-793

1.37e-143

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: 431.43 E-value: 1.37e-143

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 323 LFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEEL 402
Cdd:cd07111   24 HFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES--WSALPGHVRARHLYRIARHIQKHQRLF 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 403 ATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQgstipinQARPNRnltltrkEPVGVCGIIIPWNYPLMMLSWK 482
Cdd:cd07111  102 AVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLD-------TELAGW-------KPVGVVGQIVPWNFPLLMLAWK 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 483 TAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLvGQRLSDHPDVRKIGFTGSTEVGKHIMKSCA 562
Cdd:cd07111  168 ICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATA 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 563 ISnVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRD 642
Cdd:cd07111  247 GT-GKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKA 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 643 TDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAV 722
Cdd:cd07111  326 IDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFR--TAKEA 403

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 393195303 723 LSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLR 793
Cdd:cd07111  404 VALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLR 474

ALDH_CddD-AldA-like

cd07089

Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ...

341-799

3.04e-143

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: 429.74 E-value: 3.04e-143

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 341 INPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWgKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALKT 420
Cdd:cd07089    2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDW-STDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 421 HVGMSIQTFRYFAGWCDKIQGS-TIPINQARPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 499
Cdd:cd07089   81 QVDGPIGHLRYFADLADSFPWEfDLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 500 VTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPL 579
Cdd:cd07089  161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAA-ATLKRVLLELGGKSAN 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 580 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLME 659
Cdd:cd07089  240 IVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEG 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 660 YCQHGVKEGATLVCGGNQVPR--PGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFaDGDLDAVlSRANATEFGLASGV 737
Cdd:cd07089  320 YIARGRDEGARLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPY-DDDDEAV-RIANDSDYGLSGGV 397

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 393195303 738 FTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 799
Cdd:cd07089  398 WSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459

PLN02278

succinic semialdehyde dehydrogenase

322-797

1.55e-142

succinic semialdehyde dehydrogenase

Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 429.50 E-value: 1.55e-142

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 322 QLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEE 401
Cdd:PLN02278  26 QGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPS--WSKLTASERSKILRRWYDLIIANKED 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 402 LATIEALDAGAVYTLALkTHVGMSIQTFRYFAGWCDKIQGSTIPINQarPNRNLtLTRKEPVGVCGIIIPWNYPLMMLSW 481
Cdd:PLN02278 104 LAQLMTLEQGKPLKEAI-GEVAYGASFLEYFAEEAKRVYGDIIPSPF--PDRRL-LVLKQPVGVVGAITPWNFPLAMITR 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 482 KTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSC 561
Cdd:PLN02278 180 KVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGA 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 562 AiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDR 641
Cdd:PLN02278 260 A-ATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEE 338

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 642 DTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADgDLDA 721
Cdd:PLN02278 339 GVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKT-EEEA 417

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 393195303 722 VLSrANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 797
Cdd:PLN02278 418 IAI-ANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492

ALDH_F10_BADH

cd07110

Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ...

340-798

4.26e-140

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: 421.37 E-value: 4.26e-140

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 340 TINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALk 419
Cdd:cd07110    1 VINPATEATIGEIPAATAEDVDAAVRAARRAFP--RWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAA- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 420 THVGMSIQTFRYFAGWCDKIQgstipinqARPNRNLTL--------TRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGN 491
Cdd:cd07110   78 WDVDDVAGCFEYYADLAEQLD--------AKAERAVPLpsedfkarVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGC 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 492 TVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSL 571
Cdd:cd07110  150 TVVLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAA-QDIKPVSL 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 572 ELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHH 651
Cdd:cd07110  229 ELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQ 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 652 AHLVKLMEYCQHGVKEGATLVCGGN--QVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDlDAVLSrANAT 729
Cdd:cd07110  309 AQYEKVLSFIARGKEEGARLLCGGRrpAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATED-EAIAL-ANDS 386

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 393195303 730 EFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 798
Cdd:cd07110  387 EYGLAAAVISRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455

ALDH_MGR_2402

cd07108

Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ...

374-798

6.23e-139

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: 418.69 E-value: 6.23e-139

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 374 GRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAvytlALKTH----VGMSIQTFRYFAGWCDKIQGSTIPinqA 449
Cdd:cd07108   33 PEWAATPARERGKLLARIADALEARSEELARLLALETGN----ALRTQarpeAAVLADLFRYFGGLAGELKGETLP---F 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 450 RPNRnLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGVVNVLPGSG 529
Cdd:cd07108  106 GPDV-LTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEI-LAQVLPAGVLNVITGYG 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 530 SLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQ---MGMSsvFFNKGENC 606
Cdd:cd07108  184 EECGAALVDHPDVDKVTFTGSTEVGKIIYRAAA-DRLIPVSLELGGKSPMIVFPDADLDDAVDgaiAGMR--FTRQGQSC 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 607 IAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKE-GATLVCGGNQVP----RP 681
Cdd:cd07108  261 TAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLGLSTsGATVLRGGPLPGegplAD 340

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 682 GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNT 761
Cdd:cd07108  341 GFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWK--DEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQ 418

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 393195303 762 YNKTDVAAPFGGFKQSGFGKDLG-EAALNEYLRVKTVT 798
Cdd:cd07108  419 GGGQQPGQSYGGFKQSGLGREASlEGMLEHFTQKKTVN 456

ALDH_PADH_NahF

cd07113

Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ...

323-801

1.01e-138

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: 418.77 E-value: 1.01e-138

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 323 LFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEnGRWGKISARDRGRLMYRLADLMEQHQEEL 402
Cdd:cd07113    2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV-SAWAKTTPAERGRILLRLADLIEQHGEEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 403 ATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQARPN--RNLTLTRKEPVGVCGIIIPWNYPLMMLS 480
Cdd:cd07113   81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLAPSIPSMQgeRYTAFTRREPVGVVAGIVPWNFSVMIAV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 481 WKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMKS 560
Cdd:cd07113  161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIGRQ 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 561 cAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLD 640
Cdd:cd07113  240 -AASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 641 RDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPT--VFTDVEDHMFiaKEESFGPVMIISRFADGd 718
Cdd:cd07113  319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTlvLARSADSRLM--REETFGPVVSFVPYEDE- 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 719 lDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 798
Cdd:cd07113  396 -EELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVM 474


                 ...
gi 393195303 799 FEY 801
Cdd:cd07113  475 IRY 477

ALDH_StaphAldA1

cd07117

Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ...

321-797

1.43e-135

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: 410.69 E-value: 1.43e-135

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 321 HQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQE 400
Cdd:cd07117    1 YGLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT--WRKTTVAERANILNKIADIIDENKE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 401 ELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQarpnRNLTLTRKEPVGVCGIIIPWNYPLMMLS 480
Cdd:cd07117   79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDE----DTLSIVLREPIGVVGQIIPWNFPFLMAA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 481 WKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKS 560
Cdd:cd07117  155 WKLAPALAAGNTVVIKPSSTTSLSLLELAKI-IQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 561 CAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLD 640
Cdd:cd07117  234 AA-KKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLD 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 641 RDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAd 716
Cdd:cd07117  313 PDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFK- 391

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 717 gDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKT 796
Cdd:cd07117  392 -TEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKN 470


                 .
gi 393195303 797 V 797
Cdd:cd07117  471 I 471

ALDH_AldH-CAJ73105

cd07131

Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ...

324-801

3.33e-135

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: 409.81 E-value: 3.33e-135

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 324 FIGGEFVDAEGAKTSETINPTDGS-VICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRLADLMEQHQEEL 402
Cdd:cd07131    2 YIGGEWVDSASGETFDSRNPADLEeVVGTFPLSTASDVDAAVEAAREAF--PEWRKVPAPRRAEYLFRAAELLKKRKEEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 403 ATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPinQARPNRNLtLTRKEPVGVCGIIIPWNYPLMMLSWK 482
Cdd:cd07131   80 ARLVTREMGKPLAEG-RGDVQEAIDMAQYAAGEGRRLFGETVP--SELPNKDA-MTRRQPIGVVALITPWNFPVAIPSWK 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 483 TAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCA 562
Cdd:cd07131  156 IFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCA 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 563 ISNvKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRD 642
Cdd:cd07131  236 RPN-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEE 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 643 TDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPR----PGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFadGD 718
Cdd:cd07131  315 TDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEV--SS 392

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 719 LDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNtyNKT---DVAAPFGGFKQSGFG-KDLGEAALNEYLRV 794
Cdd:cd07131  393 LEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVN--APTigaEVHLPFGGVKKSGNGhREAGTTALDAFTEW 470


                 ....*..
gi 393195303 795 KTVTFEY 801
Cdd:cd07131  471 KAVYVDY 477

ALDH_AldA-AAD23400

cd07106

Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ...

376-799

1.32e-134

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: 406.91 E-value: 1.32e-134

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 376 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGwcdkiqgSTIP--INQARPNR 453
Cdd:cd07106   35 WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEA-QFEVGGAVAWLRYTAS-------LDLPdeVIEDDDTR 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 454 NLTLTRKePVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGVVNVLPGSGSLvG 533
Cdd:cd07106  107 RVELRRK-PLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGEL-AQEVLPPGVLNVVSGGDEL-G 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 534 QRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAV-QMGMSSvFFNKGENCIAAGRL 612
Cdd:cd07106  184 PALTSHPDIRKISFTGSTATGKKVMASAA-KTLKRVTLELGGNDAAIVLPDVDIDAVApKLFWGA-FINSGQVCAAIKRL 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 613 FVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTD 692
Cdd:cd07106  262 YVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKGAKVLAGGEPLDGPGYFIPPTIVDD 341

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 693 VEDHMFIAKEESFGPVMIISRFadGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFG 772
Cdd:cd07106  342 PPEGSRIVDEEQFGPVLPVLKY--SDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWINTHGALDPDAPFG 419

                        410       420
                 ....*....|....*....|....*..
gi 393195303 773 GFKQSGFGKDLGEAALNEYLRVKTVTF 799
Cdd:cd07106  420 GHKQSGIGVEFGIEGLKEYTQTQVINI 446

ALDH_PhdK-like

cd07107

Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ...

340-798

1.61e-134

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: 407.15 E-value: 1.61e-134

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 340 TINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTlALK 419
Cdd:cd07107    1 VINPATGQVLARVPAASAADVDRAVAAARAAFPE--WRATTPLERARMLRELATRLREHAEELALIDALDCGNPVS-AML 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 420 THVGMSIQTFRYFAGWCDKIQGSTIPInqarPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 499
Cdd:cd07107   78 GDVMVAAALLDYFAGLVTELKGETIPV----GGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 500 VTPLTALKFAELtLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPL 579
Cdd:cd07107  154 QAPLSALRLAEL-AREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAA-EGIKHVTLELGGKNAL 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 580 IIFADCDLNKAVQ---MGMSsvFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVK 656
Cdd:cd07107  232 IVFPDADPEAAADaavAGMN--FTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDR 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 657 LMEYCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADgdLDAVLSRANATEFG 732
Cdd:cd07107  310 VMHYIDSAKREGARLVTGGGRPEGPalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRD--EAEMVAQANGVEYG 387

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 393195303 733 LASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 798
Cdd:cd07107  388 LTAAIWTNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVN 453

PRK09847

gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional

322-797

8.30e-134

gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional

Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 406.59 E-value: 8.30e-134

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 322 QLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEE 401
Cdd:PRK09847  21 RLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGDWSLSSPAKRKAVLNKLADLMEAHAEE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 402 LATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINqarpNRNLTLTRKEPVGVCGIIIPWNYPLMMLSW 481
Cdd:PRK09847 101 LALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTS----SHELAMIVREPVGVIAAIVPWNFPLLLTCW 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 482 KTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSC 561
Cdd:PRK09847 177 KLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDA 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 562 AISNVKKVSLELGGKSPLIIFADC-DLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLD 640
Cdd:PRK09847 257 GDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLD 336

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 641 RDTDHGPQNHHAHLVKLMEYCQHGVKEGaTLVCGGNQVPRPGfFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdGDLD 720
Cdd:PRK09847 337 PATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAA-AIGPTIFVDVDPNASLSREEIFGPVLVVTRFT-SEEQ 413

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 393195303 721 AvLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 797
Cdd:PRK09847 414 A-LQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489

ALDH_y4uC

cd07149

Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ...

339-799

5.08e-133

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: 403.13 E-value: 5.08e-133

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 339 ETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRwgKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAL 418
Cdd:cd07149    2 EVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMK--SLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 419 KtHVGMSIQTFRYFAGWCDKIQGSTIPINQARPNRN-LTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKP 497
Cdd:cd07149   80 K-EVDRAIETLRLSAEEAKRLAGETIPFDASPGGEGrIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 498 AQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHImksCAISNVKKVSLELGGKS 577
Cdd:cd07149  159 ASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAI---ARKAGLKKVTLELGSNA 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 578 PLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKL 657
Cdd:cd07149  236 AVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERI 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 658 MEYCQHGVKEGATLVCGGNqvpRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGV 737
Cdd:cd07149  316 EEWVEEAVEGGARLLTGGK---RDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFD--TLDEAIAMANDSPYGLQAGV 390

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 393195303 738 FTRDINKALYVSDKLQAGTVFVN---TYnKTDvAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 799
Cdd:cd07149  391 FTNDLQKALKAARELEVGGVMINdssTF-RVD-HMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453

ALDH_VaniDH_like

cd07150

Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ...

342-798

5.74e-129

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: 392.46 E-value: 5.74e-129

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 342 NPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAL-KT 420
Cdd:cd07150    5 NPADGSVYARVAVGSRQDAERAIAAAYDAFPA--WAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWfET 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 421 HVGMSIqtFRYFAGWCDKIQGSTIPinQARPNRnLTLTRKEPVGVCGIIIPWNYPLMmLSWKTAA-CLAAGNTVVIKPAQ 499
Cdd:cd07150   83 TFTPEL--LRAAAGECRRVRGETLP--SDSPGT-VSMSVRRPLGVVAGITPFNYPLI-LATKKVAfALAAGNTVVLKPSE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 500 VTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPL 579
Cdd:cd07150  157 ETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAG-RHLKKITLELGGKNPL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 580 IIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLME 659
Cdd:cd07150  236 IVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKR 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 660 YCQHGVKEGATLVCGGNqvpRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADgDLDAvLSRANATEFGLASGVFT 739
Cdd:cd07150  316 QVEDAVAKGAKLLTGGK---YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKD-AEEA-LELANDTEYGLSAAILT 390

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 740 RDINKALYVSDKLQAGTVFVNTYNKTDVA-APFGGFKQSGFGKDLGEAALNEYLRVKTVT 798
Cdd:cd07150  391 NDLQRAFKLAERLESGMVHINDPTILDEAhVPFGGVKASGFGREGGEWSMEEFTELKWIT 450

ALDH_BenzADH-like

cd07104

ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ...

376-798

4.34e-128

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: 389.58 E-value: 4.34e-128

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 376 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYtlaLKTH--VGMSIQTFRYFAGWCDKIQGSTIPinQARPNR 453
Cdd:cd07104   16 WAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTR---PKAAfeVGAAIAILREAAGLPRRPEGEILP--SDVPGK 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 454 nLTLTRKEPVGVCGIIIPWNYPLMmLSWKTAA-CLAAGNTVVIKPAQVTPLT-ALKFAELTLKAGIPKGVVNVLPGSGSL 531
Cdd:cd07104   91 -ESMVRRVPLGVVGVISPFNFPLI-LAMRSVApALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVLNVVPGGGSE 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 532 VGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGR 611
Cdd:cd07104  169 IGDALVEHPRVRMISFTGSTAVGRHIGELAG-RHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGR 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 612 LFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGnqvPRPGFFFEPTVFT 691
Cdd:cd07104  248 ILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGG---TYEGLFYQPTVLS 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 692 DVEDHMFIAKEESFGPVMIISRFADgDLDAVlSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN--TYNKtDVAA 769
Cdd:cd07104  325 DVTPDMPIFREEIFGPVAPVIPFDD-DEEAV-ELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINdqTVND-EPHV 401

                        410       420
                 ....*....|....*....|....*....
gi 393195303 770 PFGGFKQSGFGKDLGEAALNEYLRVKTVT 798
Cdd:cd07104  402 PFGGVKASGGGRFGGPASLEEFTEWQWIT 430

ALDH_LactADH_F420-Bios

cd07145

Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ...

339-797

7.36e-128

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: 389.79 E-value: 7.36e-128

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 339 ETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAl 418
Cdd:cd07145    2 EVRNPANGEVIDTVPSLSREEVREAIEVAEKAKD--VMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 419 KTHVGMSIQTFRYFAGWCDKIQGSTIPINQARPNRN-LTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKP 497
Cdd:cd07145   79 RVEVERTIRLFKLAAEEAKVLRGETIPVDAYEYNERrIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 498 AQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKScAISNVKKVSLELGGKS 577
Cdd:cd07145  159 SSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASK-AGGTGKKVALELGGSD 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 578 PLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKL 657
Cdd:cd07145  238 PMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERM 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 658 MEYCQHGVKEGATLVCGGNQVprPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDlDAVlSRANATEFGLASGV 737
Cdd:cd07145  318 ENLVNDAVEKGGKILYGGKRD--EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDE-EAV-EIANSTEYGLQASV 393

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 393195303 738 FTRDINKALYVSDKLQAGTVFVN--TYNKTDvAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 797
Cdd:cd07145  394 FTNDINRALKVARELEAGGVVINdsTRFRWD-NLPFGGFKKSGIGREGVRYTMLEMTEEKTI 454

PLN02467

betaine aldehyde dehydrogenase

322-798

2.07e-126

betaine aldehyde dehydrogenase

Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 387.94 E-value: 2.07e-126

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 322 QLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGR---WGKISARDRGRLMYRLADLMEQH 398
Cdd:PLN02467   9 QLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRNKgkdWARTTGAVRAKYLRAIAAKITER 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 399 QEELATIEALDAGAVYTLALKTHVGMSiQTFRYFAGWCDKIQGS-----TIPINQARPNrnltlTRKEPVGVCGIIIPWN 473
Cdd:PLN02467  89 KSELAKLETLDCGKPLDEAAWDMDDVA-GCFEYYADLAEALDAKqkapvSLPMETFKGY-----VLKEPLGVVGLITPWN 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 474 YPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEV 553
Cdd:PLN02467 163 YPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTAT 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 554 GKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKM 633
Cdd:PLN02467 243 GRKIMTAAA-QMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNI 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 634 KVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGN--QVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMII 711
Cdd:PLN02467 322 KISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKrpEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCV 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 712 SRFADGdlDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEY 791
Cdd:PLN02467 402 KTFSTE--DEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENY 479


                 ....*..
gi 393195303 792 LRVKTVT 798
Cdd:PLN02467 480 LSVKQVT 486

ALDH_PsfA-ACA09737

cd07120

Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ...

340-798

9.18e-121

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: 371.29 E-value: 9.18e-121

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 340 TINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWgKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlK 419
Cdd:cd07120    1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDETDW-AHDPRLRARVLLELADAFEANAERLARLLALENGKILGEA-R 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 420 THVGMSIQTFRYFAGWCDKIQGSTIpinQARPNrNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ 499
Cdd:cd07120   79 FEISGAISELRYYAGLARTEAGRMI---EPEPG-SFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 500 VTPLTALKFAELTLKA-GIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSP 578
Cdd:cd07120  155 QTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAA-PTLKRLGLELGGKTP 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 579 LIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLM 658
Cdd:cd07120  234 CIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVD 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 659 EYCQHGVKEGATLVCGGNQVPR---PGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDlDAVlSRANATEFGLAS 735
Cdd:cd07120  314 RMVERAIAAGAEVVLRGGPVTEglaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEA-EAV-ALANDTDYGLAA 391

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 393195303 736 GVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 798
Cdd:cd07120  392 SVWTRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454

gabD

PRK11241

NADP-dependent succinate-semialdehyde dehydrogenase I;

321-795

5.07e-118

NADP-dependent succinate-semialdehyde dehydrogenase I;

Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 365.38 E-value: 5.07e-118

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 321 HQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQE 400
Cdd:PRK11241  11 QQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALP--AWRALTAKERANILRRWFNLMMEHQD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 401 ELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPINQarPNRNLtLTRKEPVGVCGIIIPWNYPLMMLS 480
Cdd:PRK11241  89 DLARLMTLEQGKPLAEA-KGEISYAASFIEWFAEEGKRIYGDTIPGHQ--ADKRL-IVIKQPIGVTAAITPWNFPAAMIT 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 481 WKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKS 560
Cdd:PRK11241 165 RKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQ 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 561 CAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLD 640
Cdd:PRK11241 245 CA-KDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLE 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 641 RDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFadGDLD 720
Cdd:PRK11241 324 KGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRF--KDEA 401

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 393195303 721 AVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVK 795
Cdd:PRK11241 402 DVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476

ALDH_F7_AASADH-like

cd07086

NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ...

324-801

9.17e-118

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: 364.58 E-value: 9.17e-118

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 324 FIGGEFVDAeGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRLADLMEQHQEELA 403
Cdd:cd07086    2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAF--KEWRKVPAPRRGEIVRQIGEALRKKKEALG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 404 TIEALDAGAVYTLALkTHVGMSIQTFRYFAGWCDKIQGSTIPinQARPNRNLtLTRKEPVGVCGIIIPWNYPLMMLSWKT 483
Cdd:cd07086   79 RLVSLEMGKILPEGL-GEVQEMIDICDYAVGLSRMLYGLTIP--SERPGHRL-MEQWNPLGVVGVITAFNFPVAVPGWNA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 484 AACLAAGNTVVIKPAQVTPLTALKFAELTLKA----GIPKGVVNVLPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMK 559
Cdd:cd07086  155 AIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGE 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 560 SCAISNvKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPL 639
Cdd:cd07086  234 TVARRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPL 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 640 DRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPR--PGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFadG 717
Cdd:cd07086  313 DEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKF--D 390

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 718 DLDAVLSRANATEFGLASGVFTRDINKAL-YVSDK-LQAGTVFVNT-YNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRV 794
Cdd:cd07086  391 SLEEAIAINNDVPQGLSSSIFTEDLREAFrWLGPKgSDCGIVNVNIpTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRR 470


                 ....*..
gi 393195303 795 KTVTFEY 801
Cdd:cd07086  471 STCTINY 477

ALDH_SSADH1_GabD1

cd07100

Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ...

376-797

3.00e-115

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: 356.00 E-value: 3.00e-115

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 376 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAgwcDKI----QGSTIPINQARp 451
Cdd:cd07100   15 WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA-RAEVEKCAWICRYYA---ENAeaflADEPIETDAGK- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 452 nrnlTLTRKEPVGVCGIIIPWNYPLmmlsWKT----AACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPG 527
Cdd:cd07100   90 ----AYVRYEPLGVVLGIMPWNFPF----WQVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLLI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 528 SGSLVGQrLSDHPDVRKIGFTGSTEVGKHImKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCI 607
Cdd:cd07100  162 DSDQVEA-IIADPRVRGVTLTGSERAGRAV-AAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 608 AAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEP 687
Cdd:cd07100  240 AAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFYPP 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 688 TVFTDVEDHMFIAKEESFGPVMIISRFADGDlDAV-LsrANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTD 766
Cdd:cd07100  320 TVLTDVTPGMPAYDEELFGPVAAVIKVKDEE-EAIaL--ANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSD 396

                        410       420       430
                 ....*....|....*....|....*....|.
gi 393195303 767 VAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 797
Cdd:cd07100  397 PRLPFGGVKRSGYGRELGRFGIREFVNIKTV 427

ALDH_F21_LactADH-like

cd07094

ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ...

339-799

2.64e-112

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: 349.42 E-value: 2.64e-112

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 339 ETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAL 418
Cdd:cd07094    2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAEN--RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 419 KtHVGMSIQTFRYFAGWCDKIQGSTIP--INQARPNRnLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIK 496
Cdd:cd07094   80 V-EVDRAIDTLRLAAEEAERIRGEEIPldATQGSDNR-LAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 497 PAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMkscAISNVKKVSLELGGK 576
Cdd:cd07094  158 PASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALR---ANAGGKRIALELGGN 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 577 SPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVK 656
Cdd:cd07094  235 APVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAER 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 657 LMEYCQHGVKEGATLVCGGNqvpRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASG 736
Cdd:cd07094  315 VERWVEEAVEAGARLLCGGE---RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYD--DFEEAIRIANSTDYGLQAG 389

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 393195303 737 VFTRDINKALYVSDKLQAGTVFVN--TYNKTDvAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 799
Cdd:cd07094  390 IFTRDLNVAFKAAEKLEVGGVMVNdsSAFRTD-WMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453

ALDH_ACDHII-AcoD

cd07116

Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ...

324-801

9.65e-112

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: 348.67 E-value: 9.65e-112

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 324 FIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELA 403
Cdd:cd07116    4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKE--AWGKTSVAERANILNKIADRMEANLEMLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 404 TIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINqarpNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKT 483
Cdd:cd07116   82 VAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEID----ENTVAYHFHEPLGVVGQIIPWNFPLLMATWKL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 484 AACLAAGNTVVIKPAQVTPLTALKFAELTLKAgIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKScAI 563
Cdd:cd07116  158 APALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQY-AS 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 564 SNVKKVSLELGGKSPLIIFADC----D--LNKAVQmGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGN 637
Cdd:cd07116  236 ENIIPVTLELGGKSPNIFFADVmdadDafFDKALE-GFVMFALNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGN 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 638 PLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDvEDHMFIAKEESFGPVMIISR 713
Cdd:cd07116  315 PLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGgllgGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTT 393

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 714 FAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLR 793
Cdd:cd07116  394 FK--DEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQ 471


                 ....*...
gi 393195303 794 VKTVTFEY 801
Cdd:cd07116  472 TKNLLVSY 479

ALDH_HBenzADH

cd07151

NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ...

327-798

3.14e-108

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: 339.28 E-value: 3.14e-108

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 327 GEFVDAEGAKTSETINPTDGSVICQVSLAqvTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEELATIE 406
Cdd:cd07151    1 GEWRDGTSERTIDVLNPYTGETLAEIPAA--SKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 407 ALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPIN-QARPNRnltlTRKEPVGVCGIIIPWNYPLMMLSWKTAA 485
Cdd:cd07151   79 IRESGSTRIKA-NIEWGAAMAITREAATFPLRMEGRILPSDvPGKENR----VYREPLGVVGVISPWNFPLHLSMRSVAP 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 486 CLAAGNTVVIKPAQVTPLTA-LKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiS 564
Cdd:cd07151  154 ALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAG-R 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 565 NVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTD 644
Cdd:cd07151  233 HLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTV 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 645 HGPQNHHAHLVKLMEYCQHGVKEGATLVCGGnqvPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFaDGDLDAVlS 724
Cdd:cd07151  313 VGPLINESQVDGLLDKIEQAVEEGATLLVGG---EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKA-DDEEEAL-E 387

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 393195303 725 RANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVA-APFGGFKQSGFGKDLGEAALNEYLRVKTVT 798
Cdd:cd07151  388 LANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPhVPFGGEKNSGLGRFNGEWALEEFTTDKWIS 462

ALDH_PutA-P5CDH-RocA

cd07124

Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ...

323-798

5.58e-107

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: 337.66 E-value: 5.58e-107

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 323 LFIGGEFVDAEGakTSETINPTDGS-VICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEE 401
Cdd:cd07124   35 LVIGGKEVRTEE--KIESRNPADPSeVLGTVQKATKEEAEAAVQAARAAFPT--WRRTPPEERARLLLRAAALLRRRRFE 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 402 LATIEALDAGAVYTLALkTHVGMSIQTFRYFAGWCDKIQGStiPINQARPNRNLTltRKEPVGVCGIIIPWNYPLMMLSW 481
Cdd:cd07124  111 LAAWMVLEVGKNWAEAD-ADVAEAIDFLEYYAREMLRLRGF--PVEMVPGEDNRY--VYRPLGVGAVISPWNFPLAILAG 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 482 KTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSC 561
Cdd:cd07124  186 MTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERA 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 562 A-----ISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVG 636
Cdd:cd07124  266 AkvqpgQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVG 345

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 637 NPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGaTLVCGGNqVPRP---GFFFEPTVFTDVEDHMFIAKEESFGPVMIISR 713
Cdd:cd07124  346 DPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGE-VLELaaeGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIK 423

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 714 FAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGtvfvNTY-NKTDVAA-----PFGGFKQSGFG-KDLGEA 786
Cdd:cd07124  424 AK--DFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVG----NLYaNRKITGAlvgrqPFGGFKMSGTGsKAGGPD 497

                        490
                 ....*....|..
gi 393195303 787 ALNEYLRVKTVT 798
Cdd:cd07124  498 YLLQFMQPKTVT 509

ALDH_DDALDH

cd07099

Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ...

376-798

3.83e-106

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: 333.42 E-value: 3.83e-106

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 376 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALkTHVGMSIQTFRYFAGWCDKI-QGSTIPINQARPNRN 454
Cdd:cd07099   34 WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAG-LEVLLALEAIDWAARNAPRVlAPRKVPTGLLMPNKK 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 455 LTLTRkEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSlVGQ 534
Cdd:cd07099  113 ATVEY-RPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGA-TGA 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 535 RLSDHPdVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFV 614
Cdd:cd07099  191 ALIDAG-VDKVAFTGSVATGRKVMAAAA-ERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYV 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 615 EDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVE 694
Cdd:cd07099  269 HESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVP 348

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 695 DHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN--TYNKTDVAAPFG 772
Cdd:cd07099  349 HDMDVMREETFGPVLPVMPVA--DEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINdvLLTAGIPALPFG 426

                        410       420
                 ....*....|....*....|....*.
gi 393195303 773 GFKQSGFGKDLGEAALNEYLRVKTVT 798
Cdd:cd07099  427 GVKDSGGGRRHGAEGLREFCRPKAIA 452

PRK10090

aldehyde dehydrogenase A; Provisional

388-801

1.98e-103

aldehyde dehydrogenase A; Provisional

Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 324.77 E-value: 1.98e-103

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 388 MYRLADLMEQHQEELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPINqaRPNRNLtLTRKEPVGVCG 467
Cdd:PRK10090   1 LRKIAAGIRERASEISALIVEEGGKIQQLA-EVEVAFTADYIDYMAEWARRYEGEIIQSD--RPGENI-LLFKRALGVTT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 468 IIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGF 547
Cdd:PRK10090  77 GILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSM 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 548 TGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVV 627
Cdd:PRK10090 157 TGSVSAGEKIMAAAA-KNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLG 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 628 EEVRKMKVGNPLDRDT-DHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFG 706
Cdd:PRK10090 236 EAMQAVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFG 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 707 PVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEA 786
Cdd:PRK10090 316 PVLPVVAFD--TLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKH 393

                        410
                 ....*....|....*
gi 393195303 787 ALNEYLRVKTVTFEY 801
Cdd:PRK10090 394 GLHEYLQTQVVYLQS 408

ALDH_F6_MMSDH

cd07085

Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ...

322-798

4.57e-103

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: 326.01 E-value: 4.57e-103

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 322 QLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEE 401
Cdd:cd07085    2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFP--AWSATPVLKRQQVMFKFRQLLEENLDE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 402 LATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPinQARPNRNlTLTRKEPVGVCGIIIPWNYPLMMLSW 481
Cdd:cd07085   80 LARLITLEHGKTLADA-RGDVLRGLEVVEFACSIPHLLKGEYLE--NVARGID-TYSYRQPLGVVAGITPFNFPAMIPLW 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 482 KTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVgQRLSDHPDVRKIGFTGSTEVGKHIMKSc 561
Cdd:cd07085  156 MFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAV-NALLDHPDIKAVSFVGSTPVGEYIYER- 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 562 AISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDR 641
Cdd:cd07085  234 AAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDP 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 642 DTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRfADg 717
Cdd:cd07085  314 GADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPgyenGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVR-VD- 391

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 718 DLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNtynkTDVAAP-----FGGFKQSGFGkDL---GEAALN 789
Cdd:cd07085  392 TLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN----VPIPVPlaffsFGGWKGSFFG-DLhfyGKDGVR 466


                 ....*....
gi 393195303 790 EYLRVKTVT 798
Cdd:cd07085  467 FYTQTKTVT 475

ALDH_F21_RNP123

cd07147

Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ...

339-795

6.77e-103

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: 324.58 E-value: 6.77e-103

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 339 ETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRwgKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAl 418
Cdd:cd07147    2 EVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMR--ALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDA- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 419 KTHVGMSIQTFRYFAGWCDKIQGSTIPIN-QARPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKP 497
Cdd:cd07147   79 RGEVARAIDTFRIAAEEATRIYGEVLPLDiSARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 498 AQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLvGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAisnVKKVSLELGGKS 577
Cdd:cd07147  159 ASRTPLSALILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVGWDLKARAG---KKKVVLELGGNA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 578 PLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKL 657
Cdd:cd07147  235 AVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERV 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 658 MEYCQHGVKEGATLVCGGNqvpRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGV 737
Cdd:cd07147  315 EGWVNEAVDAGAKLLTGGK---RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYD--DFDEALAAVNDSKFGLQAGV 389

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 393195303 738 FTRDINKALYVSDKLQAGTVFVNtynktDV------AAPFGGFKQSGFGKDLGEAALNEYLRVK 795
Cdd:cd07147  390 FTRDLEKALRAWDELEVGGVVIN-----DVptfrvdHMPYGGVKDSGIGREGVRYAIEEMTEPR 448

ALDH_SSADH2_GabD2

cd07101

Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ...

375-798

2.09e-100

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: 318.48 E-value: 2.09e-100

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 375 RWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALK--THVGMsiqTFRYFAGWCDKI-----QGSTIPIn 447
Cdd:cd07101   33 AWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEevLDVAI---VARYYARRAERLlkprrRRGAIPV- 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 448 qarpnrnLTLTR--KEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVL 525
Cdd:cd07101  109 -------LTRTTvnRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVV 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 526 PGSGSLVGQRLSDHPDVrkIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGEN 605
Cdd:cd07101  182 TGPGSEVGGAIVDNADY--VMFTGSTATGRVVAERAG-RRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQL 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 606 CIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPG-FF 684
Cdd:cd07101  259 CVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLAGGRARPDLGpYF 338

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 685 FEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDlDAVlSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN---- 760
Cdd:cd07101  339 YEPTVLTGVTEDMELFAEETFGPVVSIYRVADDD-EAI-ELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNegya 416

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 393195303 761 -TYNKTDvaAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 798
Cdd:cd07101  417 aAWASID--APMGGMKDSGLGRRHGAEGLLKYTETQTVA 453

ALDH_SaliADH

cd07105

Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ...

376-799

2.31e-99

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: 314.90 E-value: 2.31e-99

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 376 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTIPinQARPNRnL 455
Cdd:cd07105   16 WSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWA-GFNVDLAAGMLREAASLITQIIGGSIP--SDKPGT-L 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 456 TLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVL---PGSGSLV 532
Cdd:cd07105   92 AMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVthsPEDAPEV 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 533 GQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRL 612
Cdd:cd07105  172 VEALIAHPAVRKVNFTGSTRVGRIIAETAA-KHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERI 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 613 FVEDSIHDEFVRRVVEEVRKMKVGnpldrDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRP-GFFFEPTVFT 691
Cdd:cd07105  251 IVHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADESPsGTSMPPTILD 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 692 DVEDHMFIAKEESFGPVMIISRFADgDLDAVlSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVA-AP 770
Cdd:cd07105  326 NVTPDMDIYSEESFGPVVSIIRVKD-EEEAV-RIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVHDEPtLP 403

                        410       420
                 ....*....|....*....|....*....
gi 393195303 771 FGGFKQSGFGKDLGEAALNEYLRVKTVTF 799
Cdd:cd07105  404 HGGVKSSGYGRFNGKWGIDEFTETKWITI 432

D1pyr5carbox2

TIGR01237

delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ...

323-798

1.77e-97

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: 312.57 E-value: 1.77e-97

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  323 LFIGGEFVDAEGAKTSetINPTDGS-VICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEE 401
Cdd:TIGR01237  35 LVINGERVETENKIVS--INPCDKSeVVGTVSKASQEHAEHALQAAAKAFEA--WKKTDPEERAAILFKAAAIVRRRRHE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  402 LATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKIQGSTiPINQARPNRNLTLTrkEPVGVCGIIIPWNYPLMMLSW 481
Cdd:TIGR01237 111 FSALLVKEVGKPWNEA-DAEVAEAIDFMEYYARQMIELAKGK-PVNSREGETNQYVY--TPTGVTVVISPWNFPFAIMVG 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  482 KTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSC 561
Cdd:TIGR01237 187 MTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERA 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  562 AI-----SNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVG 636
Cdd:TIGR01237 267 AKvqpgqKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVG 346

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  637 NPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGaTLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAd 716
Cdd:TIGR01237 347 PPDSADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRAS- 424

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  717 gDLDAVLSRANATEFGLASGVFTRD---INKAlyvSDKLQAGTVFvntYNKTDVAA-----PFGGFKQSGFG-KDLGEAA 787
Cdd:TIGR01237 425 -DFDEALEIANNTEYGLTGGVISNNrdhINRA---KAEFEVGNLY---FNRNITGAivgyqPFGGFKMSGTDsKAGGPDY 497

                         490
                  ....*....|.
gi 393195303  788 LNEYLRVKTVT 798
Cdd:TIGR01237 498 LALFMQAKTVT 508

gabD2

PRK09407

succinic semialdehyde dehydrogenase; Reviewed

375-798

2.42e-96

succinic semialdehyde dehydrogenase; Reviewed

Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 309.89 E-value: 2.42e-96

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 375 RWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALK--THVGMsiqTFRYFAGWCDKI-----QGSTIPIn 447
Cdd:PRK09407  69 AWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEevLDVAL---TARYYARRAPKLlaprrRAGALPV- 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 448 qarpnrnLTLTR--KEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVL 525
Cdd:PRK09407 145 -------LTKTTelRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVV 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 526 PGSGSLVGQRLSDHPDVrkIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGEN 605
Cdd:PRK09407 218 TGPGPVVGTALVDNADY--LMFTGSTATGRVLAEQAG-RRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQL 294

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 606 CIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGnqVPRPG--- 682
Cdd:PRK09407 295 CISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGG--KARPDlgp 372

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 683 FFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN-- 760
Cdd:PRK09407 373 LFYEPTVLTGVTPDMELAREETFGPVVSVYPVA--DVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNeg 450

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 393195303 761 ---TYNKTDvaAPFGGFKQSGFGKDLGEAALNEYLRVKTVT 798
Cdd:PRK09407 451 yaaAWGSVD--APMGGMKDSGLGRRHGAEGLLKYTESQTIA 489

ALDH_BenzADH

cd07152

NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ...

376-787

5.57e-95

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: 303.83 E-value: 5.57e-95

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 376 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVytlALKTH--VGMSIQTFRYFAGWCDKIQGSTIPINQARpnr 453
Cdd:cd07152   29 WAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSI---RPKAGfeVGAAIGELHEAAGLPTQPQGEILPSAPGR--- 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 454 nLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTA-LKFAELTLKAGIPKGVVNVLPGsGSLV 532
Cdd:cd07152  103 -LSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARLFEEAGLPAGVLHVLPG-GADA 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 533 GQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRL 612
Cdd:cd07152  181 GEALVEDPNVAMISFTGSTAVGRKVGEAAG-RHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRH 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 613 FVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNqvpRPGFFFEPTVFTD 692
Cdd:cd07152  260 LVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGT---YDGLFYRPTVLSG 336

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 693 VEDHMFIAKEESFGPVMIISRFADGDLDAVLsrANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN--TYNKtDVAAP 770
Cdd:cd07152  337 VKPGMPAFDEEIFGPVAPVTVFDSDEEAVAL--ANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINdqTVND-EPHNP 413

                        410
                 ....*....|....*..
gi 393195303 771 FGGFKQSGFGKDLGEAA 787
Cdd:cd07152  414 FGGMGASGNGSRFGGPA 430

ALDH_F11_NP-GAPDH

cd07082

NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ...

324-780

6.04e-95

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: 304.49 E-value: 6.04e-95

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 324 FIGGEFVDAEGaKTSETINPTDGSVICQVSLaqvTDVDKAVAAAKDAFENGRWGK--ISARDRGRLMYRLADLMEQHQEE 401
Cdd:cd07082    5 LINGEWKESSG-KTIEVYSPIDGEVIGSVPA---LSALEILEAAETAYDAGRGWWptMPLEERIDCLHKFADLLKENKEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 402 LATIEALDAGAVYTLALKtHVGMSIQTFRYFAGWCDKIQGSTIPINQARPNRN-LTLTRKEPVGVCGIIIPWNYPLMMLS 480
Cdd:cd07082   81 VANLLMWEIGKTLKDALK-EVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKGkIAQVRREPLGVVLAIGPFNYPLNLTV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 481 WKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKs 560
Cdd:cd07082  160 SKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK- 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 561 caISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLD 640
Cdd:cd07082  239 --QHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWD 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 641 RDTDHGP---QNHHAHLVKLMEycqHGVKEGATLVCGGNQvpRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdg 717
Cdd:cd07082  317 NGVDITPlidPKSADFVEGLID---DAVAKGATVLNGGGR--EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVN-- 389

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 393195303 718 DLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNK--TDVaAPFGGFKQSGFG 780
Cdd:cd07082  390 DIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQrgPDH-FPFLGRKDSGIG 453

PRK03137

1-pyrroline-5-carboxylate dehydrogenase; Provisional

323-778

3.00e-94

1-pyrroline-5-carboxylate dehydrogenase; Provisional

Pssm-ID: 179543 Cd Length: 514 Bit Score: 304.16 E-value: 3.00e-94

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 323 LFIGGEFVDAEGAKTSetINPTDGS-VICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEE 401
Cdd:PRK03137  39 LIIGGERITTEDKIVS--INPANKSeVVGRVSKATKELAEKAMQAALEAFET--WKKWSPEDRARILLRAAAIIRRRKHE 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 402 LATIEALDAGAVYTLAlKTHVGMSIQTFRYFAGWCDKI-QGStiPINQaRPNRNLTLtRKEPVGVCGIIIPWNYPLMMLS 480
Cdd:PRK03137 115 FSAWLVKEAGKPWAEA-DADTAEAIDFLEYYARQMLKLaDGK--PVES-RPGEHNRY-FYIPLGVGVVISPWNFPFAIMA 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 481 WKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKS 560
Cdd:PRK03137 190 GMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYER 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 561 CAISN-----VKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKV 635
Cdd:PRK03137 270 AAKVQpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTV 349

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 636 GNPLDrDTDHGPQNHHAHLVKLMEYCQHGVKEGaTLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFA 715
Cdd:PRK03137 350 GNPED-NAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAK 427

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 393195303 716 dgDLDAVLSRANATEFGLASGVFTRD---INKA--------LYVSDKLQAGTVFVNtynktdvaaPFGGFKQSG 778
Cdd:PRK03137 428 --DFDHALEIANNTEYGLTGAVISNNrehLEKArrefhvgnLYFNRGCTGAIVGYH---------PFGGFNMSG 490

ALDH_F15-22

cd07098

Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ...

376-799

2.56e-92

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: 297.29 E-value: 2.56e-92

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 376 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGavytlalKTHVGMS---IQTFryfagwCDKIQ-----GSTIPIN 447
Cdd:cd07098   34 WAKTSFAERRKVLRSLLKYILENQEEICRVACRDTG-------KTMVDASlgeILVT------CEKIRwtlkhGEKALRP 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 448 QARPNRNLTLTRK-----EPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKA----GIP 518
Cdd:cd07098  101 ESRPGGLLMFYKRarveyEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIREClaacGHD 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 519 KGVVNVLPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMKsCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSV 598
Cdd:cd07098  181 PDLVQLVTCLPE-TAEALTSHPVIDHITFIGSPPVGKKVMA-AAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGT 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 599 FFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQV 678
Cdd:cd07098  259 FQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRY 338

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 679 PRP----GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADgDLDAVlSRANATEFGLASGVFTRDINKALYVSDKLQA 754
Cdd:cd07098  339 PHPeypqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASD-DEEAV-EIANSTEYGLGASVFGKDIKRARRIASQLET 416

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 393195303 755 GTVFVNTYNKT--DVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 799
Cdd:cd07098  417 GMVAINDFGVNyyVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTE 463

ALDH_PhpJ

cd07146

Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ...

339-798

1.27e-91

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: 295.04 E-value: 1.27e-91

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 339 ETINPTDGSVIcqvslAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGavytLAL 418
Cdd:cd07146    2 EVRNPYTGEVV-----GTVPAGTEEALREALALAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESG----LCL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 419 KT---HVGMSIQTFRYFAGWCDKIQGSTIPINQARP-NRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVV 494
Cdd:cd07146   73 KDtryEVGRAADVLRFAAAEALRDDGESFSCDLTANgKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 495 IKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHImksCAISNVKKVSLELG 574
Cdd:cd07146  153 LKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAI---AATAGYKRQLLELG 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 575 GKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHL 654
Cdd:cd07146  230 GNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAA 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 655 VKLMEYCQHGVKEGATLVCGGNqvpRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLA 734
Cdd:cd07146  310 IQIENRVEEAIAQGARVLLGNQ---RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVK--DLDEAIAISNSTAYGLS 384

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 393195303 735 SGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVA-APFGGFKQSGFGKDLG-EAALNEYLRVKTVT 798
Cdd:cd07146  385 SGVCTNDLDTIKRLVERLDVGTVNVNEVPGFRSElSPFGGVKDSGLGGKEGvREAMKEMTNVKTYS 450

FMT_core_FDH_N

cd08647

10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ...

1-128

2.22e-85

Pssm-ID: 187716 [Multi-domain] Cd Length: 203 Bit Score: 269.70 E-value: 2.22e-85

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303   1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADPLGLEAEKDGVPVFKYSRWRAKGQALPDVVAKYQALGAEL 80
Cdd:cd08647    1 MKIAVIGQSLFGQEVYKELRKEGHEVVGVFTIPDKDGKADPLALEAEKDGVPVFKFPRWRAKGQAIPEVVAKYKALGAEL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 393195303  81 NVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAIhNW--IRGNDK 128
Cdd:cd08647   81 NVLPFCSQFIPMEVIDAPKHGSIIYHPSILPRHRGASAI-NWtlIHGDKK 129

ALDH_EDX86601

cd07102

Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ...

341-799

2.25e-85

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: 278.75 E-value: 2.25e-85

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 341 INPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALKT 420
Cdd:cd07102    1 ISPIDGSVIAERPLASLEAVRAALERARAAQK--GWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 421 HVGMsIQTFRYFAGWCDKIQGSTIPINQARPNRNLtltRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQV 500
Cdd:cd07102   79 IRGM-LERARYMISIAEEALADIRVPEKDGFERYI---RREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQ 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 501 TPLTALKFAELTLKAGIPKGVVNVLPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLI 580
Cdd:cd07102  155 TPLCGERFAAAFAEAGLPEGVFQVLHLSHE-TSAALIADPRIDHVSFTGSVAGGRAIQRAAA-GRFIKVGLELGGKDPAY 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 581 IFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEY 660
Cdd:cd07102  233 VRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQ 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 661 CQHGVKEGATLVCGGNQVPRP---GFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADgDLDAVLsRANATEFGLASGV 737
Cdd:cd07102  313 IADAIAKGARALIDGALFPEDkagGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKS-DAEAIA-LMNDSEYGLTASV 390

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 393195303 738 FTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF 799
Cdd:cd07102  391 WTKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSYHL 452

gabD1

PRK09406

succinic semialdehyde dehydrogenase; Reviewed

340-797

1.79e-83

succinic semialdehyde dehydrogenase; Reviewed

Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 273.92 E-value: 1.79e-83

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 340 TINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRwgKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlK 419
Cdd:PRK09406   5 TINPATGETVKTFTALTDDEVDAAIARAHARFRDYR--TTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASA-K 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 420 THVGMSIQTFRYFAGWCDKIQGSTiPINQARPNRNLTLTRKEPVGVCGIIIPWNYPLmmlsWKT----AACLAAGNTVVI 495
Cdd:PRK09406  82 AEALKCAKGFRYYAEHAEALLADE-PADAAAVGASRAYVRYQPLGVVLAVMPWNFPL----WQVvrfaAPALMAGNVGLL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 496 KPAQVTPLTALKFAELTLKAGIPKGV-VNVLPGSGSlVGQRLSDhPDVRKIGFTGSTEVGKHImKSCAISNVKKVSLELG 574
Cdd:PRK09406 157 KHASNVPQTALYLADLFRRAGFPDGCfQTLLVGSGA-VEAILRD-PRVAAATLTGSEPAGRAV-AAIAGDEIKKTVLELG 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 575 GKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHL 654
Cdd:PRK09406 234 GSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGR 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 655 VKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLA 734
Cdd:PRK09406 314 DEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVA--DIDEAIEIANATTFGLG 391

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 393195303 735 SGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 797
Cdd:PRK09406 392 SNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454

ALDH_PutA-P5CDH

cd07125

Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ...

323-780

7.19e-79

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: 263.29 E-value: 7.19e-79

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 323 LFIGGEFVDAEGAktsETINPTDG-SVICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRLADLMEQHQEE 401
Cdd:cd07125   36 IINGEETETGEGA---PVIDPADHeRTIGEVSLADAEDVDAALAIAAAAF--AGWSATPVEERAEILEKAADLLEANRGE 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 402 LATIEALDAGAvyTLAlKTHVGMS--IQTFRYFAGWCDKIQGSTIPINQARPNRNLTLtrkEPVGVCGIIIPWNYPLMML 479
Cdd:cd07125  111 LIALAAAEAGK--TLA-DADAEVReaIDFCRYYAAQARELFSDPELPGPTGELNGLEL---HGRGVFVCISPWNFPLAIF 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 480 SWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMK 559
Cdd:cd07125  185 TGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINR 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 560 SCAISNVKKVSL--ELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGN 637
Cdd:cd07125  265 ALAERDGPILPLiaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGD 344

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 638 PLDRDTDHGP-------QNHHAHlVKLMEycqhgvKEgATLVCggnQVPRP---GFFFEPTVFTDVEDhmFIAKEESFGP 707
Cdd:cd07125  345 PWDLSTDVGPlidkpagKLLRAH-TELMR------GE-AWLIA---PAPLDdgnGYFVAPGIIEIVGI--FDLTTEVFGP 411

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 393195303 708 VMIISRFADGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGtvfvNTY-NKTDVAA-----PFGGFKQSGFG 780
Cdd:cd07125  412 ILHVIRFKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAG----NLYiNRNITGAivgrqPFGGWGLSGTG 486

ALDH_P5CDH

cd07083

ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ...

315-798

2.79e-74

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: 250.57 E-value: 2.79e-74

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 315 RTVRMPH-QLFIGGEFVDAEGAKTSetINPTD-GSVICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRLA 392
Cdd:cd07083   12 KEEFGRAyPLVIGGEWVDTKERMVS--VSPFApSEVVGTTAKADKAEAEAALEAAWAAF--KTWKDWPQEDRARLLLKAA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 393 DLMEQHQEELATIEALDAGAVYTLALKThVGMSIQTFRYFAGWCDKIQGSTIPINQARPNRNLTLTRKEPVGVCgiIIPW 472
Cdd:cd07083   88 DLLRRRRRELIATLTYEVGKNWVEAIDD-VAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNESFYVGLGAGVV--ISPW 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 473 NYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTE 552
Cdd:cd07083  165 NFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLE 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 553 VGKHIMKSCA-----ISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVV 627
Cdd:cd07083  245 TGKKIYEAAArlapgQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLL 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 628 EEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGaTLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGP 707
Cdd:cd07083  325 KRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGP 403

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 708 VMIISRFADGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAA--PFGGFKQSGFG-KDLG 784
Cdd:cd07083  404 VLSVIRYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGvqPFGGFKLSGTNaKTGG 483

                        490
                 ....*....|....
gi 393195303 785 EAALNEYLRVKTVT 798
Cdd:cd07083  484 PHYLRRFLEMKAVA 497

ALDH_F7_AASADH

cd07130

NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ...

334-801

8.54e-73

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: 245.58 E-value: 8.54e-73

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 334 GAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAV 413
Cdd:cd07130   10 GGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFK--EWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 414 YTLAL----------KTHVGMSIQtfryfagwcdkIQGSTIPinQARPNRNLtLTRKEPVGVCGIIIPWNYPLMMLSWKT 483
Cdd:cd07130   88 LPEGLgevqemidicDFAVGLSRQ-----------LYGLTIP--SERPGHRM-MEQWNPLGVVGVITAFNFPVAVWGWNA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 484 AACLAAGNTVVIKPAQVTPLTALK----FAELTLKAGIPKGVVNVLPGSGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMK 559
Cdd:cd07130  154 AIALVCGNVVVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCGGAD-VGEALVKDPRVPLVSFTGSTAVGRQVGQ 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 560 SCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQmgmsSVFF----NKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKV 635
Cdd:cd07130  233 AVA-ARFGRSLLELGGNNAIIVMEDADLDLAVR----AVLFaavgTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRI 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 636 GNPLDRDTDHGPQnHHAHLVKLMEYC-QHGVKEGATLVCGGNQVPRPGFFFEPTVFTdVEDHMFIAKEESFGPVMIISRF 714
Cdd:cd07130  308 GDPLDDGTLVGPL-HTKAAVDNYLAAiEEAKSQGGTVLFGGKVIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKF 385

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 715 AdgDLDAVLSRANATEFGLASGVFTRDINKAL-----YVSDklqAGTVFVNT-YNKTDVAAPFGGFKQSGFGKDLGEAAL 788
Cdd:cd07130  386 D--TLEEAIAWNNEVPQGLSSSIFTTDLRNAFrwlgpKGSD---CGIVNVNIgTSGAEIGGAFGGEKETGGGRESGSDAW 460

                        490
                 ....*....|...
gi 393195303 789 NEYLRVKTVTFEY 801
Cdd:cd07130  461 KQYMRRSTCTINY 473

PRK13968

putative succinate semialdehyde dehydrogenase; Provisional

340-797

2.14e-66

putative succinate semialdehyde dehydrogenase; Provisional

Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 228.21 E-value: 2.14e-66

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 340 TINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLAlK 419
Cdd:PRK13968  11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFR--DWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQA-R 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 420 THVGMSiqtfryfAGWCDKIQGSTIPINQARPN---RNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIK 496
Cdd:PRK13968  88 AEVAKS-------ANLCDWYAEHGPAMLKAEPTlveNQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 497 PAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDhPDVRKIGFTGSTEVGKHImKSCAISNVKKVSLELGGK 576
Cdd:PRK13968 161 HAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIND-SRIAAVTVTGSVRAGAAI-GAQAGAALKKCVLELGGS 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 577 SPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVK 656
Cdd:PRK13968 239 DPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDE 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 657 LMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISrfADGDLDAVLSRANATEFGLASG 736
Cdd:PRK13968 319 LHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAIT--VAKDAEHALELANDSEFGLSAT 396

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 393195303 737 VFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTV 797
Cdd:PRK13968 397 IFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457

ALDH_RL0313

cd07148

Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ...

339-780

6.80e-63

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: 218.44 E-value: 6.80e-63

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 339 ETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEN-GRWgkISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLA 417
Cdd:cd07148    2 EVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDrNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 418 lKTHVGMSIQTFRYFAGWCDKIQGSTIPIN--QARPNRnLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVI 495
Cdd:cd07148   80 -KVEVTRAIDGVELAADELGQLGGREIPMGltPASAGR-IAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 496 KPAQVTPLTALKFAELTLKAGIPKGVVNVLPgSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAISNvkKVSLELGG 575
Cdd:cd07148  158 KPALATPLSCLAFVDLLHEAGLPEGWCQAVP-CENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPGT--RCALEHGG 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 576 KSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLV 655
Cdd:cd07148  235 AAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVD 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 656 KLMEYCQHGVKEGATLVCGGNQVPRPgfFFEPTVFTDVEDHMFIAKEESFGPVMIIsrFADGDLDAVLSRANATEFGLAS 735
Cdd:cd07148  315 RVEEWVNEAVAAGARLLCGGKRLSDT--TYAPTVLLDPPRDAKVSTQEIFGPVVCV--YSYDDLDEAIAQANSLPVAFQA 390

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 393195303 736 GVFTRDINKALYVSDKLQAGTVFVN--TYNKTDvAAPFGGFKQSGFG 780
Cdd:cd07148  391 AVFTKDLDVALKAVRRLDATAVMVNdhTAFRVD-WMPFAGRRQSGYG 436

ALDH_AlkH-like

cd07134

Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ...

459-785

3.62e-60

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: 210.16 E-value: 3.62e-60

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 459 RKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVnVLPGsGSLVGQRLSD 538
Cdd:cd07134   97 RYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVA-VFEG-DAEVAQALLE 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 539 HPdVRKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSI 618
Cdd:cd07134  175 LP-FDHIFFTGSPAVGKIVMAAAA-KHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESV 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 619 HDEFVRRVVEEVRKMKVGNPLDRDTDHGP----QNHHAHLVKLMEycqHGVKEGATLVCGGnQVPRPGFFFEPTVFTDVE 694
Cdd:cd07134  253 KDAFVEHLKAEIEKFYGKDAARKASPDLArivnDRHFDRLKGLLD---DAVAKGAKVEFGG-QFDAAQRYIAPTVLTNVT 328

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 695 DHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNtynktDVAA----- 769
Cdd:cd07134  329 PDMKIMQEEIFGPVLPIITYE--DLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN-----DVVLhflnp 401

                        330
                 ....*....|....*...
gi 393195303 770 --PFGGFKQSGFGKDLGE 785
Cdd:cd07134  402 nlPFGGVNNSGIGSYHGV 419

ALDH_F3-13-14_CALDH-like

cd07087

ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ...

459-797

3.59e-59

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: 206.99 E-value: 3.59e-59

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 459 RKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAgIPKGVVNVLPGSGSlVGQRLSD 538
Cdd:cd07087   97 IPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVE-VATALLA 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 539 HP-DvrKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDS 617
Cdd:cd07087  175 EPfD--HIFFTGSPAVGKIVMEAAA-KHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHES 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 618 IHDEFVRRVVEEVRKMkVGNPLDRDTDHGPQNHHAHLVKLMEYcqhgvKEGATLVCGGnQVPRPGFFFEPTVFTDVEDHM 697
Cdd:cd07087  252 IKDELIEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASL-----LDDGKVVIGG-QVDKEERYIAPTILDDVSPDS 324

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 698 FIAKEESFGPVM-IISRfadGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNtynktDV-------AA 769
Cdd:cd07087  325 PLMQEEIFGPILpILTY---DDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVN-----DVllhaaipNL 396

                        330       340
                 ....*....|....*....|....*...
gi 393195303 770 PFGGFKQSGFGKDLGEAALNEYLRVKTV 797
Cdd:cd07087  397 PFGGVGNSGMGAYHGKAGFDTFSHLKSV 424

ALDH_SGSD_AstD

cd07095

N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ...

376-778

9.75e-59

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: 205.97 E-value: 9.75e-59

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 376 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGA--------VYTLALKthVGMSIQTFRYFAGwcDKiqgsTIPIN 447
Cdd:cd07095   16 WAALSLEERAAILRRFAELLKANKEELARLISRETGKplweaqteVAAMAGK--IDISIKAYHERTG--ER----ATPMA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 448 QARpnrnlTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPG 527
Cdd:cd07095   88 QGR-----AVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 528 SGSlVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCI 607
Cdd:cd07095  163 GRE-TGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCT 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 608 AAGRLFVEDS-IHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFE 686
Cdd:cd07095  242 CARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTAFLS 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 687 PTVF--TDVEDHmfiAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDinKALY--VSDKLQAGTVFVN-T 761
Cdd:cd07095  322 PGIIdvTDAADV---PDEEIFGPLLQVYRYD--DFDEAIALANATRFGLSAGLLSDD--EALFerFLARIRAGIVNWNrP 394

                        410
                 ....*....|....*..
gi 393195303 762 YNKTDVAAPFGGFKQSG 778
Cdd:cd07095  395 TTGASSTAPFGGVGLSG 411

PRK11904

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

324-780

1.57e-54

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

Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 203.89 E-value: 1.57e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  324 FIGGEFVDAEGAKTsETINPTDGS-VICQVSLAQVTDVDKAVAAAKDAFenGRWGKISARDRGRLMYRLADLMEQHQEEL 402
Cdd:PRK11904  551 WQAGPIINGEGEAR-PVVSPADRRrVVGEVAFADAEQVEQALAAARAAF--PAWSRTPVEERAAILERAADLLEANRAEL 627

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  403 ATIEALDAGavytlalKT-HVGMS-----IQTFRYFAgwcdkiqgstipiNQARpnRNLTLTRKEP-------------- 462
Cdd:PRK11904  628 IALCVREAG-------KTlQDAIAevreaVDFCRYYA-------------AQAR--RLFGAPEKLPgptgesnelrlhgr 685

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  463 -VGVCgiIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPD 541
Cdd:PRK11904  686 gVFVC--ISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPR 763

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  542 VRKIGFTGSTEVGKHI-----MKSCAIsnvkkVSL--ELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFV 614
Cdd:PRK11904  764 IAGVAFTGSTETARIInrtlaARDGPI-----VPLiaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFV 838

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  615 EDSIHDefvrRVVE----EVRKMKVGNPLDRDTDHGP---QNHHAhlvKLMEYCQHgVKEGATLVCggnQVPRP-----G 682
Cdd:PRK11904  839 QEDIAD----RVIEmlkgAMAELKVGDPRLLSTDVGPvidAEAKA---NLDAHIER-MKREARLLA---QLPLPagtenG 907

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  683 FFFEPTVFtdvE-DHMFIAKEESFGPVMIISRFADGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVnt 761
Cdd:PRK11904  908 HFVAPTAF---EiDSISQLEREVFGPILHVIRYKASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYV-- 982

                         490       500
                  ....*....|....*....|....
gi 393195303  762 yNKTDVAA-----PFGGFKQSGFG 780
Cdd:PRK11904  983 -NRNQIGAvvgvqPFGGQGLSGTG 1005

D1pyr5carbox3

TIGR01238

delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ...

376-784

5.04e-54

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: 195.13 E-value: 5.04e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  376 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALkTHVGMSIQTFRYFAgwcdkiqgstipiNQARpnRNL 455
Cdd:TIGR01238  90 WNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAI-AEVREAVDFCRYYA-------------KQVR--DVL 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  456 TLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQR 535
Cdd:TIGR01238 154 GEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAA 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  536 LSDHPDVRKIGFTGSTEVGKHIMKSCAISNVKKVSL--ELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLF 613
Cdd:TIGR01238 234 LTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLC 313

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  614 VEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGP-------QNHHAHLVKlMEYCQHGVKEgatLVCGGNQVPRPGFFFE 686
Cdd:TIGR01238 314 VQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPvidaeakQNLLAHIEH-MSQTQKKIAQ---LTLDDSRACQHGTFVA 389

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  687 PTVFTdvEDHMFIAKEESFGPVMIISRFADGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVntyNKTD 766
Cdd:TIGR01238 390 PTLFE--LDDIAELSEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYV---NRNQ 464

                         410       420
                  ....*....|....*....|...
gi 393195303  767 VAA-----PFGGFKQSGFGKDLG 784
Cdd:TIGR01238 465 VGAvvgvqPFGGQGLSGTGPKAG 487

PRK11905

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

376-780

2.36e-52

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

Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 197.78 E-value: 2.36e-52

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  376 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALkTHVGMSIQTFRYFAgwcdkiqgstipiNQARpnRNL 455
Cdd:PRK11905  606 WSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAI-AEVREAVDFLRYYA-------------AQAR--RLL 669

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  456 TLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQR 535
Cdd:PRK11905  670 NGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAA 749

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  536 LSDHPDVRKIGFTGSTEVGKHIMKSCAISNVKKVSL--ELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLF 613
Cdd:PRK11905  750 LVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPLiaETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLC 829

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  614 VEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLvcggNQVPRP-----GFFFEPT 688
Cdd:PRK11905  830 LQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLV----HQLPLPaetekGTFVAPT 905

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  689 VFtDVEDhmfIA--KEESFGPVMIISRFADGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVntyNKTD 766
Cdd:PRK11905  906 LI-EIDS---ISdlEREVFGPVLHVVRFKADELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYV---NRNI 978

                         410
                  ....*....|....*....
gi 393195303  767 VAA-----PFGGFKQSGFG 780
Cdd:PRK11905  979 IGAvvgvqPFGGEGLSGTG 997

PutA2

COG4230

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

375-780

3.47e-52

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

Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 197.47 E-value: 3.47e-52

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  375 RWGKISARDRGRLMYRLADLMEQHQEELATIEALDAG------------AVytlalkthvgmsiqTF-RYFAgwcdkiqg 441
Cdd:COG4230   608 AWSATPVEERAAILERAADLLEAHRAELMALLVREAGktlpdaiaevreAV--------------DFcRYYA-------- 665

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  442 stipiNQARpNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGV 521
Cdd:COG4230   666 -----AQAR-RLFAAPTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADV 739

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  522 VNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAISNVKKVSL--ELGGKSPLI---------IFADCdlnka 590
Cdd:COG4230   740 LQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAARDGPIVPLiaETGGQNAMIvdssalpeqVVDDV----- 814

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  591 vqmgMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGP------QNhhahlvKLMEYCQHG 664
Cdd:COG4230   815 ----LASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPvidaeaRA------NLEAHIERM 884

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  665 VKEGATLVcggnQVPRP-----GFFFEPTVF--TDVEDhmfiAKEESFGPVMIISRFADGDLDAVLSRANATEFGLASGV 737
Cdd:COG4230   885 RAEGRLVH----QLPLPeecanGTFVAPTLIeiDSISD----LEREVFGPVLHVVRYKADELDKVIDAINATGYGLTLGV 956

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 393195303  738 FTRdINK-ALYVSDKLQAGTVFVntyNKTDVAA-----PFGGFKQSGFG 780
Cdd:COG4230   957 HSR-IDEtIDRVAARARVGNVYV---NRNIIGAvvgvqPFGGEGLSGTG 1001

ALDH_CALDH_CalB

cd07133

Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ...

380-780

1.85e-50

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: 183.07 E-value: 1.85e-50

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 380 SARDRGRLMYRLADLMEQHQEELAtiEALDA-----GAVYTLALKthVGMSIQTFRY----FAGWCdkiqgstipinqaR 450
Cdd:cd07133   18 SLEERRDRLDRLKALLLDNQDALA--EAISAdfghrSRHETLLAE--ILPSIAGIKHarkhLKKWM-------------K 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 451 PNR---NLTLT------RKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGV 521
Cdd:cd07133   81 PSRrhvGLLFLpakaevEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAEL-LAEYFDEDE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 522 VNVLPGsGSLVGQRLS----DHpdvrkIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSS 597
Cdd:cd07133  160 VAVVTG-GADVAAAFSslpfDH-----LLFTGSTAVGRHVMRAAA-ENLTPVTLELGGKSPAIIAPDADLAKAAERIAFG 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 598 VFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKM---KVGNPldrdtDHGPQNHHAHLVKLMEYCQHGVKEGATLV-C 673
Cdd:cd07133  233 KLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMyptLADNP-----DYTSIINERHYARLQGLLEDARAKGARVIeL 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 674 GGNQVPRPGF-FFEPTVFTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKL 752
Cdd:cd07133  308 NPAGEDFAATrKLPPTLVLNVTDDMRVMQEEIFGPILPILTYD--SLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRT 385

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 393195303 753 QAGTVFVNtynktDVA-------APFGGFKQSGFG 780
Cdd:cd07133  386 HSGGVTIN-----DTLlhvaqddLPFGGVGASGMG 415

PLN00412

NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional

324-780

6.02e-50

NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional

Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 183.42 E-value: 6.02e-50

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 324 FIGGEFVDAEGAKTSETINPTDGSVicQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEELA 403
Cdd:PLN00412  19 YADGEWRTSSSGKSVAITNPSTRKT--QYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIA 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 404 tiEALdagaVYTLA-----LKTHVGMSIQTFRYFA-------GWCDKIQGSTIPINQarpnRN-LTLTRKEPVGVCGIII 470
Cdd:PLN00412  97 --ECL----VKEIAkpakdAVTEVVRSGDLISYTAeegvrilGEGKFLVSDSFPGNE----RNkYCLTSKIPLGVVLAIP 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 471 PWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGS 550
Cdd:PLN00412 167 PFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 551 tEVGKHIMKSCAISNVKkvsLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEV 630
Cdd:PLN00412 247 -DTGIAISKKAGMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKV 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 631 RKMKVGNPLDrDTDHGP------QNHHAHLVKlmeycqHGVKEGATLVcggNQVPRPGFFFEPTVFTDVEDHMFIAKEES 704
Cdd:PLN00412 323 AKLTVGPPED-DCDITPvvsessANFIEGLVM------DAKEKGATFC---QEWKREGNLIWPLLLDNVRPDMRIAWEEP 392

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 393195303 705 FGPVMIISRFadGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTY-NKTDVAAPFGGFKQSGFG 780
Cdd:PLN00412 393 FGPVLPVIRI--NSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSApARGPDHFPFQGLKDSGIG 467

ALDH_F14-YMR110C

cd07135

Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ...

459-797

1.85e-49

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: 180.49 E-value: 1.85e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 459 RKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGVVNVLPG----SGSLVGQ 534
Cdd:cd07135  105 RKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAEL-VPKYLDPDAFQVVQGgvpeTTALLEQ 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 535 RLSdhpdvrKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFV 614
Cdd:cd07135  184 KFD------KIFYTGSGRVGRIIAEAAA-KHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLV 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 615 EDSIHDEFVRRVVEEVRKMkVGNPLDRDTDHG---PQNHHAHLVKLMEycqhgvKEGATLVCGG--NQVPRpgfFFEPTV 689
Cdd:cd07135  257 DPSVYDEFVEELKKVLDEF-YPGGANASPDYTrivNPRHFNRLKSLLD------TTKGKVVIGGemDEATR---FIPPTI 326

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 690 FTDVEDHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN-TYNKTDV- 767
Cdd:cd07135  327 VSDVSWDDSLMSEELFGPVLPIIKVD--DLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINdTLIHVGVd 404

                        330       340       350
                 ....*....|....*....|....*....|
gi 393195303 768 AAPFGGFKQSGFGKDLGEAALNEYLRVKTV 797
Cdd:cd07135  405 NAPFGGVGDSGYGAYHGKYGFDTFTHERTV 434

PTZ00381

aldehyde dehydrogenase family protein; Provisional

459-797

2.12e-49

aldehyde dehydrogenase family protein; Provisional

Pssm-ID: 240392 Cd Length: 493 Bit Score: 181.77 E-value: 2.12e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 459 RKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAgIPKGVVNVLPGsGSLVGQRLSD 538
Cdd:PTZ00381 106 IPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTELLK 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 539 HP-DVrkIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDS 617
Cdd:PTZ00381 184 EPfDH--IFFTGSPRVGKLVMQAAA-ENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRS 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 618 IHDEFVRRVVEEVRKMKVGNPLdRDTDHGPQNHHAHLVKLME-YCQHGVKegatLVCGGnQVPRPGFFFEPTVFTDVEDH 696
Cdd:PTZ00381 261 IKDKFIEALKEAIKEFFGEDPK-KSEDYSRIVNEFHTKRLAElIKDHGGK----VVYGG-EVDIENKYVAPTIIVNPDLD 334

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 697 MFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVN--TYNKTDVAAPFGGF 774
Cdd:PTZ00381 335 SPLMQEEIFGPILPILTYE--NIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdcVFHLLNPNLPFGGV 412

                        330       340
                 ....*....|....*....|...
gi 393195303 775 KQSGFGKDLGEAALNEYLRVKTV 797
Cdd:PTZ00381 413 GNSGMGAYHGKYGFDTFSHPKPV 435

PLN02419

methylmalonate-semialdehyde dehydrogenase [acylating]

318-801

2.68e-49

methylmalonate-semialdehyde dehydrogenase [acylating]

Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 183.79 E-value: 2.68e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 318 RMPHqlFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQ 397
Cdd:PLN02419 113 RVPN--LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFP--LWRNTPITTRQRVMLKFQELIRK 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 398 HQEELATIEALDAGAVytlaLKTHVGMSIQTFRYFAGWCDKiqgSTIPINQARPNRNL---TLTRKEPVGVCGIIIPWNY 474
Cdd:PLN02419 189 NMDKLAMNITTEQGKT----LKDSHGDIFRGLEVVEHACGM---ATLQMGEYLPNVSNgvdTYSIREPLGVCAGICPFNF 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 475 PLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQrLSDHPDVRKIGFTGSTEVG 554
Cdd:PLN02419 262 PAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSNTAG 340

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 555 KHIMKSCAISNvKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGR-LFVEDSihDEFVRRVVEEVRKM 633
Cdd:PLN02419 341 MHIYARAAAKG-KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvVFVGDA--KSWEDKLVERAKAL 417

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 634 KVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGF----FFEPTVFTDVEDHMFIAKEESFGPVM 709
Cdd:PLN02419 418 KVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYekgnFIGPTILSGVTPDMECYKEEIFGPVL 497

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 710 IISRfaDGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTynKTDVAAPFGGF--KQSGFGKDL---G 784
Cdd:PLN02419 498 VCMQ--ANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV--PIPVPLPFFSFtgNKASFAGDLnfyG 573

                        490
                 ....*....|....*..
gi 393195303 785 EAALNEYLRVKTVTFEY 801
Cdd:PLN02419 574 KAGVDFFTQIKLVTQKQ 590

ALDH_YwdH-P39616

cd07136

Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ...

459-780

4.02e-48

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: 176.93 E-value: 4.02e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 459 RKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGVVNVLPG----SGSLVGQ 534
Cdd:cd07136   97 YYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKI-IEETFDEEYVAVVEGgveeNQELLDQ 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 535 RLsDHpdvrkIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFV 614
Cdd:cd07136  176 KF-DY-----IFFTGSVRVGKIVMEAAA-KHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLV 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 615 EDSIHDEFVRRVVEEVRKMKVGNPLDRDtDHGPQNHHAHLVKLMEYCQHGvkegaTLVCGGNqVPRPGFFFEPTVFTDVE 694
Cdd:cd07136  249 HESVKEKFIKELKEEIKKFYGEDPLESP-DYGRIINEKHFDRLAGLLDNG-----KIVFGGN-TDRETLYIEPTILDNVT 321

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 695 DHMFIAKEESFGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAG------TV--FVNTYnktd 766
Cdd:cd07136  322 WDDPVMQEEIFGPILPVLTYD--TLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGggcindTImhLANPY---- 395

                        330
                 ....*....|....
gi 393195303 767 vaAPFGGFKQSGFG 780
Cdd:cd07136  396 --LPFGGVGNSGMG 407

astD

PRK09457

succinylglutamic semialdehyde dehydrogenase; Reviewed

323-778

1.95e-45

succinylglutamic semialdehyde dehydrogenase; Reviewed

Pssm-ID: 181873 Cd Length: 487 Bit Score: 170.14 E-value: 1.95e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 323 LFIGGEFVDAEGAkTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFEngRWGKISARDRGRLMYRLADLMEQHQEEL 402
Cdd:PRK09457   3 LWINGDWIAGQGE-AFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFP--AWARLSFEERQAIVERFAALLEENKEEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 403 ATIEALDAGA--------VYTLALKthVGMSIQTFRYFAGwcdkiqgstipiNQARPNRNLTLT-RKEPVGVCGIIIPWN 473
Cdd:PRK09457  80 AEVIARETGKplweaateVTAMINK--IAISIQAYHERTG------------EKRSEMADGAAVlRHRPHGVVAVFGPYN 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 474 YPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGsGSLVGQRLSDHPDVRKIGFTGSTEV 553
Cdd:PRK09457 146 FPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANT 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 554 GKHIMKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIH-DEFVRRVVEEVRK 632
Cdd:PRK09457 225 GYLLHRQFAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKR 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 633 MKVGNPlDRDTD--HGPQNHHAHLVKLMEYCQHGVKEGA------TLVCGGNQVPRPGfFFEPTVFTDVEDhmfiakEES 704
Cdd:PRK09457 305 LTVGRW-DAEPQpfMGAVISEQAAQGLVAAQAQLLALGGksllemTQLQAGTGLLTPG-IIDVTGVAELPD------EEY 376

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 393195303 705 FGPVMIISRFAdgDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVfvnTYNK----TDVAAPFGGFKQSG 778
Cdd:PRK09457 377 FGPLLQVVRYD--DFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIV---NWNKpltgASSAAPFGGVGASG 449

PLN02315

aldehyde dehydrogenase family 7 member

324-801

1.10e-43

aldehyde dehydrogenase family 7 member

Pssm-ID: 177949 Cd Length: 508 Bit Score: 165.78 E-value: 1.10e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 324 FIGGEFvdAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENgrWGKISARDRGRLMYRLADLMEQHQEELA 403
Cdd:PLN02315  24 YVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKI--WMQVPAPKRGEIVRQIGDALRAKLDYLG 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 404 TIEALDAGAVYTLALKtHVGMSIQTFRYFAGWCDKIQGSTIPinQARPNrNLTLTRKEPVGVCGIIIPWNYPLMMLSWKT 483
Cdd:PLN02315 100 RLVSLEMGKILAEGIG-EVQEIIDMCDFAVGLSRQLNGSIIP--SERPN-HMMMEVWNPLGIVGVITAFNFPCAVLGWNA 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 484 AACLAAGNTVVIKPAQVTPLTALK----FAELTLKAGIPKGVVNVLPGsGSLVGQRLSDHPDVRKIGFTGSTEVGkhIMK 559
Cdd:PLN02315 176 CIALVCGNCVVWKGAPTTPLITIAmtklVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVG--LMV 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 560 SCAI-SNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNP 638
Cdd:PLN02315 253 QQTVnARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDP 332

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 639 LDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVfTDVEDHMFIAKEESFGPVMIISRFAdgD 718
Cdd:PLN02315 333 LEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTI-VEISPDADVVKEELFGPVLYVMKFK--T 409

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 719 LDAVLSRANATEFGLASGVFTRD---INKAL--YVSDklqAGTVFVNT-YNKTDVAAPFGGFKQSGFGKDLGEAALNEYL 792
Cdd:PLN02315 410 LEEAIEINNSVPQGLSSSIFTRNpetIFKWIgpLGSD---CGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQYM 486


                 ....*....
gi 393195303 793 RVKTVTFEY 801
Cdd:PLN02315 487 RRSTCTINY 495

FDH_Hydrolase_C

cd08703

The C-terminal subdomain of the hydrolase domain on the bi-functional protein ...

116-205

6.67e-42

Pssm-ID: 187731 [Multi-domain] Cd Length: 100 Bit Score: 147.88 E-value: 6.67e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 116 ASAIHNWIRGNDKVPGAWTEACEQKLTFFNSTLNTSGLVPEGdALPIPGAHRPGVVTKAGLILFGNDDKMLLVKNIQLED 195
Cdd:cd08703   12 AEALHNFIRGNDKVPGAWATIDGEQVTLFGSSLWKGGKPPGG-EVEVEGLERPGIVHKNGLLITGSDGKMVNVKRLQFED 90

                         90
                 ....*....|
gi 393195303 196 GKMILASNFF 205
Cdd:cd08703   91 GKMIPASKYG 100

putA

PRK11809

trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ...

383-780

3.97e-41

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

Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 163.22 E-value: 3.97e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  383 DRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALkTHVGMSIQTFRYFAGwcdkiqgstipinQARPN-RNLTltrKE 461
Cdd:PRK11809  705 ERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAI-AEVREAVDFLRYYAG-------------QVRDDfDNDT---HR 767

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  462 PVG--VCgiIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDH 539
Cdd:PRK11809  768 PLGpvVC--ISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVAD 845

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  540 PDVRKIGFTGSTEVGKHIMKSCA---ISNVKKVSL--ELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFV 614
Cdd:PRK11809  846 ARVRGVMFTGSTEVARLLQRNLAgrlDPQGRPIPLiaETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCL 925

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  615 EDSIHDEFVRRVVEEVRKMKVGNPlDR-DTDHGP-------QNHHAHlVKLMEYCQHGVkegatlvcggNQVPRP----- 681
Cdd:PRK11809  926 QDDVADRTLKMLRGAMAECRMGNP-DRlSTDIGPvidaeakANIERH-IQAMRAKGRPV----------FQAAREnsedw 993

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  682 --GFFFEPTVftdVE-DHMFIAKEESFGPVMIISRFADGDLDAVLSRANATEFGLASGVFTR-DINKAlYVSDKLQAGTV 757
Cdd:PRK11809  994 qsGTFVPPTL---IElDSFDELKREVFGPVLHVVRYNRNQLDELIEQINASGYGLTLGVHTRiDETIA-QVTGSAHVGNL 1069

                         410       420
                  ....*....|....*....|....*...
gi 393195303  758 FVntyNKTDVAA-----PFGGFKQSGFG 780
Cdd:PRK11809 1070 YV---NRNMVGAvvgvqPFGGEGLSGTG 1094

ALDH_F4-17_P5CDH

cd07123

Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ...

490-778

2.32e-40

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: 156.21 E-value: 2.32e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 490 GNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCA--ISNVK 567
Cdd:cd07123  197 GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGenLDRYR 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 568 ---KVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTD 644
Cdd:cd07123  277 typRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNF 356

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 645 HGPQNHHAHLVKLMEYCQHGVKE-GATLVCGGNQVPRPGFFFEPTVF--TDVEDHMFiaKEESFGPVMIISRFADGDLDA 721
Cdd:cd07123  357 MGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGYFVEPTVIetTDPKHKLM--TEEIFGPVLTVYVYPDSDFEE 434

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 393195303 722 VLSRAN-ATEFGLASGVFTRD---INKAlyvSDKLQ--AGTVFVNTYNKTDVAA--PFGGFKQSG 778
Cdd:cd07123  435 TLELVDtTSPYALTGAIFAQDrkaIREA---TDALRnaAGNFYINDKPTGAVVGqqPFGGARASG 496

ALDH_F3AB

cd07132

Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ...

450-781

1.38e-38

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: 149.29 E-value: 1.38e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 450 RPNRNLT------LTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtlkagIPK---- 519
Cdd:cd07132   82 PVKKNLAtllddvYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-----IPKyldk 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 520 ---GVVNV-LPGSGSLVGQRLsDHpdvrkIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGM 595
Cdd:cd07132  157 ecyPVVLGgVEETTELLKQRF-DY-----IFYTGSTSVGKIVMQAAA-KHLTPVTLELGGKSPCYVDKSCDIDVAARRIA 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 596 SSVFFNKGENCIAAGRLFVEDSIHDEFV---RRVVEEVrkmkVGNPLDRDTDHGP---QNHHAHLVKLMeycqhgvkEGA 669
Cdd:cd07132  230 WGKFINAGQTCIAPDYVLCTPEVQEKFVealKKTLKEF----YGEDPKESPDYGRiinDRHFQRLKKLL--------SGG 297

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 670 TLVCGGNQVPRPGfFFEPTVFTDVEDHMFIAKEESFGPVMIIsrFADGDLDAVLSRANATEFGLASGVFTRD---INKAL 746
Cdd:cd07132  298 KVAIGGQTDEKER-YIAPTVLTDVKPSDPVMQEEIFGPILPI--VTVNNLDEAIEFINSREKPLALYVFSNNkkvINKIL 374

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 393195303 747 yvsDKLQAGTVFVNtynktDV-------AAPFGGFKQSGFGK 781
Cdd:cd07132  375 ---SNTSSGGVCVN-----DTimhytldSLPFGGVGNSGMGA 408

Formyl_trans_N

pfam00551

Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...

1-132

2.71e-38

Pssm-ID: 395436 [Multi-domain] Cd Length: 181 Bit Score: 140.50 E-value: 2.71e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303    1 MKIAVI--GQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADPLGLEAEKDGVPVFKYSRWRAKGQALPDVVAKYQALGA 78
Cdd:pfam00551   1 MKIAVLisGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 393195303   79 ELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAIHNWIRGNDKVPGA 132
Cdd:pfam00551  81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGV 134

ALDH_F3FHI

cd07137

Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ...

461-797

4.06e-29

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: 120.98 E-value: 4.06e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 461 EPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGVVNVLPGSGSLVGQRLSDHP 540
Cdd:cd07137  100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL-IPEYLDTKAIKVIEGGVPETTALLEQKW 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 541 DvrKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVF-FNKGENCIAAGRLFVEDSIH 619
Cdd:cd07137  179 D--KIFFTGSPRVGRIIMAAAA-KHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEESFA 255

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 620 DEFVRRVVEEVRKMKVGNPldRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGnQVPRPGFFFEPTVFTDVEDHMFI 699
Cdd:cd07137  256 PTLIDALKNTLEKFFGENP--KESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGG-ERDEKNLYIEPTILLDPPLDSSI 332

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 700 AKEESFGPVM-IIS-RFADGDLDAVLSRANAtefgLASGVFTRdiNKALY--VSDKLQAGTVFVNtynktDVAA------ 769
Cdd:cd07137  333 MTEEIFGPLLpIITvKKIEESIEIINSRPKP----LAAYVFTK--NKELKrrIVAETSSGGVTFN-----DTVVqyaidt 401

                        330       340
                 ....*....|....*....|....*....
gi 393195303 770 -PFGGFKQSGFGKDLGEAALNEYLRVKTV 797
Cdd:cd07137  402 lPFGGVGESGFGAYHGKFSFDAFSHKKAV 430

ALDH_KGSADH-like

cd07084

ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ...

374-793

1.76e-27

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: 116.57 E-value: 1.76e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 374 GRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALKthVGMSIQTFRYFAGWCDKIQGSTIPINQARPNR 453
Cdd:cd07084   13 KAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAEN--ICGDQVQLRARAFVIYSYRIPHEPGNHLGQGL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 454 NLTLTRKE-PVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGI-PKGVVNVLPGSGSL 531
Cdd:cd07084   91 KQQSHGYRwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLlPPEDVTLINGDGKT 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 532 vGQRLSDHPDVRKIGFTGSTEVGKHImkscaISNVK--KVSLELGGKSPLIIFADCDLNKAV------QMGMSSvffnkG 603
Cdd:cd07084  171 -MQALLLHPNPKMVLFTGSSRVAEKL-----ALDAKqaRIYLELAGFNWKVLGPDAQAVDYVawqcvqDMTACS-----G 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 604 ENCIAAGRLFV-EDSIHDEFVRRVVEEVRKMKVGNPL-----DRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQ 677
Cdd:cd07084  240 QKCTAQSMLFVpENWSKTPLVEKLKALLARRKLEDLLlgpvqTFTTLAMIAHMENLLGSVLLFSGKELKNHSIPSIYGAC 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 678 VPRPGFFFEPTVFTDVEDHMfiakEESFGPVMIISRFADGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQ-AGT 756
Cdd:cd07084  320 VASALFVPIDEILKTYELVT----EEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQELIGNLWvAGR 395

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 393195303 757 VFVNTYNKTDVAAP---FGGFKQSGFGKDLGEA-ALNEYLR 793
Cdd:cd07084  396 TYAILRGRTGVAPNqnhGGGPAADPRGAGIGGPeAIKLVWR 436

PLN02174

aldehyde dehydrogenase family 3 member H1

461-799

2.37e-26

aldehyde dehydrogenase family 3 member H1

Pssm-ID: 177831 Cd Length: 484 Bit Score: 113.60 E-value: 2.37e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 461 EPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELtLKAGIPKGVVNVLPGSGSLVGQRLSDHP 540
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKL-LEQYLDSSAVRVVEGAVTETTALLEQKW 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 541 DvrKIGFTGSTEVGKHIMKSCAiSNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVF-FNKGENCIAAGRLFVEDSIH 619
Cdd:PLN02174 190 D--KIFYTGSSKIGRVIMAAAA-KHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYA 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 620 DEFVRRVVEEVRKMKVGNPLD-RDTDH-GPQNHHAHLVKLMEYcqhgvKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHM 697
Cdd:PLN02174 267 PKVIDAMKKELETFYGKNPMEsKDMSRiVNSTHFDRLSKLLDE-----KEVSDKIVYGGEKDRENLKIAPTILLDVPLDS 341

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 698 FIAKEESFGPVMIISRFADGD--LDAVLSRANAtefgLASGVFTRDINKALYVSDKLQAGTVFVNtynktDVAA------ 769
Cdd:PLN02174 342 LIMSEEIFGPLLPILTLNNLEesFDVIRSRPKP----LAAYLFTHNKKLKERFAATVSAGGIVVN-----DIAVhlalht 412

                        330       340       350
                 ....*....|....*....|....*....|.
gi 393195303 770 -PFGGFKQSGFGKDLGEAALNEYLRVKTVTF 799
Cdd:PLN02174 413 lPFGGVGESGMGAYHGKFSFDAFSHKKAVLY 443

PLN02203

aldehyde dehydrogenase

461-781

1.38e-25

aldehyde dehydrogenase

Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 111.36 E-value: 1.38e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 461 EPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTAlKFaeltLKAGIPK----GVVNVLPGsGSLVGQRL 536
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATS-AF----LAANIPKyldsKAVKVIEG-GPAVGEQL 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 537 SDHP-DvrKIGFTGSTEVGKHIMkSCAISNVKKVSLELGGKSPLIIfaDC-DLNKAVQMGMSSVFFNK-----GENCIAA 609
Cdd:PLN02203 181 LQHKwD--KIFFTGSPRVGRIIM-TAAAKHLTPVALELGGKCPCIV--DSlSSSRDTKVAVNRIVGGKwgscaGQACIAI 255

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 610 GRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHaHLVKLMEYCQHGVKEgATLVCGGNQVPRpGFFFEPTV 689
Cdd:PLN02203 256 DYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKK-HFQRLSNLLKDPRVA-ASIVHGGSIDEK-KLFIEPTI 332

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 690 FTDVEDHMFIAKEESFGPVM-IISRFADGDLDAVLsraNATEFGLASGVFTRDINKALYVSDKLQAGTVfvnTYNKTDV- 767
Cdd:PLN02203 333 LLNPPLDSDIMTEEIFGPLLpIITVKKIEDSIAFI---NSKPKPLAIYAFTNNEKLKRRILSETSSGSV---TFNDAIIq 406

                        330
                 ....*....|....*...
gi 393195303 768 ----AAPFGGFKQSGFGK 781
Cdd:PLN02203 407 yacdSLPFGGVGESGFGR 424

FMT_core

cd08369

Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...

3-128

5.58e-25

Pssm-ID: 187712 [Multi-domain] Cd Length: 173 Bit Score: 102.37 E-value: 5.58e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303   3 IAVIGQSLFGQEVYCHLR-KEGHEVVGVFTVPDKDGKADPLGLEAEKDGVpvfkysrWRAKGQALPDVVAKYQALGAELN 81
Cdd:cd08369    1 IVILGSGNIGQRVLKALLsKEGHEIVGVVTHPDSPRGTAQLSLELVGGKV-------YLDSNINTPELLELLKEFAPDLI 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 393195303  82 VLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAIHNWIRGNDK 128
Cdd:cd08369   74 VSINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEK 120

Fmt

COG0223

Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];

1-120

1.37e-21

Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];

Pssm-ID: 439993 [Multi-domain] Cd Length: 308 Bit Score: 96.33 E-value: 1.37e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303   1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKD---GK---ADPLGLEAEKDGVPVFKYSRWRAkgqalPDVVAKYQ 74
Cdd:COG0223    1 MRIVFMGTPDFAVPSLEALLAAGHEVVAVVTQPDRPagrGRkltPSPVKELALEHGIPVLQPESLKD-----PEFLEELR 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 393195303  75 ALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAIH 120
Cdd:COG0223   76 ALNPDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQ 121

FMT_core_like_2

cd08822

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...

1-131

1.40e-20

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.

Pssm-ID: 187724 [Multi-domain] Cd Length: 192 Bit Score: 90.21 E-value: 1.40e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303   1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKAdplgLEAEKDGVPVFKysrwrakGQALPDVVAKYQALGAEL 80
Cdd:cd08822    1 MKIAIAGQKWFGTAVLEALRARGIALLGVAAPEEGDRLA----AAARTAGSRGLP-------RAGVAVLPADAIPPGTDL 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 393195303  81 NVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAIHNWIRGNDKVPG 131
Cdd:cd08822   70 IVAAHCHAFISAKTRARARLGAIGYHPSLLPRHRGRDAVEWTIRMRDPITG 120

FMT_core_Met-tRNA-FMT_N

cd08646

Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...

1-131

9.99e-17

Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA formyltransferase (Met-tRNA-FMT), N-terminal formyltransferase domain. Met-tRNA-FMT transfers a formyl group from N-10 formyltetrahydrofolate to the amino terminal end of a methionyl-aminoacyl-tRNA acyl moiety, yielding formyl-Met-tRNA. Formyl-Met-tRNA plays essential role in protein translation initiation by forming complex with IF2. The formyl group plays a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and by impairing its binding to EFTU-GTP. The N-terminal domain contains a Rossmann fold and it is the catalytic domain of the enzyme.

Pssm-ID: 187715 [Multi-domain] Cd Length: 204 Bit Score: 79.41 E-value: 9.99e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303   1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKD---GK---ADPLGLEAEKDGVPVFKYSRWRAkgqalPDVVAKYQ 74
Cdd:cd08646    1 MRIVFMGTPDFAVPSLEALLKSGHEVVAVVTQPDKPrgrGKkltPSPVKELALELGLPVLQPEKLKD-----EEFLEELK 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 393195303  75 ALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAIHNWIRGNDKVPG 131
Cdd:cd08646   76 ALKPDLIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETG 132

ALDH_KGSADH

cd07129

Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ...

376-725

1.19e-16

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: 83.36 E-value: 1.19e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 376 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGavYTLALKT-HVGMSIQTFRYFA------GWCDKIQGSTIPINQ 448
Cdd:cd07129   15 YRALSPARRAAFLEAIADEIEALGDELVARAHAETG--LPEARLQgELGRTTGQLRLFAdlvregSWLDARIDPADPDRQ 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 449 ARPNRNLTLtRKEPVGVCGIIIPWNYPLM--MLSWKTAACLAAGNTVVIK--PAQvtPLTALKFAELTLKA----GIPKG 520
Cdd:cd07129   93 PLPRPDLRR-MLVPLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKahPAH--PGTSELVARAIRAAlratGLPAG 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 521 VVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAISNV-KKVSLELGGKSPLIIFADCDLNKAVQMGMS--- 596
Cdd:cd07129  170 VFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEpIPFYAELGSVNPVFILPGALAERGEAIAQGfvg 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 597 SVFFNKGENCIAAGRLFVEDSIH-DEFVRRVVEEVRKMKVGNPLdrdtDHGPQNHHahlvklmeycQHGVKE-----GAT 670
Cdd:cd07129  250 SLTLGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAAPAQTML----TPGIAEAY----------RQGVEAlaaapGVR 315

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 393195303 671 LVCGGNQvPRPGFFFEPTVF-TDVEDhmFIAK----EESFGPVMIISRFAD-GDLDAVLSR 725
Cdd:cd07129  316 VLAGGAA-AEGGNQAAPTLFkVDAAA--FLADpalqEEVFGPASLVVRYDDaAELLAVAEA 373

fmt

TIGR00460

methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ...

1-131

1.88e-16

Pssm-ID: 273088 [Multi-domain] Cd Length: 313 Bit Score: 80.91 E-value: 1.88e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303    1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDG------KADPLGLEAEKDGVPVFKYsrwraKGQALPDVVAKYQ 74
Cdd:TIGR00460   1 LRIVFFGTPTFSLPVLEELREDNFEVVGVVTQPDKPAgrgkklTPPPVKVLAEEKGIPVFQP-----EKQRQLEELPLVR 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 393195303   75 ALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAIHNWIRGNDKVPG 131
Cdd:TIGR00460  76 ELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTG 132

PRK11903

3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;

379-716

2.88e-13

3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;

Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 73.20 E-value: 2.88e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 379 ISARDRGRLMYRLADLMEQHQEELATI-----------EALDA-GAVYTLALKTHVGMSIQTFRYFAGwCDKIQGSTIPI 446
Cdd:PRK11903  60 LTYAQRAALLAAIVKVLQANRDAYYDIatansgttrndSAVDIdGGIFTLGYYAKLGAALGDARLLRD-GEAVQLGKDPA 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 447 NQARpnRNLTLTRkepvGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGI-PKGVVNVL 525
Cdd:PRK11903 139 FQGQ--HVLVPTR----GVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVV 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 526 PGSGSlvgqRLSDH---PDVrkIGFTGSTEVGKHIMKSCA-ISNVKKVSLElggkspliifADcDLNKAV---QMGMSSV 598
Cdd:PRK11903 213 CGSSA----GLLDHlqpFDV--VSFTGSAETAAVLRSHPAvVQRSVRVNVE----------AD-SLNSALlgpDAAPGSE 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 599 FFN-------------KGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHgV 665
Cdd:PRK11903 276 AFDlfvkevvremtvkSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAA-L 354

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 393195303 666 KEGATLVCGGNQV------PRPGFFFEPTVF--TDVEDHMFIAKEESFGPVMIISRFAD 716
Cdd:PRK11903 355 RAQAEVLFDGGGFalvdadPAVAACVGPTLLgaSDPDAATAVHDVEVFGPVATLLPYRD 413

FMT_core_like_4

cd08651

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...

2-144

1.27e-11

Pssm-ID: 187720 [Multi-domain] Cd Length: 180 Bit Score: 63.82 E-value: 1.27e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303   2 KIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADP----LGLEAEKDGVPVFKYSRWRAkgqalPDVVAKYQALG 77
Cdd:cd08651    1 RIVFIGCVEFSLIALEAILEAGGEVVGVITLDDSSSNNDSdyldLDSFARKNGIPYYKFTDIND-----EEIIEWIKEAN 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 393195303  78 AELNvlpFC---SQFIPMEIISAPRHGSIIYHPSLLPRHRGASAIHnW--IRGNDkvpgawteacEQKLTFF 144
Cdd:cd08651   76 PDII---FVfgwSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIP-WaiLLGLK----------ETASTFF 133

ALDH-like

cd07077

NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ...

391-638

2.70e-11

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: 66.09 E-value: 2.70e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 391 LADLMEQHQEELATIEALDAGA-VYTLALKTHVGMSIQ---------TFRYFAGWCDKIQGSTipinqaRPNRNLTLTRK 460
Cdd:cd07077   25 IANALYDTRQRLASEAVSERGAyIRSLIANWIAMMGCSesklyknidTERGITASVGHIQDVL------LPDNGETYVRA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 461 EPVGVCGIIIPWNYPLMMLSwKTAACLAAGNTVVIKPAQVTPLTALKFAELT---LKAGIPKGVVNVLPGSGSLVGQRLS 537
Cdd:cd07077   99 FPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTNRALALLFqaaDAAHGPKILVLYVPHPSDELAEELL 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 538 DHPDVRKIGFTGSTEVGKHIMKSCAISNVKKVSlelGGKSPLIIFADCDLNKAVQMGMSSVFFNkGENCIAAGRLFVEDS 617
Cdd:cd07077  178 SHPKIDLIVATGGRDAVDAAVKHSPHIPVIGFG---AGNSPVVVDETADEERASGSVHDSKFFD-QNACASEQNLYVVDD 253

                        250       260
                 ....*....|....*....|.
gi 393195303 618 IHDEFVRRVVEEVRKMKVGNP 638
Cdd:cd07077  254 VLDPLYEEFKLKLVVEGLKVP 274

ALDH_PAD-PaaZ

cd07127

Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ...

376-788

2.17e-10

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: 64.04 E-value: 2.17e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 376 WGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALK---THV---GMSIQTFRYFAgwCDKIQGSTIPINQA 449
Cdd:cd07127  100 WRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMMAFQaggPHAqdrGLEAVAYAWRE--MSRIPPTAEWEKPQ 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 450 RPNRNLTLTRK---EPVGV-----CGIIIPWN-YPLMMlswktaACLAAGNTVVIKP--AQVTPLT-ALKFAELTL-KAG 516
Cdd:cd07127  178 GKHDPLAMEKTftvVPRGValvigCSTFPTWNgYPGLF------ASLATGNPVIVKPhpAAILPLAiTVQVAREVLaEAG 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 517 I-PKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCaisNVKKVSLELGGKSPLIIFADCDLNKAVQ-MG 594
Cdd:cd07127  252 FdPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANA---RQAQVYTEKAGVNTVVVDSTDDLKAMLRnLA 328

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 595 MSSVFFNkGENCIAAGRLFV-EDSI--------HDEFVRRVVEEVRKMkVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGv 665
Cdd:cd07127  329 FSLSLYS-GQMCTTPQNIYVpRDGIqtddgrksFDEVAADLAAAIDGL-LADPARAAALLGAIQSPDTLARIAEARQLG- 405

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 666 kegatlvcggnQVPRPGFFFEPTVFTDVEDH--MFIA---------KEESFGPVMIISRFADGDLDAVLSRANATEFG-L 733
Cdd:cd07127  406 -----------EVLLASEAVAHPEFPDARVRtpLLLKldasdeaayAEERFGPIAFVVATDSTDHSIELARESVREHGaM 474

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 393195303 734 ASGVFTRD-------INKALYVSDKLQ---AGTVFVNTynktdvAAPFGGFKQSGfGKDLGEAAL 788
Cdd:cd07127  475 TVGVYSTDpevvervQEAALDAGVALSinlTGGVFVNQ------SAAFSDFHGTG-ANPAANAAL 532

ALDH_F20_ACDH_EutE-like

cd07081

Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ...

455-761

2.26e-10

Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.

Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 63.44 E-value: 2.26e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 455 LTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKP----AQVTPLTALKFAELTLKAGIPKGVVNVLPGSGS 530
Cdd:cd07081   88 GTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPENLIGWIDNPSI 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 531 LVGQRLSDHPDVRKIGFTGstevGKHIMKScAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAG 610
Cdd:cd07081  168 ELAQRLMKFPGIGLLLATG----GPAVVKA-AYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQ 242

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 611 RLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNH--HAHLVklmeycqhGVKEGATLVCGGNQVPRPG--FFFE 686
Cdd:cd07081  243 SVIVVDSVYDEVMRLFEGQGAYKLTAEELQQVQPVILKNGdvNRDIV--------GQDAYKIAAAAGLKVPQETriLIGE 314

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 687 PTVftdVEDHMFIAKEEsFGPVMIISR---FADGDLDAvLSRANATEFGLASGVFTRDIN---KALYVSDKLQAGTVFVN 760
Cdd:cd07081  315 VTS---LAEHEPFAHEK-LSPVLAMYRaanFADADAKA-LALKLEGGCGHTSAMYSDNIKaieNMNQFANAMKTSRFVKN 389


                 .
gi 393195303 761 T 761
Cdd:cd07081  390 G 390

ALDH_F12_P5CDH

cd07126

Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ...

462-762

3.10e-10

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: 63.28 E-value: 3.10e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 462 PVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDhPD 541
Cdd:cd07126  142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLE-AN 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 542 VRKIGFTGSTEVGKHImkscAISNVKKVSLELGGKSPLIIFADC-DLNKAVQMGMSSVFFNKGENCIAAGRLFV-EDSIH 619
Cdd:cd07126  221 PRMTLFTGSSKVAERL----ALELHGKVKLEDAGFDWKILGPDVsDVDYVAWQCDQDAYACSGQKCSAQSILFAhENWVQ 296

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 620 DEFVRRVVE--EVRKMK---VGNPLDRDTdhgpQNHHAHLVKLMEYcqhgvkEGATLVCGGNQVP-----------RPGF 683
Cdd:cd07126  297 AGILDKLKAlaEQRKLEdltIGPVLTWTT----ERILDHVDKLLAI------PGAKVLFGGKPLTnhsipsiygayEPTA 366

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 393195303 684 FFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDLDAVLSRANATEFGLASGVFTRDINkalyVSDKLQAGTVFVNTY 762
Cdd:cd07126  367 VFVPLEEIAIEENFELVTTEVFGPFQVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDIR----FLQEVLANTVNGTTY 441

Formyl_trans_C

pfam02911

Formyl transferase, C-terminal domain;

116-208

6.20e-10

Formyl transferase, C-terminal domain;

Pssm-ID: 460744 [Multi-domain] Cd Length: 99 Bit Score: 56.90 E-value: 6.20e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  116 ASAIHNWIRGNDKVPGAWTEACEQKLTFFNSTLntsglvpegdaLPIPGAHRPG--VVTKAGLILFGNDDKMLLVKNIQL 193
Cdd:pfam02911  15 AEEIHRLIRALDPWPGAYTFLNGKRVKLLKASV-----------LDQESGAAPGtiVTVDKGGLLVACGDGALLILELQL 83

                          90
                  ....*....|....*
gi 393195303  194 EDGKMILASNFFKGA 208
Cdd:pfam02911  84 EGKKPMSAEDFLNGF 98

ALDH_MaoC-N

cd07128

N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ...

473-741

3.44e-08

N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.

Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 56.89 E-value: 3.44e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 473 NYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGI-PKGVVNVLPGS-GSLVGQRlsDHPDVrkIGFTGS 550
Cdd:cd07128  155 NFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSvGDLLDHL--GEQDV--VAFTGS 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 551 TEVGKHIMkscAISNVKKVSLelggksPLIIFADcDLNKAV-----QMGMSSV-FFNK----------GENCIAAGRLFV 614
Cdd:cd07128  231 AATAAKLR---AHPNIVARSI------RFNAEAD-SLNAAIlgpdaTPGTPEFdLFVKevaremtvkaGQKCTAIRRAFV 300

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 615 EDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPqnhhahLVKLMEycQHGVKEG-------ATLVCGGNQVPRP------ 681
Cdd:cd07128  301 PEARVDAVIEALKARLAKVVVGDPRLEGVRMGP------LVSREQ--REDVRAAvatllaeAEVVFGGPDRFEVvgadae 372

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 393195303 682 -GFFFEPTVF--------TDVEDHmfiakeESFGPVMIIsrFADGDLDAVLSRANATEFGLASGVFTRD 741
Cdd:cd07128  373 kGAFFPPTLLlcddpdaaTAVHDV------EAFGPVATL--MPYDSLAEAIELAARGRGSLVASVVTND 433

ALDH_F20_ACDH

cd07122

Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ...

461-624

5.96e-07

Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.

Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 52.88 E-value: 5.96e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 461 EPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKP---AQVTPLTALKF-AELTLKAGIPKGVVNVLPGSGSLVGQRL 536
Cdd:cd07122   94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPhprAKKCSIEAAKImREAAVAAGAPEGLIQWIEEPSIELTQEL 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 537 SDHPDVRKIGFTGSTevgkhimkscaiSNVK------KVSLELG-GKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAA 609
Cdd:cd07122  174 MKHPDVDLILATGGP------------GMVKaayssgKPAIGVGpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASE 241

                        170
                 ....*....|....*
gi 393195303 610 GRLFVEDSIHDEFVR 624
Cdd:cd07122  242 QSVIVDDEIYDEVRA 256

FMT_core_ArnA_N

cd08644

ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...

1-122

6.31e-07

ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-L-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal dehydrogenase domain of ArnA catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O), while the N-terminal formyltransferase domain of ArnA catalyzes the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). This domain family represents the catalytic core of the N-terminal formyltransferase domain. The formyltransferase also contains a smaller C-terminal domain the may be involved in substrate binding. ArnA forms a hexameric structure, in which the dehydrogenase domains are arranged at the center of the particle with the transformylase domains on the outside of the particle.

Pssm-ID: 187713 [Multi-domain] Cd Length: 203 Bit Score: 50.81 E-value: 6.31e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303   1 MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKA---DPLGLEAEKDGVPVFkysrwRAKGQALPDVVAKYQALG 77
Cdd:cd08644    1 MKAVVFAYHEVGYRCLEALLAAGFEVVAVFTHTDNPGENiwfGSVAQLAREHGIPVF-----TPDDINHPEWVERLRALK 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 393195303  78 AELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAIhNW 122
Cdd:cd08644   76 PDLIFSFYYRHMISEDILEIARLGAFNLHGSLLPKYRGRAPL-NW 119

ALDH_EutE

cd07121

Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ...

455-629

7.87e-07

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: 52.24 E-value: 7.87e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 455 LTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKP----AQVTPLTALKFAELTLKAGIPKGVVNVL--PGS 528
Cdd:cd07121   90 LTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgaKKVSAYAVELINKAIAEAGGPDNLVVTVeePTI 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 529 GSLvgQRLSDHPDVRKIGFTGSTEVGKHIMKSCaisnvKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIA 608
Cdd:cd07121  170 ETT--NELMAHPDINLLVVTGGPAVVKAALSSG-----KKAIGAGAGNPPVVVDETADIEKAARDIVQGASFDNNLPCIA 242

                        170       180
                 ....*....|....*....|.
gi 393195303 609 AGRLFVEDSIHDEFVRRVVEE 629
Cdd:cd07121  243 EKEVIAVDSVADYLIAAMQRN 263

PRK15398

aldehyde dehydrogenase;

455-629

1.30e-06

aldehyde dehydrogenase;

Pssm-ID: 237956 Cd Length: 465 Bit Score: 51.83 E-value: 1.30e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 455 LTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKP----AQVTPLTALKFAELTLKAGIPKGVVNVL--PGS 528
Cdd:PRK15398 122 LTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPhpgaKKVSLRAIELLNEAIVAAGGPENLVVTVaePTI 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 529 GSLvgQRLSDHPDVRKIGFTGSTEVGKHIMKSCaisnvKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIA 608
Cdd:PRK15398 202 ETA--QRLMKHPGIALLVVTGGPAVVKAAMKSG-----KKAIGAGAGNPPVVVDETADIEKAARDIVKGASFDNNLPCIA 274

                        170       180
                 ....*....|....*....|.
gi 393195303 609 AGRLFVEDSIHDEFVRRVVEE 629
Cdd:PRK15398 275 EKEVIVVDSVADELMRLMEKN 295

Met_tRNA_FMT_C

cd08704

C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl ...

113-201

1.59e-06

C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl transferase and other proteins with diverse enzymatic activities. Proteins found in this family include methionyl-tRNA formyltransferase, ArnA, and 10-formyltetrahydrofolate dehydrogenase. Methionyl-tRNA formyltransferases constitute the majority of the family and also demonstrate greater sequence diversity. Although most proteins with formyltransferase activity contain the C-terminal domain, some formyltransferases ( for example, prokaryotic glycinamide ribonucleotide transformylase (GART)) only have the core catalytic domain, indicating that the C-terminal domain is not a requirement for catalytic activity and may be involved in substrate binding. For example, the C-terminal domain of methionyl-tRNA formyltransferase is involved in the tRNA binding.

Pssm-ID: 187732 [Multi-domain] Cd Length: 87 Bit Score: 46.76 E-value: 1.59e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 113 HRGASAIHNWIRGNDKVPGAWTEACEQKLTFFNSTlntsgLVPEGDALPIPGAhrpGVVTKAGLILFGNDDkMLLVKNIQ 192
Cdd:cd08704    8 SKSAEEIHNLIRALNPWPGAYTTLNGKRLKILKAE-----VLEESGEAAPGTI---LAVDKKGLLVACGDG-ALEILELQ 78


                 ....*....
gi 393195303 193 LEDGKMILA 201
Cdd:cd08704   79 PEGKKRMSA 87

PLN02285

methionyl-tRNA formyltransferase

25-131

7.68e-06

methionyl-tRNA formyltransferase

Pssm-ID: 215159 [Multi-domain] Cd Length: 334 Bit Score: 48.92 E-value: 7.68e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  25 EVVGVFTVPDKDGK------ADPLGLEAEKDGVP---VFKYSRWRAkgqalPDVVAKYQALGAELNVLPFCSQFIPMEII 95
Cdd:PLN02285  37 EVAAVVTQPPARRGrgrklmPSPVAQLALDRGFPpdlIFTPEKAGE-----EDFLSALRELQPDLCITAAYGNILPQKFL 111

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 393195303  96 SAPRHGSIIYHPSLLPRHRGASAIHNWIRGNDKVPG 131
Cdd:PLN02285 112 DIPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETG 147

FMT_core_HypX_N

cd08650

HypX protein, N-terminal hydrolase domain; The family represents the N-terminal hydrolase ...

13-128

3.16e-04

HypX protein, N-terminal hydrolase domain; The family represents the N-terminal hydrolase domain of HypX protein. HypX is involved in the maturation process of active [NiFe] hydrogenase. [NiFe] hydrogenases function in H2 metabolism in a variety of microorganisms, enabling them to use H2 as a source of reducing equivalent under aerobic and anaerobic conditions. [NiFe] hydrogenases consist of a large and a small subunit. The large subunit contains [NiFe] active site, which is synthesized as a precursor without the [NiFe] active site. This precursor then undergoes a complex post-translational maturation process that requires the presence of a number of accessory proteins. HypX has been shown to be involved in this maturation process and have been proposed to participate in the generation and transport of the CO and CN ligands. However, HypX is not present in all hydrogen-metabolizing bacteria. Furthermore, hypX deletion mutants have a reduced but detectable level of hydrogenase activity. Thus, HypX might not be a determining factor in the matur ation process. Members of this group have an N-terminal formyl transferase domain and a C-terminal enoyl-CoA hydratase/isomerase domain.

Pssm-ID: 187719 [Multi-domain] Cd Length: 151 Bit Score: 41.83 E-value: 3.16e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  13 QEVYCHLRKEGHEVVGVFTVPDkdgkadplglEAEKDGVPVFKysrwrakgqalPDVVakyqalgaelnVLPFCSQFIPM 92
Cdd:cd08650   15 QRAFLELRERGHEVSVEYALSD----------DEMREAVALFA-----------PDLI-----------ICPFLKKRIPE 62

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 393195303  93 EIISapRHGSIIYHPSlLPRHRGASAIHNWIRGNDK 128
Cdd:cd08650   63 EIWS--NYPCLIVHPG-IVGDRGPSSLDWAILEGEK 95

PRK06988

formyltransferase;

46-122

8.44e-04

formyltransferase;

Pssm-ID: 235902 [Multi-domain] Cd Length: 312 Bit Score: 42.37 E-value: 8.44e-04

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 393195303  46 AEKDGVPVFKYSrwrakGQALPDVVAKYQALGAELnVLPFCSQF-IPMEIISAPRHGSIIYHPSLLPRHRGASAIhNW 122
Cdd:PRK06988  51 AAEHGIPVITPA-----DPNDPELRAAVAAAAPDF-IFSFYYRHmIPVDLLALAPRGAYNMHGSLLPKYRGRVPV-NW 121

Arna_FMT_C

cd08702

C-terminal subdomain of the formyltransferase domain on ArnA, which modifies lipid A with ...

113-204

2.61e-03

C-terminal subdomain of the formyltransferase domain on ArnA, which modifies lipid A with 4-amino-4-deoxy-l-arabinose; Domain found in ArnA with similarity to the C-terminal domain of Formyltransferase. ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal domain of ArnA is a dehydrogenase domain that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the N-terminal domain is a formyltransferase domain that catalyzes the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). This domain family represents the C-terminal subdomain of the formyltransferase domain, downstream of the N-terminal subdomain containing the catalytic center. ArnA forms a hexameric structure (a dimer of trimers), in which the dehydrogenase domains are arranged at the center with the transformylase domains on the outside of the complex.

Pssm-ID: 187730 Cd Length: 92 Bit Score: 37.60 E-value: 2.61e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303 113 HRGASAIHNWIRG-NDKVPGAWTEACEQKLTFFNSTlntsgLVPEGDALPIPGAhrpgVVTKAG---LILFGndDKMLLV 188
Cdd:cd08702    8 RMSAREIYNLVRAvTKPYPGAFTFVGGQKIKIWKAR-----PVDDAFYNGEPGK----VLSVDGdplIVACG--DGALEI 76

                         90
                 ....*....|....*.
gi 393195303 189 KNIQLEDGKMILASNF 204
Cdd:cd08702   77 LEAELDGGLPLAGEQL 92

FMT_core_like_5

cd08823

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...

84-131

3.99e-03

Pssm-ID: 187725 [Multi-domain] Cd Length: 177 Bit Score: 38.97 E-value: 3.99e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 393195303  84 PFCSQF---IPMEIISAPRHGSIIYHPSLLPRHRGASAIHNWIRGNDKVPG 131
Cdd:cd08823   75 VVVFTFpyrIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETA 125

PurN

COG0299

Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...

25-132

6.73e-03

Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis

Pssm-ID: 440068 [Multi-domain] Cd Length: 202 Bit Score: 38.48 E-value: 6.73e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393195303  25 EVVGVFTvpdkDgKADPLGLE-AEKDGVPVF-----KYSRWRAKGQALPDVVAKYQAlgaELNVL---------PFCSQF 89
Cdd:COG0299   30 EIVLVIS----N-RPDAYGLErARAAGIPTFvldhkDFPSREAFDAALLEALDAYGP---DLVVLagfmriltpEFVRAF 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 393195303  90 ipmeiisaprHGSII-YHPSLLPRHRGASAIHNWIRGNDKVPGA 132
Cdd:COG0299  102 ----------PGRIInIHPSLLPAFPGLHAHRQALEAGVKVTGC 135

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