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Conserved domains on  [gi|15221042|ref|NP_175812|]
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aldehyde dehydrogenase 7B4 [Arabidopsis thaliana]

Protein Classification

aldehyde dehydrogenase family 7 protein( domain architecture ID 10791315)

aldehyde dehydrogenase family 7 protein is a NAD-dependent aldehyde dehydrogenase similar to Arabidopsis thaliana ALDH7B4 that appears to be an osmotic-stress-inducible aldehyde dehydrogenase (ALDH) gene encoding a turgor-responsive or stress-inducible ALDH

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02315 PLN02315
aldehyde dehydrogenase family 7 member
1-508 0e+00

aldehyde dehydrogenase family 7 member


:

Pssm-ID: 177949  Cd Length: 508  Bit Score: 1020.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042    1 MGSANNEYEFLSEIGLTSHNLGSYVAGKWQANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKR 80
Cdd:PLN02315   1 MGFARKEYEFLSEIGLSSRNLGCYVGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   81 GDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGV 160
Cdd:PLN02315  81 GEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  161 ITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLV 240
Cdd:PLN02315 161 ITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  241 SFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQL 320
Cdd:PLN02315 241 SFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  321 LTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPTIIEISADAAVVKEELFAP 400
Cdd:PLN02315 321 LTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVEISPDADVVKEELFGP 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  401 VLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSD 480
Cdd:PLN02315 401 VLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSD 480
                        490       500
                 ....*....|....*....|....*...
gi 15221042  481 SWKQYMRRSTCTINYGNELPLAQGINFG 508
Cdd:PLN02315 481 SWKQYMRRSTCTINYGNELPLAQGINFG 508
 
Name Accession Description Interval E-value
PLN02315 PLN02315
aldehyde dehydrogenase family 7 member
1-508 0e+00

aldehyde dehydrogenase family 7 member


Pssm-ID: 177949  Cd Length: 508  Bit Score: 1020.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042    1 MGSANNEYEFLSEIGLTSHNLGSYVAGKWQANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKR 80
Cdd:PLN02315   1 MGFARKEYEFLSEIGLSSRNLGCYVGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   81 GDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGV 160
Cdd:PLN02315  81 GEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  161 ITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLV 240
Cdd:PLN02315 161 ITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  241 SFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQL 320
Cdd:PLN02315 241 SFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  321 LTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPTIIEISADAAVVKEELFAP 400
Cdd:PLN02315 321 LTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVEISPDADVVKEELFGP 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  401 VLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSD 480
Cdd:PLN02315 401 VLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSD 480
                        490       500
                 ....*....|....*....|....*...
gi 15221042  481 SWKQYMRRSTCTINYGNELPLAQGINFG 508
Cdd:PLN02315 481 SWKQYMRRSTCTINYGNELPLAQGINFG 508
ALDH_F7_AASADH cd07130
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ...
24-496 0e+00

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: 913.52  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  24 YVAGKWQANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLS 103
Cdd:cd07130   2 VYDGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 104 LEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGN 183
Cdd:cd07130  82 LEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGN 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 184 CVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKT 263
Cdd:cd07130 162 VVVWKPSPTTPLTAIAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRS 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 264 LLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLH 343
Cdd:cd07130 242 LLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLH 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 344 TPESKKNFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPTIIEISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQG 423
Cdd:cd07130 322 TKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQG 401
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15221042 424 LSSSIFTRNPENIFRWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTCTINYG 496
Cdd:cd07130 402 LSSSIFTTDLRNAFRWLGPKGSDCGIVNVNIGTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 474
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
17-495 2.93e-171

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: 491.56  E-value: 2.93e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  17 TSHNLGSYVAGKWQ--ANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSK 94
Cdd:COG1012   2 TTPEYPLFIGGEWVaaASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEER 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  95 LDYLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWN 174
Cdd:COG1012  82 REELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 175 ACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLP-GAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQ 253
Cdd:COG1012 162 LAPALAAGNTVVLKPAEQTPLSALLLAELLEEA----GLPaGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIA 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 254 QTVNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPL 333
Cdd:COG1012 238 AAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPL 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 334 EKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGE-GNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFG 411
Cdd:COG1012 318 DPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGEgGYFVEPTVLAdVTPDMRIAREEIFGPVLSVIPFDDEE 397
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 412 EAVAINNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTC 491
Cdd:COG1012 398 EAIALANDTEYGLAASVFTRDLARARRVARRL--EAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTV 475

                ....
gi 15221042 492 TINY 495
Cdd:COG1012 476 TIRL 479
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
31-490 3.81e-166

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: 477.79  E-value: 3.81e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042    31 ANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKIL 110
Cdd:pfam00171   4 SESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   111 AEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSeRPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGA 190
Cdd:pfam00171  84 AEARGEVDRAIDVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   191 PTTPLITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSG 269
Cdd:pfam00171 163 ELTPLTALLLAELFEEA----GLPAGVLNVVTGsGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   270 NNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKK 349
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   350 NFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSI 428
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLAnVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGV 398
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15221042   429 FTRNPENIFRWIGPLgsDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRST 490
Cdd:pfam00171 399 FTSDLERALRVARRL--EAGMVWINDYTTGDADGLPFGGFKQSGFGREGGPYGLEEYTEVKT 458
D1pyr5carbox2 TIGR01237
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ...
36-495 4.06e-79

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: 256.33  E-value: 4.06e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042    36 VSTLNPAN-NQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGI 114
Cdd:TIGR01237  48 IVSINPCDkSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEAD 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   115 GEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTP 194
Cdd:TIGR01237 128 AEVAEAIDFMEYYARQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAP 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   195 LITIAMtklvAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSmvqqTVNARSGK----------T 263
Cdd:TIGR01237 208 VIAAKF----VEILEEAGLPKGVVQFVPGsGSEVGDYLVDHPKTSLITFTGSREVGT----RIFERAAKvqpgqkhlkrV 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   264 LLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLH 343
Cdd:TIGR01237 280 IAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVI 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   344 TPESKKNFEKGIEVIKSQgGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQ 422
Cdd:TIGR01237 360 DQKSFNKIMEYIEIGKAE-GRLVSGGCGDDSKGYFIGPTIFaDVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEY 438
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15221042   423 GLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAGS-DSWKQYMRRSTCTINY 495
Cdd:TIGR01237 439 GLTGGVISNNRDHINRAKAEF--EVGNLYFNRNITGAIVGyQPFGGFKMSGTDSKAGGpDYLALFMQAKTVTEMF 511
 
Name Accession Description Interval E-value
PLN02315 PLN02315
aldehyde dehydrogenase family 7 member
1-508 0e+00

aldehyde dehydrogenase family 7 member


Pssm-ID: 177949  Cd Length: 508  Bit Score: 1020.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042    1 MGSANNEYEFLSEIGLTSHNLGSYVAGKWQANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKR 80
Cdd:PLN02315   1 MGFARKEYEFLSEIGLSSRNLGCYVGGEWRANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   81 GDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGV 160
Cdd:PLN02315  81 GEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  161 ITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLV 240
Cdd:PLN02315 161 ITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  241 SFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQL 320
Cdd:PLN02315 241 SFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  321 LTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPTIIEISADAAVVKEELFAP 400
Cdd:PLN02315 321 LTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIVEISPDADVVKEELFGP 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  401 VLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSD 480
Cdd:PLN02315 401 VLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSD 480
                        490       500
                 ....*....|....*....|....*...
gi 15221042  481 SWKQYMRRSTCTINYGNELPLAQGINFG 508
Cdd:PLN02315 481 SWKQYMRRSTCTINYGNELPLAQGINFG 508
ALDH_F7_AASADH cd07130
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ...
24-496 0e+00

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: 913.52  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  24 YVAGKWQANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLS 103
Cdd:cd07130   2 VYDGEWGGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 104 LEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGN 183
Cdd:cd07130  82 LEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGN 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 184 CVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKT 263
Cdd:cd07130 162 VVVWKPSPTTPLTAIAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRS 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 264 LLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLH 343
Cdd:cd07130 242 LLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLH 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 344 TPESKKNFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPTIIEISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQG 423
Cdd:cd07130 322 TKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVEGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQG 401
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15221042 424 LSSSIFTRNPENIFRWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTCTINYG 496
Cdd:cd07130 402 LSSSIFTTDLRNAFRWLGPKGSDCGIVNVNIGTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 474
ALDH_F7_AASADH-like cd07086
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ...
23-496 0e+00

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: 849.93  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  23 SYVAGKWQANG-PLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRL 101
Cdd:cd07086   1 GVIGGEWVGSGgETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 102 LSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVC 181
Cdd:cd07086  81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 182 GNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSG 261
Cdd:cd07086 161 GNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 262 KTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGP 341
Cdd:cd07086 241 RVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGP 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 342 LHTPESKKNFEKGIEVIKSQGGKILTGGKAVEG--EGNFVEPTIIEISA-DAAVVKEELFAPVLYVLKFKSFGEAVAINN 418
Cdd:cd07086 321 LINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTdDARIVQEETFAPILYVIKFDSLEEAIAINN 400
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15221042 419 SVPQGLSSSIFTRNPENIFRWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTCTINYG 496
Cdd:cd07086 401 DVPQGLSSSIFTEDLREAFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCTINYS 478
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
17-495 2.93e-171

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: 491.56  E-value: 2.93e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  17 TSHNLGSYVAGKWQ--ANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSK 94
Cdd:COG1012   2 TTPEYPLFIGGEWVaaASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEER 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  95 LDYLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWN 174
Cdd:COG1012  82 REELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 175 ACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLP-GAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQ 253
Cdd:COG1012 162 LAPALAAGNTVVLKPAEQTPLSALLLAELLEEA----GLPaGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIA 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 254 QTVNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPL 333
Cdd:COG1012 238 AAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPL 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 334 EKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGE-GNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFG 411
Cdd:COG1012 318 DPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGEgGYFVEPTVLAdVTPDMRIAREEIFGPVLSVIPFDDEE 397
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 412 EAVAINNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTC 491
Cdd:COG1012 398 EAIALANDTEYGLAASVFTRDLARARRVARRL--EAGMVWINDGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTV 475

                ....
gi 15221042 492 TINY 495
Cdd:COG1012 476 TIRL 479
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
31-490 3.81e-166

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: 477.79  E-value: 3.81e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042    31 ANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKIL 110
Cdd:pfam00171   4 SESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   111 AEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSeRPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGA 190
Cdd:pfam00171  84 AEARGEVDRAIDVLRYYAGLARRLDGETLPS-DPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   191 PTTPLITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSG 269
Cdd:pfam00171 163 ELTPLTALLLAELFEEA----GLPAGVLNVVTGsGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   270 NNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKK 349
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   350 NFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSI 428
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLAnVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGV 398
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15221042   429 FTRNPENIFRWIGPLgsDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRST 490
Cdd:pfam00171 399 FTSDLERALRVARRL--EAGMVWINDYTTGDADGLPFGGFKQSGFGREGGPYGLEEYTEVKT 458
ALDH cd07078
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ...
59-493 2.15e-150

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: 436.64  E-value: 2.15e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  59 EQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSV 138
Cdd:cd07078   1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 139 IPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLeknnLPGAIF 218
Cdd:cd07078  81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAG----LPPGVL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 219 TAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAG 297
Cdd:cd07078 157 NVVTGdGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAG 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 298 QRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGE-G 376
Cdd:cd07078 237 QVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGkG 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 377 NFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIP 455
Cdd:cd07078 317 YFVPPTVLTdVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERL--EAGTVWINDY 394
                       410       420       430
                ....*....|....*....|....*....|....*...
gi 15221042 456 TNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTCTI 493
Cdd:cd07078 395 SVGAEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
ALDH_AldH-CAJ73105 cd07131
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ...
23-496 1.04e-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: 400.96  E-value: 1.04e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  23 SYVAGKW--QANGPLVSTLNPAN-NQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLG 99
Cdd:cd07131   1 NYIGGEWvdSASGETFDSRNPADlEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 100 RLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIAL 179
Cdd:cd07131  81 RLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPAL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 180 VCGNCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVnA 258
Cdd:cd07131 161 VCGNTVVFKPAEDTPACALKL----VELFAEAGLPPGVVNVVHGrGEEVGEALVEHPDVDVVSFTGSTEVGERIGETC-A 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 259 RSGKTL-LELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGT 337
Cdd:cd07131 236 RPNKRVaLEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEET 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 338 LLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEG----EGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGE 412
Cdd:cd07131 316 DMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGggyeKGYFVEPTVFTdVTPDMRIAQEEIFGPVVALIEVSSLEE 395
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 413 AVAINNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIPTNGAEIGGAFGGEKATGGG-REAGSDSWKQYMRRSTC 491
Cdd:cd07131 396 AIEIANDTEYGLSSAIYTEDVNKAFRARRDL--EAGITYVNAPTIGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAV 473

                ....*
gi 15221042 492 TINYG 496
Cdd:cd07131 474 YVDYS 478
ALDH_KGSADH-YcbD cd07097
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ...
23-480 2.33e-126

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: 376.97  E-value: 2.33e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  23 SYVAGKWQANGPLVSTLNPAN-NQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRL 101
Cdd:cd07097   3 NYIDGEWVAGGDGEENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 102 LSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVC 181
Cdd:cd07097  83 LTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAY 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 182 GNCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARS 260
Cdd:cd07097 163 GNTVVFKPAELTPASAWAL----VEILEEAGLPAGVFNLVMGsGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARG 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 261 GKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLG 340
Cdd:cd07097 239 ARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIG 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 341 PLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEG--EGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAIN 417
Cdd:cd07097 319 PVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRpdEGYYLAPALFAgVTNDMRIAREEIFGPVAAVIRVRDYDEALAIA 398
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15221042 418 NSVPQGLSSSIFTRNPENIFRWIGplGSDCGIVNVNIPTNGAEIGGAFGGEKATG-GGREAGSD 480
Cdd:cd07097 399 NDTEFGLSAGIVTTSLKHATHFKR--RVEAGVVMVNLPTAGVDYHVPFGGRKGSSyGPREQGEA 460
ALDH-SF cd06534
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
63-493 5.26e-116

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: 346.52  E-value: 5.26e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  63 KACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSE 142
Cdd:cd06534   1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 143 RPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLeknnLPGAIFTAMC 222
Cdd:cd06534  81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAG----LPPGVVNVVP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 223 G-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCT 301
Cdd:cd06534 157 GgGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 302 TCRRLLLHESVYDKVLEQLLTsykqvkignplekgtllgplhtpeskknfekgieviksqggkILTGgkavegegnfvep 381
Cdd:cd06534 237 AASRLLVHESIYDEFVEKLVT------------------------------------------VLVD------------- 261
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 382 tiieISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIPTNGAEI 461
Cdd:cd06534 262 ----VDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERL--RAGTVYINDSSIGVGP 335
                       410       420       430
                ....*....|....*....|....*....|..
gi 15221042 462 GGAFGGEKATGGGREAGSDSWKQYMRRSTCTI 493
Cdd:cd06534 336 EAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
ALDH_F5_SSADH_GabD cd07103
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ...
39-486 6.76e-110

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: 333.63  E-value: 6.76e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  39 LNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQ 118
Cdd:cd07103   2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 119 EVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITI 198
Cdd:cd07103  82 YAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSAL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 199 AMtklvAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQtvnaRSGKTL----LELSGNNAI 273
Cdd:cd07103 162 AL----AELAEEAGLPAGVLNVVTGsPAEIGEALCASPRVRKISFTGSTAVGKLLMA----QAADTVkrvsLELGGNAPF 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 274 IVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEK 353
Cdd:cd07103 234 IVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEA 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 354 GIEVIKSQGGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRN 432
Cdd:cd07103 314 LVEDAVAKGAKVLTGGKRLGLGGYFYEPTVLtDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRD 393
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15221042 433 PENIFRwigpLGS--DCGIVNVNIPTngaeIGGA---FGGEKATGGGREAGSDSWKQYM 486
Cdd:cd07103 394 LARAWR----VAEalEAGMVGINTGL----ISDAeapFGGVKESGLGREGGKEGLEEYL 444
ALDH_LactADH-AldA cd07088
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ...
24-490 2.33e-105

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: 322.68  E-value: 2.33e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  24 YVAGKW--QANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRL 101
Cdd:cd07088   1 YINGEFvpSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 102 LSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVC 181
Cdd:cd07088  81 IVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 182 GNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARS 260
Cdd:cd07088 161 GNTIVIKPSEETPLNALEFAELVDEA----GLPAGVLNIVTGrGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENI 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 261 GKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLG 340
Cdd:cd07088 237 TKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMG 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 341 PLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGE-GNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINN 418
Cdd:cd07088 317 PLVNEAALDKVEEMVERAVEAGATLLTGGKRPEGEkGYFYEPTVLTnVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELAN 396
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15221042 419 SVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIPtNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRST 490
Cdd:cd07088 397 DSEYGLTSYIYTENLNTAMRATNEL--EFGETYINRE-NFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKV 465
ALDH_DhaS cd07114
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ...
38-487 3.83e-102

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: 314.10  E-value: 3.83e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  38 TLNPANNQPIAQVVEASLEDYEQGLKACEEA--AKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIG 115
Cdd:cd07114   1 SINPATGEPWARVPEASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 116 EVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPL 195
Cdd:cd07114  81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 196 ITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAII 274
Cdd:cd07114 161 STLELAKLAEEA----GFPPGVVNVVTGfGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNI 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 275 VMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKG 354
Cdd:cd07114 237 VFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERY 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 355 IEVIKSQGGKILTGGKAVEGE----GNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIF 429
Cdd:cd07114 317 VARAREEGARVLTGGERPSGAdlgaGYFFEPTILAdVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIW 396
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15221042 430 TRNPENIFRWIGPLgsDCGIVNVNipTNGA-EIGGAFGGEKATGGGREAGSDSWKQYMR 487
Cdd:cd07114 397 TRDLARAHRVARAI--EAGTVWVN--TYRAlSPSSPFGGFKDSGIGRENGIEAIREYTQ 451
ALDH_PutA-P5CDH-RocA cd07124
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ...
24-495 1.44e-100

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: 311.85  E-value: 1.44e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  24 YVAGKWQANGPLVSTLNPAN-NQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLL 102
Cdd:cd07124  36 VIGGKEVRTEEKIESRNPADpSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWM 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 103 SLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLeMWNPLGIVGVITAFNFPCAVLGWNACIALVCG 182
Cdd:cd07124 116 VLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRY-VYRPLGVGAVISPWNFPLAILAGMTTAALVTG 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 183 NCVVWKGAPTTPLITiamtKLVAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGsmvqQTVNARSG 261
Cdd:cd07124 195 NTVVLKPAEDTPVIA----AKLVEILEEAGLPPGVVNFLPGpGEEVGDYLVEHPDVRFIAFTGSREVG----LRIYERAA 266
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 262 KT----------LLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGN 331
Cdd:cd07124 267 KVqpgqkwlkrvIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGD 346
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 332 PLEKGTLLGPLHTPESKKNFEKGIEVIKsQGGKILTGGK--AVEGEGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFK 408
Cdd:cd07124 347 PEDPEVYMGPVIDKGARDRIRRYIEIGK-SEGRLLLGGEvlELAAEGYFVQPTIFAdVPPDHRLAQEEIFGPVLAVIKAK 425
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 409 SFGEAVAINNSVPQGLSSSIFTRNPENI---FRWIgplgsDCGIVNVNIPTNGAEIG-GAFGGEKATG-GGREAGSDSWK 483
Cdd:cd07124 426 DFDEALEIANDTEYGLTGGVFSRSPEHLeraRREF-----EVGNLYANRKITGALVGrQPFGGFKMSGtGSKAGGPDYLL 500
                       490
                ....*....|..
gi 15221042 484 QYMRRSTCTINY 495
Cdd:cd07124 501 QFMQPKTVTENF 512
ALDH_BenzADH-like cd07104
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ...
57-485 3.17e-100

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: 308.31  E-value: 3.17e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  57 DYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNG 136
Cdd:cd07104   1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 137 SVIPSERPNHMMLEMWNPLGIVGVITAFNFPcAVLGWNA-CIALVCGNCVVWKGAPTTPlITIAMtkLVAEVLEKNNLPG 215
Cdd:cd07104  81 EILPSDVPGKESMVRRVPLGVVGVISPFNFP-LILAMRSvAPALALGNAVVLKPDSRTP-VTGGL--LIAEIFEEAGLPK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 216 AIFTAM-CGGAEIGEAIAKDTRIPLVSFTGSSRVGsmvqQTVNARSGKTL----LELSGNNAIIVMDDADIQLAARSVLF 290
Cdd:cd07104 157 GVLNVVpGGGSEIGDALVEHPRVRMISFTGSTAVG----RHIGELAGRHLkkvaLELGGNNPLIVLDDADLDLAVSAAAF 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 291 AAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGK 370
Cdd:cd07104 233 GAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 371 AvegEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRwIGpLGSDCGI 449
Cdd:cd07104 313 Y---EGLFYQPTVLsDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMA-FA-ERLETGM 387
                       410       420       430
                ....*....|....*....|....*....|....*.
gi 15221042 450 VNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWKQY 485
Cdd:cd07104 388 VHINDQTVNDEPHVPFGGVKASGGGRFGGPASLEEF 423
ALDH_VaniDH_like cd07150
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ...
39-481 6.74e-98

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: 303.10  E-value: 6.74e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  39 LNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQ 118
Cdd:cd07150   4 LNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETT 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 119 EVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPcAVLGWNA-CIALVCGNCVVWKGAPTTPLIT 197
Cdd:cd07150  84 FTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYP-LILATKKvAFALAAGNTVVLKPSEETPVIG 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 198 IamtkLVAEVLEKNNLPGAIFTAM-CGGAEIGEAIAKDTRIPLVSFTGSSRVGSMvqqtVNARSGKTL----LELSGNNA 272
Cdd:cd07150 163 L----KIAEIMEEAGLPKGVFNVVtGGGAEVGDELVDDPRVRMVTFTGSTAVGRE----IAEKAGRHLkkitLELGGKNP 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 273 IIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFE 352
Cdd:cd07150 235 LIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIK 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 353 KGIEVIKSQGGKILTGGKaveGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTR 431
Cdd:cd07150 315 RQVEDAVAKGAKLLTGGK---YDGNFYQPTVLtDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTN 391
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 15221042 432 NPENIFRWIgpLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDS 481
Cdd:cd07150 392 DLQRAFKLA--ERLESGMVHINDPTILDEAHVPFGGVKASGFGREGGEWS 439
ALDH_HMSADH_HapE cd07115
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ...
38-485 4.45e-95

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: 295.89  E-value: 4.45e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  38 TLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEG-IGE 116
Cdd:cd07115   1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAArRLD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 117 VQEVIDMCDFAVGLSRQLNGSVIPSERP--NHMMLEmwnPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTP 194
Cdd:cd07115  81 VPRAADTFRYYAGWADKIEGEVIPVRGPflNYTVRE---PVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 195 LITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAI 273
Cdd:cd07115 158 LSALRIAELMAEA----GFPAGVLNVVTGfGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSAN 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 274 IVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEK 353
Cdd:cd07115 234 IVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLD 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 354 GIEVIKSQGGKILTGGKAVEGEGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRN 432
Cdd:cd07115 314 YVDVGREEGARLLTGGKRPGARGFFVEPTIFAaVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRD 393
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|...
gi 15221042 433 PENIFRWIGPLGSdcGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQY 485
Cdd:cd07115 394 LGRAHRVAAALKA--GTVWINT-YNRFDPGSPFGGYKQSGFGREMGREALDEY 443
ALDH_AldA-AAD23400 cd07106
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ...
39-490 7.29e-95

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: 294.82  E-value: 7.29e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  39 LNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQ 118
Cdd:cd07106   2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 119 EVIDMCDFAVGLSRQlngSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITI 198
Cdd:cd07106  82 GAVAWLRYTASLDLP---DEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 199 AMTKLVAEVLeknnlPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGsmvqQTVNARSGKTL----LELSGNNAII 274
Cdd:cd07106 159 KLGELAQEVL-----PPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATG----KKVMASAAKTLkrvtLELGGNDAAI 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 275 VMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTpesKKNFEKG 354
Cdd:cd07106 230 VLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQN---KMQYDKV 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 355 ---IEVIKSQGGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFT 430
Cdd:cd07106 307 kelVEDAKAKGAKVLAGGEPLDGPGYFIPPTIVdDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWS 386
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15221042 431 RNPENIFRwigpLGS--DCGIVNVNiptNGAEIGGA--FGGEKATGGGREAGSDSWKQYMRRST 490
Cdd:cd07106 387 SDLERAEA----VARrlEAGTVWIN---THGALDPDapFGGHKQSGIGVEFGIEGLKEYTQTQV 443
ALDH_LactADH_F420-Bios cd07145
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ...
36-476 6.98e-93

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: 290.40  E-value: 6.98e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  36 VSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIG 115
Cdd:cd07145   1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 116 EVQEVIDMCDFAVGLSRQLNGSVIPSE----RPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAP 191
Cdd:cd07145  81 EVERTIRLFKLAAEEAKVLRGETIPVDayeyNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 192 TTPLITIAMTKLVAEVleknNLP-GAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGN 270
Cdd:cd07145 161 NTPLTAIELAKILEEA----GLPpGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGS 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 271 NAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKN 350
Cdd:cd07145 237 DPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVER 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 351 FEKGIEVIKSQGGKILTGGKAVegEGNFVEPTIIEI-SADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIF 429
Cdd:cd07145 317 MENLVNDAVEKGGKILYGGKRD--EGSFFPPTVLENdTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVF 394
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
gi 15221042 430 TRNPENIFRWIGPLgsDCGIVNVNIPTNGAEIGGAFGGEKATGGGRE 476
Cdd:cd07145 395 TNDINRALKVAREL--EAGGVVINDSTRFRWDNLPFGGFKKSGIGRE 439
ALDH_BADH-GbsA cd07119
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ...
24-486 3.92e-92

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: 289.21  E-value: 3.92e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  24 YVAGKWQ--ANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEA--AKIWMQVTAPKRGDIVRQIGDALRSKLDYLG 99
Cdd:cd07119   1 YIDGEWVeaASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 100 RLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSerPNHMM-LEMWNPLGIVGVITAFNFPCAVLGWNACIA 178
Cdd:cd07119  81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDV--PPHVIsRTVREPVGVCGLITPWNYPLLQAAWKLAPA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 179 LVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVN 257
Cdd:cd07119 159 LAAGNTVVIKPSEVTPLTTIALFELIEEA----GLPAGVVNLVTGsGATVGAELAESPDVDLVSFTGGTATGRSIMRAAA 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 258 ARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGT 337
Cdd:cd07119 235 GNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADT 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 338 LLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEG----EGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGE 412
Cdd:cd07119 315 EMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGdelaKGYFVEPTIFdDVDRTMRIVQEEIFGPVLTVERFDTEEE 394
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221042 413 AVAINNSVPQGLSSSIFTRNPENIFRWIGPLGSdcGIVNVN---IPTNGAEiggaFGGEKATGGGREAGSDSWKQYM 486
Cdd:cd07119 395 AIRLANDTPYGLAGAVWTKDIARANRVARRLRA--GTVWINdyhPYFAEAP----WGGYKQSGIGRELGPTGLEEYQ 465
PLN02278 PLN02278
succinic semialdehyde dehydrogenase
23-486 5.72e-92

succinic semialdehyde dehydrogenase


Pssm-ID: 215157 [Multi-domain]  Cd Length: 498  Bit Score: 289.28  E-value: 5.72e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   23 SYVAGKWQA--NGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGR 100
Cdd:PLN02278  27 GLIGGKWTDayDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQ 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  101 LLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALV 180
Cdd:PLN02278 107 LMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALA 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  181 CGNCVVWKGAPTTPLITIAmtklVAEVLEKNNLP-GAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNAR 259
Cdd:PLN02278 187 AGCTVVVKPSELTPLTALA----AAELALQAGIPpGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAAT 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  260 SGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLL 339
Cdd:PLN02278 263 VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQ 342
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  340 GPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINN 418
Cdd:PLN02278 343 GPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLgDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIAN 422
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15221042  419 SVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVN---IPTNGAeiggAFGGEKATGGGREAGSDSWKQYM 486
Cdd:PLN02278 423 DTEAGLAAYIFTRDLQRAWRVSEAL--EYGIVGVNeglISTEVA----PFGGVKQSGLGREGSKYGIDEYL 487
ALDH_y4uC cd07149
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ...
40-476 3.34e-91

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: 285.64  E-value: 3.34e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  40 NPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQE 119
Cdd:cd07149   5 SPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDR 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 120 VIDMCDFAVGLSRQLNGSVIP------SErpNHMMLEMWNPLGIVGVITAFNFP----CAVLGwnacIALVCGNCVVWKG 189
Cdd:cd07149  85 AIETLRLSAEEAKRLAGETIPfdaspgGE--GRIGFTIREPIGVVAAITPFNFPlnlvAHKVG----PAIAAGNAVVLKP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 190 APTTPLITIAMtklvAEVLEKNNLPGAIFTAMCGGAE-IGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARsgKTLLELS 268
Cdd:cd07149 159 ASQTPLSALKL----AELLLEAGLPKGALNVVTGSGEtVGDALVTDPRVRMISFTGSPAVGEAIARKAGLK--KVTLELG 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 269 GNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESK 348
Cdd:cd07149 233 SNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEA 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 349 KNFEKGIEVIKSQGGKILTGGKAvegEGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSS 427
Cdd:cd07149 313 ERIEEWVEEAVEGGARLLTGGKR---DGAILEPTVLTdVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAG 389
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 15221042 428 IFTRNPENIFRWIGPLgsDCGIVNVN-IPTNGAEiGGAFGGEKATGGGRE 476
Cdd:cd07149 390 VFTNDLQKALKAAREL--EVGGVMINdSSTFRVD-HMPYGGVKESGTGRE 436
ALDH_F8_HMSADH cd07093
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ...
38-481 1.58e-90

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: 284.07  E-value: 1.58e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  38 TLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGI-GE 116
Cdd:cd07093   1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 117 VQEVIDMCDFAVGLSRQLNGSVIPSErPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLi 196
Cdd:cd07093  81 IPRAAANFRFFADYILQLDGESYPQD-GGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPL- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 197 TIAMtklVAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVnARSGKTL-LELSGNNAII 274
Cdd:cd07093 159 TAWL---LAELANEAGLPPGVVNVVHGfGPEAGAALVAHPDVDLISFTGETATGRTIMRAA-APNLKPVsLELGGKNPNI 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 275 VMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKG 354
Cdd:cd07093 235 VFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGY 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 355 IEVIKSQGGKILTGGKAVE----GEGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIF 429
Cdd:cd07093 315 VELARAEGATILTGGGRPElpdlEGGYFVEPTVITgLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVW 394
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|..
gi 15221042 430 TRNPENIFRWIGPLgsDCGIVNVNIPtNGAEIGGAFGGEKATGGGREAGSDS 481
Cdd:cd07093 395 TRDLGRAHRVARRL--EAGTVWVNCW-LVRDLRTPFGGVKASGIGREGGDYS 443
ALDH_F1-2_Ald2-like cd07091
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...
22-493 8.00e-86

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: 272.55  E-value: 8.00e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  22 GSYVAGKW--QANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKI--WMQVTAPKRGDIVRQIGDALRSKLDY 97
Cdd:cd07091   5 GLFINNEFvdSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  98 LGRLLSLEMGKILAEGI-GEVQEVIDMCDFAVGLSRQLNGSVIPSERpNHMMLEMWNPLGIVGVITAFNFPCAVLGWNAC 176
Cdd:cd07091  85 LAALESLDNGKPLEESAkGDVALSIKCLRYYAGWADKIQGKTIPIDG-NFLAYTRREPIGVCGQIIPWNFPLLMLAWKLA 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 177 IALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQT 255
Cdd:cd07091 164 PALAAGNTVVLKPAEQTPLSALYLAELIKEA----GFPPGVVNIVPGfGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 256 VnARSG--KTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPL 333
Cdd:cd07091 240 A-AKSNlkKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPF 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 334 EKGTLLGPLhtpESKKNFEK---GIEVIKSQGGKILTGGKAVEGEGNFVEPTI-IEISADAAVVKEELFAPVLYVLKFKS 409
Cdd:cd07091 319 DPDTFQGPQ---VSKAQFDKilsYIESGKKEGATLLTGGERHGSKGYFIQPTVfTDVKDDMKIAKEEIFGPVVTILKFKT 395
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 410 FGEAVAINNSVPQGLSSSIFTRNPENIFR----------WIgplgsDC-GIVNVNIPtngaeiggaFGGEKATGGGREAG 478
Cdd:cd07091 396 EDEVIERANDTEYGLAAGVFTKDINKALRvsralkagtvWV-----NTyNVFDAAVP---------FGGFKQSGFGRELG 461
                       490
                ....*....|....*
gi 15221042 479 SDSWKQYMRRSTCTI 493
Cdd:cd07091 462 EEGLEEYTQVKAVTI 476
ALDH_PhdK-like cd07107
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ...
38-495 1.53e-85

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: 271.17  E-value: 1.53e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  38 TLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEV 117
Cdd:cd07107   1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 118 QEVIDMCDFAVGLSRQLNGSVIPSErPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLIT 197
Cdd:cd07107  81 MVAAALLDYFAGLVTELKGETIPVG-GRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 198 IAMTKLVAEVLEK---NNLPGaiftamcGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAII 274
Cdd:cd07107 160 LRLAELAREVLPPgvfNILPG-------DGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALI 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 275 VMDDADIQLAARSvlfAAVG----TAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKN 350
Cdd:cd07107 233 VFPDADPEAAADA---AVAGmnftWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDR 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 351 FEKGIEVIKSQGGKILTGGKAVEGE----GNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLS 425
Cdd:cd07107 310 VMHYIDSAKREGARLVTGGGRPEGPalegGFYVEPTVFaDVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLT 389
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 426 SSIFTRNPENIFRWIgpLGSDCGIVNVNiPTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTCTINY 495
Cdd:cd07107 390 AAIWTNDISQAHRTA--RRVEAGYVWIN-GSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
ALDH_HBenzADH cd07151
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ...
27-475 1.60e-85

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: 271.49  E-value: 1.60e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  27 GKWQANGP--LVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSL 104
Cdd:cd07151   1 GEWRDGTSerTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 105 EMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERP---NHMMLEmwnPLGIVGVITAFNFPCAVLGWNACIALVC 181
Cdd:cd07151  81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPgkeNRVYRE---PLGVVGVISPWNFPLHLSMRSVAPALAL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 182 GNCVVWKGAPTTPlITIAMtkLVAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDtRIP-LVSFTGSSRVGSMVQQTVNAR 259
Cdd:cd07151 158 GNAVVLKPASDTP-ITGGL--LLAKIFEEAGLPKGVLNVVVGaGSEIGDAFVEH-PVPrLISFTGSTPVGRHIGELAGRH 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 260 SGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLL 339
Cdd:cd07151 234 LKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVV 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 340 GPLHTPESKKNFEKGIEVIKSQGGKILTGGKAvegEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINN 418
Cdd:cd07151 314 GPLINESQVDGLLDKIEQAVEEGATLLVGGEA---EGNVLEPTVLsDVTNDMEIAREEIFGPVAPIIKADDEEEALELAN 390
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15221042 419 SVPQGLSSSIFTRNPE---NIFRWIgplgsDCGIVNVN-IPTNGaEIGGAFGGEKATGGGR 475
Cdd:cd07151 391 DTEYGLSGAVFTSDLErgvQFARRI-----DAGMTHINdQPVND-EPHVPFGGEKNSGLGR 445
ALDH_ABALDH-YdcW cd07092
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ...
39-487 3.25e-85

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: 270.35  E-value: 3.25e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  39 LNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGI-GEV 117
Cdd:cd07092   2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDEL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 118 QEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLIT 197
Cdd:cd07092  82 PGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 198 IAMTKLVAEVLeknnlPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIVM 276
Cdd:cd07092 162 LLLAELAAEVL-----PPGVVNVVCGgGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVF 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 277 DDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIE 356
Cdd:cd07092 237 DDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVE 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 357 VIKsQGGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPEN 435
Cdd:cd07092 317 RAP-AHARVLTGGRRAEGPGYFYEPTVVaGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGR 395
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|..
gi 15221042 436 IFRWIGPLGSDCGIVNVNIPTnGAEIggAFGGEKATGGGREAGSDSWKQYMR 487
Cdd:cd07092 396 AMRLSARLDFGTVWVNTHIPL-AAEM--PHGGFKQSGYGKDLSIYALEDYTR 444
ALDH_F9_TMBADH cd07090
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ...
38-496 9.87e-85

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: 269.17  E-value: 9.87e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  38 TLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEV 117
Cdd:cd07090   1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 118 QEVIDMCDFAVGLSRQLNGSVIP--------SERpnhmmlemwNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKG 189
Cdd:cd07090  81 DSSADCLEYYAGLAPTLSGEHVPlpggsfayTRR---------EPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKP 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 190 APTTPLITIAMtklvAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSG 269
Cdd:cd07090 152 SPFTPLTALLL----AEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGG 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 270 NNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKK 349
Cdd:cd07090 228 KSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLE 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 350 NFEKGIEVIKSQGGKILTGGKAVEGE-----GNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQG 423
Cdd:cd07090 308 KVLGYIESAKQEGAKVLCGGERVVPEdglenGFYVSPCVLtDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYG 387
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15221042 424 LSSSIFTRNPENIFRWIGPL--GSdCGIVNVNIptNGAEIggAFGGEKATGGGREAGSDSWKQYMRRSTCTINYG 496
Cdd:cd07090 388 LAAGVFTRDLQRAHRVIAQLqaGT-CWINTYNI--SPVEV--PFGGYKQSGFGRENGTAALEHYTQLKTVYVEMG 457
ALDH_F21_RNP123 cd07147
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ...
40-476 2.41e-84

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: 267.96  E-value: 2.41e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  40 NPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQE 119
Cdd:cd07147   5 NPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVAR 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 120 VIDMCDFAVGLSRQLNGSVIP---SERpNHMMLEMWN--PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTP 194
Cdd:cd07147  85 AIDTFRIAAEEATRIYGEVLPldiSAR-GEGRQGLVRrfPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTP 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 195 LITIamtkLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARsgKTLLELSGNNAII 274
Cdd:cd07147 164 LSAL----ILGEVLAETGLPKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGKK--KVVLELGGNAAVI 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 275 VMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKG 354
Cdd:cd07147 238 VDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGW 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 355 IEVIKSQGGKILTGGKAvegEGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNP 433
Cdd:cd07147 318 VNEAVDAGAKLLTGGKR---DGALLEPTILEdVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDL 394
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 15221042 434 ENIFRWIGPLgsDCGIVNVN-IPTNGAEiGGAFGGEKATGGGRE 476
Cdd:cd07147 395 EKALRAWDEL--EVGGVVINdVPTFRVD-HMPYGGVKDSGIGRE 435
ALDH_SSADH1_GabD1 cd07100
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ...
59-478 2.49e-84

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: 267.02  E-value: 2.49e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  59 EQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQEVIDMCDF-AVGLSRQLNGS 137
Cdd:cd07100   2 EAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYyAENAEAFLADE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 138 VIPSERPNHMMLemWNPLGIVGVITAFNFPCavlgWN----ACIALVCGNCVVWKGAPTTPLITIAMtklvAEVLEKNNL 213
Cdd:cd07100  82 PIETDAGKAYVR--YEPLGVVLGIMPWNFPF----WQvfrfAAPNLMAGNTVLLKHASNVPGCALAI----EELFREAGF 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 214 PGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAV 293
Cdd:cd07100 152 PEGVFQNLLIDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRL 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 294 GTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVE 373
Cdd:cd07100 232 QNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPD 311
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 374 GEGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNV 452
Cdd:cd07100 312 GPGAFYPPTVLTdVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRL--EAGMVFI 389
                       410       420
                ....*....|....*....|....*..
gi 15221042 453 NIPT-NGAEIggAFGGEKATGGGREAG 478
Cdd:cd07100 390 NGMVkSDPRL--PFGGVKRSGYGRELG 414
ALDH_MGR_2402 cd07108
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ...
38-481 2.26e-83

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: 265.76  E-value: 2.26e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  38 TLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKIL-AEGIGE 116
Cdd:cd07108   1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 117 VQEVIDMCDFAVGLSRQLNGSVIPSeRPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLI 196
Cdd:cd07108  81 AAVLADLFRYFGGLAGELKGETLPF-GPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 197 TIAMTKLVAEVLeknnlPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIV 275
Cdd:cd07108 160 VLLLAEILAQVL-----PAGVLNVITGyGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIV 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 276 MDDADIQLAARSVLFAAVGT-AGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKG 354
Cdd:cd07108 235 FPDADLDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGY 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 355 IEV-IKSQGGKILTGGKAVE----GEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSI 428
Cdd:cd07108 315 IDLgLSTSGATVLRGGPLPGegplADGFFVQPTIFsGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYV 394
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|...
gi 15221042 429 FTRNPENIFRWIGPLgsDCGIVNVNiPTNGAEIGGAFGGEKATGGGREAGSDS 481
Cdd:cd07108 395 WTRDLGRALRAAHAL--EAGWVQVN-QGGGQQPGQSYGGFKQSGLGREASLEG 444
ALDH_F6_MMSDH cd07085
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ...
21-455 4.20e-83

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: 265.53  E-value: 4.20e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  21 LGSYVAGKWQA--NGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYL 98
Cdd:cd07085   1 LKLFINGEWVEskTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  99 GRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIA 178
Cdd:cd07085  81 ARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 179 LVCGNCVVWKGAPTTPLITIamtkLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTvNA 258
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAM----RLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYER-AA 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 259 RSGKTLLELSG-NNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGT 337
Cdd:cd07085 236 ANGKRVQALGGaKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGA 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 338 LLGPLHTPESKKNFEKGIEVIKSQGGKILTGGK--AVEG--EGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGE 412
Cdd:cd07085 316 DMGPVISPAAKERIEGLIESGVEEGAKLVLDGRgvKVPGyeNGNFVGPTILDnVTPDMKIYKEEIFGPVLSIVRVDTLDE 395
                       410       420       430       440
                ....*....|....*....|....*....|....*....|...
gi 15221042 413 AVAINNSVPQGLSSSIFTRNPENIFRWIgpLGSDCGIVNVNIP 455
Cdd:cd07085 396 AIAIINANPYGNGAAIFTRSGAAARKFQ--REVDAGMVGINVP 436
ALDH_AAS00426 cd07109
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ...
39-493 1.88e-82

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: 262.94  E-value: 1.88e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  39 LNPANNQPIAQVVEASLEDYEQGLKACEEAAKI-WMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEV 117
Cdd:cd07109   2 FDPSTGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 118 QEVIDMCDFAVGLSRQLNGSVIPSErPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLIT 197
Cdd:cd07109  82 EAAARYFEYYGGAADKLHGETIPLG-PGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 198 IAMtklvAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIVM 276
Cdd:cd07109 161 LRL----AELAEEAGLPAGALNVVTGlGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVF 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 277 DDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEkGTLLGPLHTPESKKNFEKGIE 356
Cdd:cd07109 237 ADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVA 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 357 VIKSQGGKILTGGKAVEG---EGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRN 432
Cdd:cd07109 316 RARARGARIVAGGRIAEGapaGGYFVAPTLLdDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRD 395
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15221042 433 PENIFRWIGPLgsDCGIVNVNIPTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTCTI 493
Cdd:cd07109 396 GDRALRVARRL--RAGQVFVNNYGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
ALDH_PhpJ cd07146
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ...
39-493 2.64e-82

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: 262.68  E-value: 2.64e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  39 LNPANNQPIAQVvEASLEDyeQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQ 118
Cdd:cd07146   4 RNPYTGEVVGTV-PAGTEE--ALREALALAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 119 EVIDMCDFAVGLSRQLNGSVIPSERPNH----MMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTP 194
Cdd:cd07146  81 RAADVLRFAAAEALRDDGESFSCDLTANgkarKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 195 LITIAMtklvAEVLEKNNLPGAIFTAMCGG-AEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARsgKTLLELSGNNAI 273
Cdd:cd07146 161 LSAIYL----ADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYK--RQLLELGGNDPL 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 274 IVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEK 353
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 354 GIEVIKSQGGKILTGGkavEGEGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRN 432
Cdd:cd07146 315 RVEEAIAQGARVLLGN---QRQGALYAPTVLDhVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTND 391
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15221042 433 PENIFRWIGPLgsDCGIVNVNiptngaEIGG------AFGGEKATG-GGREAGSDSWKQYMRRSTCTI 493
Cdd:cd07146 392 LDTIKRLVERL--DVGTVNVN------EVPGfrselsPFGGVKDSGlGGKEGVREAMKEMTNVKTYSL 451
gabD PRK11241
NADP-dependent succinate-semialdehyde dehydrogenase I;
23-486 2.84e-81

NADP-dependent succinate-semialdehyde dehydrogenase I;


Pssm-ID: 183050 [Multi-domain]  Cd Length: 482  Bit Score: 260.99  E-value: 2.84e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   23 SYVAGKW--QANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGR 100
Cdd:PRK11241  13 ALINGEWldANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLAR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  101 LLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALV 180
Cdd:PRK11241  93 LMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALA 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  181 CGNCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTAMCGGA-EIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNAR 259
Cdd:PRK11241 173 AGCTMVLKPASQTPFSALAL----AELAIRAGIPAGVFNVVTGSAgAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKD 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  260 SGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLL 339
Cdd:PRK11241 249 IKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTI 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  340 GPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPTI-IEISADAAVVKEELFAPVLYVLKFKSFGEAVAINN 418
Cdd:PRK11241 329 GPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTIlVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQAN 408
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15221042  419 SVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIPTNGAEIgGAFGGEKATGGGREAGSDSWKQYM 486
Cdd:PRK11241 409 DTEFGLAAYFYARDLSRVFRVGEAL--EYGIVGINTGIISNEV-APFGGIKASGLGREGSKYGIEDYL 473
ALDH_F10_BADH cd07110
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ...
38-478 8.87e-81

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: 258.82  E-value: 8.87e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  38 TLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEV 117
Cdd:cd07110   1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 118 QEVIDMCDFAVGLSRQLN---GSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTP 194
Cdd:cd07110  81 DDVAGCFEYYADLAEQLDakaERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 195 LITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAI 273
Cdd:cd07110 161 LTELELAEIAAEA----GLPPGVLNVVTGtGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPI 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 274 IVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEK 353
Cdd:cd07110 237 IVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLS 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 354 GIEVIKSQGGKILTGGKAVE--GEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFT 430
Cdd:cd07110 317 FIARGKEEGARLLCGGRRPAhlEKGYFIAPTVFaDVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVIS 396
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*...
gi 15221042 431 RNPENIFRWIGPLgsDCGIVNVNIPtNGAEIGGAFGGEKATGGGREAG 478
Cdd:cd07110 397 RDAERCDRVAEAL--EAGIVWINCS-QPCFPQAPWGGYKRSGIGRELG 441
ALDH_SNDH cd07118
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ...
39-493 9.73e-81

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: 258.81  E-value: 9.73e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  39 LNPANNQPIAQVVEASLEDYEQGLKACEEA--AKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGE 116
Cdd:cd07118   2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 117 VQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPli 196
Cdd:cd07118  82 IEGAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTS-- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 197 tiAMTKLVAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIV 275
Cdd:cd07118 160 --GTTLMLAELLIEAGLPAGVVNIVTGyGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIV 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 276 MDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGI 355
Cdd:cd07118 238 FADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYV 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 356 EVIKSQGGKILTGGKAVE-GEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNP 433
Cdd:cd07118 318 DAGRAEGATLLLGGERLAsAAGLFYQPTIFtDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDI 397
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15221042 434 ENIFRWIGPLGSdcGIVNVN-IPTNGAEIggAFGGEKATGGGREAGSDSWKQYMRRSTCTI 493
Cdd:cd07118 398 DTALTVARRIRA--GTVWVNtFLDGSPEL--PFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
ALDH_F21_LactADH-like cd07094
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ...
40-476 2.06e-80

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: 257.75  E-value: 2.06e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  40 NPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQE 119
Cdd:cd07094   5 NPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDR 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 120 VIDMCDFAVGLSRQLNGSVIPSE----RPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPL 195
Cdd:cd07094  85 AIDTLRLAAEEAERIRGEEIPLDatqgSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPL 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 196 ITIAMtklvAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVqqTVNARSGKTLLELSGNNAII 274
Cdd:cd07094 165 SALEL----AKILVEAGVPEGVLQVVTGeREVLGDAFAADERVAMLSFTGSAAVGEAL--RANAGGKRIALELGGNAPVI 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 275 VMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKG 354
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 355 IEVIKSQGGKILTGGkavEGEGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNP 433
Cdd:cd07094 319 VEEAVEAGARLLCGG---ERDGALFKPTVLEdVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDL 395
                       410       420       430       440
                ....*....|....*....|....*....|....*....|...
gi 15221042 434 ENIFRWIGPLgsDCGIVNVNIPTNGAEIGGAFGGEKATGGGRE 476
Cdd:cd07094 396 NVAFKAAEKL--EVGGVMVNDSSAFRTDWMPFGGVKESGVGRE 436
D1pyr5carbox2 TIGR01237
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ...
36-495 4.06e-79

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: 256.33  E-value: 4.06e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042    36 VSTLNPAN-NQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGI 114
Cdd:TIGR01237  48 IVSINPCDkSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEAD 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   115 GEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTP 194
Cdd:TIGR01237 128 AEVAEAIDFMEYYARQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAP 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   195 LITIAMtklvAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSmvqqTVNARSGK----------T 263
Cdd:TIGR01237 208 VIAAKF----VEILEEAGLPKGVVQFVPGsGSEVGDYLVDHPKTSLITFTGSREVGT----RIFERAAKvqpgqkhlkrV 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   264 LLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLH 343
Cdd:TIGR01237 280 IAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVI 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   344 TPESKKNFEKGIEVIKSQgGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQ 422
Cdd:TIGR01237 360 DQKSFNKIMEYIEIGKAE-GRLVSGGCGDDSKGYFIGPTIFaDVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEY 438
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15221042   423 GLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAGS-DSWKQYMRRSTCTINY 495
Cdd:TIGR01237 439 GLTGGVISNNRDHINRAKAEF--EVGNLYFNRNITGAIVGyQPFGGFKMSGTDSKAGGpDYLALFMQAKTVTEMF 511
PRK03137 PRK03137
1-pyrroline-5-carboxylate dehydrogenase; Provisional
35-438 5.69e-79

1-pyrroline-5-carboxylate dehydrogenase; Provisional


Pssm-ID: 179543  Cd Length: 514  Bit Score: 256.02  E-value: 5.69e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   35 LVSTlNPAN-NQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEG 113
Cdd:PRK03137  52 IVSI-NPANkSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEA 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  114 IGEVQEVIDMCDFavgLSRQ---LNGSVIPSERP---NHMMLEmwnPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVW 187
Cdd:PRK03137 131 DADTAEAIDFLEY---YARQmlkLADGKPVESRPgehNRYFYI---PLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLL 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  188 KGAPTTPLITiamTKLVaEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSmvqqTVNARSGKT--- 263
Cdd:PRK03137 205 KPASDTPVIA---AKFV-EVLEEAGLPAGVVNFVPGsGSEVGDYLVDHPKTRFITFTGSREVGL----RIYERAAKVqpg 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  264 -------LLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPlEKG 336
Cdd:PRK03137 277 qiwlkrvIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNP-EDN 355
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  337 TLLGPLHTPESKKNFEKGIEVIKsQGGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVA 415
Cdd:PRK03137 356 AYMGPVINQASFDKIMSYIEIGK-EEGRLVLGGEGDDSKGYFIQPTIFaDVDPKARIMQEEIFGPVVAFIKAKDFDHALE 434
                        410       420
                 ....*....|....*....|...
gi 15221042  416 INNSVPQGLSSSIFTRNPENIFR 438
Cdd:PRK03137 435 IANNTEYGLTGAVISNNREHLEK 457
ALDH_CddD-AldA-like cd07089
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ...
39-486 2.44e-78

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: 252.55  E-value: 2.44e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  39 LNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAP-KRGDIVRQIGDALRSKLDYLGRLLSLEMGKILA-EGIGE 116
Cdd:cd07089   2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDWSTDAeERARCLRQLHEALEARKEELRALLVAEVGAPVMtARAMQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 117 VQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEM----WNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPT 192
Cdd:cd07089  82 VDGPIGHLRYFADLADSFPWEFDLPVPALRGGPGRrvvrREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPD 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 193 TPLITIAMTKLVAEVleknNLPGAIFTAMCGG-AEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNN 271
Cdd:cd07089 162 TPLSALLLGEIIAET----DLPAGVVNVVTGSdNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKS 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 272 AIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNF 351
Cdd:cd07089 238 ANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRV 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 352 EKGIEVIKSQGGKILTGGKAVEG--EGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSI 428
Cdd:cd07089 318 EGYIARGRDEGARLVTGGGRPAGldKGFYVEPTLFaDVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGV 397
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15221042 429 FTRNPENIFRWIGPLgsDCGIVNVNiPTNGAEIGGAFGGEKATGGGREAGSDSWKQYM 486
Cdd:cd07089 398 WSADVDRAYRVARRI--RTGSVGIN-GGGGYGPDAPFGGYKQSGLGRENGIEGLEEFL 452
ALDH_BenzADH cd07152
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ...
47-486 3.46e-78

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: 251.83  E-value: 3.46e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  47 IAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQEVIDMCDF 126
Cdd:cd07152   4 LGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 127 AVGLSRQLNGSVIPSErPNHMMLEMWNPLGIVGVITAFNFPCaVLGWNACI-ALVCGNCVVWKGAPTTPlitIAMTKLVA 205
Cdd:cd07152  84 AAGLPTQPQGEILPSA-PGRLSLARRVPLGVVGVISPFNFPL-ILAMRSVApALALGNAVVLKPDPRTP---VSGGVVIA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 206 EVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGsmvqQTVNARSGKTL----LELSGNNAIIVMDDADI 281
Cdd:cd07152 159 RLFEEAGLPAGVLHVLPGGADAGEALVEDPNVAMISFTGSTAVG----RKVGEAAGRHLkkvsLELGGKNALIVLDDADL 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 282 QLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQ 361
Cdd:cd07152 235 DLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAA 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 362 GGKILTGGKAvegEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRwi 440
Cdd:cd07152 315 GARLEAGGTY---DGLFYRPTVLsGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMA-- 389
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*....
gi 15221042 441 gpLGS--DCGIVNVNIPTNGAEIGGAFGGEKATG-GGREAGSDSWKQYM 486
Cdd:cd07152 390 --LADrlRTGMLHINDQTVNDEPHNPFGGMGASGnGSRFGGPANWEEFT 436
ALDH_AldA_AN0554 cd07143
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ...
15-494 5.27e-78

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: 252.45  E-value: 5.27e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  15 GLTSHNLGSYVAGKW--QANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKI-W-MQVTAPKRGDIVRQIGDA 90
Cdd:cd07143   1 GKYEQPTGLFINGEFvdSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETdWgLKVSGSKRGRCLSKLADL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  91 LRSKLDYLGRLLSLEMGK-ILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSErPNHMMLEMWNPLGIVGVITAFNFPCA 169
Cdd:cd07143  81 MERNLDYLASIEALDNGKtFGTAKRVDVQASADTFRYYGGWADKIHGQVIETD-IKKLTYTRHEPIGVCGQIIPWNFPLL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 170 VLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRV 248
Cdd:cd07143 160 MCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEA----GFPPGVINVVSGyGRTCGNAISSHMDIDKVAFTGSTLV 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 249 GSMVQQTVnARSG--KTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQ 326
Cdd:cd07143 236 GRKVMEAA-AKSNlkKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKK 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 327 VKIGNPLEKGTLLGPlhtPESKKNFEKGIEVI---KSQGGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVL 402
Cdd:cd07143 315 LKVGDPFAEDTFQGP---QVSQIQYERIMSYIesgKAEGATVETGGKRHGNEGYFIEPTIFtDVTEDMKIVKEEIFGPVV 391
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 403 YVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSW 482
Cdd:cd07143 392 AVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANAL--KAGTVWVNC-YNLLHHQVPFGGYKQSGIGRELGEYAL 468
                       490
                ....*....|..
gi 15221042 483 KQYMRRSTCTIN 494
Cdd:cd07143 469 ENYTQIKAVHIN 480
ALDH_AldA-Rv0768 cd07139
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ...
24-478 2.31e-77

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: 250.18  E-value: 2.31e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  24 YVAGKWQA--NGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEA--AKIWMQVTAPKRGDIVRQIGDALRSKLDYLG 99
Cdd:cd07139   2 FIGGRWVApsGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 100 RLLSLEMGK-ILAEGIGEVQEVIDMCDFAVGLSRQLNgsvIPSERPNHMM---LEMWNPLGIVGVITAFNFPCAVLGWNA 175
Cdd:cd07139  82 RLWTAENGMpISWSRRAQGPGPAALLRYYAALARDFP---FEERRPGSGGghvLVRREPVGVVAAIVPWNAPLFLAALKI 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 176 CIALVCGNCVVWKGAPTTPLitiaMTKLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQT 255
Cdd:cd07139 159 APALAAGCTVVLKPSPETPL----DAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAV 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 256 VNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEK 335
Cdd:cd07139 235 CGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDP 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 336 GTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEG--EGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGE 412
Cdd:cd07139 315 ATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGldRGWFVEPTLFaDVDNDMRIAQEEIFGPVLSVIPYDDEDD 394
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15221042 413 AVAINNSVPQGLSSSIFTRNPE---NIFRWIgplgsDCGIVNVNIPTngAEIGGAFGGEKATGGGREAG 478
Cdd:cd07139 395 AVRIANDSDYGLSGSVWTADVErglAVARRI-----RTGTVGVNGFR--LDFGAPFGGFKQSGIGREGG 456
ALDH_ACDHII_AcoD-like cd07559
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ...
22-476 2.37e-76

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: 248.03  E-value: 2.37e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  22 GSYVAGKWQA--NGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLG 99
Cdd:cd07559   2 DNFINGEWVApsKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 100 RLLSLEMGKILAEGIG-EVQEVIDMCDFAVGLSRQLNGSVIPSERpNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIA 178
Cdd:cd07559  82 VAETLDNGKPIRETLAaDIPLAIDHFRYFAGVIRAQEGSLSEIDE-DTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 179 LVCGNCVVWKGAPTTPLITIAMTKLVAEVLEK---NNLPGAiftamcgGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQT 255
Cdd:cd07559 161 LAAGNTVVLKPASQTPLSILVLMELIGDLLPKgvvNVVTGF-------GSEAGKPLASHPRIAKLAFTGSTTVGRLIMQY 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 256 VNARSGKTLLELSGNNAIIVMDDA-----DIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIG 330
Cdd:cd07559 234 AAENLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVG 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 331 NPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEG----EGNFVEPTIIE-ISADAAVVKEELFAPVLYVL 405
Cdd:cd07559 314 NPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLggldKGYFYEPTLIKgGNNDMRIFQEEIFGPVLAVI 393
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15221042 406 KFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWigPLGSDCGIVNVN----IPTngaeiGGAFGGEKATGGGRE 476
Cdd:cd07559 394 TFKDEEEAIAIANDTEYGLGGGVWTRDINRALRV--ARGIQTGRVWVNcyhqYPA-----HAPFGGYKKSGIGRE 461
ALDH_SGSD_AstD cd07095
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ...
57-478 4.00e-76

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: 246.03  E-value: 4.00e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  57 DYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNG 136
Cdd:cd07095   1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDISIKAYHERTG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 137 SViPSERPNHMMLEMWNPLGIVGVITAFNFPcAVLGwNACI--ALVCGNCVVWKGAPTTPlitiAMTKLVAEVLEKNNLP 214
Cdd:cd07095  81 ER-ATPMAQGRAVLRHRPHGVMAVFGPFNFP-GHLP-NGHIvpALLAGNTVVFKPSELTP----AVAELMVELWEEAGLP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 215 GAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTL-LELSGNNAIIVMDDADIQLAARSVLFAAV 293
Cdd:cd07095 154 PGVLNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILaLEMGGNNPLVVWDVADIDAAAYLIVQSAF 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 294 GTAGQRCTTCRRLLLHES-VYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAV 372
Cdd:cd07095 234 LTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERL 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 373 EGEGNFVEPTIIEISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPEnIFRWIGpLGSDCGIVNV 452
Cdd:cd07095 314 VAGTAFLSPGIIDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEA-LFERFL-ARIRAGIVNW 391
                       410       420
                ....*....|....*....|....*.
gi 15221042 453 NIPTNGAEIGGAFGGEKATGGGREAG 478
Cdd:cd07095 392 NRPTTGASSTAPFGGVGLSGNHRPSA 417
ALDH_PutA-P5CDH cd07125
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ...
39-494 6.61e-76

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: 247.88  E-value: 6.61e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  39 LNPA-NNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEV 117
Cdd:cd07125  51 IDPAdHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEV 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 118 QEVIDMCDFAVGLSRQLNGSVI---PSERPNHMMLEmwnPLGIVGVITAFNFPCAV-LGWNACiALVCGNCVVWKGAPTT 193
Cdd:cd07125 131 REAIDFCRYYAAQARELFSDPElpgPTGELNGLELH---GRGVFVCISPWNFPLAIfTGQIAA-ALAAGNTVIAKPAEQT 206
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 194 PLITIAMTKLV------AEVLekNNLPGAiftamcgGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLL-- 265
Cdd:cd07125 207 PLIAARAVELLheagvpRDVL--QLVPGD-------GEEIGEALVAHPRIDGVIFTGSTETAKLINRALAERDGPILPli 277
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 266 -ELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHT 344
Cdd:cd07125 278 aETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLID 357
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 345 PESKKNFEKGIEVIKSQgGKILTGGKAVEGEGNFVEPTIIEISADaAVVKEELFAPVLYVLKFKSF--GEAVAINNSVPQ 422
Cdd:cd07125 358 KPAGKLLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGIIEIVGI-FDLTTEVFGPILHVIRFKAEdlDEAIEDINATGY 435
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15221042 423 GLSSSIFTRNPENIFRWIGPLGSdcGIVNVNIPTNGAeIGGA--FGGEKATGGGREAGSDSW-KQYMRRSTCTIN 494
Cdd:cd07125 436 GLTLGIHSRDEREIEYWRERVEA--GNLYINRNITGA-IVGRqpFGGWGLSGTGPKAGGPNYlLRFGNEKTVSLN 507
ALDH_F2BC cd07142
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ...
24-487 4.93e-75

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: 244.33  E-value: 4.93e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  24 YVAGKW--QANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKI--WMQVTAPKRGDIVRQIGDALRSKLDYLG 99
Cdd:cd07142   7 FINGQFvdAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADELA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 100 RLLSLEMGKILAEG-IGEVQEVIDMCDFAVGLSRQLNGSVIPSERPnHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIA 178
Cdd:cd07142  87 ALETWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGMTLPADGP-HHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPA 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 179 LVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVN 257
Cdd:cd07142 166 LACGNTIVLKPAEQTPLSALLAAKLAAEA----GLPDGVLNIVTGfGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAA 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 258 ARSGKTL-LELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKG 336
Cdd:cd07142 242 KSNLKPVtLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKG 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 337 TLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVA 415
Cdd:cd07142 322 VEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFsDVKDDMKIARDEIFGPVQSILKFKTVDEVIK 401
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15221042 416 INNSVPQGLSSSIFTRNPENIFRWIGPLGSdcGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQYMR 487
Cdd:cd07142 402 RANNSKYGLAAGVFSKNIDTANTLSRALKA--GTVWVNC-YDVFDASIPFGGYKMSGIGREKGIYALNNYLQ 470
PRK13473 PRK13473
aminobutyraldehyde dehydrogenase;
22-432 5.64e-75

aminobutyraldehyde dehydrogenase;


Pssm-ID: 237391  Cd Length: 475  Bit Score: 244.43  E-value: 5.64e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   22 GSYVAGkwqaNGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRL 101
Cdd:PRK13473   9 GELVAG----EGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  102 LSLEMGK-ILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALV 180
Cdd:PRK13473  85 ESLNCGKpLHLALNDEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  181 CGNCVVWKGAPTTPLITIAMTKLVAEVLeknnlPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVnAR 259
Cdd:PRK13473 165 AGNTVVLKPSEITPLTALKLAELAADIL-----PPGVLNVVTGrGATVGDALVGHPKVRMVSLTGSIATGKHVLSAA-AD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  260 SGK-TLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTL 338
Cdd:PRK13473 239 SVKrTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTE 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  339 LGPLHTPESKKNFEKGIEVIKSQG-GKILTGGKAVEGEGNFVEPTIIeisADAA----VVKEELFAPVLYVLKFKSFGEA 413
Cdd:PRK13473 319 LGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLL---AGARqddeIVQREVFGPVVSVTPFDDEDQA 395
                        410
                 ....*....|....*....
gi 15221042  414 VAINNSVPQGLSSSIFTRN 432
Cdd:PRK13473 396 VRWANDSDYGLASSVWTRD 414
ALDH_ALD2-YMR170C cd07144
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ...
21-494 7.71e-75

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: 244.24  E-value: 7.71e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  21 LGSYVAGKW--QANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAK-IWMQVTAPKRGDIVRQIGDALRSKLDY 97
Cdd:cd07144   8 TGLFINNEFvkSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFEsWWSKVTGEERGELLDKLADLVEKNRDL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  98 LGRLLSLEMGKIL-AEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSErPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNAC 176
Cdd:cd07144  88 LAAIEALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIPTS-PNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLA 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 177 IALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQT 255
Cdd:cd07144 167 PALAAGNTVVIKPAENTPLSLLYFANLVKEA----GFPPGVVNIIPGyGAVAGSALAEHPDVDKIAFTGSTATGRLVMKA 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 256 VNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQV-KIGNPLE 334
Cdd:cd07144 243 AAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNyKVGSPFD 322
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 335 KGTLLGPLhtpESKKNFEK---GIEVIKSQGGKILTGG---KAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKF 407
Cdd:cd07144 323 DDTVVGPQ---VSKTQYDRvlsYIEKGKKEGAKLVYGGekaPEGLGKGYFIPPTIFtDVPQDMRIVKEEIFGPVVVISKF 399
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 408 KSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLGSdcGIVNVNiPTNGAEIGGAFGGEKATGGGREAGSDSWKQYMR 487
Cdd:cd07144 400 KTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEA--GMVWIN-SSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQ 476

                ....*..
gi 15221042 488 RSTCTIN 494
Cdd:cd07144 477 TKAVHIN 483
ALDH_F1AB_F2_RALDH1 cd07141
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ...
38-493 8.81e-75

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: 243.79  E-value: 8.81e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  38 TLNPANNQPIAQVVEASLEDYEQGLKACEEAAKI---WMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEG- 113
Cdd:cd07141  26 TINPATGEKICEVQEGDKADVDKAVKAARAAFKLgspWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSy 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 114 IGEVQEVIDMCDFAVGLSRQLNGSVIPSErPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTT 193
Cdd:cd07141 106 LVDLPGAIKVLRYYAGWADKIHGKTIPMD-GDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQT 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 194 PLITIAMTKLVAE------VLekNNLPGAIFTAmcggaeiGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTL-LE 266
Cdd:cd07141 185 PLTALYLASLIKEagfppgVV--NVVPGYGPTA-------GAAISSHPDIDKVAFTGSTEVGKLIQQAAGKSNLKRVtLE 255
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 267 LSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPlhtPE 346
Cdd:cd07141 256 LGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGP---QI 332
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 347 SKKNFEKGIEVIKS---QGGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQ 422
Cdd:cd07141 333 DEEQFKKILELIESgkkEGAKLECGGKRHGDKGYFIQPTVFsDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTY 412
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15221042 423 GLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIPtNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTCTI 493
Cdd:cd07141 413 GLAAAVFTKDIDKAITFSNAL--RAGTVWVNCY-NVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
ALDH_EDX86601 cd07102
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ...
39-434 3.29e-74

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: 241.38  E-value: 3.29e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  39 LNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQ 118
Cdd:cd07102   1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 119 EVIDMCDFavgLSRQLNGSVIPSERPNHMMLEMW---NPLGIVGVITAFNFP--CAVlgwNACI-ALVCGNCVVWKGAPT 192
Cdd:cd07102  81 GMLERARY---MISIAEEALADIRVPEKDGFERYirrEPLGVVLIIAPWNYPylTAV---NAVIpALLAGNAVILKHSPQ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 193 TPLITIAMTKLVAEVLeknnLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNA 272
Cdd:cd07102 155 TPLCGERFAAAFAEAG----LPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDP 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 273 IIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFE 352
Cdd:cd07102 231 AYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVR 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 353 KGIEVIKSQGGKILTGGK---AVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSI 428
Cdd:cd07102 311 AQIADAIAKGARALIDGAlfpEDKAGGAYLAPTVLtNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASV 390

                ....*.
gi 15221042 429 FTRNPE 434
Cdd:cd07102 391 WTKDIA 396
ALDH_DDALDH cd07099
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ...
39-487 8.46e-74

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: 240.59  E-value: 8.46e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  39 LNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQ 118
Cdd:cd07099   1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 119 EVIDMCDFAVGLSRQLNGsviPSERPNHMMleMWN--------PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGA 190
Cdd:cd07099  81 LALEAIDWAARNAPRVLA---PRKVPTGLL--MPNkkatveyrPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 191 PTTPLITIAMTKLVAEVleknNLPGAIFTAMCGGAEIGEAIAkDTRIPLVSFTGSSRVGsmvqQTVNARSGKTL----LE 266
Cdd:cd07099 156 EVTPLVGELLAEAWAAA----GPPQGVLQVVTGDGATGAALI-DAGVDKVAFTGSVATG----RKVMAAAAERLipvvLE 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 267 LSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPE 346
Cdd:cd07099 227 LGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTAR 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 347 SKKNFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLS 425
Cdd:cd07099 307 QLDIVRRHVDDAVAKGAKALTGGARSNGGGPFYEPTVLtDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLS 386
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15221042 426 SSIFTRNPENIFRWIGPLgsDCGIVNVN-IPTNGAEIGGAFGGEKATGGGREAGSDSWKQYMR 487
Cdd:cd07099 387 ASVFSRDLARAEAIARRL--EAGAVSINdVLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCR 447
ALDH_F16 cd07111
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ...
3-489 4.40e-73

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: 239.60  E-value: 4.40e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   3 SANNEYEFLSEIgltSHNLGSYVAGKWQA--NGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKR 80
Cdd:cd07111   7 SAACALAWLDAH---DRSFGHFINGKWVKpeNRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVR 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  81 GDIVRQIGDALRSKLDYLGRLLSLEMGKilaegigEVQEVIDmCD-------------FAVGLSRQLNGsvipserpnhm 147
Cdd:cd07111  84 ARHLYRIARHIQKHQRLFAVLESLDNGK-------PIRESRD-CDiplvarhfyhhagWAQLLDTELAG----------- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 148 mlemWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIamtkLVAEVLEKNNLPGAIFTAMCGGAEI 227
Cdd:cd07111 145 ----WKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTAL----LFAEICAEAGLPPGVLNIVTGNGSF 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 228 GEAIAKDTRIPLVSFTGSSRVGSMVQQTVnARSGKTL-LELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRL 306
Cdd:cd07111 217 GSALANHPGVDKVAFTGSTEVGRALRRAT-AGTGKKLsLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRL 295
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 307 LLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPTIIE- 385
Cdd:cd07111 296 LVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTn 375
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 386 ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWigPLGSDCGIVNVNiPTNGAEIGGAF 465
Cdd:cd07111 376 VPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEV--ALSLKAGVVWIN-GHNLFDAAAGF 452
                       490       500
                ....*....|....*....|....
gi 15221042 466 GGEKATGGGREAGSDSWKQYMRRS 489
Cdd:cd07111 453 GGYRESGFGREGGKEGLYEYLRPS 476
PRK10090 PRK10090
aldehyde dehydrogenase A; Provisional
85-432 5.23e-73

aldehyde dehydrogenase A; Provisional


Pssm-ID: 182233 [Multi-domain]  Cd Length: 409  Bit Score: 237.33  E-value: 5.23e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   85 RQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAF 164
Cdd:PRK10090   2 RKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPW 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  165 NFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFT 243
Cdd:PRK10090  82 NFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEI----GLPKGVFNLVLGrGETVGQELAGNPKVAMVSMT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  244 GSSRVGSMVQQTVNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTS 323
Cdd:PRK10090 158 GSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEA 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  324 YKQVKIGNPLEKGTL-LGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPT-IIEISADAAVVKEELFAPV 401
Cdd:PRK10090 238 MQAVQFGNPAERNDIaMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTlLLDVRQEMSIMHEETFGPV 317
                        330       340       350
                 ....*....|....*....|....*....|.
gi 15221042  402 LYVLKFKSFGEAVAINNSVPQGLSSSIFTRN 432
Cdd:PRK10090 318 LPVVAFDTLEEAIAMANDSDYGLTSSIYTQN 348
ALDH_F11_NP-GAPDH cd07082
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ...
24-494 6.85e-73

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: 238.62  E-value: 6.85e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  24 YVAGKW-QANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAP-KRGDIVRQIGDALRSKLDYLGRL 101
Cdd:cd07082   5 LINGEWkESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPLeERIDCLHKFADLLKENKEEVANL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 102 LSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMM----LEMWNPLGIVGVITAFNFPCAvLGWNACI 177
Cdd:cd07082  85 LMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKgkiaQVRREPLGVVLAIGPFNYPLN-LTVSKLI 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 178 -ALVCGNCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQt 255
Cdd:cd07082 164 pALIMGNTVVFKPATQGVLLGIPL----AEAFHDAGFPKGVVNVVTGrGREIGDPLVTHGRIDVISFTGSTEVGNRLKK- 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 256 vNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEK 335
Cdd:cd07082 239 -QHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDN 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 336 GTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVegEGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAV 414
Cdd:cd07082 318 GVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGRE--GGNLIYPTLLDpVTPDMRLAWEEPFGPVLPIIRVNDIEEAI 395
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 415 AINNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVN-IPTNGAEIgGAFGGEKATGGGREAGSDSWKQYMRRSTCTI 493
Cdd:cd07082 396 ELANKSNYGLQASIFTKDINKARKLADAL--EVGTVNINsKCQRGPDH-FPFLGRKDSGIGTQGIGDALRSMTRRKGIVI 472

                .
gi 15221042 494 N 494
Cdd:cd07082 473 N 473
ALDH_P5CDH cd07083
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ...
24-488 8.51e-73

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: 239.40  E-value: 8.51e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  24 YVAGKWQANGPLVSTLNPAN-NQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLL 102
Cdd:cd07083  22 VIGGEWVDTKERMVSVSPFApSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATL 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 103 SLEMGKILAEGIGEVQEVIDMCDF-AVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVC 181
Cdd:cd07083 102 TYEVGKNWVEAIDDVAEAIDFIRYyARAALRLRYPAVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAV 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 182 GNCVVWKGAPTTPLITIAmtklVAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARS 260
Cdd:cd07083 182 GNTVIAKPAEDAVVVGYK----VFEIFHEAGFPPGVVQFLPGvGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLA 257
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 261 G------KTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLE 334
Cdd:cd07083 258 PgqtwfkRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEE 337
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 335 KGTLLGPLHTPESKKNFEKGIEVIKSQgGKILTGGKAVEGEGNFVEPTIIEI-SADAAVVKEELFAPVLYVLKFKS--FG 411
Cdd:cd07083 338 NGTDLGPVIDAEQEAKVLSYIEHGKNE-GQLVLGGKRLEGEGYFVAPTVVEEvPPKARIAQEEIFGPVLSVIRYKDddFA 416
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15221042 412 EAVAINNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAGSdswKQYMRR 488
Cdd:cd07083 417 EALEVANSTPYGLTGGVYSRKREHLEEARREF--HVGNLYINRKITGALVGvQPFGGFKLSGTNAKTGG---PHYLRR 489
ALDH_GABALDH-PuuC cd07112
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ...
38-486 7.35e-72

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: 235.57  E-value: 7.35e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  38 TLNPANNQPIAQVVEASLEDYEQGLKACEEA--AKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGI- 114
Cdd:cd07112   6 TINPATGRVLAEVAACDAADVDRAVAAARRAfeSGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALa 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 115 GEVQEVIDMCDFAVGLSRQLNGSVIPSErPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTP 194
Cdd:cd07112  86 VDVPSAANTFRWYAEAIDKVYGEVAPTG-PDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSP 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 195 LITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQtvnaRSGKT-----LLELS 268
Cdd:cd07112 165 LTALRLAELALEA----GLPAGVLNVVPGfGHTAGEALGLHMDVDALAFTGSTEVGRRFLE----YSGQSnlkrvWLECG 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 269 GNNAIIVMDDA-DIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLhtpES 347
Cdd:cd07112 237 GKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGAL---VS 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 348 KKNFEK---GIEVIKSQGGKILTGGKAV--EGEGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVP 421
Cdd:cd07112 314 EAHFDKvlgYIESGKAEGARLVAGGKRVltETGGFFVEPTVFDgVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSV 393
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15221042 422 QGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQYM 486
Cdd:cd07112 394 YGLAASVWTSDLSRAHRVARRL--RAGTVWVNC-FDEGDITTPFGGFKQSGNGRDKSLHALDKYT 455
ALDH_PsfA-ACA09737 cd07120
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ...
38-486 2.15e-71

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: 234.16  E-value: 2.15e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  38 TLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPK-RGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGE 116
Cdd:cd07120   1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDETDWAHDPRlRARVLLELADAFEANAERLARLLALENGKILGEARFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 117 VQEVIDMCDFAVGLSRQLNGSVIPSErPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLI 196
Cdd:cd07120  81 ISGAISELRYYAGLARTEAGRMIEPE-PGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 197 TIAMTKLVAEVLEknnLP-GAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIV 275
Cdd:cd07120 160 NAAIIRILAEIPS---LPaGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIV 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 276 MDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGI 355
Cdd:cd07120 237 FDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMV 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 356 EVIKSQGGK-ILTGGKAVEG--EGNFVEPTIIEIS-ADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTR 431
Cdd:cd07120 317 ERAIAAGAEvVLRGGPVTEGlaKGAFLRPTLLEVDdPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTR 396
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15221042 432 NPENIFRWIGPLgsDCGIVNVNipTNGAEIGGA-FGGEKATGGGREAGSDSWKQYM 486
Cdd:cd07120 397 DLARAMRVARAI--RAGTVWIN--DWNKLFAEAeEGGYRQSGLGRLHGVAALEDFI 448
PRK13252 PRK13252
betaine aldehyde dehydrogenase; Provisional
24-487 5.09e-71

betaine aldehyde dehydrogenase; Provisional


Pssm-ID: 183918  Cd Length: 488  Bit Score: 234.39  E-value: 5.09e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   24 YVAGKWQAN--GPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRL 101
Cdd:PRK13252  10 YIDGAYVEAtsGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAAL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  102 LSLEMGKILAEGIgeVQEVI---DMCDFAVGLSRQLNGSVIPSeRPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIA 178
Cdd:PRK13252  90 ETLDTGKPIQETS--VVDIVtgaDVLEYYAGLAPALEGEQIPL-RGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  179 LVCGNCVVWKGAPTTPLITIamtKLvAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGsmvqQTVNA 258
Cdd:PRK13252 167 LAAGNAMIFKPSEVTPLTAL---KL-AEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTG----KKVMA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  259 RSGKTL----LELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLE 334
Cdd:PRK13252 239 AAAASLkevtMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMD 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  335 KGTLLGPLhtpESKKNFEK---GIEVIKSQGGKILTGGKAVE----GEGNFVEPTI-IEISADAAVVKEELFAPVLYVLK 406
Cdd:PRK13252 319 PATNFGPL---VSFAHRDKvlgYIEKGKAEGARLLCGGERLTeggfANGAFVAPTVfTDCTDDMTIVREEIFGPVMSVLT 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  407 FKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNipTNG---AEIggAFGGEKATGGGREAGSDSWK 483
Cdd:PRK13252 396 FDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQL--EAGICWIN--TWGespAEM--PVGGYKQSGIGRENGIATLE 469

                 ....
gi 15221042  484 QYMR 487
Cdd:PRK13252 470 HYTQ 473
PLN02467 PLN02467
betaine aldehyde dehydrogenase
24-486 4.29e-70

betaine aldehyde dehydrogenase


Pssm-ID: 215260 [Multi-domain]  Cd Length: 503  Bit Score: 232.32  E-value: 4.29e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   24 YVAGKWQA--NGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEA-----AKIWMQVTAPKRGDIVRQIGDALRSKLD 96
Cdd:PLN02467  11 FIGGEWREpvLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITERKS 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   97 YLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNG-SVIPSERPnhmMLE-----MWNPLGIVGVITAFNFPCAV 170
Cdd:PLN02467  91 ELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAkQKAPVSLP---METfkgyvLKEPLGVVGLITPWNYPLLM 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  171 LGWNACIALVCGNCVVWKgapttPLITIAMTKLV-AEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRV 248
Cdd:PLN02467 168 ATWKVAPALAAGCTAVLK-----PSELASVTCLElADICREVGLPPGVLNVVTGlGTEAGAPLASHPGVDKIAFTGSTAT 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  249 GSMVQQTVNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVK 328
Cdd:PLN02467 243 GRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIK 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  329 IGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEG--EGNFVEPTII-EISADAAVVKEELFAPVLYVL 405
Cdd:PLN02467 323 ISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHlkKGFFIEPTIItDVTTSMQIWREEVFGPVLCVK 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  406 KFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVN--------IPtngaeiggaFGGEKATGGGREA 477
Cdd:PLN02467 403 TFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAF--QAGIVWINcsqpcfcqAP---------WGGIKRSGFGREL 471

                 ....*....
gi 15221042  478 GSDSWKQYM 486
Cdd:PLN02467 472 GEWGLENYL 480
ALDH_CddD_SSP0762 cd07138
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ...
24-478 3.99e-68

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: 225.84  E-value: 3.99e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  24 YVAGKWQA--NGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRL 101
Cdd:cd07138   2 YIDGAWVApaGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 102 LSLEMG--KILAE------GIGEVQEVIDMC-DFAvgLSRQLNGSVIPSErpnhmmlemwnPLGIVGVITAFNFP----- 167
Cdd:cd07138  82 ITLEMGapITLARaaqvglGIGHLRAAADALkDFE--FEERRGNSLVVRE-----------PIGVCGLITPWNWPlnqiv 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 168 CAVLGwnaciALVCGNCVVWKGAPTTPLITIamtkLVAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSS 246
Cdd:cd07138 149 LKVAP-----ALAAGCTVVLKPSEVAPLSAI----ILAEILDEAGLPAGVFNLVNGdGPVVGEALSAHPDVDMVSFTGST 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 247 RVGSMVQQTVnARSGK-TLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYK 325
Cdd:cd07138 220 RAGKRVAEAA-ADTVKrVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAE 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 326 QVKIGNPLEKGTLLGPLhtpESKKNFEKGIEVIKS---QGGKILTGG-KAVEG--EGNFVEPTII-EISADAAVVKEELF 398
Cdd:cd07138 299 AYVVGDPRDPATTLGPL---ASAAQFDRVQGYIQKgieEGARLVAGGpGRPEGleRGYFVKPTVFaDVTPDMTIAREEIF 375
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 399 APVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNipTNGAEIGGAFGGEKATGGGREAG 478
Cdd:cd07138 376 GPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRL--RAGQVHIN--GAAFNPGAPFGGYKQSGNGREWG 451
ALDH_StaphAldA1 cd07117
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ...
22-476 9.45e-68

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: 225.41  E-value: 9.45e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  22 GSYVAGKW--QANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLG 99
Cdd:cd07117   2 GLFINGEWvkGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 100 RLLSLEMGKILAEGIG-EVQEVIDMCDFAVGLSRQLNGSVIPSERpNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIA 178
Cdd:cd07117  82 MVETLDNGKPIRETRAvDIPLAADHFRYFAGVIRAEEGSANMIDE-DTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 179 LVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKnnlpGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNA 258
Cdd:cd07117 161 LAAGNTVVIKPSSTTSLSLLELAKIIQDVLPK----GVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 259 RSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTL 338
Cdd:cd07117 237 KLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 339 LGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGE----GNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEA 413
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENgldkGFFIEPTLIVnVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15221042 414 VAINNSVPQGLSSSIFTRNPENIFRWigPLGSDCGIVNVNIpTNGAEIGGAFGGEKATGGGRE 476
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKDINRALRV--ARAVETGRVWVNT-YNQIPAGAPFGGYKKSGIGRE 456
ALDH_PADH_NahF cd07113
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ...
22-495 1.63e-67

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: 224.63  E-value: 1.63e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  22 GSYVAGKWQANGPL--VSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAP-KRGDIVRQIGDALRSKLDYL 98
Cdd:cd07113   1 GHFIDGRPVAGQSEkrLDITNPATEQVIASVASATEADVDAAVASAWRAFVSAWAKTTPaERGRILLRLADLIEQHGEEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  99 GRLLSLEMGKI--LAEGIgEVQEVIDMCDFAVGLSRQLNGSV----IPS---ERpnHMMLEMWNPLGIVGVITAFNFPCA 169
Cdd:cd07113  81 AQLETLCSGKSihLSRAF-EVGQSANFLRYFAGWATKINGETlapsIPSmqgER--YTAFTRREPVGVVAGIVPWNFSVM 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 170 VLGWNACIALVCGNCVVWKGAPTTPLitiamTKL-VAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRV 248
Cdd:cd07113 158 IAVWKIGAALATGCTIVIKPSEFTPL-----TLLrVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVAT 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 249 GSMVQQTVNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVK 328
Cdd:cd07113 233 GKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQ 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 329 IGNPLEKGTLLGPLhtpESKKNFEK---GIEVIKSQGGKILTGGKAVEGEGNFVEPTIIEI-SADAAVVKEELFAPVLYV 404
Cdd:cd07113 313 VGSPMDESVMFGPL---ANQPHFDKvcsYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLArSADSRLMREETFGPVVSF 389
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 405 LKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIPTNgAEIGGAFGGEKATGGGREAGSDSWKQ 484
Cdd:cd07113 390 VPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRI--EAGTVWVNMHTF-LDPAVPFGGMKQSGIGREFGSAFIDD 466
                       490
                ....*....|.
gi 15221042 485 YMRRSTCTINY 495
Cdd:cd07113 467 YTELKSVMIRY 477
MMSDH TIGR01722
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ...
22-492 4.77e-66

methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]


Pssm-ID: 130783  Cd Length: 477  Bit Score: 220.91  E-value: 4.77e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042    22 GSYVAGKWQANGPLVstlNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRL 101
Cdd:TIGR01722   7 GKFAEGASGTYIPVT---NPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAEL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   102 LSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVC 181
Cdd:TIGR01722  84 ITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIAC 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   182 GNCVVWKGAPTTPLITIamtkLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTvNARSG 261
Cdd:TIGR01722 164 GNTFVLKPSEKVPSAAV----KLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTT-GSAHG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   262 KTLLELSG-NNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVyDKVLEQLLTSYKQVKIGNPLEKGTLLG 340
Cdd:TIGR01722 239 KRVQALGGaKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIGPGDDPGAEMG 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   341 PLHTPESKKNFEKGIEVIKSQGGKILTGGKA--VEG--EGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVA 415
Cdd:TIGR01722 318 PLITPQAKDRVASLIAGGAAEGAEVLLDGRGykVDGyeEGNWVGPTLLErVPPTMKAYQEEIFGPVLCVLEADTLEEAIA 397
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15221042   416 INNSVPQGLSSSIFTRNPENIFRWigPLGSDCGIVNVNIPTNGAEIGGAFGGEKAT--GGGREAGSDSWKQYMRRSTCT 492
Cdd:TIGR01722 398 LINASPYGNGTAIFTRDGAAARRF--QHEIEVGQVGVNVPIPVPLPYFSFTGWKDSffGDHHIYGKQGTHFYTRGKTVT 474
ALDH_SSADH2_GabD2 cd07101
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ...
41-486 1.27e-64

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: 216.41  E-value: 1.27e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  41 PANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQEV 120
Cdd:cd07101   3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 121 IDMCDF-AVGLSRQLNgsviPSERPNHMML-----EMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTP 194
Cdd:cd07101  83 AIVARYyARRAERLLK----PRRRRGAIPVltrttVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 195 LITIAMTKLvaevLEKNNLPGAIFTAMCG-GAEIGEAIAKdtRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAI 273
Cdd:cd07101 159 LTALWAVEL----LIEAGLPRDLWQVVTGpGSEVGGAIVD--NADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPM 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 274 IVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEK 353
Cdd:cd07101 233 IVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTA 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 354 GIEVIKSQGGKILTGGKAVEGEGN-FVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTR 431
Cdd:cd07101 313 HVDDAVAKGATVLAGGRARPDLGPyFYEPTVLTgVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTR 392
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15221042 432 NPENIfRWIGPLgSDCGIVNVN---IPTNGAeIGGAFGGEKATGGGREAGSDSWKQYM 486
Cdd:cd07101 393 DGARG-RRIAAR-LRAGTVNVNegyAAAWAS-IDAPMGGMKDSGLGRRHGAEGLLKYT 447
ALDH_SaliADH cd07105
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ...
57-484 3.51e-64

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: 214.75  E-value: 3.51e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  57 DYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMG-------KILAEGIGEVQEVIDMCDfavg 129
Cdd:cd07105   1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGataawagFNVDLAAGMLREAASLIT---- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 130 lsrQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPcAVLGWNA-CIALVCGNCVVWKGAPTTPlitiaMT-KLVAEV 207
Cdd:cd07105  77 ---QIIGGSIPSDKPGTLAMVVKEPVGVVLGIAPWNAP-VILGTRAiAYPLAAGNTVVLKASELSP-----RThWLIGRV 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 208 LEKNNLP-GA---IFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTvnarSGK----TLLELSGNNAIIVMDDA 279
Cdd:cd07105 148 FHEAGLPkGVlnvVTHSPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAET----AAKhlkpVLLELGGKAPAIVLEDA 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 280 DIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGnplekGTLLGPLHTPESKKNFEKGIEVIK 359
Cdd:cd07105 224 DLDAAANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDAL 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 360 SQGGKILTGGKA-VEGEGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIF 437
Cdd:cd07105 299 SKGAKLVVGGLAdESPSGTSMPPTILDnVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARAL 378
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 15221042 438 RWIGPLgsDCGIVNVNIPTNGAEIGGAFGGEKATGGGR---EAGSDSWKQ 484
Cdd:cd07105 379 AVAKRI--ESGAVHINGMTVHDEPTLPHGGVKSSGYGRfngKWGIDEFTE 426
PRK11904 PRK11904
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
21-478 2.02e-62

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


Pssm-ID: 237017 [Multi-domain]  Cd Length: 1038  Bit Score: 220.46  E-value: 2.02e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042    21 LGSYVAGKWQAnGPLVST-------LNPANN-QPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALR 92
Cdd:PRK11904  543 IAAFLEKQWQA-GPIINGegearpvVSPADRrRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLE 621
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042    93 SKLDYLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERP----NHMMLEmwnPLGIVGVITAFNFPC 168
Cdd:PRK11904  622 ANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKLPGPtgesNELRLH---GRGVFVCISPWNFPL 698
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   169 AV-LGWNACiALVCGNCVVWKGAPTTPLITIAMTKLV------AEVLEKnnLPGAiftamcgGAEIGEAIAKDTRIPLVS 241
Cdd:PRK11904  699 AIfLGQVAA-ALAAGNTVIAKPAEQTPLIAAEAVKLLheagipKDVLQL--LPGD-------GATVGAALTADPRIAGVA 768
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   242 FTGSSRVGSMVQQTVNARSGK--TLL-ELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLE 318
Cdd:PRK11904  769 FTGSTETARIINRTLAARDGPivPLIaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIE 848
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   319 QLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKsQGGKILTGGKAVEG--EGNFVEPTIIEISaDAAVVKEE 396
Cdd:PRK11904  849 MLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMK-REARLLAQLPLPAGteNGHFVAPTAFEID-SISQLERE 926
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   397 LFAPVLYVLKFKSFG-EAV--AINNSvPQGLSSSIFTRNPENIfRWIgplgsdCGIVNV-NIPTNGAEIGGA-----FGG 467
Cdd:PRK11904  927 VFGPILHVIRYKASDlDKVidAINAT-GYGLTLGIHSRIEETA-DRI------ADRVRVgNVYVNRNQIGAVvgvqpFGG 998
                         490
                  ....*....|.
gi 15221042   468 EKATGGGREAG 478
Cdd:PRK11904  999 QGLSGTGPKAG 1009
PLN02466 PLN02466
aldehyde dehydrogenase family 2 member
31-487 3.73e-62

aldehyde dehydrogenase family 2 member


Pssm-ID: 215259 [Multi-domain]  Cd Length: 538  Bit Score: 212.36  E-value: 3.73e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   31 ANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEA--AKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGK 108
Cdd:PLN02466  70 ASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAfdEGPWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGK 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  109 ILAEGIG-EVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLeMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVW 187
Cdd:PLN02466 150 PYEQSAKaELPMFARLFRYYAGWADKIHGLTVPADGPHHVQT-LHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVL 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  188 KGAPTTPLITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQtVNARSG--KTL 264
Cdd:PLN02466 229 KTAEQTPLSALYAAKLLHEA----GLPPGVLNVVSGfGPTAGAALASHMDVDKLAFTGSTDTGKIVLE-LAAKSNlkPVT 303
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  265 LELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHT 344
Cdd:PLN02466 304 LELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQID 383
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  345 PEskkNFEKGIEVIKS---QGGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSV 420
Cdd:PLN02466 384 SE---QFEKILRYIKSgveSGATLECGGDRFGSKGYYIQPTVFsNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNT 460
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15221042  421 PQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVN--------IPtngaeiggaFGGEKATGGGREAGSDSWKQYMR 487
Cdd:PLN02466 461 RYGLAAGVFTQNLDTANTLSRAL--RVGTVWVNcfdvfdaaIP---------FGGYKMSGIGREKGIYSLNNYLQ 524
ALDH_ACDHII-AcoD cd07116
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ...
22-476 4.03e-62

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: 210.77  E-value: 4.03e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  22 GSYVAGKWQA--NGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLG 99
Cdd:cd07116   2 DNFIGGEWVApvKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 100 RLLSLEMGKILAEGIG-EVQEVIDMCDFAVGLSRQLNGSVipSE-RPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACI 177
Cdd:cd07116  82 VAETWDNGKPVRETLAaDIPLAIDHFRYFAGCIRAQEGSI--SEiDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 178 ALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEknnlPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVN 257
Cdd:cd07116 160 ALAAGNCVVLKPAEQTPASILVLMELIGDLLP----PGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYAS 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 258 ARSGKTLLELSGNNAII----VM--DDADIQLAARS-VLFAAvgTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIG 330
Cdd:cd07116 236 ENIIPVTLELGGKSPNIffadVMdaDDAFFDKALEGfVMFAL--NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQG 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 331 NPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKA----VEGEGNFVEPTIIEISADAAVVKEELFAPVLYVLK 406
Cdd:cd07116 314 NPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERnelgGLLGGGYYVPTTFKGGNKMRIFQEEIFGPVLAVTT 393
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15221042 407 FKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWigPLGSDCGIVNVN----IPTngaeiGGAFGGEKATGGGRE 476
Cdd:cd07116 394 FKDEEEALEIANDTLYGLGAGVWTRDGNTAYRM--GRGIQAGRVWTNcyhlYPA-----HAAFGGYKQSGIGRE 460
astD PRK09457
succinylglutamic semialdehyde dehydrogenase; Reviewed
24-475 1.41e-61

succinylglutamic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181873  Cd Length: 487  Bit Score: 209.43  E-value: 1.41e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   24 YVAGKWQA-NGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLL 102
Cdd:PRK09457   4 WINGDWIAgQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  103 SLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIpSERPNHMMLEMWNPLGIVGVITAFNFPcAVLGwNACI--ALV 180
Cdd:PRK09457  84 ARETGKPLWEAATEVTAMINKIAISIQAYHERTGEKR-SEMADGAAVLRHRPHGVVAVFGPYNFP-GHLP-NGHIvpALL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  181 CGNCVVWKGAPTTPlitiAMTKLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARS 260
Cdd:PRK09457 161 AGNTVVFKPSELTP----WVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQP 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  261 GKTL-LELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVY-DKVLEQLLTSYKQVKIGNPL-EKGT 337
Cdd:PRK09457 237 EKILaLEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRWDaEPQP 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  338 LLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPTIIEISADAAVVKEELFAPVLYVLKFKSFGEAVAIN 417
Cdd:PRK09457 317 FMGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGIIDVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLA 396
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  418 NSVPQGLSSSIFTRNPE--NIFRwigpLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGR 475
Cdd:PRK09457 397 NNTRFGLSAGLLSDDREdyDQFL----LEIRAGIVNWNKPLTGASSAAPFGGVGASGNHR 452
ALDH_F1L_FTFDH cd07140
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ...
31-495 8.56e-60

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: 204.65  E-value: 8.56e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  31 ANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKI--WMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGK 108
Cdd:cd07140  18 EGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGA 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 109 ILAEGIG-EVQEVIDMCDFAVGLSRQLNGSVIP--SERPNH-MMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNC 184
Cdd:cd07140  98 VYTLALKtHVGMSIQTFRYFAGWCDKIQGKTIPinQARPNRnLTLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNT 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 185 VVWKGAPTTPLITIAMTKLVAevleKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVnARSG-- 261
Cdd:cd07140 178 VVLKPAQVTPLTALKFAELTV----KAGFPKGVINILPGsGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSC-AVSNlk 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 262 KTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGP 341
Cdd:cd07140 253 KVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGP 332
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 342 lhtPESKKNFEKGIEVIK---SQGGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSfGEAVAI- 416
Cdd:cd07140 333 ---QNHKAHLDKLVEYCErgvKEGATLVYGGKQVDRPGFFFEPTVFtDVEDHMFIAKEESFGPIMIISKFDD-GDVDGVl 408
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 417 --NNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQYMRRSTCTIN 494
Cdd:cd07140 409 qrANDTEYGLASGVFTKDINKALYVSDKL--EAGTVFVNT-YNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTIE 485

                .
gi 15221042 495 Y 495
Cdd:cd07140 486 Y 486
PRK11905 PRK11905
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
18-488 1.63e-59

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


Pssm-ID: 237018 [Multi-domain]  Cd Length: 1208  Bit Score: 212.42  E-value: 1.63e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042    18 SHNLGSYVAGKWQAnGPLVST----------LNPAN-NQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQ 86
Cdd:PRK11905  542 DEALNAFAAKTWHA-APLLAGgdvdggtrpvLNPADhDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILER 620
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042    87 IGDALRSKLDYLGRLLSLEMGKILAEGIGEVQEVIDMCDF-AVGLSRQLNGSVIPserpnhmmlemwnPLGIVGVITAFN 165
Cdd:PRK11905  621 AADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYyAAQARRLLNGPGHK-------------PLGPVVCISPWN 687
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   166 FPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTG 244
Cdd:PRK11905  688 FPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEA----GVPKDALQLLPGdGRTVGAALVADPRIAGVMFTG 763
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   245 SSRVGSMVQQTVNARSGK-TLL--ELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLL 321
Cdd:PRK11905  764 STEVARLIQRTLAKRSGPpVPLiaETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLK 843
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   322 TSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKI--LTGGKAVEGeGNFVEPTIIEISaDAAVVKEELFA 399
Cdd:PRK11905  844 GAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVhqLPLPAETEK-GTFVAPTLIEID-SISDLEREVFG 921
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   400 PVLYVLKFKSFG-EAV--AINNSvPQGLSSSIFTRNPENIFRWIGplGSDCGIVNVNIPTNGAEIG-GAFGGEKATGGGR 475
Cdd:PRK11905  922 PVLHVVRFKADElDRVidDINAT-GYGLTFGLHSRIDETIAHVTS--RIRAGNIYVNRNIIGAVVGvQPFGGEGLSGTGP 998
                         490
                  ....*....|...
gi 15221042   476 EAGSdswKQYMRR 488
Cdd:PRK11905  999 KAGG---PLYLGR 1008
PLN02766 PLN02766
coniferyl-aldehyde dehydrogenase
31-487 5.15e-59

coniferyl-aldehyde dehydrogenase


Pssm-ID: 215410 [Multi-domain]  Cd Length: 501  Bit Score: 202.74  E-value: 5.15e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   31 ANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAK--IWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGK 108
Cdd:PLN02766  33 ASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGK 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  109 ILAEG-IGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMlEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVW 187
Cdd:PLN02766 113 LFALGkAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGY-TLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVV 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  188 KGAPTTPLITIamtkLVAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVnARSG--KTL 264
Cdd:PLN02766 192 KPAEQTPLSAL----FYAHLAKLAGVPDGVINVVTGfGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAA-ATSNlkQVS 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  265 LELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPlht 344
Cdd:PLN02766 267 LELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGP--- 343
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  345 PESKKNFEK---GIEVIKSQGGKILTGGKAVEGEGNFVEPTI-IEISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSV 420
Cdd:PLN02766 344 QVDKQQFEKilsYIEHGKREGATLLTGGKPCGDKGYYIEPTIfTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNT 423
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  421 PQGLSSSIFTRN---PENIFRWIgplgsDCGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQYMR 487
Cdd:PLN02766 424 KYGLAAGIVTKDldvANTVSRSI-----RAGTIWVNC-YFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQ 487
D1pyr5carbox3 TIGR01238
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ...
23-489 1.00e-58

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: 202.06  E-value: 1.00e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042    23 SYVAGKWQANGPLVSTLNPANNQPI-AQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRL 101
Cdd:TIGR01238  40 PIIGHSYKADGEAQPVTNPADRRDIvGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMAL 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   102 LSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSvipserpnhmmlEMWNPLGIVGVITAFNFPCAVLGWNACIALVC 181
Cdd:TIGR01238 120 CVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGE------------FSVESRGVFVCISPWNFPLAIFTGQISAALAA 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   182 GNCVVWKGAPTTPLITiamTKLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNAR-- 259
Cdd:TIGR01238 188 GNTVIAKPAEQTSLIA---YRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQRed 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   260 -SGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTL 338
Cdd:TIGR01238 265 aPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTD 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   339 LGPLHTPESKKNFEKGIEVIKSQGGKI--LTGGKAVEGE-GNFVEPTIIEISaDAAVVKEELFAPVLYVLKFKS--FGEA 413
Cdd:TIGR01238 345 VGPVIDAEAKQNLLAHIEHMSQTQKKIaqLTLDDSRACQhGTFVAPTLFELD-DIAELSEEVFGPVLHVVRYKAreLDQI 423
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221042   414 VAINNSVPQGLSSSIFTRNPENIfRWIGPlGSDCGIVNVNIPTNGAEIG-GAFGGEKATGGGREAGSDSWKQYMRRS 489
Cdd:TIGR01238 424 VDQINQTGYGLTMGVHSRIETTY-RWIEK-HARVGNCYVNRNQVGAVVGvQPFGGQGLSGTGPKAGGPHYLYRLTQV 498
gabD1 PRK09406
succinic semialdehyde dehydrogenase; Reviewed
36-476 1.77e-58

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181826 [Multi-domain]  Cd Length: 457  Bit Score: 200.35  E-value: 1.77e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   36 VSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIG 115
Cdd:PRK09406   3 IATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  116 EVQEVIDMCDF-----------------AVGLSRqlngsvipserpnhmMLEMWNPLGIVGVITAFNFPCAVLGWNACIA 178
Cdd:PRK09406  83 EALKCAKGFRYyaehaealladepadaaAVGASR---------------AYVRYQPLGVVLAVMPWNFPLWQVVRFAAPA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  179 LVCGNCVVWKGAPTTPlitiaMTKL-VAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVN 257
Cdd:PRK09406 148 LMAGNVGLLKHASNVP-----QTALyLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAG 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  258 ARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGT 337
Cdd:PRK09406 223 DEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDT 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  338 LLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAI 416
Cdd:PRK09406 303 DVGPLATEQGRDEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVItDITPDMRLYTEEVFGPVASLYRVADIDEAIEI 382
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15221042  417 NNSVPQGLSSSIFTRNPENIFRWIGPLgsDCGIVNVN-IPTNGAEIGgaFGGEKATGGGRE 476
Cdd:PRK09406 383 ANATTFGLGSNAWTRDEAEQERFIDDL--EAGQVFINgMTVSYPELP--FGGVKRSGYGRE 439
PRK13968 PRK13968
putative succinate semialdehyde dehydrogenase; Provisional
38-476 1.21e-57

putative succinate semialdehyde dehydrogenase; Provisional


Pssm-ID: 184426 [Multi-domain]  Cd Length: 462  Bit Score: 198.16  E-value: 1.21e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   38 TLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEV 117
Cdd:PRK13968  11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  118 QEVIDMCD-FAVGLSRQLNGSviPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTpli 196
Cdd:PRK13968  91 AKSANLCDwYAEHGPAMLKAE--PTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNV--- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  197 tIAMTKLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIVM 276
Cdd:PRK13968 166 -MGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVL 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  277 DDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIE 356
Cdd:PRK13968 245 NDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVE 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  357 VIKSQGGKILTGGKAVEGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPEN 435
Cdd:PRK13968 325 ATLAEGARLLLGGEKIAGAGNYYAPTVLaNVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQ 404
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 15221042  436 IFRWIGPLgsDCGIVNVN-IPTNGAEIggAFGGEKATGGGRE 476
Cdd:PRK13968 405 ARQMAARL--ECGGVFINgYCASDARV--AFGGVKKSGFGRE 442
gabD2 PRK09407
succinic semialdehyde dehydrogenase; Reviewed
16-480 3.61e-57

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236501 [Multi-domain]  Cd Length: 524  Bit Score: 198.56  E-value: 3.61e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   16 LTSHNLGSYVAGKWQANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKL 95
Cdd:PRK09407  14 LTFERLRRLTARVDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   96 DYLGRLLSLEMGKILAEGIGEVQEVIDMCDF----AVGLSRqlngsviPSERPNHMML-----EMWNPLGIVGVITAFNF 166
Cdd:PRK09407  94 EELLDLVQLETGKARRHAFEEVLDVALTARYyarrAPKLLA-------PRRRAGALPVltkttELRQPKGVVGVISPWNY 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  167 PCAVLGWNACIALVCGNCVVWKGAPTTPLITIAmtklVAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKdtRIPLVSFTGS 245
Cdd:PRK09407 167 PLTLAVSDAIPALLAGNAVVLKPDSQTPLTALA----AVELLYEAGLPRDLWQVVTGpGPVVGTALVD--NADYLMFTGS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  246 SRVGsmvqQTVNARSGKTL----LELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLL 321
Cdd:PRK09407 241 TATG----RVLAEQAGRRLigfsLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFV 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  322 TSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGEGN-FVEPTIIE-ISADAAVVKEELFA 399
Cdd:PRK09407 317 AAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGPlFYEPTVLTgVTPDMELAREETFG 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  400 PVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNP---ENIFRWIgplgsDCGIVNVN---IPTNGAeIGGAFGGEKATGG 473
Cdd:PRK09407 397 PVVSVYPVADVDEAVERANDTPYGLNASVWTGDTargRAIAARI-----RAGTVNVNegyAAAWGS-VDAPMGGMKDSGL 470

                 ....*..
gi 15221042  474 GREAGSD 480
Cdd:PRK09407 471 GRRHGAE 477
PutA2 COG4230
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
18-436 9.35e-54

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


Pssm-ID: 443374 [Multi-domain]  Cd Length: 1156  Bit Score: 195.54  E-value: 9.35e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   18 SHNLGSYVAGKWQAnGPLVST----------LNPAN-NQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQ 86
Cdd:COG4230  545 SAALAAAAEKQWQA-APLIAGeaasgearpvRNPADhSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILER 623
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   87 IGDALRSKLDYLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGsvipserpNHMMLEmwnPLGIVGVITAFNF 166
Cdd:COG4230  624 AADLLEAHRAELMALLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFA--------APTVLR---GRGVFVCISPWNF 692
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  167 PCAvlgwnacI-------ALVCGNCVVWKGAPTTPLITIAMTKLV------AEVLEKnnLPGAiftamcgGAEIGEAIAK 233
Cdd:COG4230  693 PLA-------IftgqvaaALAAGNTVLAKPAEQTPLIAARAVRLLheagvpADVLQL--LPGD-------GETVGAALVA 756
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  234 DTRIPLVSFTGSSRVGSMVQQTVNARSGK--TLL-ELSGNNAIIVmdDADIQL--AARSVLFAAVGTAGQRCTTCRRLLL 308
Cdd:COG4230  757 DPRIAGVAFTGSTETARLINRTLAARDGPivPLIaETGGQNAMIV--DSSALPeqVVDDVLASAFDSAGQRCSALRVLCV 834
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  309 HESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQgGKILTGGKAVEG--EGNFVEPTIIEI 386
Cdd:COG4230  835 QEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAE-GRLVHQLPLPEEcaNGTFVAPTLIEI 913
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15221042  387 SaDAAVVKEELFAPVLYVLKFKSFG-EAV--AINNSvPQGLSSSIFTRNPENI 436
Cdd:COG4230  914 D-SISDLEREVFGPVLHVVRYKADElDKVidAINAT-GYGLTLGVHSRIDETI 964
putA PRK11809
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ...
19-478 8.86e-52

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


Pssm-ID: 236989 [Multi-domain]  Cd Length: 1318  Bit Score: 189.80  E-value: 8.86e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042    19 HNLGSYVAG-------KWQA---------NGPLVSTLNPANNQPI-AQVVEASLEDYEQGLKACEEAAKIWmQVTAP-KR 80
Cdd:PRK11809  628 HRLASLSSAllasahqKWQAapmledpvaAGEMSPVINPADPRDIvGYVREATPAEVEQALESAVNAAPIW-FATPPaER 706
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042    81 GDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQlngsvipsERPNhmmlEMWNPLGIVGV 160
Cdd:PRK11809  707 AAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRD--------DFDN----DTHRPLGPVVC 774
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   161 ITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLV------AEVLEKnnLPGAiftamcgGAEIGEAIAKD 234
Cdd:PRK11809  775 ISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILleagvpAGVVQL--LPGR-------GETVGAALVAD 845
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   235 TRIPLVSFTGSSRVGSMVQQTVNAR---SGKT---LLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLL 308
Cdd:PRK11809  846 ARVRGVMFTGSTEVARLLQRNLAGRldpQGRPiplIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCL 925
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   309 HESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAVEGE---GNFVEPTIIE 385
Cdd:PRK11809  926 QDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVFQAARENSEDwqsGTFVPPTLIE 1005
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   386 ISaDAAVVKEELFAPVLYVLKFKS--FGEAV-AINNSvPQGLSSSIFTRNPENIFRWIGPLGSDCGIVNVNIPtnGAEIG 462
Cdd:PRK11809 1006 LD-SFDELKREVFGPVLHVVRYNRnqLDELIeQINAS-GYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMV--GAVVG 1081
                         490
                  ....*....|....*..
gi 15221042   463 -GAFGGEKATGGGREAG 478
Cdd:PRK11809 1082 vQPFGGEGLSGTGPKAG 1098
ALDH_RL0313 cd07148
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ...
39-474 6.74e-48

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: 171.83  E-value: 6.74e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  39 LNPANNQPIAQVveaSLEDYEQGLKACEEAAKIWMQVT----APKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGI 114
Cdd:cd07148   4 VNPFDLKPIGEV---PTVDWAAIDKALDTAHALFLDRNnwlpAHERIAILERLADLMEERADELALLIAREGGKPLVDAK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 115 GEVQEVIDMCDFAVGLSRQLNGSVIP----SERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGA 190
Cdd:cd07148  81 VEVTRAIDGVELAADELGQLGGREIPmgltPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 191 PTTPLITIAMTKLVAEVleknNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVnARSGKTLLELSGN 270
Cdd:cd07148 161 LATPLSCLAFVDLLHEA----GLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKL-APGTRCALEHGGA 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 271 NAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKN 350
Cdd:cd07148 236 APVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDR 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 351 FEKGIEVIKSQGGKILTGGKAVeGEGNFvEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIF 429
Cdd:cd07148 316 VEEWVNEAVAAGARLLCGGKRL-SDTTY-APTVLlDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVF 393
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 15221042 430 TRNPENIFRWIGPLgsDCGIVNVNIPTNGAEIGGAFGGEKATGGG 474
Cdd:cd07148 394 TKDLDVALKAVRRL--DATAVMVNDHTAFRVDWMPFAGRRQSGYG 436
ALDH_F15-22 cd07098
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ...
40-478 2.50e-47

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: 170.56  E-value: 2.50e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  40 NPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEG-IGEVQ 118
Cdd:cd07098   2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDAsLGEIL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 119 EVIDMCDFavgLSRQLNGSVIPSERPNHMMleMW--------NPLGIVGVITAFNFPCAVLgWNACI-ALVCGNCVVWKG 189
Cdd:cd07098  82 VTCEKIRW---TLKHGEKALRPESRPGGLL--MFykrarveyEPLGVVGAIVSWNYPFHNL-LGPIIaALFAGNAIVVKV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 190 APTTPLITIAMTKLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSG 269
Cdd:cd07098 156 SEQVAWSSGFFLSIIRECLAACGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGG 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 270 NNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESkk 349
Cdd:cd07098 236 KDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPAR-- 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 350 nFEKGIEVIK---SQGGKILTGGKAV----EGEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVP 421
Cdd:cd07098 314 -FDRLEELVAdavEKGARLLAGGKRYphpeYPQGHYFPPTLLvDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTE 392
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15221042 422 QGLSSSIFTRNPENIFRWIGPLgsDCGIVNVNiptngaEIGGA-------FGGEKATGGGREAG 478
Cdd:cd07098 393 YGLGASVFGKDIKRARRIASQL--ETGMVAIN------DFGVNyyvqqlpFGGVKGSGFGRFAG 448
PLN02419 PLN02419
methylmalonate-semialdehyde dehydrogenase [acylating]
22-484 1.16e-45

methylmalonate-semialdehyde dehydrogenase [acylating]


Pssm-ID: 166060 [Multi-domain]  Cd Length: 604  Bit Score: 168.77  E-value: 1.16e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   22 GSYVAGKwqaNGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRL 101
Cdd:PLN02419 120 GSFVESQ---SSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMN 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  102 LSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVC 181
Cdd:PLN02419 197 ITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTC 276
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  182 GNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNARSG 261
Cdd:PLN02419 277 GNTFILKPSEKDPGASVILAELAMEA----GLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGK 352
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  262 KTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLL---HESVYDKVLEQLltsyKQVKIGNPLEKGTL 338
Cdd:PLN02419 353 RIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFvgdAKSWEDKLVERA----KALKVTCGSEPDAD 428
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  339 LGPLHTPESKKNFEKGIEVIKSQGGKILTGGK--AVEG--EGNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEA 413
Cdd:PLN02419 429 LGPVISKQAKERICRLIQSGVDDGAKLLLDGRdiVVPGyeKGNFIGPTILSgVTPDMECYKEEIFGPVLVCMQANSFDEA 508
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15221042  414 VAINNSVPQGLSSSIFTRNPENIFRWigPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGR-----EAGSDSWKQ 484
Cdd:PLN02419 509 ISIINKNKYGNGAAIFTSSGAAARKF--QMDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDlnfygKAGVDFFTQ 582
PRK09847 PRK09847
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
22-476 1.14e-43

gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional


Pssm-ID: 182108 [Multi-domain]  Cd Length: 494  Bit Score: 161.22  E-value: 1.14e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   22 GSYVAGkwqANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAK--IWMQVTAPKRGDIVRQIGDALRSKLDYLG 99
Cdd:PRK09847  26 GEYTAA---AENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEELA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  100 RLLSLEMGKIL-----------AEGIGEVQEVIDmcdfavglsrQLNGSVIPSErPNHMMLEMWNPLGIVGVITAFNFPC 168
Cdd:PRK09847 103 LLETLDTGKPIrhslrddipgaARAIRWYAEAID----------KVYGEVATTS-SHELAMIVREPVGVIAAIVPWNFPL 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  169 AVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGSSR 247
Cdd:PRK09847 172 LLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEA----GLPDGVLNVVTGfGHEAGQALSRHNDIDAIAFTGSTR 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  248 VGSMVQQTVNARSGKTL-LELSGNNAIIVMDDA-DIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYK 325
Cdd:PRK09847 248 TGKQLLKDAGDSNMKRVwLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQ 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  326 QVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGGKILTGGKAveGEGNFVEPTII-EISADAAVVKEELFAPVLYV 404
Cdd:PRK09847 328 NWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNA--GLAAAIGPTIFvDVDPNASLSREEIFGPVLVV 405
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15221042  405 LKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLGSdcGIVNVNiPTNGAEIGGAFGGEKATGGGRE 476
Cdd:PRK09847 406 TRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKA--GSVFVN-NYNDGDMTVPFGGYKQSGNGRD 474
ALDH_F4-17_P5CDH cd07123
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ...
23-479 1.75e-42

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: 158.52  E-value: 1.75e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  23 SYVAGKWQANGPLVSTLNPAN-NQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKldYLGRL 101
Cdd:cd07123  35 LVIGGKEVRTGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGK--YRYEL 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 102 LSLEM---GK--ILAEgIGEVQEVIDMCDFAVGLSRQLNGsvipsERPNHMMLEMWN-----PL-GIVGVITAFNFpcAV 170
Cdd:cd07123 113 NAATMlgqGKnvWQAE-IDAACELIDFLRFNVKYAEELYA-----QQPLSSPAGVWNrleyrPLeGFVYAVSPFNF--TA 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 171 LGWN--ACIALVcGNCVVWKGAPTtplitiAM--TKLVAEVLEKNNLP-GAIFTAMCGGAEIGEAIAKDTRIPLVSFTGS 245
Cdd:cd07123 185 IGGNlaGAPALM-GNVVLWKPSDT------AVlsNYLVYKILEEAGLPpGVINFVPGDGPVVGDTVLASPHLAGLHFTGS 257
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 246 SRVGSMVQQTV-----NARSGKTLL-ELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQ 319
Cdd:cd07123 258 TPTFKSLWKQIgenldRYRTYPRIVgETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKER 337
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 320 LLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQGG-KILTGGKAVEGEGNFVEPTIIEISA-DAAVVKEEL 397
Cdd:cd07123 338 LLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPEaEIIAGGKCDDSVGYFVEPTVIETTDpKHKLMTEEI 417
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 398 FAPVL--YVLKFKSFGEAVA-INNSVPQGLSSSIFTRNPENIFRWIGPLGSDCGIVNVNIPTNGAEIGG-AFGGEKATGG 473
Cdd:cd07123 418 FGPVLtvYVYPDSDFEETLElVDTTSPYALTGAIFAQDRKAIREATDALRNAAGNFYINDKPTGAVVGQqPFGGARASGT 497

                ....*.
gi 15221042 474 GREAGS 479
Cdd:cd07123 498 NDKAGS 503
ALDH_F14-YMR110C cd07135
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ...
142-485 3.37e-40

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: 150.45  E-value: 3.37e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 142 ERPNHMMLEMWN--------PLGIVGVITAFNFP-----CAVLGwnaciALVCGNCVVWKGAPTTPlitiAMTKLVAEVL 208
Cdd:cd07135  88 EKVKDGPLAFMFgkprirkePLGVVLIIGPWNYPvllalSPLVG-----AIAAGCTVVLKPSELTP----HTAALLAELV 158
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 209 EKNnLPGAIFTAMCGG-AEIGEAIAKdtRIPLVSFTGSSRVGSMVQQTVNarsgKTL----LELSGNNAIIVMDDADIQL 283
Cdd:cd07135 159 PKY-LDPDAFQVVQGGvPETTALLEQ--KFDKIFYTGSGRVGRIIAEAAA----KHLtpvtLELGGKSPVIVTKNADLEL 231
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 284 AARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKgTLLGPLHTPeskKNFEKGIEVIKSQGG 363
Cdd:cd07135 232 AAKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANAS-PDYTRIVNP---RHFNRLKSLLDTTKG 307
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 364 KILTGGKAVEGEgNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGP 442
Cdd:cd07135 308 KVVIGGEMDEAT-RFIPPTIVsDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTR 386
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 15221042 443 LGSDCGIVN-----VNIPTngaeigGAFGGEKATGGGREAGSDSWKQY 485
Cdd:cd07135 387 TRSGGVVINdtlihVGVDN------APFGGVGDSGYGAYHGKYGFDTF 428
ALDH_F3-13-14_CALDH-like cd07087
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ...
154-436 5.71e-39

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: 146.90  E-value: 5.71e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 154 PLGIVGVITAFNFPcAVLGWNACI-ALVCGNCVVWKGAPTTPlitiAMTKLVAEVLEKNnLPGAIFTAMCGGAEIGEAIA 232
Cdd:cd07087 100 PLGVVLIIGPWNYP-LQLALAPLIgAIAAGNTVVLKPSELAP----ATSALLAKLIPKY-FDPEAVAVVEGGVEVATALL 173
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 233 KdTRIPLVSFTGSSRVGSMVQQtvnARSgKTL----LELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLL 308
Cdd:cd07087 174 A-EPFDHIFFTGSPAVGKIVME---AAA-KHLtpvtLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLV 248
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 309 HESVYDKVLEQLLTSYKQVkIGNPLEKGTLLGPLhtpESKKNFEKGIEVIksQGGKILTGGKaVEGEGNFVEPTIIE-IS 387
Cdd:cd07087 249 HESIKDELIEELKKAIKEF-YGEDPKESPDYGRI---INERHFDRLASLL--DDGKVVIGGQ-VDKEERYIAPTILDdVS 321
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 15221042 388 ADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENI 436
Cdd:cd07087 322 PDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQ 370
PTZ00381 PTZ00381
aldehyde dehydrogenase family protein; Provisional
154-502 3.50e-38

aldehyde dehydrogenase family protein; Provisional


Pssm-ID: 240392  Cd Length: 493  Bit Score: 145.94  E-value: 3.50e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  154 PLGIVGVITAFNFPcAVLGWNACI-ALVCGNCVVWKGAPTTPLITIAMTKLVAevlekNNLPGAIFTAMCGGAEIGEAIA 232
Cdd:PTZ00381 109 PLGVVLVIGAWNYP-LNLTLIPLAgAIAAGNTVVLKPSELSPHTSKLMAKLLT-----KYLDPSYVRVIEGGVEVTTELL 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  233 KDtRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESV 312
Cdd:PTZ00381 183 KE-PFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSI 261
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  313 YDKVLEQLLTSYKQVkIGNPLEKGTLLGPLHTpesKKNFEKGIEVIKSQGGKILTGGKAVEGEgNFVEPTII-EISADAA 391
Cdd:PTZ00381 262 KDKFIEALKEAIKEF-FGEDPKKSEDYSRIVN---EFHTKRLAELIKDHGGKVVYGGEVDIEN-KYVAPTIIvNPDLDSP 336
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  392 VVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLGS------DC--GIVNVNIPtngaeigg 463
Cdd:PTZ00381 337 LMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSgavvinDCvfHLLNPNLP-------- 408
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 15221042  464 aFGGEKATGGGREAGSDSWKQYMR-RSTCTINYGNELPLA 502
Cdd:PTZ00381 409 -FGGVGNSGMGAYHGKYGFDTFSHpKPVLNKSTGNSFDLS 447
ALDH_KGSADH-like cd07084
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ...
59-489 1.78e-37

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: 143.15  E-value: 1.78e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  59 EQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLD--YLGRLLSLEMGKILAEGIGEVQEVIDMCDFAVGLSRQLNG 136
Cdd:cd07084   2 ERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYdiAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSYRIPHE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 137 SV--IPSERPNHMMLEMWnPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEknnLP 214
Cdd:cd07084  82 PGnhLGQGLKQQSHGYRW-PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGL---LP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 215 GAIFTAMCGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVqqTVNARSGKTLLELSG-NNAIIVMDDADIQLAARSVLFAAV 293
Cdd:cd07084 158 PEDVTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKL--ALDAKQARIYLELAGfNWKVLGPDAQAVDYVAWQCVQDMT 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 294 GTAGQRCTTCRRLLLHES-----VYDKVLEQLLTSykqvkignpLEKGTLLGPLHTPeskkNFEKGIEVIKSQGGKILT- 367
Cdd:cd07084 236 ACSGQKCTAQSMLFVPENwsktpLVEKLKALLARR---------KLEDLLLGPVQTF----TTLAMIAHMENLLGSVLLf 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 368 GGKAV------EGEGNFVEP----TIIEISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSV-PQG-LSSSIFTRNPEN 435
Cdd:cd07084 303 SGKELknhsipSIYGACVASalfvPIDEILKTYELVTEEIFGPFAIVVEYKKDQLALVLELLErMHGsLTAAIYSNDPIF 382
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15221042 436 IFRWIGPLGSDCGIVNVNIPTNGAEIGGAFGGEKATGGGREA--GSDSWKQYMRRS 489
Cdd:cd07084 383 LQELIGNLWVAGRTYAILRGRTGVAPNQNHGGGPAADPRGAGigGPEAIKLVWRCH 438
ALDH_YwdH-P39616 cd07136
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ...
154-490 3.48e-36

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: 139.56  E-value: 3.48e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 154 PLGIVGVITAFNFPcavlgWNACI-----ALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLpgaifTAMCGGAEIG 228
Cdd:cd07136 100 PYGVVLIIAPWNYP-----FQLALapligAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYV-----AVVEGGVEEN 169
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 229 EAIAkDTRIPLVSFTGSSRVGsmvqQTVNARSGKTL----LELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCR 304
Cdd:cd07136 170 QELL-DQKFDYIFFTGSVRVG----KIVMEAAAKHLtpvtLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPD 244
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 305 RLLLHESVYDKVLEQLLtsyKQVKIGNPLEkgtllgPLHTPE-----SKKNFEKGIEVIKsqGGKILTGGKAvEGEGNFV 379
Cdd:cd07136 245 YVLVHESVKEKFIKELK---EEIKKFYGED------PLESPDygriiNEKHFDRLAGLLD--NGKIVFGGNT-DRETLYI 312
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 380 EPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIG--PLGSDC------GIV 450
Cdd:cd07136 313 EPTILdNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLEnlSFGGGCindtimHLA 392
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 15221042 451 NVNIPtngaeiggaFGGEKATGGGREAGSDSW------KQYMRRST 490
Cdd:cd07136 393 NPYLP---------FGGVGNSGMGSYHGKYSFdtfshkKSILKKST 429
PLN00412 PLN00412
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
24-432 1.90e-33

NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 215110 [Multi-domain]  Cd Length: 496  Bit Score: 132.57  E-value: 1.90e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   24 YVAGKWQ--ANGPLVSTLNPANNQPIAQVVEASLEDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRL 101
Cdd:PLN00412  19 YADGEWRtsSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAEC 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  102 LSLEMGKILAEGIGEVQEVIDMCDFA-------VGLSRQLNGSVIPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWN 174
Cdd:PLN00412  99 LVKEIAKPAKDAVTEVVRSGDLISYTaeegvriLGEGKFLVSDSFPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLAVSK 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  175 ACIALVCGNCVVWKgAPTTPLITIAMTklvAEVLEKNNLPGAIFTAMCG-GAEIGEAIAKDTRIPLVSFTGS------SR 247
Cdd:PLN00412 179 IAPALIAGNAVVLK-PPTQGAVAALHM---VHCFHLAGFPKGLISCVTGkGSEIGDFLTMHPGVNCISFTGGdtgiaiSK 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  248 VGSMVQQTvnarsgktlLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLTSYKQV 327
Cdd:PLN00412 255 KAGMVPLQ---------MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKL 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  328 KIGNPlEKGTLLGPLHTpESKKNFEKG-IEVIKSQGGKILTGGKAvegEGNFVEPTIIE-ISADAAVVKEELFAPVLYVL 405
Cdd:PLN00412 326 TVGPP-EDDCDITPVVS-ESSANFIEGlVMDAKEKGATFCQEWKR---EGNLIWPLLLDnVRPDMRIAWEEPFGPVLPVI 400
                        410       420
                 ....*....|....*....|....*..
gi 15221042  406 KFKSFGEAVAINNSVPQGLSSSIFTRN 432
Cdd:PLN00412 401 RINSVEEGIHHCNASNFGLQGCVFTRD 427
ALDH_AlkH-like cd07134
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ...
72-478 2.03e-31

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: 125.80  E-value: 2.03e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  72 WMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAE-GIGEVQEVIDMCDFAVglsRQLNGSVIPSERPNHMMLE 150
Cdd:cd07134  14 LRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEvDLTEILPVLSEINHAI---KHLKKWMKPKRVRTPLLLF 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 151 ------MWNPLGIVGVITAFNFP-CAVLGWNACiALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLpgAIFTamcG 223
Cdd:cd07134  91 gtkskiRYEPKGVCLIISPWNYPfNLAFGPLVS-AIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEV--AVFE---G 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 224 GAEIGEAIAKdtrIPL--VSFTGSSRVGSMVQqtvnARSGKTL----LELSGNNAIIVMDDADIQLAARSVLFAAVGTAG 297
Cdd:cd07134 165 DAEVAQALLE---LPFdhIFFTGSPAVGKIVM----AAAAKHLasvtLELGGKSPTIVDETADLKKAAKKIAWGKFLNAG 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 298 QRCTTCRRLLLHESVYDKVLEQLLTSYKQVKignplekGTLLGPLHTPE-----SKKNFE--KG-IEVIKSQGGKILTGG 369
Cdd:cd07134 238 QTCIAPDYVFVHESVKDAFVEHLKAEIEKFY-------GKDAARKASPDlarivNDRHFDrlKGlLDDAVAKGAKVEFGG 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 370 KAVEGEgNFVEPTIIE-ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLGS-DC 447
Cdd:cd07134 311 QFDAAQ-RYIAPTVLTnVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSgGV 389
                       410       420       430
                ....*....|....*....|....*....|....*...
gi 15221042 448 GI-------VNVNIPtngaeiggaFGGEKATGGGREAG 478
Cdd:cd07134 390 VVndvvlhfLNPNLP---------FGGVNNSGIGSYHG 418
ALDH_MaoC-N cd07128
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ...
21-489 1.13e-30

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: 124.69  E-value: 1.13e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  21 LGSYVAGKWQAN-GPLVSTLNPANNQPIAQVVEASLeDYEQGLK-ACEEAAKIWMQVTAPKRGDIVRQIGDALR------ 92
Cdd:cd07128   1 LQSYVAGQWHAGtGDGRTLHDAVTGEVVARVSSEGL-DFAAAVAyAREKGGPALRALTFHERAAMLKALAKYLMerkedl 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  93 -------------SKLD------------YLGRLLsLEMGKILAEGIGEVqevidmcdfavgLSRqlNGSVIPSerpnHM 147
Cdd:cd07128  80 yalsaatgatrrdSWIDidggigtlfayaSLGRRE-LPNAHFLVEGDVEP------------LSK--DGTFVGQ----HI 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 148 mlemWNPLGIVGV-ITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMtklVAEVLEKNNLPGAIFTAMCGGAe 226
Cdd:cd07128 141 ----LTPRRGVAVhINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAV---VKDIVESGLLPEGALQLICGSV- 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 227 iGEAIAKDTRIPLVSFTGSSRVGSM--VQQTVNARSGKTLLEL-SGNNAII----VMDDADIQLAARSVLFAAVGTAGQR 299
Cdd:cd07128 213 -GDLLDHLGEQDVVAFTGSAATAAKlrAHPNIVARSIRFNAEAdSLNAAILgpdaTPGTPEFDLFVKEVAREMTVKAGQK 291
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 300 CTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIkSQGGKILTGGKAVE------ 373
Cdd:cd07128 292 CTAIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATL-LAEAEVVFGGPDRFevvgad 370
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 374 -GEGNFVEPTII--EISADAAVVKE-ELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLGSDCGI 449
Cdd:cd07128 371 aEKGAFFPPTLLlcDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAAPYHGR 450
                       490       500       510       520
                ....*....|....*....|....*....|....*....|....*....
gi 15221042 450 VNVNIPTNGAEIGG--------AFGGEKATGGGRE-AGSDSWKQYMRRS 489
Cdd:cd07128 451 LLVLNRDSAKESTGhgsplpqlVHGGPGRAGGGEElGGLRGVKHYMQRT 499
ALDH_F3AB cd07132
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ...
152-498 8.31e-29

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: 118.48  E-value: 8.31e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 152 WNPLGIVGVITAFNFPCAVL-----GwnaciALVCGNCVVWKGAPTTPlitiAMTKLVAEVLEKNnLPGAIFTAMCGGAE 226
Cdd:cd07132  98 KEPLGVVLIIGAWNYPLQLTlvplvG-----AIAAGNCVVIKPSEVSP----ATAKLLAELIPKY-LDKECYPVVLGGVE 167
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 227 IGEAIAKDtRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRL 306
Cdd:cd07132 168 ETTELLKQ-RFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYV 246
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 307 LLHESVYDKVLEQLLTSYKQVkIGNPLEKGTLLGPLhtpESKKNFEKGIEVIKsqGGKILTGGKAVEGEgNFVEPTI-IE 385
Cdd:cd07132 247 LCTPEVQEKFVEALKKTLKEF-YGEDPKESPDYGRI---INDRHFQRLKKLLS--GGKVAIGGQTDEKE-RYIAPTVlTD 319
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 386 ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGplGSDCGIVNVN----------IP 455
Cdd:cd07132 320 VKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILS--NTSSGGVCVNdtimhytldsLP 397
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 15221042 456 tngaeiggaFGGEKATGGGREAGSDSWKQYMRRSTCTI-NYGNE 498
Cdd:cd07132 398 ---------FGGVGNSGMGAYHGKYSFDTFSHKRSCLVkSLNME 432
PRK11903 PRK11903
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
21-489 1.78e-26

3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;


Pssm-ID: 237016 [Multi-domain]  Cd Length: 521  Bit Score: 112.49  E-value: 1.78e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   21 LGSYVAGKWQA-NGPLVSTLNPANNQPIAQVVEASLeDYEQGLK-ACEEAAKIWMQVTAPKRGDIVRQIGDALR------ 92
Cdd:PRK11903   5 LANYVAGRWQAgSGAGTPLFDPVTGEELVRVSATGL-DLAAAFAfAREQGGAALRALTYAQRAALLAAIVKVLQanrday 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042   93 --------------SKLDYLGRLLSLEMGKILAEGIGEVQEVIDmcDFAVGLSRQlngsviPSERPNHMmlemWNPLGIV 158
Cdd:PRK11903  84 ydiatansgttrndSAVDIDGGIFTLGYYAKLGAALGDARLLRD--GEAVQLGKD------PAFQGQHV----LVPTRGV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  159 GV-ITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMtklVAEVLEKNNLPGAIFTAMCGGAeiGEAIAKDTRI 237
Cdd:PRK11903 152 ALfINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRM---VKDVVAAGILPAGALSVVCGSS--AGLLDHLQPF 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  238 PLVSFTGSSRVGSMVQQ--TVNARSGKTLLELSGNNAIIVMDDAD-----IQLAARSVLFAAVGTAGQRCTTCRRLLLHE 310
Cdd:PRK11903 227 DVVSFTGSAETAAVLRShpAVVQRSVRVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTAIRRIFVPE 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  311 SVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTPESKKNFEKGIEVIKSQgGKILTGGKAVE------GEGNFVEPTII 384
Cdd:PRK11903 307 ALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQ-AEVLFDGGGFAlvdadpAVAACVGPTLL 385
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  385 EIS-ADAA--VVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLGSDCGIVNVNIPTNGAEI 461
Cdd:PRK11903 386 GASdPDAAtaVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALELADSHGRVHVISPDVAALH 465
                        490       500       510
                 ....*....|....*....|....*....|....*..
gi 15221042  462 GG--------AFGGEKATGGGRE-AGSDSWKQYMRRS 489
Cdd:PRK11903 466 TGhgnvmpqsLHGGPGRAGGGEElGGLRALAFYHRRS 502
ALDH_CALDH_CalB cd07133
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ...
154-436 7.54e-23

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: 101.02  E-value: 7.54e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 154 PLGIVGVITAFNFPC--AVLGwnACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLpgAIFTamcGGAEIGEAI 231
Cdd:cd07133 101 PLGVVGIIVPWNYPLylALGP--LIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEV--AVVT---GGADVAAAF 173
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 232 akdTRIP---LVsFTGSSRVGSMVQQtvNArsGKTL----LELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCR 304
Cdd:cd07133 174 ---SSLPfdhLL-FTGSTAVGRHVMR--AA--AENLtpvtLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPD 245
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 305 RLLLHESVYDKVLEQLLTSYKQvkignplekgtllgplHTPESKKN-----------FE--KG-IEVIKSQGGKILTGGK 370
Cdd:cd07133 246 YVLVPEDKLEEFVAAAKAAVAK----------------MYPTLADNpdytsiinerhYArlQGlLEDARAKGARVIELNP 309
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15221042 371 AVE--GEGNFVEPTII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENI 436
Cdd:cd07133 310 AGEdfAATRKLPPTLVlNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQ 378
ALDH_F3FHI cd07137
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ...
154-482 4.39e-22

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: 98.64  E-value: 4.39e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 154 PLGIVGVITAFNFPCA-----VLGwnaciALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNnlpgAIfTAMCGGAEIG 228
Cdd:cd07137 101 PLGVVLVISAWNFPFLlslepVIG-----AIAAGNAVVLKPSELAPATSALLAKLIPEYLDTK----AI-KVIEGGVPET 170
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 229 EAIAkDTRIPLVSFTGSSRVGSMVQqtvnARSGKTL----LELSGNNAIIVMDDADIQLAARSVLFAAVGT-AGQRCTTC 303
Cdd:cd07137 171 TALL-EQKWDKIFFTGSPRVGRIIM----AAAAKHLtpvtLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCnNGQACIAP 245
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 304 RRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKGTLlgplHTPESKKNFE--KGIEVIKSQGGKILTGGkAVEGEGNFVEP 381
Cdd:cd07137 246 DYVLVEESFAPTLIDALKNTLEKFFGENPKESKDL----SRIVNSHHFQrlSRLLDDPSVADKIVHGG-ERDEKNLYIEP 320
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 382 TII-EISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNpENIFRWIGPLGSDCGIVNVNIPTNGAE 460
Cdd:cd07137 321 TILlDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKN-KELKRRIVAETSSGGVTFNDTVVQYAI 399
                       330       340
                ....*....|....*....|..
gi 15221042 461 IGGAFGGEKATGGGREAGSDSW 482
Cdd:cd07137 400 DTLPFGGVGESGFGAYHGKFSF 421
ALDH_KGSADH cd07129
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ...
59-428 1.99e-20

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: 93.76  E-value: 1.99e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  59 EQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLLSLEMGKILAEGIGE--------------------VQ 118
Cdd:cd07129   2 DAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGElgrttgqlrlfadlvregswLD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 119 EVIDMCDFAvglsRQlngsviPSERPNHMMLEMwnPLGIVGVITAFNFPCA--VLGWNACIALVCGNCVVWKGAPTTPLI 196
Cdd:cd07129  82 ARIDPADPD----RQ------PLPRPDLRRMLV--PLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKAHPAHPGT 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 197 TIAMTKLVAEVLEKNNLPGAIFTAM-CGGAEIGEAIAKDTRIPLVSFTGSSRVGSMVQQTVNAR-SGKTL-LELSGNNAI 273
Cdd:cd07129 150 SELVARAIRAALRATGLPAGVFSLLqGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARpEPIPFyAELGSVNPV 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 274 IVMDDAdiqLAARSVLFAA--VGT----AGQRCTTCRRLLLHESV-YDKVLEQLLTSYKQVKignpleKGTLLgplhTPE 346
Cdd:cd07129 230 FILPGA---LAERGEAIAQgfVGSltlgAGQFCTNPGLVLVPAGPaGDAFIAALAEALAAAP------AQTML----TPG 296
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 347 SKKNFEKGIEVIKSQGGKILTGGKAVEGEGNFVEPTIIEISADA----AVVKEELFAPVLYVLKFKSFGEAVAINNSVPQ 422
Cdd:cd07129 297 IAEAYRQGVEALAAAPGVRVLAGGAAAEGGNQAAPTLFKVDAAAfladPALQEEVFGPASLVVRYDDAAELLAVAEALEG 376

                ....*.
gi 15221042 423 GLSSSI 428
Cdd:cd07129 377 QLTATI 382
PLN02203 PLN02203
aldehyde dehydrogenase
154-440 9.75e-19

aldehyde dehydrogenase


Pssm-ID: 165847 [Multi-domain]  Cd Length: 484  Bit Score: 89.02  E-value: 9.75e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  154 PLGIVGVITAFNFPCAvLGWNACI-ALVCGNCVVWKGAPTTPlitiAMTKLVAEVLEKNNLPGAIfTAMCGGAEIGEAIA 232
Cdd:PLN02203 108 PLGVVLIFSSWNFPIG-LSLEPLIgAIAAGNAVVLKPSELAP----ATSAFLAANIPKYLDSKAV-KVIEGGPAVGEQLL 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  233 kDTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIV--MDDA-DIQLAARSVLFAAVGT-AGQRCTTCRRLLL 308
Cdd:PLN02203 182 -QHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSSSrDTKVAVNRIVGGKWGScAGQACIAIDYVLV 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  309 HESVYDKVLEQLLTSYKQVKIGNPLEKGTLLGPLhtpeSKKNFEKGIEVIK--SQGGKILTGGkAVEGEGNFVEPTII-E 385
Cdd:PLN02203 261 EERFAPILIELLKSTIKKFFGENPRESKSMARIL----NKKHFQRLSNLLKdpRVAASIVHGG-SIDEKKLFIEPTILlN 335
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15221042  386 ISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNpENIFRWI 440
Cdd:PLN02203 336 PPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNN-EKLKRRI 389
PLN02174 PLN02174
aldehyde dehydrogenase family 3 member H1
154-488 8.02e-18

aldehyde dehydrogenase family 3 member H1


Pssm-ID: 177831  Cd Length: 484  Bit Score: 85.87  E-value: 8.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  154 PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEknnlPGAIftAMCGGAEIGEAIAK 233
Cdd:PLN02174 112 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLD----SSAV--RVVEGAVTETTALL 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  234 DTRIPLVSFTGSSRVGSMVQQTVNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVG-TAGQRCTTCRRLLLHESV 312
Cdd:PLN02174 186 EQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTKEY 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  313 YDKVLEQLLTSYKQVKIGNPLEKGTLLGPLHTpeskKNFEKGIEVI--KSQGGKILTGGKAvEGEGNFVEPTI-IEISAD 389
Cdd:PLN02174 266 APKVIDAMKKELETFYGKNPMESKDMSRIVNS----THFDRLSKLLdeKEVSDKIVYGGEK-DRENLKIAPTIlLDVPLD 340
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  390 AAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGLSSSIFTRNPENIFRWIGPLgSDCGIVNVNIPTNGAEIGGAFGGEK 469
Cdd:PLN02174 341 SLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATV-SAGGIVVNDIAVHLALHTLPFGGVG 419
                        330
                 ....*....|....*....
gi 15221042  470 ATGGGREAGSDSWKQYMRR 488
Cdd:PLN02174 420 ESGMGAYHGKFSFDAFSHK 438
ALDH_PAD-PaaZ cd07127
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ...
154-439 6.21e-17

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: 83.68  E-value: 6.21e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 154 PLGIVGVITAFNFPCavlgWNA----CIALVCGNCVVWKGAPTTPLiTIAMTKLVA-EVLEKNNLPGAIFT--AMCGGAE 226
Cdd:cd07127 193 PRGVALVIGCSTFPT----WNGypglFASLATGNPVIVKPHPAAIL-PLAITVQVArEVLAEAGFDPNLVTlaADTPEEP 267
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 227 IGEAIAKDTRIPLVSFTGSSRVGSMVQQtvNARSGKTLLELSGNNAIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRL 306
Cdd:cd07127 268 IAQTLATRPEVRIIDFTGSNAFGDWLEA--NARQAQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNI 345
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 307 LL----------HESvYDKVLEQLLTSYKQVkIGNPLEKGTLLGPLHTPESKKNFEKGievikSQGGKILTGGKAVEG-- 374
Cdd:cd07127 346 YVprdgiqtddgRKS-FDEVAADLAAAIDGL-LADPARAAALLGAIQSPDTLARIAEA-----RQLGEVLLASEAVAHpe 418
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15221042 375 -EGNFVE-PTIIEI-SADAAVVKEELFAPVLYVLKFKSFGEAVAI-NNSVPQ--GLSSSIFTRNPENIFRW 439
Cdd:cd07127 419 fPDARVRtPLLLKLdASDEAAYAEERFGPIAFVVATDSTDHSIELaRESVREhgAMTVGVYSTDPEVVERV 489
ALDH_F12_P5CDH cd07126
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ...
23-408 2.98e-12

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: 68.68  E-value: 2.98e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  23 SYVAGKWQANGPLVSTLNPANNQP---IAQVVEASLEDYEQGLKACEEAAkIWMQVTAPKR----GDIVRQIGDALRSKL 95
Cdd:cd07126   1 NLVAGKWKGASNYTTLLDPLNGDKfisVPDTDEDEINEFVDSLRQCPKSG-LHNPLKNPERyllyGDVSHRVAHELRKPE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  96 --DYLGRLLSLEMGKILAEGIGEV---QEVI-----DMCDFavgLSRQLNgsvIPSERPNHMMLEMWNPLGIVGVITAFN 165
Cdd:cd07126  80 veDFFARLIQRVAPKSDAQALGEVvvtRKFLenfagDQVRF---LARSFN---VPGDHQGQQSSGYRWPYGPVAIITPFN 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 166 FPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTAMCGGAEIGEAIAKDTRIPLVSFTGS 245
Cdd:cd07126 154 FPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLC----GMPATDVDLIHSDGPTMNKILLEANPRMTLFTGS 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 246 SRVGsmvQQTVNARSGKTLLELSGNN-AIIVMDDADIQLAARSVLFAAVGTAGQRCTTCRRLLLHEsvyDKVLEQLLTSY 324
Cdd:cd07126 230 SKVA---ERLALELHGKVKLEDAGFDwKILGPDVSDVDYVAWQCDQDAYACSGQKCSAQSILFAHE---NWVQAGILDKL 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 325 KQVKIGNPLEKGTlLGPLHTPESKKNFEKGIEVIKSQGGKILTGGK------------AVEGEGNFVEPTIIEISADAAV 392
Cdd:cd07126 304 KALAEQRKLEDLT-IGPVLTWTTERILDHVDKLLAIPGAKVLFGGKpltnhsipsiygAYEPTAVFVPLEEIAIEENFEL 382
                       410
                ....*....|....*.
gi 15221042 393 VKEELFAPVLYVLKFK 408
Cdd:cd07126 383 VTTEVFGPFQVVTEYK 398
ALDH_F20_ACDH_EutE-like cd07081
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ...
139-462 1.50e-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: 63.05  E-value: 1.50e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 139 IPSERPNHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLP-GAI 217
Cdd:cd07081  80 VLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAGAPeNLI 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 218 FTAMCGGAEIGEAIAKDTRIPLVSFTGSSrvgSMVQQTvnARSGKTLLEL-SGNNAIIVMDDADIQLAARSVLFAAVGTA 296
Cdd:cd07081 160 GWIDNPSIELAQRLMKFPGIGLLLATGGP---AVVKAA--YSSGKPAIGVgAGNTPVVIDETADIKRAVQSIVKSKTFDN 234
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 297 GQRCTTCRRLLLHESVYDKVLEQLLTSYKQVKIGNPLEKgtllgplHTPESKKNFEKGIEVIKSQGGKILT-GGKAVEGE 375
Cdd:cd07081 235 GVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQQ-------VQPVILKNGDVNRDIVGQDAYKIAAaAGLKVPQE 307
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 376 GN--FVEPTIIEISADAAvvkEELFAPVLYVLKFKSFGEAVAINNSVPQ----GLSSSIFTRN---PENIFRWIGPLgsD 446
Cdd:cd07081 308 TRilIGEVTSLAEHEPFA---HEKLSPVLAMYRAANFADADAKALALKLeggcGHTSAMYSDNikaIENMNQFANAM--K 382
                       330
                ....*....|....*.
gi 15221042 447 CGIVNVNIPTNGAEIG 462
Cdd:cd07081 383 TSRFVKNGPCSQGGLG 398
ALDH-like cd07077
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ...
154-346 1.16e-08

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: 57.23  E-value: 1.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 154 PLGIVGVITAFNFPCAVLgWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPGAIFTAMCGGAEIGEAIAK 233
Cdd:cd07077 100 PIGVTMHILPSTNPLSGI-TSALRGIATRNQCIFRPHPSAPFTNRALALLFQAADAAHGPKILVLYVPHPSDELAEELLS 178
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 234 DTRIPLVSFTGSSrvgSMVQQTVNARSGKTLLELSGNNAIIVMDD-ADIQLAARSVLFAAVgTAGQRCTTCRRLLLHESV 312
Cdd:cd07077 179 HPKIDLIVATGGR---DAVDAAVKHSPHIPVIGFGAGNSPVVVDEtADEERASGSVHDSKF-FDQNACASEQNLYVVDDV 254
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15221042 313 YDKVLEQLLT--SYKQVKI-GNPLEKGTLLGPLHTPE 346
Cdd:cd07077 255 LDPLYEEFKLklVVEGLKVpQETKPLSKETTPSFDDE 291
ALDH_EutE cd07121
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ...
56-471 2.66e-06

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: 49.54  E-value: 2.66e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042  56 EDYEQGLKACEEAAKIWMQVTAPKRGDIVRQIGDALRSKLDYLGRLlslemgkILAE-GIGEVQEVIdmcdfavgLSRQL 134
Cdd:cd07121   4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEM-------AVEEtGMGRVEDKI--------AKNHL 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 135 NGSVIPSERP---------NHMMLEMWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVA 205
Cdd:cd07121  69 AAEKTPGTEDltttawsgdNGLTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELIN 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 206 EVLEKNNLPGAIFTAMCGGA-EIGEAIAKDTRIPLVSFTGSSRVGSMVQQtvnarSGKTLLEL-SGNNAIIVMDDADIQL 283
Cdd:cd07121 149 KAIAEAGGPDNLVVTVEEPTiETTNELMAHPDINLLVVTGGPAVVKAALS-----SGKKAIGAgAGNPPVVVDETADIEK 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 284 AARSVLFAAVGTAGQRCTTCRRLLLHESVYDKVLEQLLtSYKQVKIGNP-----LEKGTLLGPLHTPeSKKNFEKGIEVI 358
Cdd:cd07121 224 AARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAAMQ-RNGAYVLNDEqaeqlLEVVLLTNKGATP-NKKWVGKDASKI 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221042 359 KSQGGKILTGGKAVegegnfvepTIIEISADAAVVKEELFAPVLYVLKFKSFGEAVAINNSVPQGL--SSSIFTRNPENI 436
Cdd:cd07121 302 LKAAGIEVPADIRL---------IIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSKNVENL 372
                       410       420       430
                ....*....|....*....|....*....|....*
gi 15221042 437 FRWIGPLgsDCGIVNVNIPTnGAEIGgaFGGEKAT 471
Cdd:cd07121 373 TKMARAM--QTTIFVKNGPS-YAGLG--VGGEGYT 402
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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