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Conserved domains on  [gi|20129399|ref|NP_609285|]
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aldehyde dehydrogenase, isoform A [Drosophila melanogaster]

Protein Classification

ALDH_F1AB_F2_RALDH1 domain-containing protein (domain architecture ID 10163008)

ALDH_F1AB_F2_RALDH1 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ALDH_F1AB_F2_RALDH1 cd07141
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ...
34-514 0e+00

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


:

Pssm-ID: 143459  Cd Length: 481  Bit Score: 1004.56  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  34 TPDILYTGVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLGSPWRRMDASERGRLLYRLAD 113
Cdd:cd07141   1 NPEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLAD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 114 LMERDQVYLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPIL 193
Cdd:cd07141  81 LIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 194 MMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLI 272
Cdd:cd07141 161 MAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGpTAGAAISSHPDIDKVAFTGSTEVGKLI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 273 QLASGNTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGN 352
Cdd:cd07141 241 QQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGN 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 353 PFDLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPeGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKK 432
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRH-GDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKT 399
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 433 LDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVI 512
Cdd:cd07141 400 IDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVT 479

                ..
gi 20129399 513 VK 514
Cdd:cd07141 480 IK 481
 
Name Accession Description Interval E-value
ALDH_F1AB_F2_RALDH1 cd07141
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ...
34-514 0e+00

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


Pssm-ID: 143459  Cd Length: 481  Bit Score: 1004.56  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  34 TPDILYTGVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLGSPWRRMDASERGRLLYRLAD 113
Cdd:cd07141   1 NPEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLAD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 114 LMERDQVYLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPIL 193
Cdd:cd07141  81 LIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 194 MMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLI 272
Cdd:cd07141 161 MAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGpTAGAAISSHPDIDKVAFTGSTEVGKLI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 273 QLASGNTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGN 352
Cdd:cd07141 241 QQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGN 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 353 PFDLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPeGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKK 432
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRH-GDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKT 399
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 433 LDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVI 512
Cdd:cd07141 400 IDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVT 479

                ..
gi 20129399 513 VK 514
Cdd:cd07141 480 IK 481
PLN02466 PLN02466
aldehyde dehydrogenase family 2 member
9-512 0e+00

aldehyde dehydrogenase family 2 member


Pssm-ID: 215259  Cd Length: 538  Bit Score: 706.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399    9 ALLRSQAKNF--AAAVANYSS----LPQPQTTP-DILYTGVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDI 81
Cdd:PLN02466  20 ALLRSRGRNGgrGRGIRRFSTaaaaVEEPITPPvQVSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNR 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   82 AVQAARNAFKLGsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHG 161
Cdd:PLN02466 100 AVAAARKAFDEG-PWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHG 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  162 KTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVV 241
Cdd:PLN02466 179 LTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVV 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  242 PGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQC 320
Cdd:PLN02466 259 SGFGpTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQC 338
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  321 CCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRpEGLPGYF 400
Cdd:PLN02466 339 CCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDR-FGSKGYY 417
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  401 VQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLA 480
Cdd:PLN02466 418 IQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFD 497
                        490       500       510
                 ....*....|....*....|....*....|..
gi 20129399  481 AQAPFGGYKMSGHGRENGEYALSNYTEVKSVI 512
Cdd:PLN02466 498 AAIPFGGYKMSGIGREKGIYSLNNYLQVKAVV 529
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
48-511 0e+00

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


Pssm-ID: 306641  Cd Length: 458  Bit Score: 658.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399    48 WHKSKSGKIfETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYLASLET 127
Cdd:pfam00171   1 WVDSSSETI-EVINPATGEVIATVPAATAEDVDAAVAAAREAFP---AWRKTPAAERAAILRKAADLLEERRDELAELET 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   128 LDNGKPYSMSYnVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGN 207
Cdd:pfam00171  77 LETGKPLAEAR-GEVDRAIDTLRYYAGLARRLDGEVLPSDPGRLAYTRREPLGVVGAITPWNFPLLLAAWKIAPALAAGN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   208 TIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGnTNLKRVTL 286
Cdd:pfam00171 156 TVVLKPSELTPLSALLLAELFEEAGLPAGVLNVVTGSGaEVGDALVEHPDVRKVSFTGSTAVGRHIAEAAA-KNLKRVTL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   287 ELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNE 366
Cdd:pfam00171 235 ELGGKNPLIVLEDADLDAAVEGAVFGAFGNAGQVCTAGSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDVGPLISK 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   367 EQMEKILGMIKTGKKQGAKLVAGGSRPEglPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYG 446
Cdd:pfam00171 315 AQLERVLGYVEDAKEEGAKLLTGGPGLD--NGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYG 392
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20129399   447 LAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQA-PFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:pfam00171 393 LAAGVFTNDLERALRVAERLEAGMVWINDYTTGDADGqPFGGFKQSGFGREGGPYGLEEYTETKTV 458
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Energy production and ...
43-514 0e+00

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Energy production and conversion];


Pssm-ID: 223944  Cd Length: 472  Bit Score: 580.02  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  43 FINNEWHKSKSGkiFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:COG1012   4 LIDGEWVDGAST--IEVINPATGEVIATVPAATAEDVDAAVAAARAAFE---AWSRLSAEERAAILRRIADLLEARAEEL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 123 ASLETLDNGKPYSMSYnVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPA 202
Cdd:COG1012  79 AALITLETGKPISEAR-GEIARAADFIRYYAEEARRLEGETIPTDKGSKALVRREPLGVVGAITPWNFPLALAAWKLAPA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 203 LATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNtNL 281
Cdd:COG1012 158 LAAGNTVVLKPSEQTPLSALALAELAAEAGLPAGVLNVVTGGGaEVGDALVAHPDVDAISFTGSTAVGRAIAAAAAA-NL 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 282 KRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQG 361
Cdd:COG1012 237 KPVTLELGGKSPAIVLEDADLDAAVDAAVFGAFFNAGQRCTAASRLIVHESVYDEFVERLVARAASLKVGDPLDPSTDLG 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 362 PQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEglpGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERAN 441
Cdd:COG1012 317 PLISEEQLDRVEGYIEDAVAEGARLLAGGKRPG---GYFVEPTILEGVTPDMRIAREEIFGPVLPVIRFKDEEEAIELAN 393
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20129399 442 NSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLA--AQAPFGGYKMSGHGRENGEYALSNYTEVKSVIVK 514
Cdd:COG1012 394 DTEYGLAAAIFTRDLARAFRVARRLEAGMVGINDYTGGAdiAYLPFGGVKQSGLGREGGKYGLEEFTEVKTVTIK 468
BADH TIGR01804
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...
43-509 0e+00

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


Pssm-ID: 200131  Cd Length: 467  Bit Score: 544.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399    43 FINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:TIGR01804   1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQG---EWAAMSPMERGRILRRAADLIRERNEEL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   123 ASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPA 202
Cdd:TIGR01804  78 AKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   203 LATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIqLASGNTNL 281
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGaEVGPLLVNHPDVAKVSFTGGVPTGKKI-MAAAAGHL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   282 KRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQG 361
Cdd:TIGR01804 237 KHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   362 PQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEGLP---GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIE 438
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGRPENVGlqnGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20129399   439 RANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVK 509
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
 
Name Accession Description Interval E-value
ALDH_F1AB_F2_RALDH1 cd07141
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ...
34-514 0e+00

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


Pssm-ID: 143459  Cd Length: 481  Bit Score: 1004.56  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  34 TPDILYTGVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLGSPWRRMDASERGRLLYRLAD 113
Cdd:cd07141   1 NPEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLAD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 114 LMERDQVYLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPIL 193
Cdd:cd07141  81 LIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 194 MMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLI 272
Cdd:cd07141 161 MAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGpTAGAAISSHPDIDKVAFTGSTEVGKLI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 273 QLASGNTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGN 352
Cdd:cd07141 241 QQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGN 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 353 PFDLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPeGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKK 432
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRH-GDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKT 399
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 433 LDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVI 512
Cdd:cd07141 400 IDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVT 479

                ..
gi 20129399 513 VK 514
Cdd:cd07141 480 IK 481
ALDH_F1-2_Ald2-like cd07091
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...
40-511 0e+00

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


Pssm-ID: 143410  Cd Length: 476  Bit Score: 869.99  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  40 TGVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLGSpWRRMDASERGRLLYRLADLMERDQ 119
Cdd:cd07091   4 TGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGW-WRKMDPRERGRLLNKLADLIERDR 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 120 VYLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKL 199
Cdd:cd07091  83 DELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKL 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 200 GPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGN 278
Cdd:cd07091 163 APALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGpTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAK 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 279 TNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNT 358
Cdd:cd07091 243 SNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDT 322
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 359 EQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPeGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIE 438
Cdd:cd07091 323 FQGPQVSKAQFDKILSYIESGKKEGATLLTGGERH-GSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIE 401
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20129399 439 RANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:cd07091 402 RANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
ALDH_F2BC cd07142
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ...
37-512 0e+00

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


Pssm-ID: 143460  Cd Length: 476  Bit Score: 743.93  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  37 ILYTGVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLGsPWRRMDASERGRLLYRLADLME 116
Cdd:cd07142   1 VKHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEG-PWPRMTGYERSRILLRFADLLE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 117 RDQVYLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMA 196
Cdd:cd07142  80 KHADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 197 WKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLA 275
Cdd:cd07142 160 WKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGpTAGAAIASHMDVDKVAFTGSTEVGKIIMQL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 276 SGNTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFD 355
Cdd:cd07142 240 AAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFR 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 356 LNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPeGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDE 435
Cdd:cd07142 320 KGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRI-GSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDE 398
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20129399 436 VIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVI 512
Cdd:cd07142 399 VIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVV 475
PLN02466 PLN02466
aldehyde dehydrogenase family 2 member
9-512 0e+00

aldehyde dehydrogenase family 2 member


Pssm-ID: 215259  Cd Length: 538  Bit Score: 706.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399    9 ALLRSQAKNF--AAAVANYSS----LPQPQTTP-DILYTGVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDI 81
Cdd:PLN02466  20 ALLRSRGRNGgrGRGIRRFSTaaaaVEEPITPPvQVSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNR 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   82 AVQAARNAFKLGsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHG 161
Cdd:PLN02466 100 AVAAARKAFDEG-PWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHG 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  162 KTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVV 241
Cdd:PLN02466 179 LTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVV 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  242 PGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQC 320
Cdd:PLN02466 259 SGFGpTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQC 338
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  321 CCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRpEGLPGYF 400
Cdd:PLN02466 339 CCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDR-FGSKGYY 417
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  401 VQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLA 480
Cdd:PLN02466 418 IQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFD 497
                        490       500       510
                 ....*....|....*....|....*....|..
gi 20129399  481 AQAPFGGYKMSGHGRENGEYALSNYTEVKSVI 512
Cdd:PLN02466 498 AAIPFGGYKMSGIGREKGIYSLNNYLQVKAVV 529
ALDH_AldA_AN0554 cd07143
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ...
40-515 0e+00

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


Pssm-ID: 143461  Cd Length: 481  Bit Score: 672.70  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  40 TGVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgSPWRR-MDASERGRLLYRLADLMERD 118
Cdd:cd07143   7 TGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE--TDWGLkVSGSKRGRCLSKLADLMERN 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 119 QVYLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWK 198
Cdd:cd07143  85 LDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWK 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 199 LGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASG 277
Cdd:cd07143 165 IAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGrTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAA 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 278 NTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLN 357
Cdd:cd07143 245 KSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAED 324
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 358 TEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRpEGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVI 437
Cdd:cd07143 325 TFQGPQVSQIQYERIMSYIESGKAEGATVETGGKR-HGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAI 403
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20129399 438 ERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIVKV 515
Cdd:cd07143 404 KRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL 481
ALDH_ALD2-YMR170C cd07144
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ...
40-511 0e+00

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


Pssm-ID: 143462  Cd Length: 484  Bit Score: 659.87  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  40 TGVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgSPWRRMDASERGRLLYRLADLMERDQ 119
Cdd:cd07144   8 TGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFE--SWWSKVTGEERGELLDKLADLVEKNR 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 120 VYLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKL 199
Cdd:cd07144  86 DLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKL 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 200 GPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGT-AGAALANHCDVDKVAFTGSTDVGKLIQLASGN 278
Cdd:cd07144 166 APALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAvAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQ 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 279 tNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRT-VGNPFDLN 357
Cdd:cd07144 246 -NLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYkVGSPFDDD 324
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 358 TEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGS-RPEGL-PGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDE 435
Cdd:cd07144 325 TVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEkAPEGLgKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEE 404
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20129399 436 VIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:cd07144 405 AIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
48-511 0e+00

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


Pssm-ID: 306641  Cd Length: 458  Bit Score: 658.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399    48 WHKSKSGKIfETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYLASLET 127
Cdd:pfam00171   1 WVDSSSETI-EVINPATGEVIATVPAATAEDVDAAVAAAREAFP---AWRKTPAAERAAILRKAADLLEERRDELAELET 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   128 LDNGKPYSMSYnVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGN 207
Cdd:pfam00171  77 LETGKPLAEAR-GEVDRAIDTLRYYAGLARRLDGEVLPSDPGRLAYTRREPLGVVGAITPWNFPLLLAAWKIAPALAAGN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   208 TIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGnTNLKRVTL 286
Cdd:pfam00171 156 TVVLKPSELTPLSALLLAELFEEAGLPAGVLNVVTGSGaEVGDALVEHPDVRKVSFTGSTAVGRHIAEAAA-KNLKRVTL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   287 ELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNE 366
Cdd:pfam00171 235 ELGGKNPLIVLEDADLDAAVEGAVFGAFGNAGQVCTAGSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDVGPLISK 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   367 EQMEKILGMIKTGKKQGAKLVAGGSRPEglPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYG 446
Cdd:pfam00171 315 AQLERVLGYVEDAKEEGAKLLTGGPGLD--NGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYG 392
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20129399   447 LAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQA-PFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:pfam00171 393 LAAGVFTNDLERALRVAERLEAGMVWINDYTTGDADGqPFGGFKQSGFGREGGPYGLEEYTETKTV 458
PLN02766 PLN02766
coniferyl-aldehyde dehydrogenase
35-512 0e+00

coniferyl-aldehyde dehydrogenase


Pssm-ID: 215410  Cd Length: 501  Bit Score: 636.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   35 PDILYTGVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLGsPWRRMDASERGRLLYRLADL 114
Cdd:PLN02766  16 PEIKFTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHG-PWPRMSGFERGRIMMKFADL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  115 MERDQVYLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILM 194
Cdd:PLN02766  95 IEEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTM 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  195 MAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQ 273
Cdd:PLN02766 175 FFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGpTAGAAIASHMDVDKVSFTGSTEVGRKIM 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  274 LASGNTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNP 353
Cdd:PLN02766 255 QAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDP 334
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  354 FDLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGsRPEGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKL 433
Cdd:PLN02766 335 FDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGG-KPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTV 413
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20129399  434 DEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVI 512
Cdd:PLN02766 414 EEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVV 492
ALDH cd07078
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ...
80-513 0e+00

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


Pssm-ID: 143397  Cd Length: 432  Bit Score: 619.99  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  80 DIAVQAARNAFKLgspWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSYnVDLPTAIKNLRYFAGWADKN 159
Cdd:cd07078   1 DAAVAAARAAFKA---WAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEAL-GEVARAADTFRYYAGLARRL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 160 HGKTIP-MDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVV 238
Cdd:cd07078  77 HGEVIPsPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 239 NVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNtNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNM 317
Cdd:cd07078 157 NVVTGDGdEVGAALASHPRVDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 318 GQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEGLP 397
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGK 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 398 GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYN 477
Cdd:cd07078 316 GYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 20129399 478 VLA-AQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07078 396 VGAePSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
ALDH_DhaS cd07114
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ...
59-513 0e+00

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


Pssm-ID: 143432  Cd Length: 457  Bit Score: 614.94  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  59 TINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlGSPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYS--- 135
Cdd:cd07114   1 SINPATGEPWARVPEASAADVDRAVAAARAAFE-GGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRetr 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 136 --MSYnvdlptAIKNLRYFAGWADKNHGKTIPMD-GDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLK 212
Cdd:cd07114  80 aqVRY------LAEWYRYYAGLADKIEGAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 213 PAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNtNLKRVTLELGGK 291
Cdd:cd07114 154 PSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGpETGEALVEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGK 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 292 SPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEK 371
Cdd:cd07114 233 SPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEK 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 372 ILGMIKTGKKQGAKLVAGGSRPEGLP---GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLA 448
Cdd:cd07114 313 VERYVARAREEGARVLTGGERPSGADlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLA 392
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20129399 449 AAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07114 393 AGIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
ALDH_GABALDH-PuuC cd07112
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ...
54-511 0e+00

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


Pssm-ID: 143430  Cd Length: 462  Bit Score: 613.46  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  54 GKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLGSpWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKP 133
Cdd:cd07112   1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGV-WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 134 YSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKP 213
Cdd:cd07112  80 ISDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 214 AEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNTNLKRVTLELGGKS 292
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGhTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKS 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 293 PNIILSDT-DMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEK 371
Cdd:cd07112 240 PNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDK 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 372 ILGMIKTGKKQGAKLVAGGSR--PEGlPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAA 449
Cdd:cd07112 320 VLGYIESGKAEGARLVAGGKRvlTET-GGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAA 398
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20129399 450 AVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:cd07112 399 SVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
ALDH_BADH-GbsA cd07119
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ...
43-511 0e+00

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


Pssm-ID: 143437  Cd Length: 482  Bit Score: 611.62  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  43 FINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlGSPWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:cd07119   1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFD-SGEWPHLPAQERAALLFRIADKIREDAEEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 123 ASLETLDNGKPYSMSYnVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPA 202
Cdd:cd07119  80 ARLETLNTGKTLRESE-IDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 203 LATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLI-QLASGNtn 280
Cdd:cd07119 159 LAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGaTVGAELAESPDVDLVSFTGGTATGRSImRAAAGN-- 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 281 LKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQ 360
Cdd:cd07119 237 VKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEM 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 361 GPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEG---LPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVI 437
Cdd:cd07119 317 GPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGdelAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAI 396
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20129399 438 ERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:cd07119 397 RLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
ALDH_HMSADH_HapE cd07115
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ...
59-515 0e+00

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


Pssm-ID: 143433  Cd Length: 453  Bit Score: 603.28  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  59 TINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSY 138
Cdd:cd07115   1 TLNPATGELIARVAQASAEDVDAAVAAARAAFE---AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAAR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 139 NVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTS 218
Cdd:cd07115  78 RLDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 219 LTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVG-KLIQLASGntNLKRVTLELGGKSPNII 296
Cdd:cd07115 158 LSALRIAELMAEAGFPAGVLNVVTGFGeVAGAALVEHPDVDKITFTGSTAVGrKIMQGAAG--NLKRVSLELGGKSANIV 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 297 LSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMI 376
Cdd:cd07115 236 FADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYV 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 377 KTGKKQGAKLVAGGSRPeGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDL 456
Cdd:cd07115 316 DVGREEGARLLTGGKRP-GARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDL 394
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20129399 457 DKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIVKV 515
Cdd:cd07115 395 GRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Energy production and ...
43-514 0e+00

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Energy production and conversion];


Pssm-ID: 223944  Cd Length: 472  Bit Score: 580.02  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  43 FINNEWHKSKSGkiFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:COG1012   4 LIDGEWVDGAST--IEVINPATGEVIATVPAATAEDVDAAVAAARAAFE---AWSRLSAEERAAILRRIADLLEARAEEL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 123 ASLETLDNGKPYSMSYnVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPA 202
Cdd:COG1012  79 AALITLETGKPISEAR-GEIARAADFIRYYAEEARRLEGETIPTDKGSKALVRREPLGVVGAITPWNFPLALAAWKLAPA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 203 LATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNtNL 281
Cdd:COG1012 158 LAAGNTVVLKPSEQTPLSALALAELAAEAGLPAGVLNVVTGGGaEVGDALVAHPDVDAISFTGSTAVGRAIAAAAAA-NL 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 282 KRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQG 361
Cdd:COG1012 237 KPVTLELGGKSPAIVLEDADLDAAVDAAVFGAFFNAGQRCTAASRLIVHESVYDEFVERLVARAASLKVGDPLDPSTDLG 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 362 PQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEglpGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERAN 441
Cdd:COG1012 317 PLISEEQLDRVEGYIEDAVAEGARLLAGGKRPG---GYFVEPTILEGVTPDMRIAREEIFGPVLPVIRFKDEEEAIELAN 393
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20129399 442 NSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLA--AQAPFGGYKMSGHGRENGEYALSNYTEVKSVIVK 514
Cdd:COG1012 394 DTEYGLAAAIFTRDLARAFRVARRLEAGMVGINDYTGGAdiAYLPFGGVKQSGLGREGGKYGLEEFTEVKTVTIK 468
ALDH_ACDHII_AcoD-like cd07559
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ...
41-513 0e+00

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  Cd Length: 480  Bit Score: 578.91  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  41 GVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQV 120
Cdd:cd07559   2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFK---TWGKTSVAERANILNKIADRIEENLE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 121 YLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLG 200
Cdd:cd07559  79 LLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 201 PALATGNTIVLKPAEQTSLTALYIAQLVKEAgFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNt 279
Cdd:cd07559 159 PALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGsEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE- 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 280 NLKRVTLELGGKSPNIILSD-----TDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPF 354
Cdd:cd07559 237 NLIPVTLELGGKSPNIFFDDamdadDDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPL 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 355 DLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSR---PEGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFK 431
Cdd:cd07559 317 DPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERltlGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 432 KLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNI 476

                ..
gi 20129399 512 IV 513
Cdd:cd07559 477 LV 478
ALDH_F8_HMSADH cd07093
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ...
59-513 0e+00

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  Cd Length: 455  Bit Score: 576.82  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  59 TINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSY 138
Cdd:cd07093   1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFP---GWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLAR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 139 NVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTS 218
Cdd:cd07093  78 TRDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 219 LTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNtNLKRVTLELGGKSPNIIL 297
Cdd:cd07093 158 LTAWLLAELANEAGLPPGVVNVVHGFGpEAGAALVAHPDVDLISFTGETATGRTIMRAAAP-NLKPVSLELGGKNPNIVF 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 298 SDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIK 377
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVE 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 378 TGKKQGAKLVAGGSRPEGLP---GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTK 454
Cdd:cd07093 317 LARAEGATILTGGGRPELPDlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20129399 455 DLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
PRK13252 PRK13252
betaine aldehyde dehydrogenase; Provisional
43-513 0e+00

betaine aldehyde dehydrogenase; Provisional


Pssm-ID: 183918  Cd Length: 488  Bit Score: 564.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   43 FINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLgspWRRMDASERGRLLYRLADLM-ERDQVy 121
Cdd:PRK13252  10 YIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKI---WAAMTAMERSRILRRAVDILrERNDE- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  122 LASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGP 201
Cdd:PRK13252  86 LAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  202 ALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGTAGAALANHCDVDKVAFTGSTDVGKLIqLASGNTNL 281
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKV-MAAAAASL 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  282 KRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQG 361
Cdd:PRK13252 245 KEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFG 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  362 PQVNEEQMEKILGMIKTGKKQGAKLVAGGSR--PEGLP-GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIE 438
Cdd:PRK13252 325 PLVSFAHRDKVLGYIEKGKAEGARLLCGGERltEGGFAnGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIA 404
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20129399  439 RANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:PRK13252 405 RANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQV 479
ALDH_F1L_FTFDH cd07140
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ...
43-514 0e+00

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


Pssm-ID: 143458  Cd Length: 486  Bit Score: 550.95  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  43 FINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlGSPWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:cd07140   9 FINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFE-NGEWGKMNARDRGRLMYRLADLMEEHQEEL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 123 ASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMD----GDFFTYTRHEPVGVCGQIIPWNFPILMMAWK 198
Cdd:cd07140  88 ATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINqarpNRNLTLTKREPIGVCGIVIPWNYPLMMLAWK 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 199 LGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGT-AGAALANHCDVDKVAFTGSTDVGKLIQLASG 277
Cdd:cd07140 168 MAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSlVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCA 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 278 NTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLN 357
Cdd:cd07140 248 VSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRS 327
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 358 TEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEgLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFK--KLDE 435
Cdd:cd07140 328 TDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVD-RPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDdgDVDG 406
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20129399 436 VIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIVK 514
Cdd:cd07140 407 VLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTIE 485
ALDH_F9_TMBADH cd07090
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ...
59-513 0e+00

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  Cd Length: 457  Bit Score: 550.37  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  59 TINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLgspWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSy 138
Cdd:cd07090   1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKE---WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEA- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 139 NVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTS 218
Cdd:cd07090  77 RVDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 219 LTALYIAQLVKEAGFPEGVVNVVPGFGTAGAALANHCDVDKVAFTGSTDVGKLIQLASGNtNLKRVTLELGGKSPNIILS 298
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAK-GIKHVTLELGGKSPLIIFD 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 299 DTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIKT 378
Cdd:cd07090 236 DADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIES 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 379 GKKQGAKLVAGGSRPEGLP----GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTK 454
Cdd:cd07090 316 AKQEGAKVLCGGERVVPEDglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTR 395
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20129399 455 DLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07090 396 DLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYV 454
BADH TIGR01804
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...
43-509 0e+00

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


Pssm-ID: 200131  Cd Length: 467  Bit Score: 544.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399    43 FINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:TIGR01804   1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQG---EWAAMSPMERGRILRRAADLIRERNEEL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   123 ASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPA 202
Cdd:TIGR01804  78 AKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   203 LATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIqLASGNTNL 281
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGaEVGPLLVNHPDVAKVSFTGGVPTGKKI-MAAAAGHL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   282 KRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQG 361
Cdd:TIGR01804 237 KHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   362 PQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEGLP---GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIE 438
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGRPENVGlqnGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20129399   439 RANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVK 509
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
ALDH_StaphAldA1 cd07117
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ...
41-513 0e+00

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: 537.04  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  41 GVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQV 120
Cdd:cd07117   2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFK---TWRKTTVAERANILNKIADIIDENKE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 121 YLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLG 200
Cdd:cd07117  79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 201 PALATGNTIVLKPAEQTSLTALYIAQLVKEAgFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNt 279
Cdd:cd07117 159 PALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGsKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK- 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 280 NLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTE 359
Cdd:cd07117 237 KLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 360 QGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSR--PEGLP-GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEV 436
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRltENGLDkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20129399 437 IERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
ALDH_AAS00426 cd07109
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ...
60-513 0e+00

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  Cd Length: 454  Bit Score: 535.28  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  60 INPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgSPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSYN 139
Cdd:cd07109   2 FDPSTGEVFARIARGGAADVDRAVQAARRAFE--SGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 140 vDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSL 219
Cdd:cd07109  80 -DVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 220 TALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNtNLKRVTLELGGKSPNIILS 298
Cdd:cd07109 159 TALRLAELAEEAGLPAGALNVVTGLGaEAGAALVAHPGVDHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIVFA 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 299 DTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDlNTEQGPQVNEEQMEKILGMIKT 378
Cdd:cd07109 238 DADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVAR 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 379 GKKQGAKLVAGGSRPEGLP--GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDL 456
Cdd:cd07109 317 ARARGARIVAGGRIAEGAPagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDG 396
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 20129399 457 DKANYIVGGLRAGTVWVNTYNVLAA-QAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07109 397 DRALRVARRLRAGQVFVNNYGAGGGiELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
ALDH_CddD_SSP0762 cd07138
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ...
43-512 0e+00

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  Cd Length: 466  Bit Score: 526.30  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  43 FINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:cd07138   2 YIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFP---AWSATSVEERAALLERIAEAYEARADEL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 123 ASLETLDNGKPYSMSYNVDLPTAIKNLRYFAG------WADKNHGKTIpmdgdfftytRHEPVGVCGQIIPWNFPILMMA 196
Cdd:cd07138  79 AQAITLEMGAPITLARAAQVGLGIGHLRAAADalkdfeFEERRGNSLV----------VREPIGVCGLITPWNWPLNQIV 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 197 WKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLA 275
Cdd:cd07138 149 LKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGpVVGEALSAHPDVDMVSFTGSTRAGKRVAEA 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 276 SGNTnLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFD 355
Cdd:cd07138 229 AADT-VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRD 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 356 LNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGS-RPEGLP-GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKL 433
Cdd:cd07138 308 PATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPgRPEGLErGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDE 387
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20129399 434 DEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNtYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVI 512
Cdd:cd07138 388 DEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
ALDH_F5_SSADH_GabD cd07103
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ...
60-511 6.94e-179

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  Cd Length: 451  Bit Score: 515.06  E-value: 6.94e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  60 INPTTAEVIAEIQCADKEDIDIAVQAARNAFKLgspWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSYN 139
Cdd:cd07103   2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKT---WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 140 -VDLptAIKNLRYFAGWADKNHGKTIP-MDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQT 217
Cdd:cd07103  79 eVDY--AASFLEWFAEEARRIYGRTIPsPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEET 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 218 SLTALYIAQLVKEAGFPEGVVNVVPGFGTA-GAALANHCDVDKVAFTGSTDVGK-LIQLASgnTNLKRVTLELGGKSPNI 295
Cdd:cd07103 157 PLSALALAELAEEAGLPAGVLNVVTGSPAEiGEALCASPRVRKISFTGSTAVGKlLMAQAA--DTVKRVSLELGGNAPFI 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 296 ILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGM 375
Cdd:cd07103 235 VFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEAL 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 376 IKTGKKQGAKLVAGGSRPeGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKD 455
Cdd:cd07103 315 VEDAVAKGAKVLTGGKRL-GLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRD 393
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20129399 456 LDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:cd07103 394 LARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
ALDH_AldA-Rv0768 cd07139
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ...
43-513 1.87e-177

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  Cd Length: 471  Bit Score: 512.12  E-value: 1.87e-177
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  43 FINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLGsPWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:cd07139   2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNG-PWPRLSPAERAAVLRRLADALEARADEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 123 ASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTI---PMDGDffTYTRHEPVGVCGQIIPWNFPILMMAWKL 199
Cdd:cd07139  81 ARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEERrpgSGGGH--VLVRREPVGVVAAIVPWNAPLFLAALKI 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 200 GPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGTAGAALANHCDVDKVAFTGSTDVGKLIQLASGNt 279
Cdd:cd07139 159 APALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGE- 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 280 NLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTE 359
Cdd:cd07139 238 RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQ 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 360 QGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEGLP-GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIE 438
Cdd:cd07139 318 IGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGLDrGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVR 397
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20129399 439 RANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYnVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07139 398 IANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
ALDH_F10_BADH cd07110
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ...
59-512 4.78e-177

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  Cd Length: 456  Bit Score: 510.36  E-value: 4.78e-177
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  59 TINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSy 138
Cdd:cd07110   1 VINPATEATIGEIPAATAEDVDAAVRAARRAFP---RWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 139 NVDLPTAIKNLRYFAGWA---DKNHGKTIPM-DGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPA 214
Cdd:cd07110  77 AWDVDDVAGCFEYYADLAeqlDAKAERAVPLpSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 215 EQTSLTALYIAQLVKEAGFPEGVVNVVPGFGT-AGAALANHCDVDKVAFTGSTDVGKLIQLASGNTnLKRVTLELGGKSP 293
Cdd:cd07110 157 ELTSLTELELAEIAAEAGLPPGVLNVVTGTGDeAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQD-IKPVSLELGGKSP 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 294 NIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKIL 373
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 374 GMIKTGKKQGAKLVAGGSRPEGLP-GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVF 452
Cdd:cd07110 316 SFIARGKEEGARLLCGGRRPAHLEkGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 453 TKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVI 512
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
ALDH_SNDH cd07118
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ...
60-511 1.56e-175

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  Cd Length: 454  Bit Score: 506.49  E-value: 1.56e-175
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  60 INPTTAEVIAEIQCADKEDIDIAVQAARNAFKLGsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSYN 139
Cdd:cd07118   2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKG-PWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 140 vDLPTAIKNLRYFAGWADKNHGKTIPMDG-DFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTS 218
Cdd:cd07118  81 -EIEGAADLWRYAASLARTLHGDSYNNLGdDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 219 LTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNtNLKRVTLELGGKSPNIIL 297
Cdd:cd07118 160 GTTLMLAELLIEAGLPAGVVNIVTGYGaTVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVF 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 298 SDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIK 377
Cdd:cd07118 239 ADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVD 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 378 TGKKQGAKLVAGGSRPEGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLD 457
Cdd:cd07118 319 AGRAEGATLLLGGERLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDID 398
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....
gi 20129399 458 KANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:cd07118 399 TALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
ALDH_CddD-AldA-like cd07089
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ...
60-513 4.19e-173

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  Cd Length: 459  Bit Score: 500.62  E-value: 4.19e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  60 INPTTAEVIAEIQCADKEDIDIAVQAARNAFKlGSPWRrMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSYN 139
Cdd:cd07089   2 INPATEEVIGTAPDAGAADVDAAIAAARRAFD-TGDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 140 VDLPTAIKNLRYFAGWADKNHGK-TIPMDGDFFTYT----RHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPA 214
Cdd:cd07089  80 MQVDGPIGHLRYFADLADSFPWEfDLPVPALRGGPGrrvvRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 215 EQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNTnLKRVTLELGGKSP 293
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDnAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAAT-LKRVLLELGGKSA 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 294 NIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKIL 373
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 374 GMIKTGKKQGAKLVAGGSRPEGLP-GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVF 452
Cdd:cd07089 319 GYIARGRDEGARLVTGGGRPAGLDkGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20129399 453 TKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
PRK13473 PRK13473
gamma-aminobutyraldehyde dehydrogenase; Provisional
43-514 6.53e-173

gamma-aminobutyraldehyde dehydrogenase; Provisional


Pssm-ID: 237391  Cd Length: 475  Bit Score: 500.59  E-value: 6.53e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   43 FINNEWHKSkSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:PRK13473   6 LINGELVAG-EGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFP---EWSQTTPKERAEALLKLADAIEENADEF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  123 ASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGK-TIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGP 201
Cdd:PRK13473  82 ARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKaAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  202 ALATGNTIVLKPAEQTSLTALYIAQLVKEAgFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIqLASGNTN 280
Cdd:PRK13473 162 ALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGaTVGDALVGHPKVRMVSLTGSIATGKHV-LSAAADS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  281 LKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQ 360
Cdd:PRK13473 240 VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTEL 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  361 GPQVNEEQMEKILGMIKTGKKQG-AKLVAGGSRPEGlPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIER 439
Cdd:PRK13473 320 GPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDG-KGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRW 398
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20129399  440 ANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIVK 514
Cdd:PRK13473 399 ANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVK 473
ALDH_F16 cd07111
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ...
41-505 9.76e-171

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  Cd Length: 480  Bit Score: 495.38  E-value: 9.76e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  41 GVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQV 120
Cdd:cd07111  23 GHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFE---SWSALPGHVRARHLYRIARHIQKHQR 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 121 YLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKnhgktipMDGDFftyTRHEPVGVCGQIIPWNFPILMMAWKLG 200
Cdd:cd07111 100 LFAVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQL-------LDTEL---AGWKPVGVVGQIVPWNFPLLMLAWKIC 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 201 PALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGTAGAALANHCDVDKVAFTGSTDVGKLIQLASGNTN 280
Cdd:cd07111 170 PALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTG 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 281 lKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQ 360
Cdd:cd07111 250 -KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDM 328
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 361 GPQVNEEQMEKILGMIKTGKKQGA-KLVAGGSRPEglPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIER 439
Cdd:cd07111 329 GAIVDPAQLKRIRELVEEGRAEGAdVFQPGADLPS--KGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVAL 406
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20129399 440 ANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNY 505
Cdd:cd07111 407 ANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
ALDH_ABALDH-YdcW cd07092
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ...
60-513 2.88e-170

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  Cd Length: 450  Bit Score: 493.00  E-value: 2.88e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  60 INPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSYN 139
Cdd:cd07092   2 VDPATGEEIATVPDASAADVDAAVAAAHAAFP---SWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 140 VDLPTAIKNLRYFAGWADKNHGktiPMDGDFF----TYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAE 215
Cdd:cd07092  79 DELPGAVDNFRFFAGAARTLEG---PAAGEYLpghtSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSE 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 216 QTSLTALYIAQLVKEaGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNTnLKRVTLELGGKSPN 294
Cdd:cd07092 156 TTPLTTLLLAELAAE-VLPPGVVNVVCGGGaSAGDALVAHPRVRMVSLTGSVRTGKKVARAAADT-LKRVHLELGGKAPV 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 295 IILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILG 374
Cdd:cd07092 234 IVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAG 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 375 MIkTGKKQGAKLVAGGSRPEGlPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTK 454
Cdd:cd07092 314 FV-ERAPAHARVLTGGRRAEG-PGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTR 391
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20129399 455 DLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07092 392 DVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
ALDH-SF cd06534
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
84-513 2.85e-166

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  Cd Length: 367  Bit Score: 479.42  E-value: 2.85e-166
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  84 QAARNAFKLgspWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSYnVDLPTAIKNLRYFAGWADKNHGKT 163
Cdd:cd06534   1 AAARAAFKA---WAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEAL-GEVARAIDTFRYAAGLADKLGGPE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 164 IP-MDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVP 242
Cdd:cd06534  77 LPsPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 243 GFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNtNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCC 321
Cdd:cd06534 157 GGGdEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQIC 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 322 CAGSRTFVEDKIYDEFVERSAerakkrtvgnpfdlnteqgpqvneeqmekilgmiktgkkqgaklvaggsrpeglpgyfv 401
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLV----------------------------------------------------------- 256
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 402 qpTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLA- 480
Cdd:cd06534 257 --TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVg 334
                       410       420       430
                ....*....|....*....|....*....|...
gi 20129399 481 AQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd06534 335 PEAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
PLN02467 PLN02467
betaine aldehyde dehydrogenase
41-511 5.83e-164

betaine aldehyde dehydrogenase


Pssm-ID: 215260  Cd Length: 503  Bit Score: 478.84  E-value: 5.83e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   41 GVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFK--LGSPWRRMDASERGRLLYRLADLMERD 118
Cdd:PLN02467   9 QLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKrnKGKDWARTTGAVRAKYLRAIAAKITER 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  119 QVYLASLETLDNGKPYSMSyNVDLPTAIKNLRYFAGWADKNHGK-----TIPMDgDFFTYTRHEPVGVCGQIIPWNFPIL 193
Cdd:PLN02467  89 KSELAKLETLDCGKPLDEA-AWDMDDVAGCFEYYADLAEALDAKqkapvSLPME-TFKGYVLKEPLGVVGLITPWNYPLL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  194 MMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGT-AGAALANHCDVDKVAFTGSTDVGKLI 272
Cdd:PLN02467 167 MATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTeAGAPLASHPGVDKIAFTGSTATGRKI 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  273 qLASGNTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGN 352
Cdd:PLN02467 247 -MTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISD 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  353 PFDLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEGLP-GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFK 431
Cdd:PLN02467 326 PLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHLKkGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFS 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  432 KLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:PLN02467 406 TEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQV 485
ALDH_AldA-AAD23400 cd07106
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ...
60-511 9.27e-164

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  Cd Length: 446  Bit Score: 476.25  E-value: 9.27e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  60 INPTTAEVIAEIQCADKEDIDIAVQAARNAFKLgspWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSyN 139
Cdd:cd07106   2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPG---WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEA-Q 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 140 VDLPTAIKNLRYFAGWADKNhgKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTSL 219
Cdd:cd07106  78 FEVGGAVAWLRYTASLDLPD--EVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 220 TALYIAQLVKEAgFPEGVVNVVPGFGTAGAALANHCDVDKVAFTGSTDVGKLIqLASGNTNLKRVTLELGGKSPNIILSD 299
Cdd:cd07106 156 CTLKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKV-MASAAKTLKRVTLELGGNDAAIVLPD 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 300 TDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMIKTG 379
Cdd:cd07106 234 VDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDA 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 380 KKQGAKLVAGGSRPEGlPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFTKDLDKA 459
Cdd:cd07106 314 KAKGAKVLAGGEPLDG-PGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERA 392
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|..
gi 20129399 460 NYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:cd07106 393 EAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
HpaE TIGR02299
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ...
41-513 8.14e-160

5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the dehydrogenase responsible for the conversion of 5-carboxymethyl-2-hydroxymuconate semialdehyde to 5-carboxymethyl-2-hydroxymuconate (a tricarboxylic acid). This is the step in the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate following the oxidative opening of the aromatic ring.


Pssm-ID: 131352  Cd Length: 488  Bit Score: 467.75  E-value: 8.14e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399    41 GVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQV 120
Cdd:TIGR02299   2 GHFIDGEFVPSESGETFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFK---RWAELKAAERKRYLHKIADLIEQHAD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   121 YLASLETLDNGKPYSMSYNVdLPTAIKNLRYFAGWA-DKNHGKTIPMDgDFFTYTRHEPVGVCGQIIPWNFPILMMAWKL 199
Cdd:TIGR02299  79 EIAVLECLDCGQPLRQTRQQ-VIRAAENFRFFADKCeEAMDGRTYPVD-THLNYTVRVPVGPVGLITPWNAPFMLSTWKI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   200 GPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQlASGN 278
Cdd:TIGR02299 157 APALAFGNTVVLKPAEWSPLTAARLAEIAKEAGLPDGVFNLVHGFGeEAGKALVAHPDVKAVSFTGETATGSIIM-RNGA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   279 TNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNT 358
Cdd:TIGR02299 236 DTLKRFSMELGGKSPVIVFDDADLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLDPET 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   359 EQGPQVNEEQMEKILGMIKTGKKQGAKLVAGG-SRPEGLP-----GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKK 432
Cdd:TIGR02299 316 EVGPLIHPEHLAKVLGYVEAAEKEGATILVGGeRAPTFRGedlgrGNYVLPTVFTGADNHMRIAQEEIFGPVLTVIPFKD 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   433 LDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVI 512
Cdd:TIGR02299 396 EEEAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDFYTETKNVA 475

                  .
gi 20129399   513 V 513
Cdd:TIGR02299 476 L 476
ALDH_AldH-CAJ73105 cd07131
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ...
43-513 8.14e-160

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  Cd Length: 478  Bit Score: 467.21  E-value: 8.14e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  43 FINNEWHKSKSGKIFETINP-TTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVY 121
Cdd:cd07131   2 YIGGEWVDSASGETFDSRNPaDLEEVVGTFPLSTASDVDAAVEAAREAFP---EWRKVPAPRRAEYLFRAAELLKKRKEE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 122 LASLETLDNGKPYSMSYNvDLPTAIKNLRYFAGWADKNHGKTIPMD-GDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLG 200
Cdd:cd07131  79 LARLVTREMGKPLAEGRG-DVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 201 PALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNT 279
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGeEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 280 NlKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTE 359
Cdd:cd07131 238 N-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 360 QGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEG---LPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEV 436
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGggyEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20129399 437 IERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLA-AQAPFGGYKMSGHG-RENGEYALSNYTEVKSVIV 513
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAeVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYV 475
ALDH_KGSADH-YcbD cd07097
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ...
43-511 9.16e-160

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  Cd Length: 473  Bit Score: 467.11  E-value: 9.16e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  43 FINNEWHKSKSGKifETINPT-TAEVIAEIQCADKEDIDIAVQAARNAFKLgspWRRMDASERGRLLYRLADLMERDQVY 121
Cdd:cd07097   4 YIDGEWVAGGDGE--ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPA---WRRTSPEARADILDKAGDELEARKEE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 122 LASLETLDNGKPysmsynvdLPTAIKN-------LRYFAGWADKNHGKTIP-MDGDFFTYTRHEPVGVCGQIIPWNFPIL 193
Cdd:cd07097  79 LARLLTREEGKT--------LPEARGEvtragqiFRYYAGEALRLSGETLPsTRPGVEVETTREPLGVVGLITPWNFPIA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 194 MMAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGTA-GAALANHCDVDKVAFTGSTDVGKLI 272
Cdd:cd07097 151 IPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEvGQALVEHPDVDAVSFTGSTAVGRRI 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 273 QLASGNtNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGN 352
Cdd:cd07097 231 AAAAAA-RGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGD 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 353 PFDLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSR-PEGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFK 431
Cdd:cd07097 310 ALDEGVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERlKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVR 389
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 432 KLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNV-LAAQAPFGGYKMSGHG-RENGEYALSNYTEVK 509
Cdd:cd07097 390 DYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAgVDYHVPFGGRKGSSYGpREQGEAALEFYTTIK 469

                ..
gi 20129399 510 SV 511
Cdd:cd07097 470 TV 471
PRK09847 PRK09847
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
40-511 2.03e-155

gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional


Pssm-ID: 182108  Cd Length: 494  Bit Score: 456.67  E-value: 2.03e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399   40 TGVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLGSpWRRMDASERGRLLYRLADLMERDQ 119
Cdd:PRK09847  20 NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGD-WSLSSPAKRKAVLNKLADLMEAHA 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  120 VYLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKL 199
Cdd:PRK09847  99 EELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKL 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  200 GPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGN 278
Cdd:PRK09847 179 GPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGhEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGD 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  279 TNLKRVTLELGGKSPNIILSDT-DMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLN 357
Cdd:PRK09847 259 SNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPA 338
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  358 TEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGgsRPEGLPGYfVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVI 437
Cdd:PRK09847 339 TTMGTLIDCAHADSVHSFIREGESKGQLLLDG--RNAGLAAA-IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQAL 415
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20129399  438 ERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSV 511
Cdd:PRK09847 416 QLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
ALDH_MGR_2402 cd07108
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ...
59-513 2.28e-155

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: 455.28  E-value: 2.28e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  59 TINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSY 138
Cdd:cd07108   1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFP---EWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 139 NVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTS 218
Cdd:cd07108  78 RPEAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 219 LTALYIAQLVKEAgFPEGVVNVVPGFGT-AGAALANHCDVDKVAFTGSTDVGKLIQLASGNtNLKRVTLELGGKSPNIIL 297
Cdd:cd07108 158 LAVLLLAEILAQV-LPAGVLNVITGYGEeCGAALVDHPDVDKVTFTGSTEVGKIIYRAAAD-RLIPVSLELGGKSPMIVF 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 298 SDTDMDYAVETAHFGL-FFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMI 376
Cdd:cd07108 236 PDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYI 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 377 KTGKK-QGAKLVAGGSRPEGL---PGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVF 452
Cdd:cd07108 316 DLGLStSGATVLRGGPLPGEGplaDGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVW 395
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20129399 453 TKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENG-EYALSNYTEVKSVIV 513
Cdd:cd07108 396 TRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASlEGMLEHFTQKKTVNI 457
ALDH_ACDHII-AcoD cd07116
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ...
43-513 2.97e-155

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  Cd Length: 479  Bit Score: 455.76  E-value: 2.97e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  43 FINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:cd07116   4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKE---AWGKTSVAERANILNKIADRMEANLEML 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 123 ASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPA 202
Cdd:cd07116  81 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 203 LATGNTIVLKPAEQTSLTALYIAQLVKEAgFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLI-QLASgnTN 280
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGlEAGKPLASSKRIAKVAFTGETTTGRLImQYAS--EN 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 281 LKRVTLELGGKSPNIILSDTDM------DYAVETahFGLF-FNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNP 353
Cdd:cd07116 238 IIPVTLELGGKSPNIFFADVMDaddaffDKALEG--FVMFaLNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNP 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 354 FDLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSR---PEGLPGYFVQPTVFADvQDDMTIAREEIFGPVQQLIRF 430
Cdd:cd07116 316 LDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERnelGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVTTF 394
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 431 KKLDEVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKS 510
Cdd:cd07116 395 KDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKN 474

                ...
gi 20129399 511 VIV 513
Cdd:cd07116 475 LLV 477
ALDH_LactADH-AldA cd07088
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ...
43-513 1.78e-154

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  Cd Length: 468  Bit Score: 453.26  E-value: 1.78e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  43 FINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKLgspWRRMDASERGRLLYRLADLMERDQVYL 122
Cdd:cd07088   1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKA---WERLPAIERAAYLRKLADLIRENADEL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 123 ASLETLDNGKPYSMSYnVDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFT-YTRHEPVGVCGQIIPWNFPILMMAWKLGP 201
Cdd:cd07088  78 AKLIVEEQGKTLSLAR-VEVEFTADYIDYMAEWARRIEGEIIPSDRPNENiFIFKVPIGVVAGILPWNFPFFLIARKLAP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 202 ALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIqLASGNTN 280
Cdd:cd07088 157 ALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGsVVGDALVAHPKVGMISLTGSTEAGQKI-MEAAAEN 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 281 LKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQ 360
Cdd:cd07088 236 ITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDM 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 361 GPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEGLPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERA 440
Cdd:cd07088 316 GPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELA 395
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20129399 441 NNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
ALDH_PADH_NahF cd07113
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ...
41-514 2.68e-153

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: 450.74  E-value: 2.68e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  41 GVFINNEWHKSKSGKIFETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgSPWRRMDASERGRLLYRLADLMERDQV 120
Cdd:cd07113   1 GHFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV--SAWAKTTPAERGRILLRLADLIEQHGE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 121 YLASLETLDNGKPYSMSYNVDLPTAIKNLRYFAGWADKNHGKT----IP-MDGDFFT-YTRHEPVGVCGQIIPWNFPILM 194
Cdd:cd07113  79 ELAQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETlapsIPsMQGERYTaFTRREPVGVVAGIVPWNFSVMI 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 195 MAWKLGPALATGNTIVLKPAEQTSLTALYIAQLVKEAGFPEGVVNVVPGFGTAGAALANHCDVDKVAFTGSTDVGKLIQl 274
Cdd:cd07113 159 AVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIG- 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 275 ASGNTNLKRVTLELGGKSPNIILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPF 354
Cdd:cd07113 238 RQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPM 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 355 DLNTEQGPQVNEEQMEKILGMIKTGKKQGAKLVAGGSRPEGlPGYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLD 434
Cdd:cd07113 318 DESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAG-EGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEE 396
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 435 EVIERANNSEYGLAAAVFTKDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIVK 514
Cdd:cd07113 397 ELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
ALDH_PhdK-like cd07107
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ...
59-513 2.95e-149

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  Cd Length: 456  Bit Score: 439.50  E-value: 2.95e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  59 TINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSMSY 138
Cdd:cd07107   1 VINPATGQVLARVPAASAADVDRAVAAARAAFP---EWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAML 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 139 NvDLPTAIKNLRYFAGWADKNHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAEQTS 218
Cdd:cd07107  78 G-DVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 219 LTALYIAQLVKEAgFPEGVVNVVPGFG-TAGAALANHCDVDKVAFTGSTDVGKLIQLASGNTnLKRVTLELGGKSPNIIL 297
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGaTAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVF 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 298 SDTDMDYAVETAHFGLFFN-MGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILGMI 376
Cdd:cd07107 235 PDADPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYI 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 377 KTGKKQGAKLVAGGSRPEGLP---GYFVQPTVFADVQDDMTIAREEIFGPVQQLIRFKKLDEVIERANNSEYGLAAAVFT 453
Cdd:cd07107 315 DSAKREGARLVTGGGRPEGPAlegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWT 394
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 454 KDLDKANYIVGGLRAGTVWVNTYNVLAAQAPFGGYKMSGHGRENGEYALSNYTEVKSVIV 513
Cdd:cd07107 395 NDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNV 454
ALDH_VaniDH_like cd07150
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ...
57-513 4.93e-147

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  Cd Length: 451  Bit Score: 433.68  E-value: 4.93e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399  57 FETINPTTAEVIAEIQCADKEDIDIAVQAARNAFKlgsPWRRMDASERGRLLYRLADLMERDQVYLASLETLDNGKPYSM 136
Cdd:cd07150   1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFP---AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 137 SYnVDLPTAIKNLRYFAGWADKNHGKTIPMDG-DFFTYTRHEPVGVCGQIIPWNFPILMMAWKLGPALATGNTIVLKPAE 215
Cdd:cd07150  78 AW-FETTFTPELLRAAAGECRRVRGETLPSDSpGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 216 QTSLTALYIAQLVKEAGFPEGVVNVVPGFGTA-GAALANHCDVDKVAFTGSTDVGKLIQLASGNtNLKRVTLELGGKSPN 294
Cdd:cd07150 157 ETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEvGDELVDDPRVRMVTFTGSTAVGREIAEKAGR-HLKKITLELGGKNPL 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129399 295 IILSDTDMDYAVETAHFGLFFNMGQCCCAGSRTFVEDKIYDEFVERSAERAKKRTVGNPFDLNTEQGPQVNEEQMEKILG 374
Cdd:cd07150 236 IVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKR 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....