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Conserved domains on  [gi|7106242|ref|NP_036051|]
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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 ...
15-494 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 [Multi-domain]  Cd Length: 481  Bit Score: 992.24  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   15 NLKIQHTKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSPWRTMDASERGRLLNKLAD 94
Cdd:cd07141   1 NPEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLAD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   95 LMERDRLLLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLI 174
Cdd:cd07141  81 LIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  175 IFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLI 254
Cdd:cd07141 161 MAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  255 KEAAGKSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGN 334
Cdd:cd07141 241 QQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGN 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  335 PLNSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSM 414
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTI 400
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  415 DDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
 
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 ...
15-494 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 [Multi-domain]  Cd Length: 481  Bit Score: 992.24  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   15 NLKIQHTKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSPWRTMDASERGRLLNKLAD 94
Cdd:cd07141   1 NPEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLAD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   95 LMERDRLLLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLI 174
Cdd:cd07141  81 LIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  175 IFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLI 254
Cdd:cd07141 161 MAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  255 KEAAGKSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGN 334
Cdd:cd07141 241 QQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGN 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  335 PLNSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSM 414
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTI 400
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  415 DDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
PLN02466 PLN02466
aldehyde dehydrogenase family 2 member
4-492 0e+00

aldehyde dehydrogenase family 2 member


Pssm-ID: 215259 [Multi-domain]  Cd Length: 538  Bit Score: 690.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242     4 PAQPAVpaplanlKIQHTKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGsPWRTMDAS 83
Cdd:PLN02466  48 PITPPV-------QVSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEG-PWPKMTAY 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    84 ERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVC 163
Cdd:PLN02466 120 ERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVA 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   164 GQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVS 243
Cdd:PLN02466 200 GQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLA 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   244 FTGSTEVGKLIKEAAGKSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRS 323
Cdd:PLN02466 280 FTGSTDTGKIVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKA 359
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   324 VERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFG 403
Cdd:PLN02466 360 KARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFG 439
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   404 PVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGL 483
Cdd:PLN02466 440 PVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSL 519

                 ....*....
gi 7106242   484 YEYTELKTV 492
Cdd:PLN02466 520 NNYLQVKAV 528
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
29-492 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: 333898 [Multi-domain]  Cd Length: 462  Bit Score: 671.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242     29 WHDSvSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATMES 108
Cdd:pfam00171   1 WVDS-ESETIEVINPATGEVIATVPAATAEDVDAAVAAAREAFP---AWRKTPAAERARILRKAADLLEERRDELAELET 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    109 MNAGKVFAHAyLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGN 188
Cdd:pfam00171  77 LETGKPLAEA-RGEVDRAIDTLRYYAGLARRLEGEVLPSDPGRLAYTRREPLGVVGAITPWNFPLLLAAWKIAPALAAGN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    189 TVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTL 268
Cdd:pfam00171 156 TVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGDALVEHPDVRKVSFTGSTAVGRHIAEAAAK-NLKRVTL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    269 ELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDK 348
Cdd:pfam00171 235 ELGGKNPLIVLEDADLDAAVEAIVFGAFGNAGQVCTAASRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDVGPLISE 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    349 EQHNKILGLIESGKKEGAKLECGGGRW---GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTT 425
Cdd:pfam00171 315 AQLERVLKYVEDAKEEGAKLLTGGERDepgLDNGYFVEPTVLADVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTE 394
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7106242    426 YGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAV-PVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:pfam00171 395 YGLAAGVFTSDLERALRVAERLEAGMVYINDYTTGdADGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 462
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Energy production and ...
21-492 0e+00

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


Pssm-ID: 223944 [Multi-domain]  Cd Length: 472  Bit Score: 589.65  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   21 TKIFINNEWHDSVSskKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDR 100
Cdd:COG1012   1 YKLLIDGEWVDGAS--TIEVINPATGEVIATVPAATAEDVDAAVAAARAAF---EAWSRLSAEERAAILRRIADLLEARA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  101 LLLATMESMNAGKVFAHAYLlDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKL 180
Cdd:COG1012  76 EELAALITLETGKPISEARG-EIARAADFIRYYAEEARRLEGETIPTDKGSKALVRREPLGVVGAITPWNFPLALAAWKL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  181 GPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGK 260
Cdd:COG1012 155 APALAAGNTVVLKPSEQTPLSALALAELAAEAGLPAGVLNVVTGGGAEVGDALVAHPDVDAISFTGSTAVGRAIAAAAAA 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  261 sNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGI 340
Cdd:COG1012 235 -NLKPVTLELGGKSPAIVLEDADLDAAVDAAVFGAFFNAGQRCTAASRLIVHESVYDEFVERLVARAASLKVGDPLDPST 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  341 NQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRwgNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKR 420
Cdd:COG1012 314 DLGPLISEEQLDRVEGYIEDAVAEGARLLAGGKR--PGGYFVEPTILEGVTPDMRIAREEIFGPVLPVIRFKDEEEAIEL 391
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7106242  421 ANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYL--AVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:COG1012 392 ANDTEYGLAAAIFTRDLARAFRVARRLEAGMVGINDYTggADIAYLPFGGVKQSGLGREGGKYGLEEFTEVKTV 465
BADH TIGR01804
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...
24-490 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 [Multi-domain]  Cd Length: 467  Bit Score: 529.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242     24 FINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:TIGR01804   1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGE---WAAMSPMERGRILRRAADLIRERNEEL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    104 ATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPA 183
Cdd:TIGR01804  78 AKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    184 LSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGkSNL 263
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAA-GHL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    264 KRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQG 343
Cdd:TIGR01804 237 KHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    344 PQIDKEQHNKILGLIESGKKEGAKLECGGGRWGN----KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIK 419
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGRPENvglqNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7106242    420 RANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELK 490
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 ...
15-494 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 [Multi-domain]  Cd Length: 481  Bit Score: 992.24  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   15 NLKIQHTKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSPWRTMDASERGRLLNKLAD 94
Cdd:cd07141   1 NPEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSPWRTMDASERGRLLNKLAD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   95 LMERDRLLLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLI 174
Cdd:cd07141  81 LIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  175 IFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLI 254
Cdd:cd07141 161 MAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  255 KEAAGKSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGN 334
Cdd:cd07141 241 QQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGN 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  335 PLNSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSM 414
Cdd:cd07141 321 PFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTI 400
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  415 DDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07141 401 DEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
ALDH_F1-2_Ald2-like cd07091
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...
19-492 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 [Multi-domain]  Cd Length: 476  Bit Score: 883.86  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   19 QHTKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSpWRTMDASERGRLLNKLADLMER 98
Cdd:cd07091   2 QPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGW-WRKMDPRERGRLLNKLADLIER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   99 DRLLLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTW 178
Cdd:cd07091  81 DRDELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAW 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  179 KLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAA 258
Cdd:cd07091 161 KLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAA 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  259 GKSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNS 338
Cdd:cd07091 241 AKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDP 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  339 GINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVI 418
Cdd:cd07091 321 DTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVI 400
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7106242  419 KRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07091 401 ERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
ALDH_F2BC cd07142
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ...
18-494 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 [Multi-domain]  Cd Length: 476  Bit Score: 730.83  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   18 IQHTKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGsPWRTMDASERGRLLNKLADLME 97
Cdd:cd07142   1 VKHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEG-PWPRMTGYERSRILLRFADLLE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   98 RDRLLLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFT 177
Cdd:cd07142  80 KHADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  178 WKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEA 257
Cdd:cd07142 160 WKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  258 AGKSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLN 337
Cdd:cd07142 240 AAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFR 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  338 SGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDV 417
Cdd:cd07142 320 KGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEV 399
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7106242  418 IKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07142 400 IKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVVM 476
PLN02466 PLN02466
aldehyde dehydrogenase family 2 member
4-492 0e+00

aldehyde dehydrogenase family 2 member


Pssm-ID: 215259 [Multi-domain]  Cd Length: 538  Bit Score: 690.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242     4 PAQPAVpaplanlKIQHTKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGsPWRTMDAS 83
Cdd:PLN02466  48 PITPPV-------QVSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEG-PWPKMTAY 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    84 ERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVC 163
Cdd:PLN02466 120 ERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVA 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   164 GQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVS 243
Cdd:PLN02466 200 GQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLA 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   244 FTGSTEVGKLIKEAAGKSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRS 323
Cdd:PLN02466 280 FTGSTDTGKIVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKA 359
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   324 VERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFG 403
Cdd:PLN02466 360 KARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFG 439
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   404 PVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGL 483
Cdd:PLN02466 440 PVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSL 519

                 ....*....
gi 7106242   484 YEYTELKTV 492
Cdd:PLN02466 520 NNYLQVKAV 528
ALDH_AldA_AN0554 cd07143
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ...
18-492 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 [Multi-domain]  Cd Length: 481  Bit Score: 684.26  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   18 IQHTKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPW-RTMDASERGRLLNKLADLM 96
Cdd:cd07143   4 EQPTGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE--TDWgLKVSGSKRGRCLSKLADLM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   97 ERDRLLLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIF 176
Cdd:cd07143  82 ERNLDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMC 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  177 TWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKE 256
Cdd:cd07143 162 AWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVME 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  257 AAGKSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPL 336
Cdd:cd07143 242 AAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPF 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  337 NSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDD 416
Cdd:cd07143 322 AEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEE 401
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7106242  417 VIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07143 402 AIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAV 477
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
29-492 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: 333898 [Multi-domain]  Cd Length: 462  Bit Score: 671.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242     29 WHDSvSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATMES 108
Cdd:pfam00171   1 WVDS-ESETIEVINPATGEVIATVPAATAEDVDAAVAAAREAFP---AWRKTPAAERARILRKAADLLEERRDELAELET 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    109 MNAGKVFAHAyLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGN 188
Cdd:pfam00171  77 LETGKPLAEA-RGEVDRAIDTLRYYAGLARRLEGEVLPSDPGRLAYTRREPLGVVGAITPWNFPLLLAAWKIAPALAAGN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    189 TVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTL 268
Cdd:pfam00171 156 TVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGDALVEHPDVRKVSFTGSTAVGRHIAEAAAK-NLKRVTL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    269 ELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDK 348
Cdd:pfam00171 235 ELGGKNPLIVLEDADLDAAVEAIVFGAFGNAGQVCTAASRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDVGPLISE 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    349 EQHNKILGLIESGKKEGAKLECGGGRW---GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTT 425
Cdd:pfam00171 315 AQLERVLKYVEDAKEEGAKLLTGGERDepgLDNGYFVEPTVLADVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTE 394
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7106242    426 YGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAV-PVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:pfam00171 395 YGLAAGVFTSDLERALRVAERLEAGMVYINDYTTGdADGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 462
ALDH_ALD2-YMR170C cd07144
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ...
19-492 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 [Multi-domain]  Cd Length: 484  Bit Score: 666.80  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   19 QHTKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPWRTMDASERGRLLNKLADLMER 98
Cdd:cd07144   6 QPTGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFE--SWWSKVTGEERGELLDKLADLVEK 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   99 DRLLLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTW 178
Cdd:cd07144  84 NRDLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAW 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  179 KLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAA 258
Cdd:cd07144 164 KLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAA 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  259 GkSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKK-YILGNPLN 337
Cdd:cd07144 244 A-QNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFD 322
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  338 SGINQGPQIDKEQHNKILGLIESGKKEGAKLECGG---GRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSM 414
Cdd:cd07144 323 DDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGekaPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTY 402
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7106242  415 DDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07144 403 EEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
PLN02766 PLN02766
coniferyl-aldehyde dehydrogenase
17-496 0e+00

coniferyl-aldehyde dehydrogenase


Pssm-ID: 215410  Cd Length: 501  Bit Score: 658.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    17 KIQHTKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGsPWRTMDASERGRLLNKLADLM 96
Cdd:PLN02766  17 EIKFTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHG-PWPRMSGFERGRIMMKFADLI 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    97 ERDRLLLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIF 176
Cdd:PLN02766  96 EEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMF 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   177 TWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKE 256
Cdd:PLN02766 176 FMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQ 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   257 AAGKSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPL 336
Cdd:PLN02766 256 AAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPF 335
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   337 NSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDD 416
Cdd:PLN02766 336 DPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEE 415
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   417 VIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMQI 496
Cdd:PLN02766 416 AIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTPL 495
ALDH_BADH-GbsA cd07119
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ...
24-492 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 [Multi-domain]  Cd Length: 482  Bit Score: 620.10  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   24 FINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQiGSPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:cd07119   1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFD-SGEWPHLPAQERAALLFRIADKIREDAEEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  104 ATMESMNAGKVFAHAYLlDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPA 183
Cdd:cd07119  80 ARLETLNTGKTLRESEI-DIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  184 LSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNL 263
Cdd:cd07119 159 LAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAG-NV 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  264 KRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQG 343
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  344 PQIDKEQHNKILGLIESGKKEGAKLECGGGRWGN----KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIK 419
Cdd:cd07119 318 PLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIR 397
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7106242  420 RANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07119 398 LANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
ALDH_GABALDH-PuuC cd07112
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ...
36-492 0e+00

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


Pssm-ID: 143430 [Multi-domain]  Cd Length: 462  Bit Score: 616.15  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   36 KKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSpWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVF 115
Cdd:cd07112   2 ETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGV-WSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  116 AHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPA 195
Cdd:cd07112  81 SDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  196 EQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKSNLKRVTLELGGKSP 275
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKSP 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  276 CIVFADA-DLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKI 354
Cdd:cd07112 241 NIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKV 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  355 LGLIESGKKEGAKLECGGGR--WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGV 432
Cdd:cd07112 321 LGYIESGKAEGARLVAGGKRvlTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASV 400
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  433 FTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07112 401 WTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
ALDH cd07078
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ...
61-494 0e+00

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


Pssm-ID: 143397 [Multi-domain]  Cd Length: 432  Bit Score: 612.68  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   61 DKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAhAYLLDVEISIKALQYFAGWADKI 140
Cdd:cd07078   1 DAAVAAARAAFKA---WAALPPAERAAILRKLADLLEERREELAALETLETGKPIE-EALGEVARAADTFRYYAGLARRL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  141 HGQTIPS-DGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVV 219
Cdd:cd07078  77 HGEVIPSpDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  220 NIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQ 299
Cdd:cd07078 157 NVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  300 GQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGN-K 378
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGgK 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  379 GFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYL 458
Cdd:cd07078 316 GYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 7106242  459 AVPV-QCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07078 396 VGAEpSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
ALDH_HMSADH_HapE cd07115
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ...
40-496 0e+00

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


Pssm-ID: 143433 [Multi-domain]  Cd Length: 453  Bit Score: 598.65  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAY 119
Cdd:cd07115   1 TLNPATGELIARVAQASAEDVDAAVAAARAAFE---AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAAR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  120 LLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTP 199
Cdd:cd07115  78 RLDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  200 LTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGkSNLKRVTLELGGKSPCIVF 279
Cdd:cd07115 158 LSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA-GNLKRVSLELGGKSANIVF 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  280 ADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIE 359
Cdd:cd07115 237 ADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVD 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  360 SGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDK 439
Cdd:cd07115 317 VGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 7106242  440 AITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAMQI 496
Cdd:cd07115 397 AHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
ALDH_DhaS cd07114
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ...
40-492 0e+00

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


Pssm-ID: 143432 [Multi-domain]  Cd Length: 457  Bit Score: 598.00  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQiGSPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAH-- 117
Cdd:cd07114   1 SINPATGEPWARVPEASAADVDRAVAAARAAFE-GGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIREtr 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  118 ---AYLldveisIKALQYFAGWADKIHGQTIPSD-GNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVK 193
Cdd:cd07114  80 aqvRYL------AEWYRYYAGLADKIEGAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  194 PAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGK 273
Cdd:cd07114 154 PSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGK 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  274 SPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNK 353
Cdd:cd07114 233 SPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEK 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  354 ILGLIESGKKEGAKLECGGGR----WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLA 429
Cdd:cd07114 313 VERYVARAREEGARVLTGGERpsgaDLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLA 392
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7106242  430 AGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07114 393 AGIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Energy production and ...
21-492 0e+00

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


Pssm-ID: 223944 [Multi-domain]  Cd Length: 472  Bit Score: 589.65  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   21 TKIFINNEWHDSVSskKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDR 100
Cdd:COG1012   1 YKLLIDGEWVDGAS--TIEVINPATGEVIATVPAATAEDVDAAVAAARAAF---EAWSRLSAEERAAILRRIADLLEARA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  101 LLLATMESMNAGKVFAHAYLlDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKL 180
Cdd:COG1012  76 EELAALITLETGKPISEARG-EIARAADFIRYYAEEARRLEGETIPTDKGSKALVRREPLGVVGAITPWNFPLALAAWKL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  181 GPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGK 260
Cdd:COG1012 155 APALAAGNTVVLKPSEQTPLSALALAELAAEAGLPAGVLNVVTGGGAEVGDALVAHPDVDAISFTGSTAVGRAIAAAAAA 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  261 sNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGI 340
Cdd:COG1012 235 -NLKPVTLELGGKSPAIVLEDADLDAAVDAAVFGAFFNAGQRCTAASRLIVHESVYDEFVERLVARAASLKVGDPLDPST 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  341 NQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRwgNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKR 420
Cdd:COG1012 314 DLGPLISEEQLDRVEGYIEDAVAEGARLLAGGKR--PGGYFVEPTILEGVTPDMRIAREEIFGPVLPVIRFKDEEEAIEL 391
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7106242  421 ANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYL--AVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:COG1012 392 ANDTEYGLAAAIFTRDLARAFRVARRLEAGMVGINDYTggADIAYLPFGGVKQSGLGREGGKYGLEEFTEVKTV 465
ALDH_F8_HMSADH cd07093
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ...
40-494 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 [Multi-domain]  Cd Length: 455  Bit Score: 586.07  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAY 119
Cdd:cd07093   1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG---WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLAR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  120 LLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTP 199
Cdd:cd07093  78 TRDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  200 LTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07093 158 LTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAP-NLKPVSLELGGKNPNIVF 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  280 ADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIE 359
Cdd:cd07093 237 ADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVE 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  360 SGKKEGAKLECGGGRWG----NKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTK 435
Cdd:cd07093 317 LARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 7106242  436 DLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
ALDH_F1L_FTFDH cd07140
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ...
16-495 0e+00

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


Pssm-ID: 143458 [Multi-domain]  Cd Length: 486  Bit Score: 583.69  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   16 LKIQHtKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQiGSPWRTMDASERGRLLNKLADL 95
Cdd:cd07140   2 LKMPH-QLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFE-NGEWGKMNARDRGRLMYRLADL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   96 MERDRLLLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSD----GNIFTYTRREPIGVCGQIIPWNG 171
Cdd:cd07140  80 MEEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINqarpNRNLTLTKREPIGVCGIVIPWNY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  172 PLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVG 251
Cdd:cd07140 160 PLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIG 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  252 KLIKEAAGKSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYI 331
Cdd:cd07140 240 KHIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMK 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  332 LGNPLNSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKF 411
Cdd:cd07140 320 IGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKF 399
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  412 KS--MDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTEL 489
Cdd:cd07140 400 DDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKT 479

                ....*.
gi 7106242  490 KTVAMQ 495
Cdd:cd07140 480 KTVTIE 485
PRK13252 PRK13252
betaine aldehyde dehydrogenase; Provisional
24-492 0e+00

betaine aldehyde dehydrogenase; Provisional


Pssm-ID: 183918  Cd Length: 488  Bit Score: 553.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    24 FINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLM-ERDRLL 102
Cdd:PRK13252  10 YIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKI---WAAMTAMERSRILRRAVDILrERNDEL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   103 lATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGP 182
Cdd:PRK13252  87 -AALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   183 ALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTaGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKSn 262
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS- 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   263 LKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQ 342
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNF 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   343 GPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGN----KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVI 418
Cdd:PRK13252 324 GPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVI 403
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7106242   419 KRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:PRK13252 404 ARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSV 477
ALDH_F5_SSADH_GabD cd07103
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ...
40-494 0e+00

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


Pssm-ID: 143421 [Multi-domain]  Cd Length: 451  Bit Score: 549.73  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAy 119
Cdd:cd07103   1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKT---WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  120 LLDVEISIKALQYFAGWADKIHGQTIPS-DGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQT 198
Cdd:cd07103  77 RGEVDYAASFLEWFAEEARRIYGRTIPSpAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEET 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  199 PLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGK-LIKEAAgkSNLKRVTLELGGKSPCI 277
Cdd:cd07103 157 PLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKlLMAQAA--DTVKRVSLELGGNAPFI 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  278 VFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGL 357
Cdd:cd07103 235 VFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEAL 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  358 IESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDL 437
Cdd:cd07103 315 VEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDL 394
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 7106242  438 DKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07103 395 ARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
ALDH_F9_TMBADH cd07090
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ...
40-492 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 [Multi-domain]  Cd Length: 457  Bit Score: 539.20  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAy 119
Cdd:cd07090   1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKE---WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEA- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  120 LLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTP 199
Cdd:cd07090  77 RVDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  200 LTALHMASLIKEAGFPPGVVNIVPGYGPTaGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAK-GIKHVTLELGGKSPLIIF 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  280 ADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIE 359
Cdd:cd07090 235 DDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIE 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  360 SGKKEGAKLECGGGRWGNK-----GFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFT 434
Cdd:cd07090 315 SAKQEGAKVLCGGERVVPEdglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFT 394
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 7106242  435 KDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07090 395 RDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
ALDH_CddD_SSP0762 cd07138
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ...
23-493 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 [Multi-domain]  Cd Length: 466  Bit Score: 533.62  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   23 IFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMER--DR 100
Cdd:cd07138   1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAF---PAWSATSVEERAALLERIAEAYEAraDE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  101 LLLATMESMNAGKVFAHAY-----LLDVEISIKALQYFAgWADKIHGQTIpsdgniftytRREPIGVCGQIIPWNGPLII 175
Cdd:cd07138  78 LAQAITLEMGAPITLARAAqvglgIGHLRAAADALKDFE-FEERRGNSLV----------VREPIGVCGLITPWNWPLNQ 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  176 FTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIK 255
Cdd:cd07138 147 IVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVA 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  256 EAAGKSnLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNP 335
Cdd:cd07138 227 EAAADT-VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDP 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  336 LNSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGG-GR--WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFK 412
Cdd:cd07138 306 RDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGpGRpeGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYD 385
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  413 SMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNcYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07138 386 DEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSI 464

                .
gi 7106242  493 A 493
Cdd:cd07138 465 Q 465
ALDH_AAS00426 cd07109
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ...
40-493 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 [Multi-domain]  Cd Length: 454  Bit Score: 531.42  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAY 119
Cdd:cd07109   1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFE--SGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  120 LlDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTP 199
Cdd:cd07109  79 A-DVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  200 LTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07109 158 LTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIVF 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  280 ADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLnSGINQGPQIDKEQHNKILGLIE 359
Cdd:cd07109 237 ADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGL-EDPDLGPLISAKQLDRVEGFVA 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  360 SGKKEGAKLECGGGRWGN---KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKD 436
Cdd:cd07109 316 RARARGARIVAGGRIAEGapaGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRD 395
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 7106242  437 LDKAITVSSALQAGMVWVNCYLAVP-VQCPFGGFKMSGNGRELGEHGLYEYTELKTVA 493
Cdd:cd07109 396 GDRALRVARRLRAGQVFVNNYGAGGgIELPFGGVKKSGHGREKGLEALYNYTQTKTVA 453
BADH TIGR01804
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ...
24-490 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 [Multi-domain]  Cd Length: 467  Bit Score: 529.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242     24 FINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:TIGR01804   1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGE---WAAMSPMERGRILRRAADLIRERNEEL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    104 ATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPA 183
Cdd:TIGR01804  78 AKLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    184 LSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGkSNL 263
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAA-GHL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    264 KRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQG 343
Cdd:TIGR01804 237 KHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    344 PQIDKEQHNKILGLIESGKKEGAKLECGGGRWGN----KGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIK 419
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGRPENvglqNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7106242    420 RANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELK 490
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
ALDH_ACDHII_AcoD-like cd07559
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ...
22-490 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 [Multi-domain]  Cd Length: 480  Bit Score: 527.68  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   22 KIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRL 101
Cdd:cd07559   2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFK---TWGKTSVAERANILNKIADRIEENLE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  102 LLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLG 181
Cdd:cd07559  79 LLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  182 PALSCGNTVVVKPAEQTPLTALHMASLIKEAgFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKs 261
Cdd:cd07559 159 PALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE- 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  262 NLKRVTLELGGKSPCIVFADA-----DLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPL 336
Cdd:cd07559 237 NLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPL 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  337 NSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRW----GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFK 412
Cdd:cd07559 317 DPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLtlggLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7106242  413 SMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELK 490
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTK 474
ALDH_SNDH cd07118
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ...
41-494 0e+00

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


Pssm-ID: 143436 [Multi-domain]  Cd Length: 454  Bit Score: 514.19  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   41 LNPATEEVICHVEEGDKADVDKAVKAARQAFQIGsPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAyL 120
Cdd:cd07118   2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKG-PWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQA-R 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  121 LDVEISIKALQYFAGWADKIHGQTIPSDG-NIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTP 199
Cdd:cd07118  80 GEIEGAADLWRYAASLARTLHGDSYNNLGdDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  200 LTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07118 160 GTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVF 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  280 ADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIE 359
Cdd:cd07118 239 ADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVD 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  360 SGKKEGAKLECGGGRW-GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLD 438
Cdd:cd07118 319 AGRAEGATLLLGGERLaSAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDID 398
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7106242  439 KAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07118 399 TALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
ALDH_CddD-AldA-like cd07089
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ...
40-494 3.36e-174

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


Pssm-ID: 143408 [Multi-domain]  Cd Length: 459  Bit Score: 497.92  E-value: 3.36e-174
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQiGSPWRtMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAY 119
Cdd:cd07089   1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFD-TGDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTAR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  120 LLDVEISIKALQYFAGWADKIHG-QTIPSDGNIFTYT----RREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKP 194
Cdd:cd07089  79 AMQVDGPIGHLRYFADLADSFPWeFDLPVPALRGGPGrrvvRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  195 AEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGkSNLKRVTLELGGKS 274
Cdd:cd07089 159 APDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAA-ATLKRVLLELGGKS 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  275 PCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKI 354
Cdd:cd07089 238 ANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRV 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  355 LGLIESGKKEGAKLECGGGR--WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGV 432
Cdd:cd07089 318 EGYIARGRDEGARLVTGGGRpaGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGV 397
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7106242  433 FTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07089 398 WSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
ALDH_F10_BADH cd07110
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ...
40-492 2.60e-173

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


Pssm-ID: 143428 [Multi-domain]  Cd Length: 456  Bit Score: 495.33  E-value: 2.60e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAy 119
Cdd:cd07110   1 VINPATEATIGEIPAATAEDVDAAVRAARRAF---PRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  120 LLDVEISIKALQYFAGWADKIH---GQTIPSDGNIFT-YTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPA 195
Cdd:cd07110  77 AWDVDDVAGCFEYYADLAEQLDakaERAVPLPSEDFKaRVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  196 EQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSP 275
Cdd:cd07110 157 ELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQ-DIKPVSLELGGKSP 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  276 CIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKIL 355
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  356 GLIESGKKEGAKLECGGGR--WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVF 433
Cdd:cd07110 316 SFIARGKEEGARLLCGGRRpaHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 7106242  434 TKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
ALDH_AldA-AAD23400 cd07106
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ...
40-492 8.54e-172

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


Pssm-ID: 143424 [Multi-domain]  Cd Length: 446  Bit Score: 491.27  E-value: 8.54e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAY 119
Cdd:cd07106   1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFP---GWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  120 LlDVEISIKALQYFAGWADKIHgqTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTP 199
Cdd:cd07106  78 F-EVGGAVAWLRYTASLDLPDE--VIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTP 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  200 LTALHMASLIKEAgFPPGVVNIVPGyGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07106 155 LCTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAK-TLKRVTLELGGNDAAIVL 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  280 ADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIE 359
Cdd:cd07106 232 PDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVE 311
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  360 SGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDK 439
Cdd:cd07106 312 DAKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLER 391
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|...
gi 7106242  440 AITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07106 392 AEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
ALDH_StaphAldA1 cd07117
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ...
22-492 2.38e-171

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 [Multi-domain]  Cd Length: 475  Bit Score: 491.20  E-value: 2.38e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   22 KIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRL 101
Cdd:cd07117   2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFK---TWRKTTVAERANILNKIADIIDENKE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  102 LLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLG 181
Cdd:cd07117  79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  182 PALSCGNTVVVKPAEQTPLTALHMASLIKEAgFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKs 261
Cdd:cd07117 159 PALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK- 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  262 NLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGIN 341
Cdd:cd07117 237 KLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  342 QGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWG----NKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDV 417
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTenglDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7106242  418 IKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNI 471
ALDH_KGSADH-YcbD cd07097
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ...
24-492 2.12e-170

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


Pssm-ID: 143415 [Multi-domain]  Cd Length: 473  Bit Score: 488.68  E-value: 2.12e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   24 FINNEWHDSVSSKkfPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLL 102
Cdd:cd07097   4 YIDGEWVAGGDGE--ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAF---PAWRRTSPEARADILDKAGDELEARKEE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  103 LATMESMNAGKVFAHAyLLDVEISIKALQYFAGWADKIHGQTIPS-DGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLG 181
Cdd:cd07097  79 LARLLTREEGKTLPEA-RGEVTRAGQIFRYYAGEALRLSGETLPStRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  182 PALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGkS 261
Cdd:cd07097 158 PALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA-A 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  262 NLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGIN 341
Cdd:cd07097 237 RGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVD 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  342 QGPQIDKEQHNKILGLIESGKKEGAKLECGGGRW--GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIK 419
Cdd:cd07097 317 IGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLkrPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALA 396
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7106242  420 RANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLA-VPVQCPFGGFKMSGNG-RELGEHGLYEYTELKTV 492
Cdd:cd07097 397 IANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAgVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
ALDH-SF cd06534
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
65-494 2.22e-170

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


Pssm-ID: 143395 [Multi-domain]  Cd Length: 367  Bit Score: 484.43  E-value: 2.22e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   65 KAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAhAYLLDVEISIKALQYFAGWADKIHGQT 144
Cdd:cd06534   1 AAARAAFKA---WAALPPAERAAILRKIADLLEERREELAALETLETGKPIE-EALGEVARAIDTFRYAAGLADKLGGPE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  145 IPS-DGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVP 223
Cdd:cd06534  77 LPSpDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  224 GYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQIC 303
Cdd:cd06534 157 GGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQIC 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  304 VAASRLFVEESIYDEFVRRSVerakkyilgnplnsginqgpqidkeqhnkilgliesgkkegaklecgggrwgnkgffvq 383
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLV----------------------------------------------------------- 256
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  384 pTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLA-VPV 462
Cdd:cd06534 257 -TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGP 335
                       410       420       430
                ....*....|....*....|....*....|..
gi 7106242  463 QCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd06534 336 EAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
ALDH_AldH-CAJ73105 cd07131
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ...
24-492 4.56e-169

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


Pssm-ID: 143449 [Multi-domain]  Cd Length: 478  Bit Score: 485.70  E-value: 4.56e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   24 FINNEWHDSVSSKKFPVLNPA-TEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERDRLL 102
Cdd:cd07131   2 YIGGEWVDSASGETFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAF---PEWRKVPAPRRAEYLFRAAELLKKRKEE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  103 LATMESMNAGKVFAHAyLLDVEISIKALQYFAGWADKIHGQTIPSD-GNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLG 181
Cdd:cd07131  79 LARLVTREMGKPLAEG-RGDVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  182 PALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKS 261
Cdd:cd07131 158 PALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARP 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  262 NlKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGIN 341
Cdd:cd07131 238 N-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETD 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  342 QGPQIDKEQHNKILGLIESGKKEGAKLECGGGR----WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDV 417
Cdd:cd07131 317 MGPLINEAQLEKVLNYNEIGKEEGATLLLGGERltggGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEA 396
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7106242  418 IKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNC-YLAVPVQCPFGGFKMSGNG-RELGEHGLYEYTELKTV 492
Cdd:cd07131 397 IEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNApTIGAEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
ALDH_LactADH-AldA cd07088
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ...
24-494 5.18e-169

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


Pssm-ID: 143407 [Multi-domain]  Cd Length: 468  Bit Score: 484.85  E-value: 5.18e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   24 FINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:cd07088   1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQK---AWERLPAIERAAYLRKLADLIRENADEL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  104 ATMESMNAGKVFAHAYLlDVEISIKALQYFAGWADKIHGQTIPSDG---NIFTYtrREPIGVCGQIIPWNGPLIIFTWKL 180
Cdd:cd07088  78 AKLIVEEQGKTLSLARV-EVEFTADYIDYMAEWARRIEGEIIPSDRpneNIFIF--KVPIGVVAGILPWNFPFFLIARKL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  181 GPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGK 260
Cdd:cd07088 155 APALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  261 sNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGI 340
Cdd:cd07088 235 -NITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAAT 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  341 NQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRW-GNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIK 419
Cdd:cd07088 314 DMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPeGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIE 393
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7106242  420 RANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07088 394 LANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
ALDH_MGR_2402 cd07108
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ...
40-492 2.21e-168

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 [Multi-domain]  Cd Length: 457  Bit Score: 483.02  E-value: 2.21e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAY 119
Cdd:cd07108   1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFP---EWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  120 LLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTP 199
Cdd:cd07108  78 RPEAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  200 LTALHMASLIKEAgFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVF 279
Cdd:cd07108 158 LAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAAD-RLIPVSLELGGKSPMIVF 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  280 ADADLDSAVEFAHQGVFFH-QGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLI 358
Cdd:cd07108 236 PDADLDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYI 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  359 ESGKKE-GAK-LECG---GGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVF 433
Cdd:cd07108 316 DLGLSTsGATvLRGGplpGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVW 395
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  434 TKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYE-YTELKTV 492
Cdd:cd07108 396 TRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGMLEhFTQKKTV 455
ALDH_AldA-Rv0768 cd07139
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ...
23-494 6.70e-167

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


Pssm-ID: 143457 [Multi-domain]  Cd Length: 471  Bit Score: 479.76  E-value: 6.70e-167
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   23 IFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGsPWRTMDASERGRLLNKLADLMERDRLL 102
Cdd:cd07139   1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNG-PWPRLSPAERAAVLRRLADALEARADE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  103 LATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADK---IHGQTIPSDGNifTYTRREPIGVCGQIIPWNGPLIIFTWK 179
Cdd:cd07139  80 LARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDfpfEERRPGSGGGH--VLVRREPVGVVAAIVPWNAPLFLAALK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  180 LGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGyGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAG 259
Cdd:cd07139 158 IAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCG 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  260 kSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSG 339
Cdd:cd07139 237 -ERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPA 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  340 INQGPQIDKEQHNKILGLIESGKKEGAKLECGGGR--WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDV 417
Cdd:cd07139 316 TQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRpaGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDA 395
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7106242  418 IKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNcYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07139 396 VRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
PLN02467 PLN02467
betaine aldehyde dehydrogenase
8-499 2.07e-164

betaine aldehyde dehydrogenase


Pssm-ID: 215260 [Multi-domain]  Cd Length: 503  Bit Score: 474.61  E-value: 2.07e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242     8 AVPAPLANLkiqhtkiFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAF--QIGSPWRTMDASER 85
Cdd:PLN02467   2 AIPVPRRQL-------FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrNKGKDWARTTGAVR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    86 GRLLNKLADLMERDRLLLATMESMNAGKVFAHAyLLDVEISIKALQYFAGWADKIHGQ-----TIPSDgNIFTYTRREPI 160
Cdd:PLN02467  75 AKYLRAIAAKITERKSELAKLETLDCGKPLDEA-AWDMDDVAGCFEYYADLAEALDAKqkapvSLPME-TFKGYVLKEPL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   161 GVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDID 240
Cdd:PLN02467 153 GVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVD 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   241 KVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFV 320
Cdd:PLN02467 233 KIAFTGSTATGRKIMTAAAQ-MVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFL 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   321 RRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWG--NKGFFVQPTVFSNVTDEMRIAK 398
Cdd:PLN02467 312 EKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEhlKKGFFIEPTIITDVTTSMQIWR 391
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   399 EEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGREL 478
Cdd:PLN02467 392 EEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGREL 471
                        490       500
                 ....*....|....*....|.
gi 7106242   479 GEHGLYEYTELKTVAMQISQK 499
Cdd:PLN02467 472 GEWGLENYLSVKQVTKYISDE 492
ALDH_F16 cd07111
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ...
24-486 7.13e-164

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


Pssm-ID: 143429 [Multi-domain]  Cd Length: 480  Bit Score: 472.27  E-value: 7.13e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   24 FINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:cd07111  25 FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFE---SWSALPGHVRARHLYRIARHIQKHQRLF 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  104 ATMESMNAGKVFAHAYLLDVEISIKALQYFAGWAdkihgQTIPSDGNiftytRREPIGVCGQIIPWNGPLIIFTWKLGPA 183
Cdd:cd07111 102 AVLESLDNGKPIRESRDCDIPLVARHFYHHAGWA-----QLLDTELA-----GWKPVGVVGQIVPWNFPLLMLAWKICPA 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  184 LSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTaGGAISSHMDIDKVSFTGSTEVGKLIKEA-AGKSn 262
Cdd:cd07111 172 LAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRAtAGTG- 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  263 lKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQ 342
Cdd:cd07111 250 -KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDM 328
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  343 GPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRAN 422
Cdd:cd07111 329 GAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALAN 408
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7106242  423 NTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEY 486
Cdd:cd07111 409 NTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
ALDH_ABALDH-YdcW cd07092
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ...
40-492 8.87e-163

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


Pssm-ID: 143411 [Multi-domain]  Cd Length: 450  Bit Score: 468.34  E-value: 8.87e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAY 119
Cdd:cd07092   1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPS---WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  120 LLDVEISIKALQYFAGWADKIHGqtiPSDG----NIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPA 195
Cdd:cd07092  78 DDELPGAVDNFRFFAGAARTLEG---PAAGeylpGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  196 EQTPLTALHMASLIKEaGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSP 275
Cdd:cd07092 155 ETTPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAAD-TLKRVHLELGGKAP 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  276 CIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKIL 355
Cdd:cd07092 233 VIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVA 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  356 GLIEsGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTK 435
Cdd:cd07092 313 GFVE-RAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTR 391
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 7106242  436 DLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:cd07092 392 DVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
HpaE TIGR02299
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ...
24-496 9.55e-163

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 [Multi-domain]  Cd Length: 488  Bit Score: 469.67  E-value: 9.55e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242     24 FINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:TIGR02299   4 FIDGEFVPSESGETFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFK---RWAELKAAERKRYLHKIADLIEQHADEI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    104 ATMESMNAGKVFAHAYlldvEISIKALQYFAGWADK----IHGQTIPSDGNIfTYTRREPIGVCGQIIPWNGPLIIFTWK 179
Cdd:TIGR02299  81 AVLECLDCGQPLRQTR----QQVIRAAENFRFFADKceeaMDGRTYPVDTHL-NYTVRVPVGPVGLITPWNAPFMLSTWK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    180 LGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKeAAG 259
Cdd:TIGR02299 156 IAPALAFGNTVVLKPAEWSPLTAARLAEIAKEAGLPDGVFNLVHGFGEEAGKALVAHPDVKAVSFTGETATGSIIM-RNG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    260 KSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSG 339
Cdd:TIGR02299 235 ADTLKRFSMELGGKSPVIVFDDADLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLDPE 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    340 INQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWG-------NKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFK 412
Cdd:TIGR02299 315 TEVGPLIHPEHLAKVLGYVEAAEKEGATILVGGERAPtfrgedlGRGNYVLPTVFTGADNHMRIAQEEIFGPVLTVIPFK 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    413 SMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:TIGR02299 395 DEEEAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDFYTETKNV 474

                  ....
gi 7106242    493 AMQI 496
Cdd:TIGR02299 475 ALAL 478
ALDH_VaniDH_like cd07150
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ...
38-494 2.85e-160

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


Pssm-ID: 143468 [Multi-domain]  Cd Length: 451  Bit Score: 462.18  E-value: 2.85e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   38 FPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAH 117
Cdd:cd07150   1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFP---AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  118 AYLlDVEISIKALQYFAGWADKIHGQTIPSDGN-IFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAE 196
Cdd:cd07150  78 AWF-ETTFTPELLRAAAGECRRVRGETLPSDSPgTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  197 QTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPC 276
Cdd:cd07150 157 ETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR-HLKKITLELGGKNPL 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  277 IVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILG 356
Cdd:cd07150 236 IVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKR 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  357 LIESGKKEGAKLECGGGRWGNkgfFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKD 436
Cdd:cd07150 316 QVEDAVAKGAKLLTGGKYDGN---FYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTND 392
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7106242  437 LDKAITVSSALQAGMVWVNCylaVPV----QCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07150 393 LQRAFKLAERLESGMVHIND---PTIldeaHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
PRK13473 PRK13473
gamma-aminobutyraldehyde dehydrogenase; Provisional
20-492 5.27e-159

gamma-aminobutyraldehyde dehydrogenase; Provisional


Pssm-ID: 237391 [Multi-domain]  Cd Length: 475  Bit Score: 459.76  E-value: 5.27e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    20 HTKIFINNEWHDSvSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFqigSPWRTMDASERGRLLNKLADLMERD 99
Cdd:PRK13473   2 QTKLLINGELVAG-EGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAF---PEWSQTTPKERAEALLKLADAIEEN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   100 RLLLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGqtiPSDGNI---FT-YTRREPIGVCGQIIPWNGPLII 175
Cdd:PRK13473  78 ADEFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEG---KAAGEYlegHTsMIRRDPVGVVASIAPWNYPLMM 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   176 FTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAgFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIK 255
Cdd:PRK13473 155 AAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVL 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   256 EAAGKSnLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNP 335
Cdd:PRK13473 234 SAAADS-VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDP 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   336 LNSGINQGPQIDKEQHNKILGLIESGKKEG-AKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSM 414
Cdd:PRK13473 313 DDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDE 392
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7106242   415 DDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:PRK13473 393 DQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470
ALDH_PADH_NahF cd07113
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ...
24-494 2.60e-156

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 [Multi-domain]  Cd Length: 477  Bit Score: 453.05  E-value: 2.60e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   24 FINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigSPWRTMDASERGRLLNKLADLMERDRLLL 103
Cdd:cd07113   3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV--SAWAKTTPAERGRILLRLADLIEQHGEEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  104 ATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQT----IPS-DGNIFT-YTRREPIGVCGQIIPWNGPLIIFT 177
Cdd:cd07113  81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETlapsIPSmQGERYTaFTRREPVGVVAGIVPWNFSVMIAV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  178 WKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTaGGAISSHMDIDKVSFTGSTEVGKLIKEA 257
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQ 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  258 AgKSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLN 337
Cdd:cd07113 240 A-ASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  338 SGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDV 417
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEEL 398
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7106242  418 IKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07113 399 IQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMI 475
ALDH_BenzADH-like cd07104
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ...
59-494 3.25e-156

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


Pssm-ID: 143422 [Multi-domain]  Cd Length: 431  Bit Score: 450.83  E-value: 3.25e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   59 DVDKAVKAARQAFQigsPWRTMDASERGRLLNKLADLMERDR----LLLATmESmnaGKVFAHAYLlDVEISIKALQYFA 134
Cdd:cd07104   1 DVDRAYAAAAAAQK---AWAATPPQERAAILRKAAEILEERRdeiaDWLIR-ES---GSTRPKAAF-EVGAAIAILREAA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  135 GWADKIHGQTIPSDGN-IFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLT-ALHMASLIKEA 212
Cdd:cd07104  73 GLPRRPEGEILPSDVPgKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  213 GFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKsNLKRVTLELGGKSPCIVFADADLDSAVEFAH 292
Cdd:cd07104 153 GLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAA 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  293 QGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGG 372
Cdd:cd07104 232 FGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGG 311
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  373 GRWGNkgfFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMV 452
Cdd:cd07104 312 TYEGL---FYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMV 388
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*.
gi 7106242  453 WVNCylaVPVQC----PFGGFKMSGNGRELGEHGLYEYTELKTVAM 494
Cdd:cd07104 389 HIND---QTVNDephvPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
PLN02278 PLN02278
succinic semialdehyde dehydrogenase
2-494 3.01e-155

succinic semialdehyde dehydrogenase


Pssm-ID: 215157 [Multi-domain]  Cd Length: 498  Bit Score: 451.07  E-value: 3.01e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242     2 SSPAQPAVPAPLANLKIQHTKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQigsPWRTMD 81
Cdd:PLN02278   6 SSMDAQSALVKLRNAGLLRTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP---SWSKLT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    82 ASERGRLLNKLADLMERDRLLLATMESMNAGKVFAHAYlldVEISIKA--LQYFAGWADKIHGQTIPS---DGNIFTYtr 156
Cdd:PLN02278  83 ASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAI---GEVAYGAsfLEYFAEEAKRVYGDIIPSpfpDRRLLVL-- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   157 REPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSH 236
Cdd:PLN02278 158 KQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLAS 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   237 MDIDKVSFTGSTEVGKLIKEAAGKSnLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIY 316
Cdd:PLN02278 238 PKVRKITFTGSTAVGKKLMAGAAAT-VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIY 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   317 DEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLIESGKKEGAKLECGGGRWGNKGFFVQPTVFSNVTDEMRI 396
Cdd:PLN02278 317 DKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLI 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   397 AKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGR 476
Cdd:PLN02278 397 FREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGR 476
                        490
                 ....*....|....*...
gi 7106242   477 ELGEHGLYEYTELKTVAM 494
Cdd:PLN02278 477 EGSKYGIDEYLEIKYVCL 494
PRK09847 PRK09847
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
14-496 2.08e-154

gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional


Pssm-ID: 182108 [Multi-domain]  Cd Length: 494  Bit Score: 448.96  E-value: 2.08e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    14 ANLKIQhTKIFINNEWHDSVSSKKFPVLNPATEEVICHVEEGDKADVDKAVKAARQAFQIGSpWRTMDASERGRLLNKLA 93
Cdd:PRK09847  14 LSLAIE-NRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGD-WSLSSPAKRKAVLNKLA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242    94 DLMERDRLLLATMESMNAGKVFAHAYLLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPL 173
Cdd:PRK09847  92 DLMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPL 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   174 IIFTWKLGPALSCGNTVVVKPAEQTPLTALHMASLIKEAGFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKL 253
Cdd:PRK09847 172 LLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQ 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   254 IKEAAGKSNLKRVTLELGGKSPCIVFADA-DLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFVRRSVERAKKYIL 332
Cdd:PRK09847 252 LLKDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQP 331
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   333 GNPLNSGINQGPQIDKEQHNKILGLIESGKKEGAKLEcgGGRWGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFK 412
Cdd:PRK09847 332 GHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLL--DGRNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFT 409
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   413 SMDDVIKRANNTTYGLAAGVFTKDLDKAITVSSALQAGMVWVNCYLAVPVQCPFGGFKMSGNGRELGEHGLYEYTELKTV 492
Cdd:PRK09847 410 SEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489

                 ....
gi 7106242   493 AMQI 496
Cdd:PRK09847 490 WISL 493
ALDH_PhdK-like cd07107
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ...
40-496 2.28e-154

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


Pssm-ID: 143425 [Multi-domain]  Cd Length: 456  Bit Score: 447.21  E-value: 2.28e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242   40 VLNPATEEVICHVEEGDKADVDKAVKAARQAFQIgspWRTMDASERGRLLNKLADLMERDRLLLATMESMNAGKVFAhAY 119
Cdd:cd07107   1 VINPATGQVLARVPAASAADVDRAVAAARAAFPE---WRATTPLERARMLRELATRLREHAEELALIDALDCGNPVS-AM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  120 LLDVEISIKALQYFAGWADKIHGQTIPSDGNIFTYTRREPIGVCGQIIPWNGPLIIFTWKLGPALSCGNTVVVKPAEQTP 199
Cdd:cd07107  77 LGDVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  200 LTALHMASLIKEAgFPPGVVNIVPGYGPTAGGAISSHMDIDKVSFTGSTEVGKLIKEAAGKSnLKRVTLELGGKSPCIVF 279
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVF 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  280 ADADLDSAVEFAHQGVFFH-QGQICVAASRLFVEESIYDEFVRRSVERAKKYILGNPLNSGINQGPQIDKEQHNKILGLI 358
Cdd:cd07107 235 PDADPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYI 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106242  359 ESGKKEGAKLECGGGR----WGNKGFFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSMDDVIKRANNTTYGLAAGVFT 434
Cdd:cd07107 315 DSAKREGARLVTGGGRpegpALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWT 394
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7106242  435 KDLDKAITVSSALQAGMVWVNC----YLAVpvqcPFGGFKMSGNGRELGEHGLYEYTELKTVAMQI 496
Cdd:cd07107 395 NDISQAHRTARRVEAGYVWINGssrhFLGA----PFGGVK