|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
1-495 |
0e+00 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 947.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 1 MEFHDLTYWQNKAARLTIEGRLFYQGDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFERGDWSQAAP 80
Cdd:PRK09847 1 MNFHHLAYWQDKALSLAIENRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGDWSLSSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 81 AARKAVLMRLAALMEQHHEELALLESLDTGKPIRHSLRDDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIVREPVGV 160
Cdd:PRK09847 81 AKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 161 VAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVM 240
Cdd:PRK09847 161 IAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 241 TFTGSTRTGKQLLKDAGESNMKRVWLEAGGKSANIVFADCPDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLA 320
Cdd:PRK09847 241 AFTGSTRTGKQLLKDAGDSNMKRVWLEAGGKSANIVFADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 321 RVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASVRRYIELGQAQGaTLWLDGRAQTHPACIGPTIFTDVDNQMRVAREEIF 400
Cdd:PRK09847 321 LLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAAIGPTIFVDVDPNASLSREEIF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 401 GPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHA 480
Cdd:PRK09847 400 GPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHA 479
|
490
....*....|....*
gi 1258251391 481 LEKFTELKTIWMSLE 495
Cdd:PRK09847 480 LEKFTELKTIWISLE 494
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
34-492 |
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: 789.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 34 GDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFERGDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPI 113
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 114 RHSLRDDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPS 193
Cdd:cd07112 81 SDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 194 EKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGESNMKRVWLEAGGKSA 273
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKSP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 274 NIVFADCPDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASV 353
Cdd:cd07112 241 NIVFADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 354 RRYIELGQAQGATLWLDG---RAQTHPACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAV 430
Cdd:cd07112 321 LGYIESGKAEGARLVAGGkrvLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASV 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1258251391 431 WTRSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWM 492
Cdd:cd07112 401 WTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
17-494 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 629.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 17 TIEGRLFYQGDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFerGDWSQAAPAARKAVLMRLAALMEQ 96
Cdd:COG1012 3 TPEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAF--PAWAATPPAERAAILLRAADLLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 97 HHEELALLESLDTGKPIRHSlRDDIPGAARALRWYAEAVDKLYGEVAPTDNA-SLAMIVREpvgvvaavvpWNFPLLLAC 175
Cdd:COG1012 81 RREELAALLTLETGKPLAEA-RGEVDRAADFLRYYAGEARRLYGETIPSDAPgTRAYVRREplgvvgaitpWNFPLALAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 176 WKLGPALAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKD 255
Cdd:COG1012 160 WKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 256 AGEsNMKRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPL 335
Cdd:COG1012 240 AAE-NLKRVTLELGGKNPAIVLDDA-DLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 336 DPQTTMGTLIDDDHAASVRRYIELGQAQGATLWLDGRAQTHP--ACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEE 413
Cdd:COG1012 318 DPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGEggYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 414 EALRLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYN-DGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWM 492
Cdd:COG1012 398 EAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTtGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTI 477
|
..
gi 1258251391 493 SL 494
Cdd:COG1012 478 RL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
31-490 |
0e+00 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 597.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 31 AASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFERgdWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTG 110
Cdd:pfam00171 3 DSESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPA--WRKTPAAERAAILRKAADLLEERKDELAELETLENG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 111 KPIRHSlRDDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVL 190
Cdd:pfam00171 81 KPLAEA-RGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 191 KPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGEsNMKRVWLEAGG 270
Cdd:pfam00171 160 KPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ-NLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 271 KSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHA 350
Cdd:pfam00171 239 KNPLIVLEDA-DLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 351 ASVRRYIELGQAQGATLWLDGRAQT-HPACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAA 429
Cdd:pfam00171 318 ERVLKYVEDAKEEGAKLLTGGEAGLdNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAG 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1258251391 430 VWTRSLSRAHRMARRLKAGSVFINNYNDGDM-TVPFGGYKQSGNGRDKSLHALEKFTELKTI 490
Cdd:pfam00171 398 VFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
22-490 |
0e+00 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 595.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 22 LFYQGDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFERGDWSQAAPAARKAVLMRLAALMEQHHEEL 101
Cdd:cd07091 6 LFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIERDRDEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 102 ALLESLDTGKPIRHSLRDDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPA 181
Cdd:cd07091 86 AALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 182 LAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGESNM 261
Cdd:cd07091 166 LAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSNL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 262 KRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTM 341
Cdd:cd07091 246 KKVTLELGGKSPNIVFDDA-DLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 342 GTLIDDDHAASVRRYIELGQAQGATLWLDG-RAQTHPACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLAN 420
Cdd:cd07091 325 GPQVSKAQFDKILSYIESGKKEGATLLTGGeRHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERAN 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 421 DSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 490
Cdd:cd07091 405 DTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
39-494 |
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: 552.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 39 VLNPATGEPLAEVARGAKRDVDAAVASARAVFERgdWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRHSLR 118
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEA--WSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 119 DDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPL 198
Cdd:cd07115 79 LDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 199 SALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGeSNMKRVWLEAGGKSANIVFA 278
Cdd:cd07115 159 SALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA-GNLKRVSLELGGKSANIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 279 DCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASVRRYIE 358
Cdd:cd07115 238 DA-DLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 359 LGQAQGATLWLDGRAQTHPAC-IGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSLSR 437
Cdd:cd07115 317 VGREEGARLLTGGKRPGARGFfVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1258251391 438 AHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWMSL 494
Cdd:cd07115 397 AHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
39-490 |
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: 546.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 39 VLNPATGEPLAEVARGAKRDVDAAVASARAVFErgDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRHSLR 118
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFP--GWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLART 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 119 DDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPL 198
Cdd:cd07093 79 RDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 199 SALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGEsNMKRVWLEAGGKSANIVFA 278
Cdd:cd07093 159 TAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAP-NLKPVSLELGGKNPNIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 279 DCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASVRRYIE 358
Cdd:cd07093 238 DA-DLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 359 LGQAQGATLWLDGRAQTHPACIG-----PTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTR 433
Cdd:cd07093 317 LARAEGATILTGGGRPELPDLEGgyfvePTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1258251391 434 SLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 490
Cdd:cd07093 397 DLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNV 453
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
39-492 |
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: 539.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 39 VLNPATGEPLAEVARGAKRDVDAAVASARAVFERGDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRHSlR 118
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRET-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 119 DDIPGAARALRWYAEAVDKLYGEVAPTDNAS-LAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSP 197
Cdd:cd07114 80 AQVRYLAEWYRYYAGLADKIEGAVIPVDKGDyLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 198 LSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGEsNMKRVWLEAGGKSANIVF 277
Cdd:cd07114 160 ASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGKSPNIVF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 278 ADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASVRRYI 357
Cdd:cd07114 239 DDA-DLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 358 ELGQAQGATLWLDGRAQTHPACIG-----PTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWT 432
Cdd:cd07114 318 ARAREEGARVLTGGERPSGADLGAgyffePTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWT 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 433 RSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWM 492
Cdd:cd07114 398 RDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
23-495 |
0e+00 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 539.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 23 FYQGDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFERGDWSQAAPAARKAVLMRLAALMEQHHEELA 102
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 103 LLESLDTGKPIRHSlRDDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPAL 182
Cdd:cd07119 81 RLETLNTGKTLRES-EIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 183 AAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGEsNMK 262
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAG-NVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 263 RVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMG 342
Cdd:cd07119 239 KVALELGGKNPNIVFADA-DFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 343 TLIDDDHAASVRRYIELGQAQGATLWLDGRAQTHPAC-----IGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALR 417
Cdd:cd07119 318 PLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELakgyfVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1258251391 418 LANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWMSLE 495
Cdd:cd07119 398 LANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININLS 475
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
60-492 |
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: 534.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 60 DAAVASARAVFErgDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRhSLRDDIPGAARALRWYAEAVDKLY 139
Cdd:cd07078 1 DAAVAAARAAFK--AWAALPPAERAAILRKLADLLEERREELAALETLETGKPIE-EALGEVARAADTFRYYAGLARRLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 140 GEVAPTDNA-SLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLN 218
Cdd:cd07078 78 GEVIPSPDPgELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 219 VIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGEsNMKRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQ 298
Cdd:cd07078 158 VVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDA-DLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 299 GQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASVRRYIELGQAQGATLWLDGRAQTHP- 377
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGk 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 378 -ACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYN 456
Cdd:cd07078 316 gYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
|
410 420 430
....*....|....*....|....*....|....*..
gi 1258251391 457 DG-DMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWM 492
Cdd:cd07078 396 VGaEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
26-490 |
1.31e-177 |
|
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: 506.66 E-value: 1.31e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 26 GDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFERgdWSQAAPAARKAVLMRLAALMEQHHEELALLE 105
Cdd:cd07138 5 GAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPA--WSATSVEERAALLERIAEAYEARADELAQAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 106 SLDTGKPIRHSLRDDIPGAARALRWYAEAVDKlYGEVAPTDNAslaMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAG 185
Cdd:cd07138 83 TLEMGAPITLARAAQVGLGIGHLRAAADALKD-FEFEERRGNS---LVVREPIGVCGLITPWNWPLNQIVLKVAPALAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 186 NSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGESnMKRVW 265
Cdd:cd07138 159 CTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADT-VKRVA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 266 LEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLI 345
Cdd:cd07138 238 LELGGKSANIILDDA-DLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 346 DDDHAASVRRYIELGQAQGATLWLDGRAqtHPAC------IGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLA 419
Cdd:cd07138 317 SAAQFDRVQGYIQKGIEEGARLVAGGPG--RPEGlergyfVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIA 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1258251391 420 NDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFInNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 490
Cdd:cd07138 395 NDTPYGLAGYVWSADPERARAVARRLRAGQVHI-NGAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSI 464
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
22-494 |
4.19e-177 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 506.17 E-value: 4.19e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 22 LFYQGDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFErGDWSQAAPAARKAVLMRLAALMEQHHEEL 101
Cdd:cd07144 10 LFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFE-SWWSKVTGEERGELLDKLADLVEKNRDLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 102 ALLESLDTGKPIRHSLRDDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPA 181
Cdd:cd07144 89 AAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 182 LAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGeSNM 261
Cdd:cd07144 169 LAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAA-QNL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 262 KRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHA-QSFTPGDPLDPQTT 340
Cdd:cd07144 248 KAVTLECGGKSPALVFEDA-DLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNYKVGSPFDDDTV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 341 MGTLIDDDHAASVRRYIELGQAQGATLWLDGRAQTHPAC----IGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEAL 416
Cdd:cd07144 327 VGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGLGkgyfIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAI 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1258251391 417 RLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWMSL 494
Cdd:cd07144 407 KKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHINL 484
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
39-490 |
3.46e-175 |
|
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: 500.22 E-value: 3.46e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 39 VLNPATGEPLAEVARGAKRDVDAAVASARAVFErGDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRHSlR 118
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFE-SGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQA-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 119 DDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPL 198
Cdd:cd07109 79 ADVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 199 SALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGEsNMKRVWLEAGGKSANIVFA 278
Cdd:cd07109 159 TALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 279 DCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDpQTTMGTLIDDDHAASVRRYIE 358
Cdd:cd07109 238 DA-DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 359 LGQAQGATLWLDGRAQTHPACIG----PTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRS 434
Cdd:cd07109 316 RARARGARIVAGGRIAEGAPAGGyfvaPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRD 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1258251391 435 LSRAHRMARRLKAGSVFINNYND-GDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 490
Cdd:cd07109 396 GDRALRVARRLRAGQVFVNNYGAgGGIELPFGGVKKSGHGREKGLEALYNYTQTKTV 452
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
21-493 |
6.82e-171 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 490.32 E-value: 6.82e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 21 RLFYQGDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFERGD-WSQAAPAARKAVLMRLAALMEQHHE 99
Cdd:cd07141 8 KIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGSpWRTMDASERGRLLNKLADLIERDRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 100 ELALLESLDTGKPIRHSLRDDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLG 179
Cdd:cd07141 88 YLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 180 PALAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGES 259
Cdd:cd07141 168 PALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 260 NMKRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQT 339
Cdd:cd07141 248 NLKRVTLELGGKSPNIVFADA-DLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 340 TMGTLIDDDHAASVRRYIELGQAQGATLWLDG-RAQTHPACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRL 418
Cdd:cd07141 327 EQGPQIDEEQFKKILELIESGKKEGAKLECGGkRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIER 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1258251391 419 ANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWMS 493
Cdd:cd07141 407 ANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 481
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
21-494 |
2.29e-170 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 489.39 E-value: 2.29e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 21 RLFYQGDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFErgDWSQAAPAARKAVLMRLAALMEQHHEE 100
Cdd:PRK13252 8 SLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQK--IWAAMTAMERSRILRRAVDILRERNDE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 101 LALLESLDTGKPIRHSLRDDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGP 180
Cdd:PRK13252 86 LAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 181 ALAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGhEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGESn 260
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 261 MKRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTT 340
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDDA-DLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 341 MGTLIDDDHAASVRRYIELGQAQGATLWLDGRAQTHPAC-----IGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEA 415
Cdd:PRK13252 323 FGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFangafVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEV 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1258251391 416 LRLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWMSL 494
Cdd:PRK13252 403 IARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQVEM 481
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
22-494 |
3.17e-167 |
|
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: 481.07 E-value: 3.17e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 22 LFYQGDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFERgdWSQAAPAARKAVLMRLAALMEQHHEEL 101
Cdd:cd07559 3 NFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT--WGKTSVAERANILNKIADRIEENLELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 102 ALLESLDTGKPIRHSLRDDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPA 181
Cdd:cd07559 81 AVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 182 LAAGNSVVLKPSEKSPLSALRLAGLAREAgLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGEsNM 261
Cdd:cd07559 161 LAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE-NL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 262 KRVWLEAGGKSANIVFADCPDLDQAAASAAAGIF----YNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDP 337
Cdd:cd07559 239 IPVTLELGGKSPNIFFDDAMDADDDFDDKAEEGQlgfaFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 338 QTTMGTLIDDDHAASVRRYIELGQAQGATLWLDGRAQTHPACIG-----PTIFTDVDNQMRVAREEIFGPVLAVTTFTGE 412
Cdd:cd07559 319 ETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKgyfyePTLIKGGNNDMRIFQEEIFGPVLAVITFKDE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 413 EEALRLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWM 492
Cdd:cd07559 399 EEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNILV 478
|
..
gi 1258251391 493 SL 494
Cdd:cd07559 479 SY 480
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
40-490 |
3.26e-166 |
|
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: 477.60 E-value: 3.26e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 40 LNPATGEPLAEVARGAKRDVDAAVASARAVFERGDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRHSlRD 119
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQA-RG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 120 DIPGAARALRWYAEAVDKLYGEVAPT-DNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPL 198
Cdd:cd07118 81 EIEGAADLWRYAASLARTLHGDSYNNlGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 199 SALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGEsNMKRVWLEAGGKSANIVFA 278
Cdd:cd07118 161 TTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVFA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 279 DCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASVRRYIE 358
Cdd:cd07118 240 DA-DLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 359 LGQAQGATLWLDGRAQTHPA--CIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSLS 436
Cdd:cd07118 319 AGRAEGATLLLGGERLASAAglFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDID 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1258251391 437 RAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 490
Cdd:cd07118 399 TALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
39-490 |
5.72e-166 |
|
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: 477.12 E-value: 5.72e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 39 VLNPATGEPLAEVARGAKRDVDAAVASARAVFERGDWSqAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRHSLR 118
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 119 DDIPGAARALRWYAEAVDKLYGEVAPTDNASLAM-----IVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPS 193
Cdd:cd07089 80 MQVDGPIGHLRYFADLADSFPWEFDLPVPALRGGpgrrvVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 194 EKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGEsNMKRVWLEAGGKSA 273
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAA-TLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 274 NIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASV 353
Cdd:cd07089 239 NIVLDDA-DLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 354 RRYIELGQAQGATLWLDGRAqthPAC------IGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLG 427
Cdd:cd07089 318 EGYIARGRDEGARLVTGGGR---PAGldkgfyVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLS 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1258251391 428 AAVWTRSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 490
Cdd:cd07089 395 GGVWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
39-490 |
6.73e-166 |
|
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: 476.80 E-value: 6.73e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 39 VLNPATGEPLAEVARGAKRDVDAAVASARAVFERgdWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIrHSLR 118
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKE--WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPI-EEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 119 DDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPL 198
Cdd:cd07090 78 VDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 199 SALRLAGLAREAGLPDGVLNVIPGFGhEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGeSNMKRVWLEAGGKSANIVFA 278
Cdd:cd07090 158 TALLLAEILTEAGLPDGVFNVVQGGG-ETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAA-KGIKHVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 279 DCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASVRRYIE 358
Cdd:cd07090 236 DA-DLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 359 LGQAQGATLWLDG-RAQTHPAC-----IGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWT 432
Cdd:cd07090 315 SAKQEGAKVLCGGeRVVPEDGLengfyVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFT 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1258251391 433 RSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 490
Cdd:cd07090 395 RDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
21-492 |
4.13e-165 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 475.45 E-value: 4.13e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 21 RLFYQGDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFERGDWSQAAPAARKAVLMRLAALMEQHHEE 100
Cdd:cd07142 5 KLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYERSRILLRFADLLEKHADE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 101 LALLESLDTGKPIRHSLRDDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGP 180
Cdd:cd07142 85 LAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 181 ALAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGESN 260
Cdd:cd07142 165 ALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 261 MKRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTT 340
Cdd:cd07142 245 LKPVTLELGGKSPFIVCEDA-DVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 341 MGTLIDDDHAASVRRYIELGQAQGATLWLDG-RAQTHPACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLA 419
Cdd:cd07142 324 QGPQVDKEQFEKILSYIEHGKEEGATLITGGdRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRA 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1258251391 420 NDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWM 492
Cdd:cd07142 404 NNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVVM 476
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
22-492 |
4.49e-165 |
|
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: 475.14 E-value: 4.49e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 22 LFYQGDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFERGDWSQAAPAARKAVLMRLAALMEQHHEEL 101
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 102 ALLESLDTGKPIRHSLRDDIPGAARALRWYAEAVDKL-YGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGP 180
Cdd:cd07139 81 ARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFpFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 181 ALAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGfGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGEsN 260
Cdd:cd07139 161 ALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGE-R 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 261 MKRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTT 340
Cdd:cd07139 239 LARVTLELGGKSAAIVLDDA-DLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 341 MGTLIDDDHAASVRRYIELGQAQGATLWLDGRAQTHPA---CIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALR 417
Cdd:cd07139 318 IGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGLDrgwFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1258251391 418 LANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYnDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWM 492
Cdd:cd07139 398 IANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
23-488 |
1.17e-164 |
|
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: 473.91 E-value: 1.17e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 23 FYQGDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFerGDWSQAAPAARKAVLMRLAALMEQHHEELA 102
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ--GEWAAMSPMERGRILRRAADLIRERNEELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 103 LLESLDTGKPIRHSLRDDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPAL 182
Cdd:TIGR01804 79 KLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 183 AAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGEsNMK 262
Cdd:TIGR01804 159 AAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAG-HLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 263 RVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMG 342
Cdd:TIGR01804 238 HVTMELGGKSPLIVFDDA-DLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 343 TLIDDDHAASVRRYIELGQAQGATLWLDGRAQTHPAC-----IGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALR 417
Cdd:TIGR01804 317 PLISAAHRDKVLSYIEKGKAEGATLATGGGRPENVGLqngffVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1258251391 418 LANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELK 488
Cdd:TIGR01804 397 RANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
22-494 |
4.24e-163 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 470.47 E-value: 4.24e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 22 LFYQGDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFErGDWS-QAAPAARKAVLMRLAALMEQHHEE 100
Cdd:cd07143 9 LFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE-TDWGlKVSGSKRGRCLSKLADLMERNLDY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 101 LALLESLDTGKPIRHSLRDDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGP 180
Cdd:cd07143 88 LASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 181 ALAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGESN 260
Cdd:cd07143 168 ALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 261 MKRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTT 340
Cdd:cd07143 248 LKKVTLELGGKSPNIVFDDA-DLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTF 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 341 MGTLIDDDHAASVRRYIELGQAQGATLWLDG-RAQTHPACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLA 419
Cdd:cd07143 327 QGPQVSQIQYERIMSYIESGKAEGATVETGGkRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRA 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1258251391 420 NDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWMSL 494
Cdd:cd07143 407 NDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHINL 481
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
22-498 |
6.24e-161 |
|
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the dehydrogenase responsible for the conversion of 5-carboxymethyl-2-hydroxymuconate semialdehyde to 5-carboxymethyl-2-hydroxymuconate (a tricarboxylic acid). This is the step in the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate following the oxidative opening of the aromatic ring.
Pssm-ID: 131352 Cd Length: 488 Bit Score: 465.43 E-value: 6.24e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 22 LFYQGDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFERgdWSQAAPAARKAVLMRLAALMEQHHEEL 101
Cdd:TIGR02299 3 HFIDGEFVPSESGETFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFKR--WAELKAAERKRYLHKIADLIEQHADEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 102 ALLESLDTGKPIRHsLRDDIPGAARALRWYAEAV-DKLYGEVAPTDNaSLAMIVREPVGVVAAVVPWNFPLLLACWKLGP 180
Cdd:TIGR02299 81 AVLECLDCGQPLRQ-TRQQVIRAAENFRFFADKCeEAMDGRTYPVDT-HLNYTVRVPVGPVGLITPWNAPFMLSTWKIAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 181 ALAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKdAGESN 260
Cdd:TIGR02299 159 ALAFGNTVVLKPAEWSPLTAARLAEIAKEAGLPDGVFNLVHGFGEEAGKALVAHPDVKAVSFTGETATGSIIMR-NGADT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 261 MKRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTT 340
Cdd:TIGR02299 238 LKRFSMELGGKSPVIVFDDA-DLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLDPETE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 341 MGTLIDDDHAASVRRYIELGQAQGATLWLDGRA--QTHPACIG------PTIFTDVDNQMRVAREEIFGPVLAVTTFTGE 412
Cdd:TIGR02299 317 VGPLIHPEHLAKVLGYVEAAEKEGATILVGGERapTFRGEDLGrgnyvlPTVFTGADNHMRIAQEEIFGPVLTVIPFKDE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 413 EEALRLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWM 492
Cdd:TIGR02299 397 EEAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDFYTETKNVAL 476
|
....*.
gi 1258251391 493 SLEHNH 498
Cdd:TIGR02299 477 ALGPHH 482
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
39-490 |
6.75e-158 |
|
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: 456.12 E-value: 6.75e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 39 VLNPATGEPLAEVARGAKRDVDAAVASARAVFErgDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRHSlR 118
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFK--TWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 119 DDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIV-REPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSP 197
Cdd:cd07103 78 GEVDYAASFLEWFAEEARRIYGRTIPSPAPGKRILViKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 198 LSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGEsNMKRVWLEAGGKSANIVF 277
Cdd:cd07103 158 LSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAAD-TVKRVSLELGGNAPFIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 278 ADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASVRRYI 357
Cdd:cd07103 237 DDA-DLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 358 ELGQAQGATLWLDGRAQTHPAC-IGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSLS 436
Cdd:cd07103 316 EDAVAKGAKVLTGGKRLGLGGYfYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1258251391 437 RAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 490
Cdd:cd07103 396 RAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
21-494 |
1.42e-156 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 454.66 E-value: 1.42e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 21 RLFYQGDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFERGDWSQAAPAARKAVLMRLAALMEQHHEE 100
Cdd:PLN02766 22 KLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFERGRIMMKFADLIEEHIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 101 LALLESLDTGKPIRHSLRDDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGP 180
Cdd:PLN02766 102 LAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 181 ALAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGESN 260
Cdd:PLN02766 182 ALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 261 MKRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTT 340
Cdd:PLN02766 262 LKQVSLELGGKSPLLIFDDA-DVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRAR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 341 MGTLIDDDHAASVRRYIELGQAQGATLWLDGRAQTHPA-CIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLA 419
Cdd:PLN02766 341 QGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGyYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKA 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1258251391 420 NDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWMSL 494
Cdd:PLN02766 421 NNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTPL 495
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
15-488 |
3.47e-152 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 442.43 E-value: 3.47e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 15 RLTIEGRLfyqgdyrAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFERgdWSQAAPAARKAVLMRLAALM 94
Cdd:PRK13473 4 KLLINGEL-------VAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPE--WSQTTPKERAEALLKLADAI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 95 EQHHEELALLESLDTGKPIRHSLRDDIPGAARALRWYAEAVDKLYGEVAP---TDNASlaMIVREPVGVVAAVVPWNFPL 171
Cdd:PRK13473 75 EENADEFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKAAGeylEGHTS--MIRRDPVGVVASIAPWNYPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 172 LLACWKLGPALAAGNSVVLKPSEKSPLSALRLAGLAREAgLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQ 251
Cdd:PRK13473 153 MMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 252 LLKDAGeSNMKRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTP 331
Cdd:PRK13473 232 VLSAAA-DSVKRTHLELGGKAPVIVFDDA-DLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 332 GDPLDPQTTMGTLIDDDHAASVRRYIELGQAQG-ATLWLDGRAQTHPAC-IGPTIFTDVDNQMRVAREEIFGPVLAVTTF 409
Cdd:PRK13473 310 GDPDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYyYEPTLLAGARQDDEIVQREVFGPVVSVTPF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 410 TGEEEALRLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFInnyNDGDMTV---PFGGYKQSGNGRDKSLHALEKFTE 486
Cdd:PRK13473 390 DDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWV---NTHFMLVsemPHGGQKQSGYGKDMSLYGLEDYTV 466
|
..
gi 1258251391 487 LK 488
Cdd:PRK13473 467 VR 468
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
21-494 |
4.44e-152 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 444.64 E-value: 4.44e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 21 RLFYQGDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFERGDWSQAAPAARKAVLMRLAALMEQHHEE 100
Cdd:PLN02466 59 QLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRILLRFADLLEKHNDE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 101 LALLESLDTGKPIRHSLRDDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGP 180
Cdd:PLN02466 139 LAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 181 ALAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGESN 260
Cdd:PLN02466 219 ALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSN 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 261 MKRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTT 340
Cdd:PLN02466 299 LKPVTLELGGKSPFIVCEDA-DVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVE 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 341 MGTLIDDDHAASVRRYIELGQAQGATLWLDG-RAQTHPACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLA 419
Cdd:PLN02466 378 QGPQIDSEQFEKILRYIKSGVESGATLECGGdRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRA 457
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1258251391 420 NDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWMSL 494
Cdd:PLN02466 458 NNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAVVTPL 532
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
39-494 |
4.63e-148 |
|
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: 431.41 E-value: 4.63e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 39 VLNPATGEPLAEVARGAKRDVDAAVASARAVFErgDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRhSLR 118
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFP--EWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVS-AML 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 119 DDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPL 198
Cdd:cd07107 78 GDVMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 199 SALRLAGLAREAgLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGESnMKRVWLEAGGKSANIVFA 278
Cdd:cd07107 158 SALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVFP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 279 DCpDLDQAAASAAAGI-FYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASVRRYI 357
Cdd:cd07107 236 DA-DPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 358 ELGQAQGATLWLDGRAQTHPAC-----IGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWT 432
Cdd:cd07107 315 DSAKREGARLVTGGGRPEGPALeggfyVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWT 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1258251391 433 RSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWMSL 494
Cdd:cd07107 395 NDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
22-494 |
1.33e-147 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 430.72 E-value: 1.33e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 22 LFYQGDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFERgdWSQAAPAARKAVLMRLAALMEQHHEEL 101
Cdd:cd07117 3 LFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT--WRKTTVAERANILNKIADIIDENKELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 102 ALLESLDTGKPIRHSLRDDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPA 181
Cdd:cd07117 81 AMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 182 LAAGNSVVLKPSEKSPLSALRLAGLAREAgLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGEsNM 261
Cdd:cd07117 161 LAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK-KL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 262 KRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTM 341
Cdd:cd07117 239 IPATLELGGKSANIIFDDA-NWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 342 GTLIDDDHAASVRRYIELGQAQGATLWLDGRAQTHPAC-----IGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEAL 416
Cdd:cd07117 318 GAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLdkgffIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1258251391 417 RLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWMSL 494
Cdd:cd07117 398 DMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL 475
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
64-492 |
4.22e-144 |
|
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: 417.79 E-value: 4.22e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 64 ASARAVFErgDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRhSLRDDIPGAARALRWYAEAVDKLYG-EV 142
Cdd:cd06534 1 AAARAAFK--AWAALPPAERAAILRKIADLLEERREELAALETLETGKPIE-EALGEVARAIDTFRYAAGLADKLGGpEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 143 APTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPG 222
Cdd:cd06534 78 PSPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 223 FGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGEsNMKRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQAC 302
Cdd:cd06534 158 GGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAE-NLKPVTLELGGKSPVIVDEDA-DLDAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 303 IAGTRLLVEASIKDAFLARVKahaqsftpgdpldpqttmgtlidddhaasvrryielgqaqgatlwldgraqthpacigp 382
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLV----------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 383 TIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDM-T 461
Cdd:cd06534 257 TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGpE 336
|
410 420 430
....*....|....*....|....*....|.
gi 1258251391 462 VPFGGYKQSGNGRDKSLHALEKFTELKTIWM 492
Cdd:cd06534 337 APFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
39-488 |
8.95e-144 |
|
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: 420.19 E-value: 8.95e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 39 VLNPATGEPLAEVARGAKRDVDAAVASARAVFErgDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRHSLR 118
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFP--SWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 119 DDIPGAARALRWYAEAVDKLYGEVAPTDNAS-LAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSP 197
Cdd:cd07092 79 DELPGAVDNFRFFAGAARTLEGPAAGEYLPGhTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 198 LSALRLAGLAREaGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGeSNMKRVWLEAGGKSANIVF 277
Cdd:cd07092 159 LTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAA-DTLKRVHLELGGKAPVIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 278 ADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASVRRYI 357
Cdd:cd07092 237 DDA-DLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 358 ElGQAQGATLWLDGRAQTHPAC-IGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSLS 436
Cdd:cd07092 316 E-RAPAHARVLTGGRRAEGPGYfYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1258251391 437 RAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELK 488
Cdd:cd07092 395 RAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIK 446
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
39-490 |
9.17e-144 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 420.23 E-value: 9.17e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 39 VLNPATGEPLAEVARGAKRDVDAAVASARAVFerGDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRHSLR 118
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAF--PEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 119 DDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPL 198
Cdd:cd07108 79 PEAAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 199 SALRLAGLAREAgLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGEsNMKRVWLEAGGKSANIVFA 278
Cdd:cd07108 159 AVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAAD-RLIPVSLELGGKSPMIVFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 279 DCpDLDQAAASAAAGI-FYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASVRRYI 357
Cdd:cd07108 237 DA-DLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 358 ELGQA-QGATLWLDGRAQTHPAC-----IGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVW 431
Cdd:cd07108 316 DLGLStSGATVLRGGPLPGEGPLadgffVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVW 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 432 TRSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHA-LEKFTELKTI 490
Cdd:cd07108 396 TRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTV 455
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
21-490 |
2.73e-143 |
|
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: 420.36 E-value: 2.73e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 21 RLFYQGDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFERGDWSQAAPAARKAVLMRLAALMEQHHEE 100
Cdd:cd07140 7 QLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLMEEHQEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 101 LALLESLDTGKPIRHSLRDDIPGAARALRWYAEAVDKLYGEVAPTDNA----SLAMIVREPVGVVAAVVPWNFPLLLACW 176
Cdd:cd07140 87 LATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQArpnrNLTLTKREPIGVCGIVIPWNYPLMMLAW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 177 KLGPALAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDA 256
Cdd:cd07140 167 KMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 257 GESNMKRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLD 336
Cdd:cd07140 247 AVSNLKKVSLELGGKSPLIIFADC-DMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 337 PQTTMGTLIDDDHAASVRRYIELGQAQGATLWLDGRAQTHPAC-IGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGE--E 413
Cdd:cd07140 326 RSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFfFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGdvD 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1258251391 414 EALRLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 490
Cdd:cd07140 406 GVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
39-490 |
2.18e-141 |
|
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: 414.44 E-value: 2.18e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 39 VLNPATGEPLAEVARGAKRDVDAAVASARAVFERgdWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRHSLR 118
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPR--WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 119 DdIPGAARALRWYA---EAVDKLYGEVAPTDNASLAMIVR-EPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSE 194
Cdd:cd07110 79 D-VDDVAGCFEYYAdlaEQLDAKAERAVPLPSEDFKARVRrEPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 195 KSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGEsNMKRVWLEAGGKSAN 274
Cdd:cd07110 158 LTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQ-DIKPVSLELGGKSPI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 275 IVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASVR 354
Cdd:cd07110 237 IVFDDA-DLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 355 RYIELGQAQGATLWLDGRAQTHPA---CIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVW 431
Cdd:cd07110 316 SFIARGKEEGARLLCGGRRPAHLEkgyFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1258251391 432 TRSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 490
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
32-492 |
2.07e-140 |
|
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: 412.41 E-value: 2.07e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 32 ASGDTFSVLNPA-TGEPLAEVARGAKRDVDAAVASARAVFERgdWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTG 110
Cdd:cd07097 11 AGGDGEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPA--WRRTSPEARADILDKAGDELEARKEELARLLTREEG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 111 KPIRHSlRDDIPGAARALRWYAEAVDKLYGEVAP-TDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVV 189
Cdd:cd07097 89 KTLPEA-RGEVTRAGQIFRYYAGEALRLSGETLPsTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 190 LKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGeSNMKRVWLEAG 269
Cdd:cd07097 168 FKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAA-ARGARVQLEMG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 270 GKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDH 349
Cdd:cd07097 247 GKNPLVVLDDA-DLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 350 AASVRRYIELGQAQGATLWLDGRAQTHPA---CIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGL 426
Cdd:cd07097 326 LEKDLRYIEIARSEGAKLVYGGERLKRPDegyYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGL 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1258251391 427 GAAVWTRSLSRAHRMARRLKAGSVFINNYNDG-DMTVPFGGYKQSGNG-RDKSLHALEKFTELKTIWM 492
Cdd:cd07097 406 SAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGvDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTVYV 473
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
21-493 |
1.99e-139 |
|
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: 410.25 E-value: 1.99e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 21 RLFYQGDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFERgdWSQAAPAARKAVLMRLAALMEQHHEE 100
Cdd:cd07111 23 GHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES--WSALPGHVRARHLYRIARHIQKHQRL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 101 LALLESLDTGKPIRHSlRD-DIPGAARALRWYAEAVDKLYGEVAPTDNASL-AMIVrepvgvvaavvPWNFPLLLACWKL 178
Cdd:cd07111 101 FAVLESLDNGKPIRES-RDcDIPLVARHFYHHAGWAQLLDTELAGWKPVGVvGQIV-----------PWNFPLLMLAWKI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 179 GPALAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHeAGQALSLHPDVDVMTFTGSTRTGKQLLKD-AG 257
Cdd:cd07111 169 CPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGSTEVGRALRRAtAG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 258 ESnmKRVWLEAGGKSANIVFaDCPDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDP 337
Cdd:cd07111 248 TG--KKLSLELGGKSPFIVF-DDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 338 QTTMGTLIDDDHAASVRRYIELGQAQGATLWLDGRAQTHPACI-GPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEAL 416
Cdd:cd07111 325 AIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFyPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAV 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1258251391 417 RLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFteLKTIWMS 493
Cdd:cd07111 405 ALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY--LRPSWEP 479
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
26-490 |
6.64e-134 |
|
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: 395.95 E-value: 6.64e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 26 GDYRAAASGDTFSVLNPATGEPL-AEVARGAKRDVDAAVASARAVFerGDWsQAAPAARKA-VLMRLAALMEQHHEELAL 103
Cdd:cd07131 5 GEWVDSASGETFDSRNPADLEEVvGTFPLSTASDVDAAVEAAREAF--PEW-RKVPAPRRAeYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 104 LESLDTGKPIRHSlRDDIPGAARALRWYAEAVDKLYGEVAPTDNAS-LAMIVREPVGVVAAVVPWNFPLLLACWKLGPAL 182
Cdd:cd07131 82 LVTREMGKPLAEG-RGDVQEAIDMAQYAAGEGRRLFGETVPSELPNkDAMTRRQPIGVVALITPWNFPVAIPSWKIFPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 183 AAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGESNmK 262
Cdd:cd07131 161 VCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPN-K 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 263 RVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMG 342
Cdd:cd07131 240 RVALEMGGKNPIIVMDDA-DLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 343 TLIDDDHAASVRRYIELGQAQGATLWLDGRAQTHPAC-----IGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALR 417
Cdd:cd07131 319 PLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYekgyfVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1258251391 418 LANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDG-DMTVPFGGYKQSGNG-RDKSLHALEKFTELKTI 490
Cdd:cd07131 399 IANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGaEVHLPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
22-490 |
5.20e-133 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 394.48 E-value: 5.20e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 22 LFYQGDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFER---GDWSQAAPAARKAVLMRLAALMEQHH 98
Cdd:PLN02467 10 LFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgKDWARTTGAVRAKYLRAIAAKITERK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 99 EELALLESLDTGKPIRHSLRDdIPGAARALRWYAEAVDKLYG-EVAPTdnaSLAM------IVREPVGVVAAVVPWNFPL 171
Cdd:PLN02467 90 SELAKLETLDCGKPLDEAAWD-MDDVAGCFEYYADLAEALDAkQKAPV---SLPMetfkgyVLKEPLGVVGLITPWNYPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 172 LLACWKLGPALAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQ 251
Cdd:PLN02467 166 LMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 252 LLKDAGEsNMKRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTP 331
Cdd:PLN02467 246 IMTAAAQ-MVKPVSLELGGKSPIIVFDDV-DLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 332 GDPLDPQTTMGTLIDDDHAASVRRYIELGQAQGATLWLDGRAQTHPA---CIGPTIFTDVDNQMRVAREEIFGPVLAVTT 408
Cdd:PLN02467 324 SDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHLKkgfFIEPTIITDVTTSMQIWREEVFGPVLCVKT 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 409 FTGEEEALRLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELK 488
Cdd:PLN02467 404 FSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVK 483
|
..
gi 1258251391 489 TI 490
Cdd:PLN02467 484 QV 485
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
39-492 |
8.52e-133 |
|
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: 391.89 E-value: 8.52e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 39 VLNPATGEPLAEVARGAKRDVDAAVASARAVFErgDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRHSlR 118
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFP--GWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEA-Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 119 DDIPGAARALRWYAEAvdKLYGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPL 198
Cdd:cd07106 78 FEVGGAVAWLRYTASL--DLPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 199 SALRLAGLAREAgLPDGVLNVIPGfGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGEsNMKRVWLEAGGKSANIVFA 278
Cdd:cd07106 156 CTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAK-TLKRVTLELGGNDAAIVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 279 DCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASVRRYIE 358
Cdd:cd07106 233 DV-DIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 359 LGQAQGATLWLDGRAQTHPAC-IGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSLSR 437
Cdd:cd07106 312 DAKAKGAKVLAGGEPLDGPGYfIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLER 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1258251391 438 AHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWM 492
Cdd:cd07106 392 AEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
23-492 |
1.09e-131 |
|
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: 390.09 E-value: 1.09e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 23 FYQGDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFErgDWSQAAPAARKAVLMRLAALMEQHHEELA 102
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQK--AWERLPAIERAAYLRKLADLIRENADELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 103 LLESLDTGKPIRHSlRDDIPGAARALRWYAEAVDKLYGEVAPTDNAS-LAMIVREPVGVVAAVVPWNFPLLLACWKLGPA 181
Cdd:cd07088 79 KLIVEEQGKTLSLA-RVEVEFTADYIDYMAEWARRIEGEIIPSDRPNeNIFIFKVPIGVVAGILPWNFPFFLIARKLAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 182 LAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGEsNM 261
Cdd:cd07088 158 LVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE-NI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 262 KRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTM 341
Cdd:cd07088 237 TKVSLELGGKAPAIVMKDA-DLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 342 GTLIDDDHAASVRRYIELGQAQGATLWLDGRA--QTHPACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLA 419
Cdd:cd07088 316 GPLVNEAALDKVEEMVERAVEAGATLLTGGKRpeGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1258251391 420 NDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWM 492
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
23-493 |
2.51e-131 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 389.50 E-value: 2.51e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 23 FYQGDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFERgdWSQAAPAARKAVLMRLAALMEQHHEELA 102
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA--WGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 103 LLESLDTGKPIRHSLRDDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPAL 182
Cdd:cd07116 82 VAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 183 AAGNSVVLKPSEKSPLSALRLAGLAREAgLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGEsNMK 262
Cdd:cd07116 162 AAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASE-NII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 263 RVWLEAGGKSANIVFADCPDLDQAAASAAAGIF----YNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQ 338
Cdd:cd07116 240 PVTLELGGKSPNIFFADVMDADDAFFDKALEGFvmfaLNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 339 TTMGTLIDDDHAASVRRYIELGQAQGATLWLDGRAQTHPACIG------PTIFTdvDNQMRVAREEIFGPVLAVTTFTGE 412
Cdd:cd07116 320 TMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGggyyvpTTFKG--GNKMRIFQEEIFGPVLAVTTFKDE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 413 EEALRLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWM 492
Cdd:cd07116 398 EEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLV 477
|
.
gi 1258251391 493 S 493
Cdd:cd07116 478 S 478
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
58-494 |
9.82e-131 |
|
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: 386.12 E-value: 9.82e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 58 DVDAAVASARAVFErgDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKpIRHSLRDDIPGAARALRWYAEAVDK 137
Cdd:cd07104 1 DVDRAYAAAAAAQK--AWAATPPQERAAILRKAAEILEERRDEIADWLIRESGS-TRPKAAFEVGAAIAILREAAGLPRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 138 LYGEVAPTDNAS-LAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPLS-ALRLAGLAREAGLPDG 215
Cdd:cd07104 78 PEGEILPSDVPGkESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 216 VLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGEsNMKRVWLEAGGKSANIVFADCpDLDQAAASAAAGIF 295
Cdd:cd07104 158 VLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDA-DLDLAVSAAAFGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 296 YNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASVRRYIELGQAQGATLWLDGRAQT 375
Cdd:cd07104 236 LHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYEG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 376 hpACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINny 455
Cdd:cd07104 316 --LFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIN-- 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1258251391 456 ndgDMTV------PFGGYKQSGNGRDKSLHALEKFTELKtiWMSL 494
Cdd:cd07104 392 ---DQTVndephvPFGGVKASGGGRFGGPASLEEFTEWQ--WITV 431
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
40-492 |
1.27e-130 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 386.70 E-value: 1.27e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 40 LNPATGEPLAEVARGAKRDVDAAVASARAVFERGDWSQAaPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRHSlRD 119
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFDETDWAHD-PRLRARVLLELADAFEANAERLARLLALENGKILGEA-RF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 120 DIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPLS 199
Cdd:cd07120 80 EISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 200 ALRLAGLAREA-GLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKdAGESNMKRVWLEAGGKSANIVFA 278
Cdd:cd07120 160 NAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMA-AAAPTLKRLGLELGGKTPCIVFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 279 DCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASVRRYIE 358
Cdd:cd07120 239 DA-DLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 359 LGQAQGATLWLDGRAQTHPACIG----PTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRS 434
Cdd:cd07120 318 RAIAAGAEVVLRGGPVTEGLAKGaflrPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1258251391 435 LSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWM 492
Cdd:cd07120 398 LARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
37-490 |
1.53e-130 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 386.57 E-value: 1.53e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 37 FSVLNPATGEPLAEVARGAKRDVDAAVASARAVFERgdwSQAAPAARKA-VLMRLAALMEQHHEELALLESLDTGKPIRH 115
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKE---MKSLPAYERAeILERAAQLLEERREEFARTIALEAGKPIKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 116 SlRDDIPGAARALRWYAEAVDKLYGEVAPTDNAS-----LAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVL 190
Cdd:cd07149 78 A-RKEVDRAIETLRLSAEEAKRLAGETIPFDASPggegrIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 191 KPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGesnMKRVWLEAGG 270
Cdd:cd07149 157 KPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG---LKKVTLELGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 271 KSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHA 350
Cdd:cd07149 234 NAAVIVDADA-DLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 351 ASVRRYIELGQAQGATLWLDGRAQThpACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAV 430
Cdd:cd07149 313 ERIEEWVEEAVEGGARLLTGGKRDG--AILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1258251391 431 WTRSLSRAHRMARRLKAGSVFIN---NYNDGDMtvPFGGYKQSGNGRDKSLHALEKFTELKTI 490
Cdd:cd07149 391 FTNDLQKALKAARELEVGGVMINdssTFRVDHM--PYGGVKESGTGREGPRYAIEEMTEIKLV 451
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
10-492 |
2.42e-130 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 387.51 E-value: 2.42e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 10 QNKAARLTIEGRLFYQG----DYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFErgDWSQAAPAARKA 85
Cdd:PLN02278 11 QSALVKLRNAGLLRTQGliggKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP--SWSKLTASERSK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 86 VLMRLAALMEQHHEELALLESLDTGKPIRHSlRDDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIV-REPVGVVAAV 164
Cdd:PLN02278 89 ILRRWYDLIIANKEDLAQLMTLEQGKPLKEA-IGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVlKQPVGVVGAI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 165 VPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTG 244
Cdd:PLN02278 168 TPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 245 STRTGKQLLKDAGESnMKRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKA 324
Cdd:PLN02278 248 STAVGKKLMAGAAAT-VKRVSLELGGNAPFIVFDDA-DLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 325 HAQSFTPGDPLDPQTTMGTLIDDDHAASVRRYIELGQAQGATLWLDG-RAQTHPACIGPTIFTDVDNQMRVAREEIFGPV 403
Cdd:PLN02278 326 AVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGkRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 404 LAVTTFTGEEEALRLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEK 483
Cdd:PLN02278 406 APLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDE 485
|
....*....
gi 1258251391 484 FTELKTIWM 492
Cdd:PLN02278 486 YLEIKYVCL 494
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
22-492 |
4.77e-130 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 386.03 E-value: 4.77e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 22 LFYQGDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFeRGDWSQAAPAARKAVLMRLAALMEQHHEEL 101
Cdd:cd07113 2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAF-VSAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 102 ALLESLDTGKPIRHSLRDDIPGAARALRWYAEAVDKLYGEvapTDNASL---------AMIVREPVGVVAAVVPWNFPLL 172
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGE---TLAPSIpsmqgerytAFTRREPVGVVAGIVPWNFSVM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 173 LACWKLGPALAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGhEAGQALSLHPDVDVMTFTGSTRTGKQL 252
Cdd:cd07113 158 IAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKKI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 253 LKDAgESNMKRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPG 332
Cdd:cd07113 237 GRQA-ASDLTRVTLELGGKNAAAFLKDA-DIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 333 DPLDPQTTMGTLIDDDHAASVRRYIELGQAQGATLWLDGRAQTHPA-CIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTG 411
Cdd:cd07113 315 SPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGyFVQPTLVLARSADSRLMREETFGPVVSFVPYED 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 412 EEEALRLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIW 491
Cdd:cd07113 395 EEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVM 474
|
.
gi 1258251391 492 M 492
Cdd:cd07113 475 I 475
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
37-490 |
2.29e-129 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 383.62 E-value: 2.29e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 37 FSVLNPATGEPLAEVARGAKRDVDAAVASARAVFERgdWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRHS 116
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDV--MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 117 lRDDIPGAARALRWYAEAVDKLYGEVAPTDNAS-----LAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLK 191
Cdd:cd07145 79 -RVEVERTIRLFKLAAEEAKVLRGETIPVDAYEynerrIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 192 PSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGeSNMKRVWLEAGGK 271
Cdd:cd07145 158 PSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAG-GTGKKVALELGGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 272 SANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAA 351
Cdd:cd07145 237 DPMIVLKDA-DLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 352 SVRRYIELGQAQGATLWLDGRAQTHpACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVW 431
Cdd:cd07145 316 RMENLVNDAVEKGGKILYGGKRDEG-SFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVF 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1258251391 432 TRSLSRAHRMARRLKAGSVFINN---YNDGDMtvPFGGYKQSGNGRDKSLHALEKFTELKTI 490
Cdd:cd07145 395 TNDINRALKVARELEAGGVVINDstrFRWDNL--PFGGFKKSGIGREGVRYTMLEMTEEKTI 454
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
37-490 |
1.63e-128 |
|
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: 381.29 E-value: 1.63e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 37 FSVLNPATGEPLAEVARGAKRDVDAAVASARAVFErgDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRHS 116
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFP--AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 117 LRDdIPGAARALRWYAEAVDKLYGEVAPTDNASL-AMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEK 195
Cdd:cd07150 79 WFE-TTFTPELLRAAAGECRRVRGETLPSDSPGTvSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 196 SPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGeSNMKRVWLEAGGKSANI 275
Cdd:cd07150 158 TPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAG-RHLKKITLELGGKNPLI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 276 VFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASVRR 355
Cdd:cd07150 237 VLADA-DLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 356 YIELGQAQGATL----WLDGRaqthpaCIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVW 431
Cdd:cd07150 316 QVEDAVAKGAKLltggKYDGN------FYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAIL 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 432 TRSLSRAHRMARRLKAGSVFINNYN-DGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 490
Cdd:cd07150 390 TNDLQRAFKLAERLESGMVHINDPTiLDEAHVPFGGVKASGFGREGGEWSMEEFTELKWI 449
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
26-496 |
3.02e-122 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 365.86 E-value: 3.02e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 26 GDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVfeRGDWSQAAPAARKAVLMRLAALMEQHHEELALLE 105
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA--QKEWAATLPQERAEILEKAAQILEERRDEIVEWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 106 SLDTGKPIrhsLRDDIP-GAARA-LRWYAEAVDKLYGEVAPTD-NASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPAL 182
Cdd:cd07151 79 IRESGSTR---IKANIEwGAAMAiTREAATFPLRMEGRILPSDvPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 183 AAGNSVVLKPSEKSPLSA-LRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGEsNM 261
Cdd:cd07151 156 ALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGR-HL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 262 KRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTM 341
Cdd:cd07151 235 KKVALELGGNNPFVVLEDA-DIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 342 GTLIDDDHAASVRRYIELGQAQGATLWLDGRAQTHpaCIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLAND 421
Cdd:cd07151 314 GPLINESQVDGLLDKIEQAVEEGATLLVGGEAEGN--VLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAND 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 422 SDYGLGAAVWTRSLSRAHRMARRLKAGSVFINnyndgDMTV------PFGGYKQSGNGRDKSLHALEKFTELKtiWMSLE 495
Cdd:cd07151 392 TEYGLSGAVFTSDLERGVQFARRIDAGMTHIN-----DQPVndephvPFGGEKNSGLGRFNGEWALEEFTTDK--WISVQ 464
|
.
gi 1258251391 496 H 496
Cdd:cd07151 465 H 465
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
33-490 |
1.51e-114 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 347.67 E-value: 1.51e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 33 SGDTFSVLNPA-TGEPLAEVARGAKRDVDAAVASARAVFErgDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGK 111
Cdd:cd07124 44 TEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFP--TWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 112 PIRHSLrDDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLK 191
Cdd:cd07124 122 NWAEAD-ADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 192 PSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDA-----GESNMKRVWL 266
Cdd:cd07124 201 PAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAakvqpGQKWLKRVIA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 267 EAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLID 346
Cdd:cd07124 281 EMGGKNAIIVDEDA-DLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVID 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 347 DDHAASVRRYIELGQaQGATLWLDGRAQTHPA---CIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSD 423
Cdd:cd07124 360 KGARDRIRRYIEIGK-SEGRLLLGGEVLELAAegyFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTE 438
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1258251391 424 YGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDMtV---PFGGYKQSG-NGRDKSLHALEKFTELKTI 490
Cdd:cd07124 439 YGLTGGVFSRSPEHLERARREFEVGNLYANRKITGAL-VgrqPFGGFKMSGtGSKAGGPDYLLQFMQPKTV 508
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
39-492 |
3.99e-114 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 344.42 E-value: 3.99e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 39 VLNPATGEPLAEVARGAKRDVDAAVASARAVFERgdWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRHSLR 118
Cdd:cd07094 3 VHNPYDGEVIGKVPADDRADAEEALATARAGAEN--RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 119 DdIPGAARALRWYAEAVDKLYGEVAPTD-----NASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPS 193
Cdd:cd07094 81 E-VDRAIDTLRLAAEEAERIRGEEIPLDatqgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 194 EKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGesnMKRVWLEAGGKSA 273
Cdd:cd07094 160 SKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG---GKRIALELGGNAP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 274 NIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASV 353
Cdd:cd07094 237 VIVDRDA-DLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 354 RRYIELGQAQGATLWLDGRAQThpACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTR 433
Cdd:cd07094 316 ERWVEEAVEAGARLLCGGERDG--ALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTR 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 434 SLSRAHRMARRLKAGSVFINNYNDGDM-TVPFGGYKQSGNGRDKSLHALEKFTELKTIWM 492
Cdd:cd07094 394 DLNVAFKAAEKLEVGGVMVNDSSAFRTdWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
40-490 |
2.63e-112 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 339.97 E-value: 2.63e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 40 LNPATGEPLAEVARGAKRDVDAAVASARAVFErgDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPiRHSLRD 119
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQR--AWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKP-RADAGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 120 DIPGAARALRWYAEAVDKLYG-EVAPTDNAS---LAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEK 195
Cdd:cd07099 78 EVLLALEAIDWAARNAPRVLApRKVPTGLLMpnkKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 196 SPLSALRLAGLAREAGLPDGVLNVIPGFGhEAGQALSLHPdVDVMTFTGSTRTGKQLLKDAGEsNMKRVWLEAGGKSANI 275
Cdd:cd07099 158 TPLVGELLAEAWAAAGPPQGVLQVVTGDG-ATGAALIDAG-VDKVAFTGSVATGRKVMAAAAE-RLIPVVLELGGKDPMI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 276 VFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASVRR 355
Cdd:cd07099 235 VLADA-DLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 356 YIELGQAQGATLWLDG-RAQTHPACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRS 434
Cdd:cd07099 314 HVDDAVAKGAKALTGGaRSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1258251391 435 LSRAHRMARRLKAGSVFINN--YNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 490
Cdd:cd07099 394 LARAEAIARRLEAGAVSINDvlLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
59-491 |
1.11e-109 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 332.12 E-value: 1.11e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 59 VDAAVASARAVFErgDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRHSlRDDIPGAARALRWYAE-AVDK 137
Cdd:cd07100 1 IEAALDRAHAAFL--AWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA-RAEVEKCAWICRYYAEnAEAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 138 LYGEVAPTDnASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVL 217
Cdd:cd07100 78 LADEPIETD-AGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 218 NVIPGFGHEAGQALSlHPDVDVMTFTGSTRTGKQLLKDAGEsNMKRVWLEAGGKSANIVFADcPDLDQAAASAAAGIFYN 297
Cdd:cd07100 157 QNLLIDSDQVEAIIA-DPRVRGVTLTGSERAGRAVAAEAGK-NLKKSVLELGGSDPFIVLDD-ADLDKAVKTAVKGRLQN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 298 QGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASVRRYIELGQAQGATLWLDGRAQTHP 377
Cdd:cd07100 234 AGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 378 -ACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYN 456
Cdd:cd07100 314 gAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMV 393
|
410 420 430
....*....|....*....|....*....|....*
gi 1258251391 457 DGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIW 491
Cdd:cd07100 394 KSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVW 428
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
30-494 |
6.40e-109 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 333.38 E-value: 6.40e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 30 AAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVfeRGDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDT 109
Cdd:PRK09407 27 DGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA--QRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLET 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 110 GKPIRHSLrDDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIVREPVGVV---AAVVPWNFPLLLACWKLGPALAAGN 186
Cdd:PRK09407 105 GKARRHAF-EEVLDVALTARYYARRAPKLLAPRRRAGALPVLTKTTELRQPKgvvGVISPWNYPLTLAVSDAIPALLAGN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 187 SVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSlhPDVDVMTFTGSTRTGKQLLKDAGEsNMKRVWL 266
Cdd:PRK09407 184 AVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALV--DNADYLMFTGSTATGRVLAEQAGR-RLIGFSL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 267 EAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLID 346
Cdd:PRK09407 261 ELGGKNPMIVLDDA-DLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLIS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 347 DDHAASVRRYIELGQAQGATLWLDGRAQTH--PACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDY 424
Cdd:PRK09407 340 EAQLETVSAHVDDAVAKGATVLAGGKARPDlgPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPY 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 425 GLGAAVWTRSLSRAHRMARRLKAGSVfinNYNDG------DMTVPFGGYKQSGNGRDKSLHALEKFTELKTI----WMSL 494
Cdd:PRK09407 420 GLNASVWTGDTARGRAIAARIRAGTV---NVNEGyaaawgSVDAPMGGMKDSGLGRRHGAEGLLKYTESQTIatqrVLPL 496
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
21-490 |
1.30e-108 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 331.02 E-value: 1.30e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 21 RLFYQGDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFErgDWSQAAPAARKAVLMRLAALMEQHHEE 100
Cdd:cd07085 2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFP--AWSATPVLKRQQVMFKFRQLLEENLDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 101 LALLESLDTGKPIRHSlRDDIpgaARALrwyaEAVD-------KLYGEVapTDNASLAMIV---REPVGVVAAVVPWNFP 170
Cdd:cd07085 80 LARLITLEHGKTLADA-RGDV---LRGL----EVVEfacsiphLLKGEY--LENVARGIDTysyRQPLGVVAGITPFNFP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 171 LLLACWKLGPALAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGfGHEAGQALSLHPDVDVMTFTGSTRTGK 250
Cdd:cd07085 150 AMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 251 QLLKDAGESNmKRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFT 330
Cdd:cd07085 229 YIYERAAANG-KRVQALGGAKNHAVVMPDA-DLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 331 PGDPLDPQTTMGTLIDDDHAASVRRYIELGQAQGATLWLDGRAQTHPAC-----IGPTIFTDVDNQMRVAREEIFGPVLA 405
Cdd:cd07085 307 VGAGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYengnfVGPTILDNVTPDMKIYKEEIFGPVLS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 406 VTTFTGEEEALRLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINnyndgdMTVP-------FGGYKQSGNGrdkSL 478
Cdd:cd07085 387 IVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN------VPIPvplaffsFGGWKGSFFG---DL 457
|
490
....*....|....*..
gi 1258251391 479 HALEK-----FTELKTI 490
Cdd:cd07085 458 HFYGKdgvrfYTQTKTV 474
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
58-490 |
1.93e-108 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 329.15 E-value: 1.93e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 58 DVDAAVASARAVFErgDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPiRHSLRDDIPGAARALRWYAEAVDK 137
Cdd:cd07105 1 DADQAVEAAAAAFP--AWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGAT-AAWAGFNVDLAAGMLREAASLITQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 138 LYGEVAPTDNA-SLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGV 216
Cdd:cd07105 78 IIGGSIPSDKPgTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 217 LNVI---PGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGEsNMKRVWLEAGGKSANIVFADCpDLDQAAASAAAG 293
Cdd:cd07105 158 LNVVthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDA-DLDAAANAALFG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 294 IFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDpldpqTTMGTLIDDDHAASVRRYIELGQAQGATLWLDGRA 373
Cdd:cd07105 236 AFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 374 QTHP--ACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVF 451
Cdd:cd07105 311 DESPsgTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVH 390
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1258251391 452 INNYNDGD-MTVPFGGYKQSGNGRDKSLHALEKFTELKTI 490
Cdd:cd07105 391 INGMTVHDePTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
38-490 |
2.80e-107 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 327.01 E-value: 2.80e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 38 SVLNPATGEPLAEVARGAKRDVDAAVASARavferGDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRHSL 117
Cdd:cd07146 2 EVRNPYTGEVVGTVPAGTEEALREALALAA-----SYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 118 RDdIPGAARALRWYAEAVDKLYGEVAPTDNAS-----LAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKP 192
Cdd:cd07146 77 YE-VGRAADVLRFAAAEALRDDGESFSCDLTAngkarKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 193 SEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGesnMKRVWLEAGGKS 272
Cdd:cd07146 156 SEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG---YKRQLLELGGND 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 273 ANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAAS 352
Cdd:cd07146 233 PLIVMDDA-DLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 353 VRRYIELGQAQGATLWLDGRAQThpACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWT 432
Cdd:cd07146 312 IENRVEEAIAQGARVLLGNQRQG--ALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1258251391 433 RSLSRAHRMARRLKAGSVfinNYNDG----DMTVPFGGYKQSGNG-RDKSLHALEKFTELKTI 490
Cdd:cd07146 390 NDLDTIKRLVERLDVGTV---NVNEVpgfrSELSPFGGVKDSGLGgKEGVREAMKEMTNVKTY 449
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
45-494 |
1.66e-105 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 321.94 E-value: 1.66e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 45 GEPLAEVARGAKRDVDAAVASARAVfeRGDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKpIRHSLRDDIPGA 124
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAA--QRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGS-IRPKAGFEVGAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 125 ARALRWYAEAVDKLYGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPLSA-LRL 203
Cdd:cd07152 78 IGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 204 AGLAREAGLPDGVLNVIPGfGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGEsNMKRVWLEAGGKSANIVFADCpDL 283
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLDDA-DL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 284 DQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASVRRYIELGQAQ 363
Cdd:cd07152 235 DLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 364 GATLWLDGRAQThpACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSLSRAHRMAR 443
Cdd:cd07152 315 GARLEAGGTYDG--LFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALAD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1258251391 444 RLKAGSVFINnyndgDMTV------PFGGYKQSGNGRDKSLHA-LEKFTELKtiWMSL 494
Cdd:cd07152 393 RLRTGMLHIN-----DQTVndephnPFGGMGASGNGSRFGGPAnWEEFTQWQ--WVTV 443
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
23-490 |
1.04e-104 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 321.05 E-value: 1.04e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 23 FYQGDYRAAAsGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFerGDWsQAAPAARKA-VLMRLAALMEQHHEEL 101
Cdd:cd07086 2 VIGGEWVGSG-GETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAF--KEW-RKVPAPRRGeIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 102 ALLESLDTGKPIRHSLRDdipgaaralrwYAEAVD----------KLYGEVAPTDNASLAMI-VREPVGVVAAVVPWNFP 170
Cdd:cd07086 78 GRLVSLEMGKILPEGLGE-----------VQEMIDicdyavglsrMLYGLTIPSERPGHRLMeQWNPLGVVGVITAFNFP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 171 LLLACWKLGPALAAGNSVVLKPSEKSPLSALRLAGLAREA----GLPDGVLNVIPGFGhEAGQALSLHPDVDVMTFTGST 246
Cdd:cd07086 147 VAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGG-DGGELLVHDPRVPLVSFTGST 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 247 RTGKQLLKDAGESNmKRVWLEAGGKSANIVFaDCPDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHA 326
Cdd:cd07086 226 EVGRRVGETVARRF-GRVLLELGGNNAIIVM-DDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 327 QSFTPGDPLDPQTTMGTLIDDDHAASVRRYIELGQAQGATLWLDGRAQTH--PAC-IGPTIFTDVDNQMRVAREEIFGPV 403
Cdd:cd07086 304 KQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGgePGNyVEPTIVTGVTDDARIVQEETFAPI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 404 LAVTTFTGEEEALRLANDSDYGLGAAVWTRSLSRAHRM--ARRLKAGSVFINNYNDG-DMTVPFGGYKQSGNGRDKSLHA 480
Cdd:cd07086 384 LYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIPTSGaEIGGAFGGEKETGGGRESGSDA 463
|
490
....*....|
gi 1258251391 481 LEKFTELKTI 490
Cdd:cd07086 464 WKQYMRRSTC 473
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
37-488 |
4.29e-104 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 318.81 E-value: 4.29e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 37 FSVLNPATGEPLAEVARGAKRDVDAAVASARAVFERgdWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRHS 116
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRP--MRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 117 lRDDIPGAARALRWYAEAVDKLYGEVAPTDNAS-----LAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLK 191
Cdd:cd07147 79 -RGEVARAIDTFRIAAEEATRIYGEVLPLDISArgegrQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 192 PSEKSPLSALRLAGLAREAGLPDGVLNVIPgFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGEsnmKRVWLEAGGK 271
Cdd:cd07147 158 PASRTPLSALILGEVLAETGLPKGAFSVLP-CSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELGGN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 272 SANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAA 351
Cdd:cd07147 234 AAVIVDSDA-DLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 352 SVRRYIELGQAQGATLWLDGRaqTHPACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVW 431
Cdd:cd07147 313 RVEGWVNEAVDAGAKLLTGGK--RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 432 TRSLSRAHRMARRLKAGSVFINN---YNDGDMtvPFGGYKQSGNGRDKSLHALEKFTELK 488
Cdd:cd07147 391 TRDLEKALRAWDELEVGGVVINDvptFRVDHM--PYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
42-490 |
8.84e-102 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 312.71 E-value: 8.84e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 42 PATGEPLAEVARGAKRDVDAAVASARAVfeRGDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRHSLrDDI 121
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAA--QRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAF-EEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 122 PGAARALRWYAEAVDKLYGEVAPTDNASLAMIVREPVGVV---AAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPL 198
Cdd:cd07101 80 LDVAIVARYYARRAERLLKPRRRRGAIPVLTRTTVNRRPKgvvGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 199 SALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVdVMtFTGSTRTGKQLLKDAGEsNMKRVWLEAGGKSANIVFA 278
Cdd:cd07101 160 TALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNADY-VM-FTGSTATGRVVAERAGR-RLIGCSLELGGKNPMIVLE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 279 DCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASVRRYIE 358
Cdd:cd07101 237 DA-DLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 359 LGQAQGATLWLDGRAQTH--PACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSLS 436
Cdd:cd07101 316 DAVAKGATVLAGGRARPDlgPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 437 RAHRMARRLKAGSVfinNYNDG------DMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 490
Cdd:cd07101 396 RGRRIAARLRAGTV---NVNEGyaaawaSIDAPMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
33-490 |
4.18e-100 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 309.12 E-value: 4.18e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 33 SGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFeRGDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKP 112
Cdd:cd07082 14 SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAG-RGWWPTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 113 IRHSLRDDIPGAARaLRWYAEAVDKLYGEVAPTDNA-----SLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNS 187
Cdd:cd07082 93 LKDALKEVDRTIDY-IRDTIEELKRLDGDSLPGDWFpgtkgKIAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 188 VVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGesnMKRVWLE 267
Cdd:cd07082 172 VVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHP---MKRLVLE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 268 AGGKSANIVFADCpDLDQAAASAAAGIF-YNqGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLID 346
Cdd:cd07082 249 LGGKDPAIVLPDA-DLELAAKEIVKGALsYS-GQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLID 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 347 DDHAASVRRYIELGQAQGATLwLDGRAQTHPACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGL 426
Cdd:cd07082 327 PKSADFVEGLIDDAVAKGATV-LNGGGREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGL 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1258251391 427 GAAVWTRSLSRAHRMARRLKAGSVFINNYND-GDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 490
Cdd:cd07082 406 QASIFTKDINKARKLADALEVGTVNINSKCQrGPDHFPFLGRKDSGIGTQGIGDALRSMTRRKGI 470
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
40-490 |
1.56e-98 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 304.17 E-value: 1.56e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 40 LNPATGEPLAEVARGAKRDVDAAVASARAVFErgDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRHSlRD 119
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQK--GWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQA-GG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 120 DIPGAARALRWYAE-AVDKLYGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPL 198
Cdd:cd07102 78 EIRGMLERARYMISiAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 199 SALRLAGLAREAGLPDGVLNVIPGfGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGEsNMKRVWLEAGGKSANIVFA 278
Cdd:cd07102 158 CGERFAAAFAEAGLPEGVFQVLHL-SHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAG-RFIKVGLELGGKDPAYVRP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 279 DCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASVRRYIE 358
Cdd:cd07102 236 DA-DLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 359 LGQAQGATLWLDG----RAQTHPACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRS 434
Cdd:cd07102 315 DAIAKGARALIDGalfpEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKD 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1258251391 435 LSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 490
Cdd:cd07102 395 IARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
1-494 |
5.79e-98 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 303.75 E-value: 5.79e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 1 MEFHDLTYWQNKAarltiegrlFYQGDYRAAASGDTFSVLNPATGEPLAEVAR-GAKRDVDAAVASARAVFErgdWSQAA 79
Cdd:PRK11241 1 MQLNDSTLFRQQA---------LINGEWLDANNGEVIDVTNPANGDKLGSVPKmGADETRAAIDAANRALPA---WRALT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 80 PAARKAVLMRLAALMEQHHEELALLESLDTGKPIRHSlRDDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIV-REPV 158
Cdd:PRK11241 69 AKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEA-KGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIViKQPI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 159 GVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVD 238
Cdd:PRK11241 148 GVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 239 VMTFTGSTRTGKQLLKDAGEsNMKRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAF 318
Cdd:PRK11241 228 KLSFTGSTEIGRQLMEQCAK-DIKKVSLELGGNAPFIVFDDA-DLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 319 LARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASVRRYIELGQAQGATLWLDGRaqthPACIG-----PTIFTDVDNQMR 393
Cdd:PRK11241 306 AEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGK----AHELGgnffqPTILVDVPANAK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 394 VAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNG 473
Cdd:PRK11241 382 VAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLG 461
|
490 500
....*....|....*....|.
gi 1258251391 474 RDKSLHALEKFTELKTIWMSL 494
Cdd:PRK11241 462 REGSKYGIEDYLEIKYMCIGL 482
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
35-490 |
2.66e-88 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 279.90 E-value: 2.66e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 35 DTFSVLNPA-TGEPLAEVARGAKRDVDAAVASARAVFErgDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPI 113
Cdd:PRK03137 50 DKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFE--TWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPW 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 114 RHSLRDdipgaaralrwYAEAVDKL--YGEVAPTDNASLAMIVREPVGVVAAVVP---------WNFPLLLACWKLGPAL 182
Cdd:PRK03137 128 AEADAD-----------TAEAIDFLeyYARQMLKLADGKPVESRPGEHNRYFYIPlgvgvvispWNFPFAIMAGMTLAAI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 183 AAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDA-----G 257
Cdd:PRK03137 197 VAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYERAakvqpG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 258 ESNMKRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDP 337
Cdd:PRK03137 277 QIWLKRVIAEMGGKDAIVVDEDA-DLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDN 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 338 qTTMGTLIDDDHAASVRRYIELGQAQGATLWLDGRAQTHPACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALR 417
Cdd:PRK03137 356 -AYMGPVINQASFDKIMSYIEIGKEEGRLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALE 434
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1258251391 418 LANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDM--TVPFGGYKQSG-NGRDKSLHALEKFTELKTI 490
Cdd:PRK03137 435 IANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIvgYHPFGGFNMSGtDSKAGGPDYLLLFLQAKTV 510
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
40-490 |
2.66e-84 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 269.43 E-value: 2.66e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 40 LNPA-TGEPLAEVARGAKRDVDAAVASARAVFErgDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRHSlR 118
Cdd:TIGR01237 51 INPCdKSEVVGTVSKASQEHAEHALQAAAKAFE--AWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEA-D 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 119 DDIPGAARALRWYAEAVDKLYGEVAPTD-NASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSP 197
Cdd:TIGR01237 128 AEVAEAIDFMEYYARQMIELAKGKPVNSrEGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAP 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 198 LSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDA-----GESNMKRVWLEAGGKS 272
Cdd:TIGR01237 208 VIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAakvqpGQKHLKRVIAEMGGKD 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 273 ANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAAS 352
Cdd:TIGR01237 288 TVIVDEDA-DIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNK 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 353 VRRYIELGQAQGATLWLDGRAQTHPACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWT 432
Cdd:TIGR01237 367 IMEYIEIGKAEGRLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVIS 446
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1258251391 433 RSLSRAHRMARRLKAGSVFINNYNDGDMT--VPFGGYKQSGNG-RDKSLHALEKFTELKTI 490
Cdd:TIGR01237 447 NNRDHINRAKAEFEVGNLYFNRNITGAIVgyQPFGGFKMSGTDsKAGGPDYLALFMQAKTV 507
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
41-474 |
2.18e-83 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 265.70 E-value: 2.18e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 41 NPATGEPLAEVARGAKRDVDAAVASARAVFErgDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRHSLRDD 120
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQR--EWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 121 IPGAARALRWYAEavdklYGEVA--PTDNAS-------LAMIVREPVGVVAAVVPWNFPLLLAcwkLGPALAA---GNSV 188
Cdd:cd07098 80 ILVTCEKIRWTLK-----HGEKAlrPESRPGgllmfykRARVEYEPLGVVGAIVSWNYPFHNL---LGPIIAAlfaGNAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 189 VLKPSEKSPLSALRLAGLAREA----GLPDGVLNVIPGFGhEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGESnMKRV 264
Cdd:cd07098 152 VVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAES-LTPV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 265 WLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTL 344
Cdd:cd07098 230 VLELGGKDPAIVLDDA-DLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 345 IDDDHAASVRRYIELGQAQGATLWLDGRAQTHPACIG-----PTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLA 419
Cdd:cd07098 309 ISPARFDRLEELVADAVEKGARLLAGGKRYPHPEYPQghyfpPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIA 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1258251391 420 NDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDMTV--PFGGYKQSGNGR 474
Cdd:cd07098 389 NSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQqlPFGGVKGSGFGR 445
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
40-491 |
2.44e-80 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 257.36 E-value: 2.44e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 40 LNPATGEPLAEVARGAKRDVDAAVASARAVFErgDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRhSLRD 119
Cdd:PRK09406 6 INPATGETVKTFTALTDDEVDAAIARAHARFR--DYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLA-SAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 120 DIPGAARALRWYAEAVDKLYGEV---APTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKS 196
Cdd:PRK09406 83 EALKCAKGFRYYAEHAEALLADEpadAAAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 197 PLSALRLAGLAREAGLPDGVLNVIPgFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGESNMKRVwLEAGGKSANIV 276
Cdd:PRK09406 163 PQTALYLADLFRRAGFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTV-LELGGSDPFIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 277 FADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASVRRY 356
Cdd:PRK09406 241 MPSA-DLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 357 IELGQAQGATLWLDGRAQTHPACI-GPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSL 435
Cdd:PRK09406 320 VDDAVAAGATILCGGKRPDGPGWFyPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDE 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1258251391 436 SRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIW 491
Cdd:PRK09406 400 AEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVW 455
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
40-491 |
9.00e-80 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 256.33 E-value: 9.00e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 40 LNPATGEPLAEVARGAKRDVDAAVASARAVFERgdWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRHSlRD 119
Cdd:PRK13968 12 VNPATGEQLSVLPWAGADDIENALQLAAAGFRD--WRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQA-RA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 120 DIPGAARALRWYAE-AVDKLYGEVAPTDNASlAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPL 198
Cdd:PRK13968 89 EVAKSANLCDWYAEhGPAMLKAEPTLVENQQ-AVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 199 SALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSlHPDVDVMTFTGSTRTGKQLLKDAGESnMKRVWLEAGGKSANIVFA 278
Cdd:PRK13968 168 CAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIN-DSRIAAVTVTGSVRAGAAIGAQAGAA-LKKCVLELGGSDPFIVLN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 279 DCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASVRRYIE 358
Cdd:PRK13968 246 DA-DLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 359 LGQAQGATLWLDGRAQTHPA-CIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSLSR 437
Cdd:PRK13968 325 ATLAEGARLLLGGEKIAGAGnYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQ 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1258251391 438 AHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIW 491
Cdd:PRK13968 405 ARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTVW 458
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
87-492 |
9.72e-79 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 251.96 E-value: 9.72e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 87 LMRLAALMEQHHEELALLESLDTGKpIRHSLRDDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIV-REPVGVVAAVV 165
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGK-IQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLfKRALGVTTGIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 166 PWNFPLLLACWKLGPALAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGS 245
Cdd:PRK10090 80 PWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 246 TRTGKQLLkDAGESNMKRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAH 325
Cdd:PRK10090 160 VSAGEKIM-AAAAKNITKVCLELGGKAPAIVMDDA-DLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 326 AQSFTPGDPLD-PQTTMGTLIDDDHAASVRRYIELGQAQGATLWLDGRAQT-----HPacigPTIFTDVDNQMRVAREEI 399
Cdd:PRK10090 238 MQAVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEgkgyyYP----PTLLLDVRQEMSIMHEET 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 400 FGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDMTVPFGGYKQSGNGRDKSLH 479
Cdd:PRK10090 314 FGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKH 393
|
410
....*....|...
gi 1258251391 480 ALEKFTELKTIWM 492
Cdd:PRK10090 394 GLHEYLQTQVVYL 406
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
21-490 |
6.95e-77 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 249.03 E-value: 6.95e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 21 RLFYQGDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFErgDWSQAAPAARKAVLMRLAALMEQHHEE 100
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFL--TWGQTSLAQRTSVLLRYQALLKEHRDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 101 LALLESLDTGKPIRHSLRDdipgAARALRWYAEAVD---KLYGEVAP--TDNASLAMIvREPVGVVAAVVPWNFPLLLAC 175
Cdd:TIGR01722 80 IAELITAEHGKTHSDALGD----VARGLEVVEHACGvnsLLKGETSTqvATRVDVYSI-RQPLGVCAGITPFNFPAMIPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 176 WKLGPALAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGfGHEAGQALSLHPDVDVMTFTGSTRTGkQLLKD 255
Cdd:TIGR01722 155 WMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIG-RYIHT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 256 AGESNMKRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIA-GTRLLVEASikDAFLARVKAHAQSFTPGDP 334
Cdd:TIGR01722 233 TGSAHGKRVQALGGAKNHMVVMPDA-DKDAAADALVGAAYGAAGQRCMAiSAAVLVGAA--DEWVPEIRERAEKIRIGPG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 335 LDPQTTMGTLIDDDHAASVRRYIELGQAQGATLWLDGRAQT---HPA--CIGPTIFTDVDNQMRVAREEIFGPVLAVTTF 409
Cdd:TIGR01722 310 DDPGAEMGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKvdgYEEgnWVGPTLLERVPPTMKAYQEEIFGPVLCVLEA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 410 TGEEEALRLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNyndgDMTVP-----FGGYKQSGNGrdkSLHALEK- 483
Cdd:TIGR01722 390 DTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNV----PIPVPlpyfsFTGWKDSFFG---DHHIYGKq 462
|
490
....*....|.
gi 1258251391 484 ----FTELKTI 490
Cdd:TIGR01722 463 gthfYTRGKTV 473
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
39-473 |
7.86e-72 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 235.39 E-value: 7.86e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 39 VLNPATGEPLAEVARGAKRDVDAAVASARAVF-ERGDWsqAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPirhsL 117
Cdd:cd07148 3 VVNPFDLKPIGEVPTVDWAAIDKALDTAHALFlDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKP----L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 118 RDDIPGAARAL---RWYAEAVDKLYGEVAPTD--NAS---LAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVV 189
Cdd:cd07148 77 VDAKVEVTRAIdgvELAADELGQLGGREIPMGltPASagrIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 190 LKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGfGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGESNmkRVWLEAG 269
Cdd:cd07148 157 VKPALATPLSCLAFVDLLHEAGLPEGWCQAVPC-ENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPGT--RCALEHG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 270 GkSANIVFADCPDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDH 349
Cdd:cd07148 234 G-AAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPRE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 350 AASVRRYIELGQAQGATLwLDGRAQTHPACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAA 429
Cdd:cd07148 313 VDRVEEWVNEAVAAGARL-LCGGKRLSDTTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAA 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1258251391 430 VWTRSLSRAHRMARRLKAGSVFINnyndgDMT------VPFGGYKQSGNG 473
Cdd:cd07148 392 VFTKDLDVALKAVRRLDATAVMVN-----DHTafrvdwMPFAGRRQSGYG 436
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
33-490 |
1.75e-70 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 232.85 E-value: 1.75e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 33 SGDTFSVLNP-ATGEPLAEVARGAKRDVDAAVASARAVFerGDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGK 111
Cdd:cd07083 30 TKERMVSVSPfAPSEVVGTTAKADKAEAEAALEAAWAAF--KTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 112 PIRHSLrDDIPGAARALRWYAEAVDKLYG--EVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVV 189
Cdd:cd07083 108 NWVEAI-DDVAEAIDFIRYYARAALRLRYpaVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 190 LKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGE-----SNMKRV 264
Cdd:cd07083 187 AKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARlapgqTWFKRL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 265 WLEAGGKSANIVfADCPDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTL 344
Cdd:cd07083 267 YVETGGKNAIIV-DETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPV 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 345 IDDDHAASVRRYIELGQAQGATLWLDGRAQTHPACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEE--EALRLANDS 422
Cdd:cd07083 346 IDAEQEAKVLSYIEHGKNEGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANST 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1258251391 423 DYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDMT--VPFGGYKQSG-NGRDKSLHALEKFTELKTI 490
Cdd:cd07083 426 PYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVgvQPFGGFKLSGtNAKTGGPHYLRRFLEMKAV 496
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
29-473 |
1.38e-69 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 230.93 E-value: 1.38e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 29 RAAASGDTFSVLNPATGE-PLAEVARGAKRDVDAAVASARAVFERgdWSQAAPAARKAVLMRLAALMEQHHEELALLESL 107
Cdd:cd07125 40 EETETGEGAPVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAG--WSATPVEERAEILEKAADLLEANRGELIALAAA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 108 DTGKPIRHSLrDDIPGAARALRWYAEAVDKLYGEVA---PTDnaSLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAA 184
Cdd:cd07125 118 EAGKTLADAD-AEVREAIDFCRYYAAQARELFSDPElpgPTG--ELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 185 GNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGESNMKRV 264
Cdd:cd07125 195 GNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALAERDGPIL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 265 WL--EAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAgTRLL-VEASIKDAFLARVKAHAQSFTPGDPLDPQTTM 341
Cdd:cd07125 275 PLiaETGGKNAMIVDSTA-LPEQAVKDVVQSAFGSAGQRCSA-LRLLyLQEEIAERFIEMLKGAMASLKVGDPWDLSTDV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 342 GTLIDDDHAASVRRYIELGQAQGatlWLDGRAQTH---PACIGPTIFTDVDNqmRVAREEIFGPVLAVTTFTGE--EEAL 416
Cdd:cd07125 353 GPLIDKPAGKLLRAHTELMRGEA---WLIAPAPLDdgnGYFVAPGIIEIVGI--FDLTTEVFGPILHVIRFKAEdlDEAI 427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1258251391 417 RLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNyndgDMT---V---PFGGYKQSGNG 473
Cdd:cd07125 428 EDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINR----NITgaiVgrqPFGGWGLSGTG 486
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
22-474 |
3.25e-66 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 221.37 E-value: 3.25e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 22 LFYQGDYRAAaSGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFErgDWSQAAPAARKAVLMRLAALMEQHHEEL 101
Cdd:PRK09457 3 LWINGDWIAG-QGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFP--AWARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 102 ALLESLDTGKPIRHSL------------------------RDDIPGAARALRwyaeavDKLYGEVA---Ptdnaslamiv 154
Cdd:PRK09457 80 AEVIARETGKPLWEAAtevtaminkiaisiqayhertgekRSEMADGAAVLR------HRPHGVVAvfgP---------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 155 repvgvvaavvpWNFPLLLACWKLGPALAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGfGHEAGQALSLH 234
Cdd:PRK09457 144 ------------YNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAH 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 235 PDVDVMTFTGSTRTGKQLLKDAGESNMKRVWLEAGGKSAnIVFADCPDLDQAAASAAAGIFYNQGQACIAGTRLLVEASI 314
Cdd:PRK09457 211 PDIDGLLFTGSANTGYLLHRQFAGQPEKILALEMGGNNP-LVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 315 K-DAFLARVKAHAQSFTPGDPL-DPQTTMGTLIDDDHA----ASVRRYIELGqaqGATLWLDGRAQTHPACIGPTIFtDV 388
Cdd:PRK09457 290 QgDAFLARLVAVAKRLTVGRWDaEPQPFMGAVISEQAAqglvAAQAQLLALG---GKSLLEMTQLQAGTGLLTPGII-DV 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 389 DNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVfinNYND----GDMTVPF 464
Cdd:PRK09457 366 TGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIV---NWNKpltgASSAAPF 442
|
490
....*....|
gi 1258251391 465 GGYKQSGNGR 474
Cdd:PRK09457 443 GGVGASGNHR 452
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
58-474 |
1.36e-64 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 215.60 E-value: 1.36e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 58 DVDAAVASARAVFerGDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRHSLRDDIPGAAR---ALRWYAEA 134
Cdd:cd07095 1 QVDAAVAAARAAF--PGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKidiSIKAYHER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 135 VdklyGEVApTDNASLAMIVREPVGVVAAVVP-WNFPLLLACWKLGPALAAGNSVVLKPSEKSPLSALRLAGLAREAGLP 213
Cdd:cd07095 79 T----GERA-TPMAQGRAVLRHRPHGVMAVFGpFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 214 DGVLNVIPGfGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGESNMKRVWLEAGGKSANIVFADcPDLDQAAASAAAG 293
Cdd:cd07095 154 PGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDV-ADIDAAAYLIVQS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 294 IFYNQGQACIAGTRLLVEASIK-DAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAAsvrRYIELGQAQ---GATLWL 369
Cdd:cd07095 232 AFLTAGQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAA---RYLLAQQDLlalGGEPLL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 370 DGRA-QTHPACIGPTIFtDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSLSRAHRMARRLKAG 448
Cdd:cd07095 309 AMERlVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAG 387
|
410 420
....*....|....*....|....*..
gi 1258251391 449 SVFINNYNDG-DMTVPFGGYKQSGNGR 474
Cdd:cd07095 388 IVNWNRPTTGaSSTAPFGGVGLSGNHR 414
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
23-474 |
9.45e-62 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 208.99 E-value: 9.45e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 23 FYQGDYRAaaSGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFERgdWSQaAPAARKAVLMRL--AALMEqHHEE 100
Cdd:cd07130 2 VYDGEWGG--GGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKE--WRD-VPAPKRGEIVRQigDALRK-KKEA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 101 LALLESLDTGKPIRHSLRD-----DIPGAARAL-RwyaeavdKLYGEVAPTDNASLAMIvrepvgvvaavVPW------- 167
Cdd:cd07130 76 LGKLVSLEMGKILPEGLGEvqemiDICDFAVGLsR-------QLYGLTIPSERPGHRMM-----------EQWnplgvvg 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 168 -----NFPLLLACWKLGPALAAGNSVVLKPSEKSPLSALR----LAGLAREAGLPDGVLNVIPGfGHEAGQALSLHPDVD 238
Cdd:cd07130 138 vitafNFPVAVWGWNAAIALVCGNVVVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 239 VMTFTGSTRTGKQLLKDAGEsNMKRVWLEAGGKSANIVFaDCPDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAF 318
Cdd:cd07130 217 LVSFTGSTAVGRQVGQAVAA-RFGRSLLELGGNNAIIVM-EDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 319 LARVKAHAQSFTPGDPLDPQTTMGTLIDDdhaASVRRY---IELGQAQGATLWLDGRAQTHPAC-IGPTIFTdVDNQMRV 394
Cdd:cd07130 295 LERLKKAYKQVRIGDPLDDGTLVGPLHTK---AAVDNYlaaIEEAKSQGGTVLFGGKVIDGPGNyVEPTIVE-GLSDAPI 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 395 AREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSLSRAHR-MArrlKAGS-VFINNYNDG----DMTVPFGGYK 468
Cdd:cd07130 371 VKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRwLG---PKGSdCGIVNVNIGtsgaEIGGAFGGEK 447
|
....*.
gi 1258251391 469 QSGNGR 474
Cdd:cd07130 448 ETGGGR 453
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
21-495 |
1.27e-60 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 206.92 E-value: 1.27e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 21 RLFYQGDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFERgdWSQAAPAARKAVLMRLAALMEQHHEE 100
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKA--WAKTPLWKRAELLHKAAAILKEHKAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 101 LAllESLDtgKPIRHSLRDDIPGAARA---LRWYAEAVDKLYGE--------VAPTDNASLAMIVREPVGVVAAVVPWNF 169
Cdd:PLN00412 95 IA--ECLV--KEIAKPAKDAVTEVVRSgdlISYTAEEGVRILGEgkflvsdsFPGNERNKYCLTSKIPLGVVLAIPPFNY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 170 PLLLACWKLGPALAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTrTG 249
Cdd:PLN00412 171 PVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGD-TG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 250 KQLLKDAGesnMKRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSF 329
Cdd:PLN00412 250 IAISKKAG---MVPLQMELGGKDACIVLEDA-DLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 330 TPGDPLDpQTTMGTLIDDDHAASVRRYIELGQAQGATLWLDGRAQTHpaCIGPTIFTDVDNQMRVAREEIFGPVLAVTTF 409
Cdd:PLN00412 326 TVGPPED-DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKREGN--LIWPLLLDNVRPDMRIAWEEPFGPVLPVIRI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 410 TGEEEALRLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNY-NDGDMTVPFGGYKQSGNGRDKSLHALEKFTELK 488
Cdd:PLN00412 403 NSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSApARGPDHFPFQGLKDSGIGSQGITNSINMMTKVK 482
|
....*..
gi 1258251391 489 TIWMSLE 495
Cdd:PLN00412 483 STVINLP 489
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
60-490 |
6.74e-57 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 195.05 E-value: 6.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 60 DAAVASARAVFERGdwsQAAP-AARKAVLMRLAALMEQHHEEL--ALLEslDTGKP--------IrHSLRDDIPGAARAL 128
Cdd:cd07087 1 AELVARLRETFLTG---KTRSlEWRKAQLKALKRMLTENEEEIaaALYA--DLGKPpaeaylteI-AVVLGEIDHALKHL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 129 RWYAE----AVDKLYGEvaptdnASlAMIVREPVGVVAAVVPWNFPLLLAcwkLGP---ALAAGNSVVLKPSEKSPLSAL 201
Cdd:cd07087 75 KKWMKprrvSVPLLLQP------AK-AYVIPEPLGVVLIIGPWNYPLQLA---LAPligAIAAGNTVVLKPSELAPATSA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 202 RLAGLAREAgLPDGVLNVIPGFGHEAgQALSLHPdVDVMTFTGSTRTGKQLLKDAGEsNMKRVWLEAGGKSANIVFADCp 281
Cdd:cd07087 145 LLAKLIPKY-FDPEAVAVVEGGVEVA-TALLAEP-FDHIFFTGSPAVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDA- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 282 DLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDpQTTMGTLIDDDHAASVRRYIElgq 361
Cdd:cd07087 220 NLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKE-SPDYGRIINERHFDRLASLLD--- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 362 aqGATLWLDGRAQTHPACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSLSRAHRM 441
Cdd:cd07087 296 --DGKVVIGGQVDKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERV 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1258251391 442 ARRLKAGSVFInnyNDGDM-----TVPFGGYKQSGNGRDKSLHALEKFTELKTI 490
Cdd:cd07087 374 LAETSSGGVCV---NDVLLhaaipNLPFGGVGNSGMGAYHGKAGFDTFSHLKSV 424
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
67-474 |
1.35e-56 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 194.37 E-value: 1.35e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 67 RAVFE-----RGDWSQAAPAARKAVLMRLAALMEQHHEEL--ALLEslDTGKPIR-------HSLRDDIPGAARAL-RWY 131
Cdd:cd07134 1 RRVFAaqqahALALRASTAAERIAKLKRLKKAILARREEIiaALAA--DFRKPAAevdlteiLPVLSEINHAIKHLkKWM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 132 AEAvdklygEVAPTdnasLAM------IVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPLSALRLAG 205
Cdd:cd07134 79 KPK------RVRTP----LLLfgtkskIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 206 LAREAGLPDGVlNVIPGfGHEAGQALSLHPdVDVMTFTGSTRTGKQLLKDAGEsNMKRVWLEAGGKSANIVFADCpDLDQ 285
Cdd:cd07134 149 IIREAFDEDEV-AVFEG-DAEVAQALLELP-FDHIFFTGSPAVGKIVMAAAAK-HLASVTLELGGKSPTIVDETA-DLKK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 286 AAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTT-MGTLIDDDHAASVRRYIELGQAQG 364
Cdd:cd07134 224 AAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKASPdLARIVNDRHFDRLKGLLDDAVAKG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 365 ATLWLDGRAQTHPACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSLSRAHRMARR 444
Cdd:cd07134 304 AKVEFGGQFDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLAR 383
|
410 420 430
....*....|....*....|....*....|....
gi 1258251391 445 LKAGSVFINN----YNDGDMtvPFGGYKQSGNGR 474
Cdd:cd07134 384 TSSGGVVVNDvvlhFLNPNL--PFGGVNNSGIGS 415
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
26-490 |
7.46e-51 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 183.02 E-value: 7.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 26 GDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFERgdWSQAAPAARKAVLMRLAALMEQHHEELALLE 105
Cdd:PLN02419 120 GSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPL--WRNTPITTRQRVMLKFQELIRKNMDKLAMNI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 106 SLDTGKPIRHSLRDDIPGAARALRWYAEAVDKLyGEVAPT-DNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAA 184
Cdd:PLN02419 198 TTEQGKTLKDSHGDIFRGLEVVEHACGMATLQM-GEYLPNvSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTC 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 185 GNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGfGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGESNmKRV 264
Cdd:PLN02419 277 GNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHG-TNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKG-KRI 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 265 WLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIK---DAFLARVKahAQSFTPGDplDPQTTM 341
Cdd:PLN02419 355 QSNMGAKNHGLVLPDA-NIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKsweDKLVERAK--ALKVTCGS--EPDADL 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 342 GTLIDDDHAASVRRYIELGQAQGATLWLDGRAQTHPA-----CIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEAL 416
Cdd:PLN02419 430 GPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGyekgnFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAI 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 417 RLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNyndgDMTVPFGGYKQSGN----GRDKSLH---ALEKFTELKT 489
Cdd:PLN02419 510 SIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV----PIPVPLPFFSFTGNkasfAGDLNFYgkaGVDFFTQIKL 585
|
.
gi 1258251391 490 I 490
Cdd:PLN02419 586 V 586
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
167-474 |
6.44e-50 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 176.52 E-value: 6.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 167 WNFPLLLAcwkLGP---ALAAGNSVVLKPSEKSP-LSALrLAGLAREAGLPDgVLNVIPGfGHEAGQALSLHPdVDVMTF 242
Cdd:cd07133 111 WNYPLYLA---LGPliaALAAGNRVMIKPSEFTPrTSAL-LAELLAEYFDED-EVAVVTG-GADVAAAFSSLP-FDHLLF 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 243 TGSTRTGKQLLKDAGEsNMKRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARV 322
Cdd:cd07133 184 TGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDA-DLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAA 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 323 KAHAQSFTPGDPLDPQTTmgTLIDDDHAASVRRYIELGQAQGATLW-LDGRAQTHPAC--IGPTIFTDVDNQMRVAREEI 399
Cdd:cd07133 262 KAAVAKMYPTLADNPDYT--SIINERHYARLQGLLEDARAKGARVIeLNPAGEDFAATrkLPPTLVLNVTDDMRVMQEEI 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 400 FGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFInnyNDGDMTV-----PFGGYKQSGNGR 474
Cdd:cd07133 340 FGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTI---NDTLLHVaqddlPFGGVGASGMGA 416
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
57-490 |
5.40e-48 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 171.63 E-value: 5.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 57 RDVDAAVASARAVFERGdwsQAAPAA-RKAVLMRLAALMEQHHEELALLESLDTGKPIRHSLRDDIPGAARALRWYAEAV 135
Cdd:cd07135 5 DEIDSIHSRLRATFRSG---KTKDLEyRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 136 DKLYGEVAPTDNASLAM-----IVREPVGVVAAVVPWNFPLLLAcwkLGP---ALAAGNSVVLKPSEKSPLSALRLAGLA 207
Cdd:cd07135 82 KKWAKDEKVKDGPLAFMfgkprIRKEPLGVVLIIGPWNYPVLLA---LSPlvgAIAAGCTVVLKPSELTPHTAALLAELV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 208 REAgLPDGVLNVIPGFGHEAGQALSLHpdVDVMTFTGSTRTGKQLLKDAGEsNMKRVWLEAGGKSANIVFADCpDLDQAA 287
Cdd:cd07135 159 PKY-LDPDAFQVVQGGVPETTALLEQK--FDKIFYTGSGRVGRIIAEAAAK-HLTPVTLELGGKSPVIVTKNA-DLELAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 288 ASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPlDPQTTMGTLIDDDHAASVRRYIElgqAQGATL 367
Cdd:cd07135 234 KRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGA-NASPDYTRIVNPRHFNRLKSLLD---TTKGKV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 368 WLDGRAQTHPACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSLSRAHRMARRLKA 447
Cdd:cd07135 310 VIGGEMDEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRS 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1258251391 448 GSVFInnyNDGDM-----TVPFGGYKQSGNGRDKSLHALEKFTELKTI 490
Cdd:cd07135 390 GGVVI---NDTLIhvgvdNAPFGGVGDSGYGAYHGKYGFDTFTHERTV 434
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
29-488 |
5.60e-48 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 172.79 E-value: 5.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 29 RAAASGDTFSVLNPATGEPLAEVARGAKRD-VDAAVASARAVFErgDWSQAAPAARKAVLMRLAALMEQHHEELALLESL 107
Cdd:TIGR01238 45 SYKADGEAQPVTNPADRRDIVGQVFHANLAhVQAAIDSAQQAFP--TWNATPAKERAAKLDRLADLLELHMPELMALCVR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 108 DTGKPIRHSLrDDIPGAARALRWYAEAVDKLYGEVAPTDNASLAMIvrepvgvvaavVPWNFPLLLACWKLGPALAAGNS 187
Cdd:TIGR01238 123 EAGKTIHNAI-AEVREAVDFCRYYAKQVRDVLGEFSVESRGVFVCI-----------SPWNFPLAIFTGQISAALAAGNT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 188 VVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGESNMKRVWL- 266
Cdd:TIGR01238 191 VIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLi 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 267 -EAGGKSANIVfaDCPDL-DQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTL 344
Cdd:TIGR01238 271 aETGGQNAMIV--DSTALpEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPV 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 345 IDDDHAASVRRYIELGQAQGATLWL----DGRAQTHPACIGPTIFtDVDNqMRVAREEIFGPVLAVTTFTGEE--EALRL 418
Cdd:TIGR01238 349 IDAEAKQNLLAHIEHMSQTQKKIAQltldDSRACQHGTFVAPTLF-ELDD-IAELSEEVFGPVLHVVRYKAREldQIVDQ 426
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1258251391 419 ANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDM--TVPFGGYKQSGNG-RDKSLHALEKFTELK 488
Cdd:TIGR01238 427 INQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVvgVQPFGGQGLSGTGpKAGGPHYLYRLTQVQ 499
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
31-473 |
2.56e-45 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 170.43 E-value: 2.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 31 AASGDTFSVLNPA-TGEPLAEVARGAKRDVDAAVASARAVFErgDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDT 109
Cdd:PRK11905 563 DVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFP--EWSATPAAERAAILERAADLMEAHMPELFALAVREA 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 110 GKpirhSLRDDIPGAARA---LRWYAEAVDKLygeVAPTDNASLAMIVrepvgvvaAVVPWNFPLLLACWKLGPALAAGN 186
Cdd:PRK11905 641 GK----TLANAIAEVREAvdfLRYYAAQARRL---LNGPGHKPLGPVV--------CISPWNFPLAIFTGQIAAALVAGN 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 187 SVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTG----KQLLKDAGESnmk 262
Cdd:PRK11905 706 TVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVArliqRTLAKRSGPP--- 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 263 rVWL--EAGGKSANIVfaDCPDL-DQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQT 339
Cdd:PRK11905 783 -VPLiaETGGQNAMIV--DSSALpEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLST 859
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 340 TMGTLIDDDHAASVRRYIELGQAQGATLWldgRAQTHPAC-----IGPTIFtDVDNqMRVAREEIFGPVLAVTTFTGEE- 413
Cdd:PRK11905 860 DVGPVIDAEAQANIEAHIEAMRAAGRLVH---QLPLPAETekgtfVAPTLI-EIDS-ISDLEREVFGPVLHVVRFKADEl 934
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1258251391 414 EALRLA-NDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFIN-NyndgdmTV-------PFGGYKQSGNG 473
Cdd:PRK11905 935 DRVIDDiNATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNrN------IIgavvgvqPFGGEGLSGTG 997
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
167-490 |
9.79e-45 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 163.06 E-value: 9.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 167 WNFPLLLAcwkLGP---ALAAGNSVVLKPSEKSPLSALRLAGLAREAgLPDGVLNVIPGfGHEAGQALsLHPDVDVMTFT 243
Cdd:cd07136 110 WNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG-GVEENQEL-LDQKFDYIFFT 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 244 GSTRTGKQLLKDAGEsNMKRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVK 323
Cdd:cd07136 184 GSVRVGKIVMEAAAK-HLTPVTLELGGKSPCIVDEDA-NLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVKEKFIKELK 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 324 AHAQSFTPGDPLDpQTTMGTLIDDDHAASVRRYIElgqaqGATLWLDGRAQTHPACIGPTIFTDVDNQMRVAREEIFGPV 403
Cdd:cd07136 262 EEIKKFYGEDPLE-SPDYGRIINEKHFDRLAGLLD-----NGKIVFGGNTDRETLYIEPTILDNVTWDDPVMQEEIFGPI 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 404 LAVTTFTGEEEALRLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNyndgdmTV--------PFGGYKQSGNGRD 475
Cdd:cd07136 336 LPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIND------TImhlanpylPFGGVGNSGMGSY 409
|
330
....*....|....*
gi 1258251391 476 KSLHALEKFTELKTI 490
Cdd:cd07136 410 HGKYSFDTFSHKKSI 424
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
30-473 |
8.94e-44 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 165.88 E-value: 8.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 30 AAASGDTFSVLNPA-TGEPLAEVARGAKRDVDAAVASARAVFERgdWSQAAPAARKAVLMRLAALMEQHHEELALLESLD 108
Cdd:COG4230 565 EAASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPA--WSATPVEERAAILERAADLLEAHRAELMALLVRE 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 109 TGKPIRHSLrDDIPGAARALRWYAEAVDKLYGevAPTDNASLAMIVrepvgvvaAVVPWNFPL------LLAcwklgpAL 182
Cdd:COG4230 643 AGKTLPDAI-AEVREAVDFCRYYAAQARRLFA--APTVLRGRGVFV--------CISPWNFPLaiftgqVAA------AL 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 183 AAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVD-VMtFTGSTRTGK----QLLKDAG 257
Cdd:COG4230 706 AAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAgVA-FTGSTETARlinrTLAARDG 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 258 ESnmkrVWL--EAGGKSANIVfadcpD----LDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTP 331
Cdd:COG4230 785 PI----VPLiaETGGQNAMIV-----DssalPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRV 855
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 332 GDPLDPQTTMGTLIDDDHAASVRRYIELGQAQGATLWldgRAQTHPAC-----IGPTIFtDVDNqMRVAREEIFGPVLAV 406
Cdd:COG4230 856 GDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVH---QLPLPEECangtfVAPTLI-EIDS-ISDLEREVFGPVLHV 930
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1258251391 407 TTFTGEE-----EALrlaNDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNyndgDMT---V---PFGGYKQSGNG 473
Cdd:COG4230 931 VRYKADEldkviDAI---NATGYGLTLGVHSRIDETIDRVAARARVGNVYVNR----NIIgavVgvqPFGGEGLSGTG 1001
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
167-488 |
1.48e-43 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 160.58 E-value: 1.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 167 WNFPLLLACWKLGPALAAGNSVVLKPSEKSPLSALRLAGLAREAgLPDGVLNVIPGfGHEAGQALSLHPdVDVMTFTGST 246
Cdd:PTZ00381 119 WNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTELLKEP-FDHIFFTGSP 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 247 RTGKQLLKDAGEsNMKRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHA 326
Cdd:PTZ00381 196 RVGKLVMQAAAE-NLTPCTLELGGKSPVIVDKSC-NLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIEALKEAI 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 327 QSFTPGDPLDpQTTMGTLIDDDHAasvRRYIELGQAQGATLWLDGRAQTHPACIGPTIFTDVDNQMRVAREEIFGPVLAV 406
Cdd:PTZ00381 274 KEFFGEDPKK-SEDYSRIVNEFHT---KRLAELIKDHGGKVVYGGEVDIENKYVAPTIIVNPDLDSPLMQEEIFGPILPI 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 407 TTFTGEEEALRLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINN--YNDGDMTVPFGGYKQSGNGRDKSLHALEKF 484
Cdd:PTZ00381 350 LTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDcvFHLLNPNLPFGGVGNSGMGAYHGKYGFDTF 429
|
....
gi 1258251391 485 TELK 488
Cdd:PTZ00381 430 SHPK 433
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
32-473 |
3.35e-43 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 164.22 E-value: 3.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 32 ASGDTFSVLNPA-TGEPLAEVARGAKRDVDAAVASARAVFERgdWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTG 110
Cdd:PRK11904 559 GEGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPA--WSRTPVEERAAILERAADLLEANRAELIALCVREAG 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 111 KPIRHSLrDDIPGAARALRWYAEAVDKLYGE----VAPT--DNAslamIVREPVGVVAAVVPWNFPLLLACWKLGPALAA 184
Cdd:PRK11904 637 KTLQDAI-AEVREAVDFCRYYAAQARRLFGApeklPGPTgeSNE----LRLHGRGVFVCISPWNFPLAIFLGQVAAALAA 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 185 GNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGESNMKRV 264
Cdd:PRK11904 712 GNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTLAARDGPIV 791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 265 WL--EAGGKSANIVfaDCPDL-DQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTM 341
Cdd:PRK11904 792 PLiaETGGQNAMIV--DSTALpEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDV 869
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 342 GTLIDDDHAASVRRYIELGQAQGATLW-LDGRAQTHPAC-IGPTIFtDVDNqMRVAREEIFGPVLAVTTFTGEEEALRLA 419
Cdd:PRK11904 870 GPVIDAEAKANLDAHIERMKREARLLAqLPLPAGTENGHfVAPTAF-EIDS-ISQLEREVFGPILHVIRYKASDLDKVID 947
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1258251391 420 --NDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNyndgDMT---V---PFGGYKQSGNG 473
Cdd:PRK11904 948 aiNATGYGLTLGIHSRIEETADRIADRVRVGNVYVNR----NQIgavVgvqPFGGQGLSGTG 1005
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
33-490 |
7.24e-43 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 159.29 E-value: 7.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 33 SGDTFSVLNPAT-GEPLAEVARGAKRDVDAAVASARAVfeRGDWSQAAPAARKAVLMRLAALME-QHHEELALLESLDTG 110
Cdd:cd07123 44 TGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEA--RKEWARMPFEDRAAIFLKAADLLSgKYRYELNAATMLGQG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 111 KPIRHSLRDDIPGAARALRWYAEAVDKLYGE--VAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAaGNSV 188
Cdd:cd07123 122 KNVWQAEIDAACELIDFLRFNVKYAEELYAQqpLSSPAGVWNRLEYRPLEGFVYAVSPFNFTAIGGNLAGAPALM-GNVV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 189 VLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGES-----NMKR 263
Cdd:cd07123 201 LWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENldryrTYPR 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 264 VWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGT 343
Cdd:cd07123 281 IVGETGGKNFHLVHPSA-DVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGA 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 344 LIDDDHAASVRRYIELGQAQ-GATLWLDGRaqthpaC-------IGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGE--E 413
Cdd:cd07123 360 VIDEKAFDRIKGYIDHAKSDpEAEIIAGGK------CddsvgyfVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSdfE 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 414 EALRLAND-SDYGLGAAVW------TRSLSRAHRMArrlkAGSVFINNYNDGdmTV----PFGGYKQSG-NgrDK--SLH 479
Cdd:cd07123 434 ETLELVDTtSPYALTGAIFaqdrkaIREATDALRNA----AGNFYINDKPTG--AVvgqqPFGGARASGtN--DKagSPL 505
|
490
....*....|.
gi 1258251391 480 ALEKFTELKTI 490
Cdd:cd07123 506 NLLRWVSPRTI 516
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
30-473 |
3.84e-34 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 137.03 E-value: 3.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 30 AAASGDTFSVLNPA-TGEPLAEVARGAKRDVDAAVASARAVFERgdWSQAAPAARKAVLMRLAALMEQHHEELALLESLD 108
Cdd:PRK11809 654 PVAAGEMSPVINPAdPRDIVGYVREATPAEVEQALESAVNAAPI--WFATPPAERAAILERAADLMEAQMQTLMGLLVRE 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 109 TGKpirhslrdDIPGAARALRwyaEAVDKLY---GEVAPT-DNAS---LAMIVrepvgvvaAVVPWNFPLLLACWKLGPA 181
Cdd:PRK11809 732 AGK--------TFSNAIAEVR---EAVDFLRyyaGQVRDDfDNDThrpLGPVV--------CISPWNFPLAIFTGQVAAA 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 182 LAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGST-------RTGKQLLK 254
Cdd:PRK11809 793 LAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTevarllqRNLAGRLD 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 255 DAGesnmKRVWL--EAGGKSANIVfaDCPDL-DQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTP 331
Cdd:PRK11809 873 PQG----RPIPLiaETGGQNAMIV--DSSALtEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRM 946
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 332 GDPLDPQTTMGTLIDDDHAASVRRYIELGQAQGATLWLDGRAQT----HPACIGPTIFtDVDNQMRVAReEIFGPVLAVT 407
Cdd:PRK11809 947 GNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPVFQAARENSedwqSGTFVPPTLI-ELDSFDELKR-EVFGPVLHVV 1024
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 408 TFTGEE--EALRLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSVFINNYNDGDM--TVPFGGYKQSGNG 473
Cdd:PRK11809 1025 RYNRNQldELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVvgVQPFGGEGLSGTG 1094
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
61-488 |
4.06e-34 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 133.50 E-value: 4.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 61 AAVASARAVFERGdwsQAAPAA-RKAVLMRLAALMEQHHEELalLESL--DTGKPIRHSLRDDIPGAARALRwyaEAVDK 137
Cdd:cd07132 2 EAVRRAREAFSSG---KTRPLEfRIQQLEALLRMLEENEDEI--VEALakDLRKPKFEAVLSEILLVKNEIK---YAISN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 138 LYGEVAP----TDNASL---AMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPLSALRLAGLarea 210
Cdd:cd07132 74 LPEWMKPepvkKNLATLlddVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 211 gLPDGVLN----VIPGFGHEAGQALSLHpdVDVMTFTGSTRTGKQLLKDAGEsNMKRVWLEAGGKSANIVFADCpDLDQA 286
Cdd:cd07132 150 -IPKYLDKecypVVLGGVEETTELLKQR--FDYIFYTGSTSVGKIVMQAAAK-HLTPVTLELGGKSPCYVDKSC-DIDVA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 287 AASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTpGDplDPQTT--MGTLIDDDHAASVRRYIElgqaqG 364
Cdd:cd07132 225 ARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFY-GE--DPKESpdYGRIINDRHFQRLKKLLS-----G 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 365 ATLWLDGRAQTHPACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSLSRAHRMARR 444
Cdd:cd07132 297 GKVAIGGQTDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSN 376
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1258251391 445 LKAGSVFInnyNDGDM-----TVPFGGYKQSGNGRDKSLHALEKFTELK 488
Cdd:cd07132 377 TSSGGVCV---NDTIMhytldSLPFGGVGNSGMGAYHGKYSFDTFSHKR 422
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
63-490 |
8.37e-32 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 126.76 E-value: 8.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 63 VASARAVFERGdwsQAAPAA-RKAVLMRLAALMEQHHEEL--ALLEslDTGKPIRHSLRDDI----PGAARALR----WY 131
Cdd:cd07137 5 VRELRETFRSG---RTRSAEwRKSQLKGLLRLVDENEDDIfaALRQ--DLGKPSAESFRDEVsvlvSSCKLAIKelkkWM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 132 AEAVDKLYGEVAPtdnaSLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPLSALRLAGLArEAG 211
Cdd:cd07137 80 APEKVKTPLTTFP----AKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLI-PEY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 212 LPDGVLNVIPGfGHEAGQALsLHPDVDVMTFTGSTRTGKQLLKdAGESNMKRVWLEAGGKSANIVFADCpDLDQAAASAA 291
Cdd:cd07137 155 LDTKAIKVIEG-GVPETTAL-LEQKWDKIFFTGSPRVGRIIMA-AAAKHLTPVTLELGGKCPVIVDSTV-DLKVAVRRIA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 292 AGIF-YNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQtTMGTLIDDDHAASVRRYIELGQAQGATLWlD 370
Cdd:cd07137 231 GGKWgCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESK-DLSRIVNSHHFQRLSRLLDDPSVADKIVH-G 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 371 GRAQTHPACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSLSRAHRMARRLKAGSV 450
Cdd:cd07137 309 GERDEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGV 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1258251391 451 FINN-----YNDgdmTVPFGGYKQSGNGRDKSLHALEKFTELKTI 490
Cdd:cd07137 389 TFNDtvvqyAID---TLPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
59-473 |
2.35e-31 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 125.81 E-value: 2.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 59 VDAAVASARAVfeRGDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRhsLRDDIPGAARALRWYAEAVDKL 138
Cdd:cd07084 1 PERALLAADIS--TKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWM--FAENICGDQVQLRARAFVIYSY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 139 YGEVAPTDNASL-----AMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPLSALRLAGLAREAG-L 212
Cdd:cd07084 77 RIPHEPGNHLGQglkqqSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 213 PDGVLNVIPGFGHeAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGESnmkRVWLEAGGKSANIVFADCPDLDQAAASAAA 292
Cdd:cd07084 157 PPEDVTLINGDGK-TMQALLLHPNPKMVLFTGSSRVAEKLALDAKQA---RIYLELAGFNWKVLGPDAQAVDYVAWQCVQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 293 GIFYNQGQACIAGTRLLV-EASIKDAFLARVKAHAQSFTPGDpldpqTTMGTLIDDDHAASVrryIELGQAQGATLWLDG 371
Cdd:cd07084 233 DMTACSGQKCTAQSMLFVpENWSKTPLVEKLKALLARRKLED-----LLLGPVQTFTTLAMI---AHMENLLGSVLLFSG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 372 RAQTHP-------ACIGPTIFTDVDNQMRVAR---EEIFGPVLAVTTF--TGEEEALRLANDSDYGLGAAVWTRSLSRAH 439
Cdd:cd07084 305 KELKNHsipsiygACVASALFVPIDEILKTYElvtEEIFGPFAIVVEYkkDQLALVLELLERMHGSLTAAIYSNDPIFLQ 384
|
410 420 430
....*....|....*....|....*....|....*...
gi 1258251391 440 RMARRL-KAGSVFINNYNDGD---MTVPFGGYKQSGNG 473
Cdd:cd07084 385 ELIGNLwVAGRTYAILRGRTGvapNQNHGGGPAADPRG 422
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
32-475 |
1.99e-30 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 123.79 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 32 ASGDTFSVLNPATGEPLAEVARGAKRDVDAavaSARAVFE-RGDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTG 110
Cdd:PLN02315 31 ANGPLVSSVNPANNQPIAEVVEASLEDYEE---GLRACEEaAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 111 KPIrhslrddipgaARALRWYAEAVD----------KLYGEVAPTDNASLAMI-VREPVGVVAAVVPWNFPLLLACWKLG 179
Cdd:PLN02315 108 KIL-----------AEGIGEVQEIIDmcdfavglsrQLNGSIIPSERPNHMMMeVWNPLGIVGVITAFNFPCAVLGWNAC 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 180 PALAAGNSVVLKPSEKSPLSALRL----AGLAREAGLPDGVLNVIPGfGHEAGQALSLHPDVDVMTFTGSTRTGkQLLKD 255
Cdd:PLN02315 177 IALVCGNCVVWKGAPTTPLITIAMtklvAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVG-LMVQQ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 256 AGESNMKRVWLEAGGKSANIVFADCpDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLAR-VKAHAQSFTpGDP 334
Cdd:PLN02315 255 TVNARFGKCLLELSGNNAIIVMDDA-DIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQlLTVYKQVKI-GDP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 335 LDPQTTMGTLIDDDHAASVRRYIELGQAQGATLWLDGRA-QTHPACIGPTIfTDVDNQMRVAREEIFGPVLAVTTFTGEE 413
Cdd:PLN02315 333 LEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAiESEGNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLE 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1258251391 414 EALRLANDSDYGLGAAVWTRSLSRAHRMARRLKA--GSVFIN-NYNDGDMTVPFGGYKQSGNGRD 475
Cdd:PLN02315 412 EAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSdcGIVNVNiPTNGAEIGGAFGGEKATGGGRE 476
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
54-490 |
1.12e-29 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 121.37 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 54 GAKRDVDAAVASARAVFERGDWSQAApaARKAVLMRLAALMEQHHEEL--ALLEslDTGKPIRHSLRDDIPGAARALRWY 131
Cdd:PLN02203 3 APGETLEGSVAELRETYESGRTRSLE--WRKSQLKGLLRLLKDNEEAIfkALHQ--DLGKHRVEAYRDEVGVLTKSANLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 132 AEAVDKLygevAPTDNASL--------AMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPLSALRL 203
Cdd:PLN02203 79 LSNLKKW----MAPKKAKLplvafpatAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 204 AGlAREAGLPDGVLNVIPGfGHEAGQALSLHPdVDVMTFTGSTRTGKQLLKDAGEsNMKRVWLEAGGKSANIVfaDCPDL 283
Cdd:PLN02203 155 AA-NIPKYLDSKAVKVIEG-GPAVGEQLLQHK-WDKIFFTGSPRVGRIIMTAAAK-HLTPVALELGGKCPCIV--DSLSS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 284 DQAAASAAAGIFYNQ-----GQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQtTMGTLIDDDHAASVRRYIE 358
Cdd:PLN02203 229 SRDTKVAVNRIVGGKwgscaGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESK-SMARILNKKHFQRLSNLLK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 359 LGQAQGATLWlDGRAQTHPACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSLSRA 438
Cdd:PLN02203 308 DPRVAASIVH-GGSIDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLK 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1258251391 439 HRMARRLKAGSVfinNYND-----GDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 490
Cdd:PLN02203 387 RRILSETSSGSV---TFNDaiiqyACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAV 440
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
54-490 |
2.54e-26 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 111.68 E-value: 2.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 54 GAKRDVDAAVASARAVFERGDWSQAAPAARKAVLMRLAALM---EQHHEELALLESLDTGKPIRHS-------LRDDIPG 123
Cdd:PLN02174 2 AAKKMFGAADASILVTELRRSFDDGVTRGYEWRVTQLKKLMiicDNHEPEIVAALRDDLGKPELESsvyevslLRNSIKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 124 AARALR-WYAEAVDKLYGEVAPTDnaslAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPLSALR 202
Cdd:PLN02174 82 ALKQLKnWMAPEKAKTSLTTFPAS----AEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 203 LAGLArEAGLPDGVLNVIPGFGHEAgQALsLHPDVDVMTFTGSTRTGKQLLKDAGEsNMKRVWLEAGGKSANIVFADCpD 282
Cdd:PLN02174 158 LAKLL-EQYLDSSAVRVVEGAVTET-TAL-LEQKWDKIFYTGSSKIGRVIMAAAAK-HLTPVVLELGGKSPVVVDSDT-D 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 283 LDQAAASAAAGIF-YNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQtTMGTLIDDDHAASVRRYIELGQ 361
Cdd:PLN02174 233 LKVTVRRIIAGKWgCNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESK-DMSRIVNSTHFDRLSKLLDEKE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 362 AQGATLWlDGRAQTHPACIGPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWTRSLSRAHRM 441
Cdd:PLN02174 312 VSDKIVY-GGEKDRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERF 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1258251391 442 ARRLKAGSVFINN--YNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 490
Cdd:PLN02174 391 AATVSAGGIVVNDiaVHLALHTLPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
31-432 |
4.75e-24 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 105.17 E-value: 4.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 31 AASGDTFSVLNPATGEPLAEV-ARGAkrDVDAAVASARavfERGDWSQAAP--AARKAVLMRLAALMEQHHEELALLESL 107
Cdd:PRK11903 15 AGSGAGTPLFDPVTGEELVRVsATGL--DLAAAFAFAR---EQGGAALRALtyAQRAALLAAIVKVLQANRDAYYDIATA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 108 DTGKpIRHSLRDDIPGAARALRWYAEAVDKLyGEVAPTDNASLAMIVREPVGVVAAVV-----------PWNFPLLLACW 176
Cdd:PRK11903 90 NSGT-TRNDSAVDIDGGIFTLGYYAKLGAAL-GDARLLRDGEAVQLGKDPAFQGQHVLvptrgvalfinAFNFPAWGLWE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 177 KLGPALAAGNSVVLKPSEKSPLSALRLAGLAREAG-LPDGVLNVIPGFGheAGQALSLHPdVDVMTFTGSTRTGKQL-LK 254
Cdd:PRK11903 168 KAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSS--AGLLDHLQP-FDVVSFTGSAETAAVLrSH 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 255 DAGESNMKRVWLEAGGKSANIVFAD----CPDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFT 330
Cdd:PRK11903 245 PAVVQRSVRVNVEADSLNSALLGPDaapgSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTT 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 331 PGDPLDPQTTMGTLIDDDHAASVRRYIELGQAQgATLWLDGRAQ----THPA---CIGPTIF--TDVDNQMRVAREEIFG 401
Cdd:PRK11903 325 VGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQ-AEVLFDGGGFalvdADPAvaaCVGPTLLgaSDPDAATAVHDVEVFG 403
|
410 420 430
....*....|....*....|....*....|.
gi 1258251391 402 PVLAVTTFTGEEEALRLANDSDYGLGAAVWT 432
Cdd:PRK11903 404 PVATLLPYRDAAHALALARRGQGSLVASVYS 434
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
23-432 |
5.45e-22 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 98.88 E-value: 5.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 23 FYQGDYRAAaSGDTFSVLNPATGEPLAEVaRGAKRDVDAAVASARAVfergdwsqAAPAARK-------AVLMRLAALME 95
Cdd:cd07128 4 YVAGQWHAG-TGDGRTLHDAVTGEVVARV-SSEGLDFAAAVAYAREK--------GGPALRAltfheraAMLKALAKYLM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 96 QHHEELALLeSLDTGKPIRHSLRDdIPGAARALRWYAEAVDKLY--------GEVAP-TDNASLA--MIVREPVGVVAAV 164
Cdd:cd07128 74 ERKEDLYAL-SAATGATRRDSWID-IDGGIGTLFAYASLGRRELpnahflveGDVEPlSKDGTFVgqHILTPRRGVAVHI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 165 VPWNFPlllaCW----KLGPALAAGNSVVLKPSEKSPLSALRLAGLAREAG-LPDGVLNVIPG-----FGHEAGQalslh 234
Cdd:cd07128 152 NAFNFP----VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGsvgdlLDHLGEQ----- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 235 pdvDVMTFTGSTRTGKQL-LKDAGESNMKRVWLEAGGKSANIVFADC----PDLDQAAASAAAGIFYNQGQACIAGTRLL 309
Cdd:cd07128 223 ---DVVAFTGSAATAAKLrAHPNIVARSIRFNAEADSLNAAILGPDAtpgtPEFDLFVKEVAREMTVKAGQKCTAIRRAF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 310 VEASIKDAFLARVKAHAQSFTPGDPLDPQTTMGTLIDDDHAASVRRYIELgQAQGATLWLDGRAQTHP--------ACIG 381
Cdd:cd07128 300 VPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVAT-LLAEAEVVFGGPDRFEVvgadaekgAFFP 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1258251391 382 PTIFT--DVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGLGAAVWT 432
Cdd:cd07128 379 PTLLLcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVT 431
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
59-453 |
1.43e-18 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 87.98 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 59 VDAAVASARAVFErgDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRH----------SLRddipGAARAL 128
Cdd:cd07129 1 VDAAAAAAAAAFE--SYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARlqgelgrttgQLR----LFADLV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 129 R---WYAEAVD---------------KLYGEVAPTDN--ASlamivrepvgvvaavvpwNFPLllACWKLG----PALAA 184
Cdd:cd07129 75 RegsWLDARIDpadpdrqplprpdlrRMLVPLGPVAVfgAS------------------NFPL--AFSVAGgdtaSALAA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 185 GNSVVLKPSEKSPLSALRLAGLAREA----GLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKqLLKDAGEsn 260
Cdd:cd07129 135 GCPVVVKAHPAHPGTSELVARAIRAAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGR-ALFDAAA-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 261 mKR-----VWLEAGgkSANIVF----ADCPDLDQAAASAAAGIFYNQGQACIA-GTRLLVEASIKDAFLARVKAHAQSFT 330
Cdd:cd07129 212 -ARpepipFYAELG--SVNPVFilpgALAERGEAIAQGFVGSLTLGAGQFCTNpGLVLVPAGPAGDAFIAALAEALAAAP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 331 PGDPLDPQttmgtlIDDDHAASVRRyieLGQAQGATLWLDGRAQTHPACIGPTIF-TDVDNQMR--VAREEIFGPVLAVT 407
Cdd:cd07129 289 AQTMLTPG------IAEAYRQGVEA---LAAAPGVRVLAGGAAAEGGNQAAPTLFkVDAAAFLAdpALQEEVFGPASLVV 359
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1258251391 408 TFTGEEEALRLANDSDYGLGAAVW--TRSLSRAHRMARRL--KAGSVFIN 453
Cdd:cd07129 360 RYDDAAELLAVAEALEGQLTATIHgeEDDLALARELLPVLerKAGRLLFN 409
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
58-453 |
5.94e-12 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 67.89 E-value: 5.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 58 DVDAAVASARAVFErgDWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTGKPIRHSLRddiPGAARALRWYAEAVDK 137
Cdd:cd07127 85 DPDALLAAARAAMP--GWRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMMAFQ---AGGPHAQDRGLEAVAY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 138 LYGEVAPTDNASLAMIVREPVGVVAAVVPWN-----FPLLLAC-----WKLGP----ALAAGNSVVLKPSEKSPLSALRL 203
Cdd:cd07127 160 AWREMSRIPPTAEWEKPQGKHDPLAMEKTFTvvprgVALVIGCstfptWNGYPglfaSLATGNPVIVKPHPAAILPLAIT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 204 AGLAR----EAGL-PDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGSTRTGKQLLKDAGEsnmKRVWLEAGGKSaNIVFA 278
Cdd:cd07127 240 VQVARevlaEAGFdPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQ---AQVYTEKAGVN-TVVVD 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 279 DCPDLDQAAASAAAGIFYNQGQACIAGTRLLVEAS-IK--------DAFLARVKAHAQSFTpGDPLDPQTTMGTLIDDDH 349
Cdd:cd07127 316 STDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRDgIQtddgrksfDEVAADLAAAIDGLL-ADPARAAALLGAIQSPDT 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 350 AASVRRyielgQAQGATLWLDGRAQTHPACIGPTIFT------DVDNQMRVArEEIFGPVLAVTTFTGEEEALRLANDSD 423
Cdd:cd07127 395 LARIAE-----ARQLGEVLLASEAVAHPEFPDARVRTplllklDASDEAAYA-EERFGPIAFVVATDSTDHSIELARESV 468
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1258251391 424 YGLGA---AVWTRS---LSRAHRMARRLKA-------GSVFIN 453
Cdd:cd07127 469 REHGAmtvGVYSTDpevVERVQEAALDAGValsinltGGVFVN 511
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
167-418 |
5.56e-09 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 58.28 E-value: 5.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 167 WNFPLLLACWKLGPALAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVLNVIPGFGHEAGQALsLHPDVDVMTFTGST 246
Cdd:cd07126 152 FNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKIL-LEANPRMTLFTGSS 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 247 RTGKQLLKDagesnMK-RVWLEAGGKSANIVFADCPDLDQAAASAAAGIFYNQGQACIAGTRLLV-EASIKDAFLARVKA 324
Cdd:cd07126 231 KVAERLALE-----LHgKVKLEDAGFDWKILGPDVSDVDYVAWQCDQDAYACSGQKCSAQSILFAhENWVQAGILDKLKA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 325 HA-----QSFTPGdpldPQTTMGTLIDDDHAASvrryieLGQAQGATLWLDGRA---QTHPACIG---PT-IF-----TD 387
Cdd:cd07126 306 LAeqrklEDLTIG----PVLTWTTERILDHVDK------LLAIPGAKVLFGGKPltnHSIPSIYGayePTaVFvpleeIA 375
|
250 260 270
....*....|....*....|....*....|.
gi 1258251391 388 VDNQMRVAREEIFGPVLAVTTFTGEEEALRL 418
Cdd:cd07126 376 IEENFELVTTEVFGPFQVVTEYKDEQLPLVL 406
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
39-454 |
9.22e-09 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 57.60 E-value: 9.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 39 VLNPATGEPLAEVAR-GAKRDVDAAVASARAVFERgdWSQAAPAARKAVL--MRLAALmeQHHEELALLESLDTG----- 110
Cdd:PRK15398 17 MLSSQTVSPPAAVGEmGVFASVDDAVAAAKVAQQR--YQQKSLAMRQRIIdaIREALL--PHAEELAELAVEETGmgrve 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 111 -KPIRHSLR-DDIPGaARALRWYAEAVDK---LY--------GEVAPTDNASLAMIvrepvgvvaavvpwnfplllaCWK 177
Cdd:PRK15398 93 dKIAKNVAAaEKTPG-VEDLTTEALTGDNgltLIeyapfgviGAVTPSTNPTETII---------------------NNA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 178 LGpALAAGNSVVLKPSEKSPLSALRLAGL----AREAGLPDGVLNVI--PGFghEAGQALSLHPDVDVMTFTGstrtGKQ 251
Cdd:PRK15398 151 IS-MLAAGNSVVFSPHPGAKKVSLRAIELlneaIVAAGGPENLVVTVaePTI--ETAQRLMKHPGIALLVVTG----GPA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 252 LLKDAGESNmKRVwLEAGGKSANIVFADCPDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLAR-VKAHAQSFT 330
Cdd:PRK15398 224 VVKAAMKSG-KKA-IGAGAGNPPVVVDETADIEKAARDIVKGASFDNNLPCIAEKEVIVVDSVADELMRLmEKNGAVLLT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 331 PGdplDPQTTMGTLIDDDHAASvRRYIelgqAQGATLWLDG---RAQTHPACigptIFTDVDNQMRVAREEIFGPVLAVT 407
Cdd:PRK15398 302 AE---QAEKLQKVVLKNGGTVN-KKWV----GKDAAKILEAagiNVPKDTRL----LIVETDANHPFVVTELMMPVLPVV 369
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1258251391 408 TFTGEEEALRLANDSDYGL--GAAVWTRSLSRAHRMARRLKAgSVFINN 454
Cdd:PRK15398 370 RVKDVDEAIALAVKLEHGNrhTAIMHSRNVDNLNKMARAIQT-SIFVKN 417
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
54-454 |
7.29e-08 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 54.55 E-value: 7.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 54 GAKRDVDAAVASARAVFERgdWSQAAPAARKAVL--MRLAALMeqHHEELALLESLDTG------KPIRHSLRDDIPGAA 125
Cdd:cd07121 1 GVFATVDDAVAAAKAAQKQ--YRKCTLADREKIIeaIREALLS--NAEELAEMAVEETGmgrvedKIAKNHLAAEKTPGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 126 RALRWYAEAVDK---LY--------GEVAPTDNASLAMIvrepvgvvaavvpwnfplllaCWKLGpALAAGNSVVLKP-- 192
Cdd:cd07121 77 EDLTTTAWSGDNgltLVeyapfgviGAITPSTNPTETII---------------------NNSIS-MLAAGNAVVFNPhp 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 193 -SEKSPLSALRLAGLA-REAGLPDGVLNVI--PGFghEAGQALSLHPDVDVMTFTGSTRTGKQLLKdAGesnmKRVwLEA 268
Cdd:cd07121 135 gAKKVSAYAVELINKAiAEAGGPDNLVVTVeePTI--ETTNELMAHPDINLLVVTGGPAVVKAALS-SG----KKA-IGA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 269 GGKSANIVFADCPDLDQAAASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLDPQTTMgTLIDDD 348
Cdd:cd07121 207 GAGNPPVVVDETADIEKAARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAAMQRNGAYVLNDEQAEQLLEV-VLLTNK 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 349 HAASVRRYIelgqAQGATLWLDGRAQTHPACIgPTIFTDVDNQMRVAREEIFGPVLAVTTFTGEEEALRLANDSDYGL-- 426
Cdd:cd07121 286 GATPNKKWV----GKDASKILKAAGIEVPADI-RLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrh 360
|
410 420
....*....|....*....|....*...
gi 1258251391 427 GAAVWTRSLSRAHRMARRLKAgSVFINN 454
Cdd:cd07121 361 TAIIHSKNVENLTKMARAMQT-TIFVKN 387
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
181-453 |
7.38e-06 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 48.26 E-value: 7.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 181 ALAAGNSVVLKPSEKSPLSALRLAGL----AREAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGstrtGKQLLKDA 256
Cdd:cd07122 119 ALKTRNAIIFSPHPRAKKCSIEAAKImreaAVAAGAPEGLIQWIEEPSIELTQELMKHPDVDLILATG----GPGMVKAA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 257 ----------GESNMKrVWLEaggKSANIVFA----------DCpdldqaaasaaagifynqGQACIAGTRLLVEASIKD 316
Cdd:cd07122 195 yssgkpaigvGPGNVP-AYID---ETADIKRAvkdiilsktfDN------------------GTICASEQSVIVDDEIYD 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 317 AFLARVKAHAqsftpgdpldpqttmGTLIDDDHAASVRRYielgqaqgatLWLDGRAQThPACIG---PTI--------- 384
Cdd:cd07122 253 EVRAELKRRG---------------AYFLNEEEKEKLEKA----------LFDDGGTLN-PDIVGksaQKIaelagievp 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 385 ---------FTDVDNQMRVAREEIFgPVLAVTTFTGEEEALRLAND--SDYGLG--AAVWTRSLSRAHRMARRLKAGSVF 451
Cdd:cd07122 307 edtkvlvaeETGVGPEEPLSREKLS-PVLAFYRAEDFEEALEKAREllEYGGAGhtAVIHSNDEEVIEEFALRMPVSRIL 385
|
..
gi 1258251391 452 IN 453
Cdd:cd07122 386 VN 387
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
80-325 |
1.03e-05 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 47.60 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 80 PAARKAVLMRLAALMEQHHEELALLESLDTGKPIRhslRDDIPGAARALRwyaeAVDKLYGEVAPTDN--ASLAMIVREP 157
Cdd:cd07077 15 DEQRDLIINAIANALYDTRQRLASEAVSERGAYIR---SLIANWIAMMGC----SESKLYKNIDTERGitASVGHIQDVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 158 VGVVAAVVPWNFPL------------LLACWKLGPALAAGNSVVLKPSEKSPLSALRLAGLAREA---GLPDGVLNVIPG 222
Cdd:cd07077 88 LPDNGETYVRAFPIgvtmhilpstnpLSGITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAAdaaHGPKILVLYVPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 223 FGHEAGQALSLHPDVDVMTFTGstrtGKQLLKDA-GESNMKRVwLEAGGKSANIVFADCPDLDQAAASAAAGIFYNQgQA 301
Cdd:cd07077 168 PSDELAEELLSHPKIDLIVATG----GRDAVDAAvKHSPHIPV-IGFGAGNSPVVVDETADEERASGSVHDSKFFDQ-NA 241
|
250 260
....*....|....*....|....
gi 1258251391 302 CIAGTRLLVEASIKDAFLARVKAH 325
Cdd:cd07077 242 CASEQNLYVVDDVLDPLYEEFKLK 265
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
59-453 |
9.11e-04 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 41.48 E-value: 9.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 59 VDAAVASARaVFERGdWSQAAPAARKAVLMRLAALMEQHHEELALLESLDTG------KPIR-HSLRDDIPGAARalrwy 131
Cdd:cd07081 1 LDDAVAAAK-VAQQG-LSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGmgrvedKVIKnHFAAEYIYNVYK----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 132 aeavDKLYGEVAPTDNASLAMIVREPVGVVAAVVPWNFPLLLACWKLGPALAAGNSVVLKPSEKSPLSALRLAGL----A 207
Cdd:cd07081 74 ----DEKTCGVLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLllqaA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 208 REAGLPDGVLNVIPGFGHEAGQALSLHPDVDVMTFTGstrtGKQLLKdAGESNMKRVwLEAGGKSANIVFADCPDLDQAA 287
Cdd:cd07081 150 VAAGAPENLIGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVK-AAYSSGKPA-IGVGAGNTPVVIDETADIKRAV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 288 ASAAAGIFYNQGQACIAGTRLLVEASIKDAFLARVKAHAQSFTPGDPLdpQTTMGTLIDDdhaASVRRYIeLGQAQGATL 367
Cdd:cd07081 224 QSIVKSKTFDNGVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEEL--QQVQPVILKN---GDVNRDI-VGQDAYKIA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 368 WLDGRA--QTHPACIGPTifTDVDNQMRVAREEIfGPVLAVTTF----TGEEEALRLANDSDYGLGAAVWTRSLS---RA 438
Cdd:cd07081 298 AAAGLKvpQETRILIGEV--TSLAEHEPFAHEKL-SPVLAMYRAanfaDADAKALALKLEGGCGHTSAMYSDNIKaieNM 374
|
410
....*....|....*
gi 1258251391 439 HRMARRLKAGSVFIN 453
Cdd:cd07081 375 NQFANAMKTSRFVKN 389
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
26-217 |
6.79e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 39.38 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 26 GDYRAAASGDTFSVLNPATGEPLAEVARGAKRDVDAAVASARAVFER-----------GDWSQAAPAARKAVLMRLAALM 94
Cdd:PHA03307 608 ADTGAGAAAPAPAAPRPDAAAAGGASARPLRELADACVLACRAVLEAllegpdglsavPGLAFPRPACPPRALEACPARL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1258251391 95 EQHHEELALLESLDTGKPIRHSLRDdiPGAARALRWYAEAVDKLYGEVAPtdnaslaMIVREPVGVVAAVVPWNFP-LLL 173
Cdd:PHA03307 688 ESWLRELRDLRDAVYLARLRGDLPV--AGGREERVAAVRAVSLVARTVAP-------LVRYSPRRARARASAWDITdALF 758
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1258251391 174 ACWKLGPALAAGNSVVLKPSEKSPLSALRLAGLAREAGLPDGVL 217
Cdd:PHA03307 759 SNPSLVPAKLAEALALLEPAEPQRGAGSSPPVRAEAAFRRPGRL 802
|
|
| |
