|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
55-423 |
0e+00 |
|
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: 690.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 55 ADTLQRLREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESEVSEIHISQSEIDLALRNLRSWMKD 134
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 135 EKVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRYLDQSCFA 214
Cdd:cd07132 81 EPVKKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 215 VVLGGPQETGQLLEHKFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTC 294
Cdd:cd07132 161 VVLGGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 295 VAPDYVLCSPHTRERLLPALQSAITRFYGEDPRRSPSLGRVVSDKHFRRLRGLLGCGRVAIGGQSDEDERYIAPTVLVDV 374
Cdd:cd07132 241 IAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVLTDV 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1886245108 375 QETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRSSQD 423
Cdd:cd07132 321 KPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKV 369
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
55-422 |
0e+00 |
|
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: 595.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 55 ADTLQRLREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESEVSEIHISQSEIDLALRNLRSWMKD 134
Cdd:cd07087 1 AELVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 135 EKVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRYLDQSCFA 214
Cdd:cd07087 81 RRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 215 VVLGGPQETGQLLEHKFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTC 294
Cdd:cd07087 161 VVEGGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 295 VAPDYVLCSPHTRERLLPALQSAITRFYGEDPRRSPSLGRVVSDKHFRRLRGLLGCGRVAIGGQSDEDERYIAPTVLVDV 374
Cdd:cd07087 241 IAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGKVVIGGQVDKEERYIAPTILDDV 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1886245108 375 QETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRSSQ 422
Cdd:cd07087 321 SPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKA 368
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
55-422 |
0e+00 |
|
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: 526.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 55 ADTLQRLREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESEVSEIHISQSEIDLALRNLRSWMKD 134
Cdd:cd07136 1 ESLVEKQRAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 135 EKVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRYLDQSCFA 214
Cdd:cd07136 81 KRVKTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 215 VVLGGPQETGQLLEHKFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTC 294
Cdd:cd07136 161 VVEGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 295 VAPDYVLCSPHTRERLLPALQSAITRFYGEDPRRSPSLGRVVSDKHFRRLRGLLGCGRVAIGGQSDEDERYIAPTVLVDV 374
Cdd:cd07136 241 VAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGKIVFGGNTDRETLYIEPTILDNV 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1886245108 375 QETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRSSQ 422
Cdd:cd07136 321 TWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKK 368
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
52-422 |
4.13e-180 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 511.11 E-value: 4.13e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 52 DPLADTLQRLREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESEVSEIHISQSEIDLALRNLRSW 131
Cdd:PTZ00381 7 EIIPPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 132 MKDEKVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRYLDQS 211
Cdd:PTZ00381 87 LKPEKVDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 212 CFAVVLGGPQETGQLLEHKFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCG 291
Cdd:PTZ00381 167 YVRVIEGGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 292 QTCVAPDYVLCSPHTRERLLPALQSAITRFYGEDPRRSPSLGRVVSDKHFRRLRGLLGC--GRVAIGGQSDEDERYIAPT 369
Cdd:PTZ00381 247 QTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKDhgGKVVYGGEVDIENKYVAPT 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1886245108 370 VLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRSSQ 422
Cdd:PTZ00381 327 IIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKR 379
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
53-420 |
1.87e-172 |
|
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: 489.42 E-value: 1.87e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 53 PLAD---TLQRLREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESEVSEIHISQSEIDLALRNLR 129
Cdd:cd07135 3 PLDEidsIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 130 SWMKDEKVPKNLATQ-LDSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRYL 208
Cdd:cd07135 83 KWAKDEKVKDGPLAFmFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 209 DQSCFAVVLGGPQETGQLLEHKFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYF 288
Cdd:cd07135 163 DPDAFQVVQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 289 NCGQTCVAPDYVLCSPHTRERLLPALQSAITRFYGEDPRRSPSLGRVVSDKHFRRLRGLLGC--GRVAIGGQSDEDERYI 366
Cdd:cd07135 243 NAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDTtkGKVVIGGEMDEATRFI 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1886245108 367 APTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRS 420
Cdd:cd07135 323 PPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDD 376
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
59-420 |
2.15e-152 |
|
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: 438.58 E-value: 2.15e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 59 QRLREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESEVSEIHISQSEIDLALRNLRSWMKDEKVP 138
Cdd:cd07134 5 AAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKPKRVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 139 KNLATQLDSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRYLDQSCFAVVLG 218
Cdd:cd07134 85 TPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFEG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 219 GPQETGQLLEHKFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTCVAPD 298
Cdd:cd07134 165 DAEVAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 299 YVLCSPHTRERLLPALQSAITRFYGEDP--RRSPSLGRVVSDKHFRRLRGLL-----GCGRVAIGGQSDEDERYIAPTVL 371
Cdd:cd07134 245 YVFVHESVKDAFVEHLKAEIEKFYGKDAarKASPDLARIVNDRHFDRLKGLLddavaKGAKVEFGGQFDAAQRYIAPTVL 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1886245108 372 VDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRS 420
Cdd:cd07134 325 TNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKD 373
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
54-419 |
2.61e-150 |
|
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: 432.99 E-value: 2.61e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 54 LADTLQRLREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESEVSEIHISQSEIDLALRNLRSWMK 133
Cdd:cd07137 1 APRLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 134 DEKVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRYLDQSCF 213
Cdd:cd07137 81 PEKVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 214 AVVLGGPQETGQLLEHKFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNC-GQ 292
Cdd:cd07137 161 KVIEGGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCNnGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 293 TCVAPDYVLCSPHTRERLLPALQSAITRFYGEDPRRSPSLGRVVSDKHFRRLRGLLGCGRVAI----GGQSDEDERYIAP 368
Cdd:cd07137 241 ACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADkivhGGERDEKNLYIEP 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1886245108 369 TVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSR 419
Cdd:cd07137 321 TILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTK 371
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
56-423 |
1.37e-137 |
|
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: 400.71 E-value: 1.37e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 56 DTLQRLREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDL-HKSTFESEVSEIHISQSEIDLALRNLRSWMKD 134
Cdd:cd07133 2 ALLERQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFgHRSRHETLLAEILPSIAGIKHARKHLKKWMKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 135 EKVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRYLDQSCFA 214
Cdd:cd07133 82 SRRHVGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 215 VVLGGPQETGQLLEHKFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTC 294
Cdd:cd07133 162 VVTGGADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 295 VAPDYVLCSPHTRERLLPALQSAITRFYGeDPRRSPSLGRVVSDKHFRRLRGLL------GCGRVAIGGQSDEDE--RYI 366
Cdd:cd07133 242 VAPDYVLVPEDKLEEFVAAAKAAVAKMYP-TLADNPDYTSIINERHYARLQGLLedarakGARVIELNPAGEDFAatRKL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1886245108 367 APTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRSSQD 423
Cdd:cd07133 321 PPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAE 377
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
48-419 |
9.53e-132 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 387.93 E-value: 9.53e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 48 PPRMDPLADTLQRLREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESEVSEIHISQSEIDLALRN 127
Cdd:PLN02203 2 EAPGETLEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 128 LRSWMKDEKVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRY 207
Cdd:PLN02203 82 LKKWMAPKKAKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 208 LDQSCFAVVLGGPQETGQLLEHKFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVD---DDCDPQTVANRVAW 284
Cdd:PLN02203 162 LDSKAVKVIEGGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 285 FRYFNC-GQTCVAPDYVLCSPHTRERLLPALQSAITRFYGEDPRRSPSLGRVVSDKHFRRLRGLLGCGRVAI----GGQS 359
Cdd:PLN02203 242 GKWGSCaGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAAsivhGGSI 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 360 DEDERYIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSR 419
Cdd:PLN02203 322 DEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTN 381
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
57-419 |
8.29e-114 |
|
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: 339.95 E-value: 8.29e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 57 TLQRLREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESEVsEIHISQSEIDLALRNLRSWMKDEK 136
Cdd:cd07078 3 AVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALG-EVARAADTFRYYAGLARRLHGEVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 137 VPKNLATQldsAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRY-LDQSCFAV 215
Cdd:cd07078 82 PSPDPGEL---AIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLPPGVLNV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 216 VLGGPQETGQ-LLEH-KFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQT 293
Cdd:cd07078 159 VTGDGDEVGAaLASHpRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 294 CVAPDYVLCSPHTRERLLPALQSAITRFYGEDPRR-SPSLGRVVSDKHFRRLRGLL-----GCGRVAIGGQSDEDE--RY 365
Cdd:cd07078 239 CTAASRLLVHESIYDEFVERLVERVKALKVGNPLDpDTDMGPLISAAQLDRVLAYIedakaEGAKLLCGGKRLEGGkgYF 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1886245108 366 IAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSR 419
Cdd:cd07078 319 VPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTR 372
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
61-422 |
2.16e-94 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 292.34 E-value: 2.16e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 61 LREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESEVSEIHISQSEIDLALRNLRSWMKDEKVPKN 140
Cdd:PLN02174 19 LRRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEKAKTS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 141 LATQLDSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRYLDQSCFAVVLGGP 220
Cdd:PLN02174 99 LTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVEGAV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 221 QETGQLLEHKFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRY-FNCGQTCVAPDY 299
Cdd:PLN02174 179 TETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDY 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 300 VLCSPHTRERLLPALQSAITRFYGEDPRRSPSLGRVVSDKHFRRLRGLLG----CGRVAIGGQSDEDERYIAPTVLVDVQ 375
Cdd:PLN02174 259 ILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDekevSDKIVYGGEKDRENLKIAPTILLDVP 338
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1886245108 376 ETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRSSQ 422
Cdd:PLN02174 339 LDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKK 385
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
62-420 |
5.16e-91 |
|
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: 283.17 E-value: 5.16e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKStfesevseIHISQSEIDLALRNLRSW------MKDE 135
Cdd:COG1012 53 RAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKP--------LAEARGEVDRAADFLRYYagearrLYGE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 136 KVPKNLATQLdsAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEV-----LPRYLdq 210
Cdd:COG1012 125 TIPSDAPGTR--AYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELleeagLPAGV-- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 211 scFAVVLGGPQETGQ-LLEH-KFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYF 288
Cdd:COG1012 201 --LNVVTGDGSEVGAaLVAHpDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 289 NCGQTCVAPDYVLCSPHTRERLLPALQSAITRF-YGeDPRR-SPSLGRVVSDKHFRRLRGLLGCG-----RVAIGGQSDE 361
Cdd:COG1012 279 NAGQRCTAASRLLVHESIYDEFVERLVAAAKALkVG-DPLDpGTDMGPLISEAQLERVLAYIEDAvaegaELLTGGRRPD 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1886245108 362 DER--YIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRS 420
Cdd:COG1012 358 GEGgyFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRD 418
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
62-419 |
3.63e-88 |
|
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: 272.18 E-value: 3.63e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESeVSEIHISQSEIDLALRNLRSWMKDEKVPKNL 141
Cdd:cd06534 4 RAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEA-LGEVARAIDTFRYAAGLADKLGGPELPSPDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 142 ATQldsAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRY-LDQSCFAVVLGGP 220
Cdd:cd06534 83 GGE---AYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 221 QETGQ-LLEH-KFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTCVAPD 298
Cdd:cd06534 160 DEVGAaLLSHpRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 299 YVLCSPHTRERLLPALQsaitrfygedprrspslgrvvsdkhfrrlrgllgcgrvaiggqsdederyiapTVLVDVQETE 378
Cdd:cd06534 240 RLLVHESIYDEFVEKLV-----------------------------------------------------TVLVDVDPDM 266
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1886245108 379 PVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSR 419
Cdd:cd06534 267 PIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTR 307
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
62-420 |
1.56e-78 |
|
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: 250.14 E-value: 1.56e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKStfesevseIHISQSEIDLALRNLRSW------MKDE 135
Cdd:pfam00171 39 RAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKP--------LAEARGEVDRAIDVLRYYaglarrLDGE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 136 KVPKNLATQldsAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEV-----LPRYLdq 210
Cdd:pfam00171 111 TLPSDPGRL---AYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELfeeagLPAGV-- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 211 scFAVVLGGPQETGQ-LLEHK-FDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYF 288
Cdd:pfam00171 186 --LNVVTGSGAEVGEaLVEHPdVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 289 NCGQTCVAPDYVLCSPHTRERLLPALQSAITRFYGEDPR-RSPSLGRVVSDKHFRRLRGLL-----GCGRVAIGGQSDED 362
Cdd:pfam00171 264 NAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLdPDTDMGPLISKAQLERVLKYVedakeEGAKLLTGGEAGLD 343
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1886245108 363 E-RYIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRS 420
Cdd:pfam00171 344 NgYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSD 402
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
49-420 |
2.16e-78 |
|
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: 249.83 E-value: 2.16e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 49 PRMDP--LADTLQRLREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKStfesevseIHISQSEIDLALR 126
Cdd:cd07099 13 PVTDPaeVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKP--------RADAGLEVLLALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 127 NLRSW-------MKDEKVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFS-RSTEK 198
Cdd:cd07099 85 AIDWAarnaprvLAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTpLVGEL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 199 ---VLAEVLPrylDQSCFAVVLGGpQETGQ-LLEHKFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCD 274
Cdd:cd07099 165 laeAWAAAGP---PQGVLQVVTGD-GATGAaLIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 275 PQTVANRVAWFRYFNCGQTCVAPD--YVLCSPHtrERLLPALQSAITRF-YGEDPRRSPSLGRVVSDKHFRRLRG----- 346
Cdd:cd07099 241 LERAAAAAVWGAMVNAGQTCISVErvYVHESVY--DEFVARLVAKARALrPGADDIGDADIGPMTTARQLDIVRRhvdda 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1886245108 347 LLGCGRVAIGG-QSDEDERYIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRS 420
Cdd:cd07099 319 VAKGAKALTGGaRSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
60-420 |
3.87e-61 |
|
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: 205.23 E-value: 3.87e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 60 RLREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESEVSEIHISQSEIDLALRNLRSWMKDEKVPK 139
Cdd:cd07098 26 AARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEILVTCEKIRWTLKHGEKALRPESRPG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 140 NLATQLDSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSE--------FSRSTEKVLAEV-LPRYLDQ 210
Cdd:cd07098 106 GLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEqvawssgfFLSIIRECLAACgHDPDLVQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 211 S--CFAvvlggpqETGQ-LLEH-KFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANrvAWFR 286
Cdd:cd07098 186 LvtCLP-------ETAEaLTSHpVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIAS--IIMR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 287 --YFNCGQTCVAPDYVLCSPHTRERLLPALQSAITRFygedPRRSPSLGRV-----VSDKHFRRLRGLLG-----CGRVA 354
Cdd:cd07098 257 gtFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQAL----RQGPPLDGDVdvgamISPARFDRLEELVAdavekGARLL 332
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1886245108 355 IGG---QSDEDER--YIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRS 420
Cdd:cd07098 333 AGGkryPHPEYPQghYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKD 403
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
40-406 |
5.71e-59 |
|
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: 199.01 E-value: 5.71e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 40 VWVRRPLLPPrmDPLADTLQRLREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKStfesevseIHISQS 119
Cdd:cd07102 8 VIAERPLASL--EAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRP--------IAQAGG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 120 EIDLALRNLRsWMKD--EKVPKNLATQLDSAF---IRKEPFGLVLIIAPWNYPVnLTLV-PLVGALAAGNCVVLKPSEFS 193
Cdd:cd07102 78 EIRGMLERAR-YMISiaEEALADIRVPEKDGFeryIRREPLGVVLIIAPWNYPY-LTAVnAVIPALLAGNAVILKHSPQT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 194 RSTEKVLAEV-----LPRYLdqscFAVVLGGPQETGQLLE-HKFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPC 267
Cdd:cd07102 156 PLCGERFAAAfaeagLPEGV----FQVLHLSHETSAALIAdPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 268 YVDDDCDPQTVANRVAWFRYFNCGQTCVAPD--YVlcspHTR--ERLLPALQsAITRFY--GEDPRRSPSLGRVVSDKHF 341
Cdd:cd07102 232 YVRPDADLDAAAESLVDGAFFNSGQSCCSIEriYV----HESiyDAFVEAFV-AVVKGYklGDPLDPSTTLGPVVSARAA 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1886245108 342 RRLRGLL------GcGRVAIGGQ----SDEDERYIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFIN 406
Cdd:cd07102 307 DFVRAQIadaiakG-ARALIDGAlfpeDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMN 380
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
62-406 |
3.86e-58 |
|
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: 196.60 E-value: 3.86e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESevseihisQSEIDLALrnlrSWMK-------- 133
Cdd:cd07106 29 KAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEA--------QFEVGGAV----AWLRytasldlp 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 134 DEKVPKNlATQldSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSR-STEK---VLAEVLPRYLD 209
Cdd:cd07106 97 DEVIEDD-DTR--RVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPlCTLKlgeLAQEVLPPGVL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 210 QscfavVLGGPQETGQLL-EH-KFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRY 287
Cdd:cd07106 174 N-----VVSGGDELGPALtSHpDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 288 FNCGQTCVAPD--YVlcspHTR--ERLLPALQSAITRFY---GEDPrrSPSLGRVVSDKHFRRLRGLL-----GCGRVAI 355
Cdd:cd07106 249 INSGQVCAAIKrlYV----HESiyDEFCEALVALAKAAVvgdGLDP--GTTLGPVQNKMQYDKVKELVedakaKGAKVLA 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1886245108 356 GGQSDEDERY-IAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFIN 406
Cdd:cd07106 323 GGEPLDGPGYfIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARAN 374
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
62-422 |
3.66e-57 |
|
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: 194.49 E-value: 3.66e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESEVS--------EIHISQSEidlALRNlrswMK 133
Cdd:cd07110 29 RRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDvddvagcfEYYADLAE---QLDA----KA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 134 DEKVPknLATQLDSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEV-----LPRyl 208
Cdd:cd07110 102 ERAVP--LPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIaaeagLPP-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 209 dqSCFAVVLGGPQETGQ-LLEHK-FDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFR 286
Cdd:cd07110 178 --GVLNVVTGTGDEAGApLAAHPgIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGC 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 287 YFNCGQTCVAPDYVLCSPHTRERLLPALQSAITRFYGEDPR-RSPSLGRVVSDKHFRRLRGLLGCG-----RVAIGGQSD 360
Cdd:cd07110 256 FWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLeEGVRLGPLVSQAQYEKVLSFIARGkeegaRLLCGGRRP 335
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1886245108 361 EDER---YIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRSSQ 422
Cdd:cd07110 336 AHLEkgyFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAE 400
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
62-419 |
4.70e-57 |
|
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: 194.08 E-value: 4.70e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHK---STFESEVSEIhisqseIDL------ALRNLRSWM 132
Cdd:cd07092 29 HAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKplhLVRDDELPGA------VDNfrffagAARTLEGPA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 133 KDEKVPKNlatqldSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRYLDQSC 212
Cdd:cd07092 103 AGEYLPGH------TSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 213 FAVVLGGPQETGQLL--EHKFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNC 290
Cdd:cd07092 177 VNVVCGGGASAGDALvaHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 291 GQTCVAPDYVLCSPHTRERLLPALQSAITRFYGEDPRRSPS-LGRVVSDKHFRRLRGLL----GCGRVAIGGQS-DEDER 364
Cdd:cd07092 257 GQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTeMGPLNSAAQRERVAGFVerapAHARVLTGGRRaEGPGY 336
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1886245108 365 YIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSR 419
Cdd:cd07092 337 FYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTR 391
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
62-419 |
7.28e-57 |
|
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: 193.60 E-value: 7.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAGRTR-SPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESevseihisQSEIDLALRNLRSW--MKDEKVP 138
Cdd:cd07109 29 RRAFESGWLRlSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQA--------RADVEAAARYFEYYggAADKLHG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 139 KNLATQLD-SAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRY-LDQSCFAVV 216
Cdd:cd07109 101 ETIPLGPGyFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAgLPAGALNVV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 217 LGGPQETGQ-LLEHK-FDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTC 294
Cdd:cd07109 181 TGLGAEAGAaLVAHPgVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTC 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 295 VAPDYVLCSPHTRERLLPALQS---AITRFYGEDprrSPSLGRVVSDKHFRRLRGLL-----GCGRVAIGGQSDEDER-- 364
Cdd:cd07109 261 SAGSRLLVHRSIYDEVLERLVErfrALRVGPGLE---DPDLGPLISAKQLDRVEGFVararaRGARIVAGGRIAEGAPag 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1886245108 365 --YIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSR 419
Cdd:cd07109 338 gyFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTR 394
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
62-420 |
6.59e-56 |
|
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: 191.30 E-value: 6.59e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAG-RTRSPEFRAAQLKGLGRFLQENKQLLQEALaqdlhkstfeseVSEIHISQS-----EIDLALRNLRSW---- 131
Cdd:cd07089 29 RRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALL------------VAEVGAPVMtaramQVDGPIGHLRYFadla 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 132 ----MKDEKVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEV---- 203
Cdd:cd07089 97 dsfpWEFDLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIiaet 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 204 -LPRyldqSCFAVVLGGPQETGQLL--EHKFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVAN 280
Cdd:cd07089 177 dLPA----GVVNVVTGSDNAVGEALttDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 281 RVAWFRYFNCGQTCVAPDYVLCSPHTRERLLPALQSAITRFYGEDPrRSPS--LGRVVSDKHFRRLRGLLGCGR------ 352
Cdd:cd07089 253 AAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDP-ADPGtvMGPLISAAQRDRVEGYIARGRdegarl 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 353 VAIGGQSDEDER--YIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRS 420
Cdd:cd07089 332 VTGGGRPAGLDKgfYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSAD 401
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
54-420 |
2.69e-54 |
|
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: 186.20 E-value: 2.69e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 54 LADTLQRLREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQD----LHKSTFESEVSEIHISQSeIDLALRnlr 129
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIREsgstRPKAAFEVGAAIAILREA-AGLPRR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 130 swMKDEKVPKNLATQLdsAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSR-STEKVLAEV----- 203
Cdd:cd07104 78 --PEGEILPSDVPGKE--SMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPvTGGLLIAEIfeeag 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 204 LPRYLdqscFAVVLGGPQETGQ-LLEHK-FDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANR 281
Cdd:cd07104 154 LPKGV----LNVVPGGGSEIGDaLVEHPrVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 282 VAWFRYFNCGQTCVAPDYVLCSPHTRERLLPALQSAITRF-YGeDPRRSP-SLGRVVSDKHFRRLRGLL------GcGRV 353
Cdd:cd07104 230 AAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALpVG-DPRDPDtVIGPLINERQVDRVHAIVedavaaG-ARL 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1886245108 354 AIGGqsDEDERYIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRS 420
Cdd:cd07104 308 LTGG--TYEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRD 372
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
68-420 |
1.47e-53 |
|
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: 185.16 E-value: 1.47e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 68 GRTRSPEfRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESEVsEIHISQSEIDLALRNLRSwMKDEKVPKNLATQldS 147
Cdd:cd07088 52 ERLPAIE-RAAYLRKLADLIRENADELAKLIVEEQGKTLSLARV-EVEFTADYIDYMAEWARR-IEGEIIPSDRPNE--N 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 148 AFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEV-----LPRYLdqscFAVVLGGPQE 222
Cdd:cd07088 127 IFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELvdeagLPAGV----LNIVTGRGSV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 223 TGQLL-EH-KFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTCVAPD-- 298
Cdd:cd07088 203 VGDALvAHpKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAErv 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 299 YVLCSPHTR--ERLLPALQSAItrfYGEDPRRSPSLGRVVSDKHFRRLRGLL------GcGRVAIGGQSDEDER--YIAP 368
Cdd:cd07088 283 YVHEDIYDEfmEKLVEKMKAVK---VGDPFDAATDMGPLVNEAALDKVEEMVeraveaG-ATLLTGGKRPEGEKgyFYEP 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1886245108 369 TVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRS 420
Cdd:cd07088 359 TVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTEN 410
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
63-420 |
9.43e-53 |
|
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: 182.63 E-value: 9.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 63 EAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKStfeseVSEihiSQSEIDLALRNLRsWMKDEK------ 136
Cdd:cd07103 30 AAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKP-----LAE---ARGEVDYAASFLE-WFAEEArriygr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 137 -VPKNLATQldSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRY-LDQSCFA 214
Cdd:cd07103 101 tIPSPAPGK--RILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEAgLPAGVLN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 215 VVLGGPQETGQ-LLEH----KfdyIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFN 289
Cdd:cd07103 179 VVTGSPAEIGEaLCASprvrK---ISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 290 CGQTCVAPD--YVlcspHTR--ERLLPALQSAITRF---YGEDPrrSPSLGRVVSDKHFRRLRGL----LGCG-RVAIGG 357
Cdd:cd07103 256 AGQTCVCANriYV----HESiyDEFVEKLVERVKKLkvgNGLDE--GTDMGPLINERAVEKVEALvedaVAKGaKVLTGG 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1886245108 358 QSDEDE-RYIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRS 420
Cdd:cd07103 330 KRLGLGgYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRD 393
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
62-419 |
1.00e-52 |
|
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: 182.70 E-value: 1.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSA-GRTrSPEFRAAQLKGLGRFLQENKQLLQEALAQdlhkstfesEV-SEIHISQS-EIDLALRNLRSWMKdekVP 138
Cdd:cd07138 46 RRAFPAwSAT-SVEERAALLERIAEAYEARADELAQAITL---------EMgAPITLARAaQVGLGIGHLRAAAD---AL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 139 KNLA--TQLDSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEV-----LPRyldqS 211
Cdd:cd07138 113 KDFEfeERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEIldeagLPA----G 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 212 CFAVVLGGPQETGQLL-EH-KFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCD-----PQTVANrvaw 284
Cdd:cd07138 189 VFNLVNGDGPVVGEALsAHpDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADlekavPRGVAA---- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 285 fRYFNCGQTCVAPDYVLCsPHTR----ERLLPALQSAITRFYGEDPrrSPSLGRVVSDKHFRRLRGLLGCG-----RVAI 355
Cdd:cd07138 265 -CFANSGQSCNAPTRMLV-PRSRyaeaEEIAAAAAEAYVVGDPRDP--ATTLGPLASAAQFDRVQGYIQKGieegaRLVA 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1886245108 356 GG----QSDEDERYIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSR 419
Cdd:cd07138 341 GGpgrpEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSA 408
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
63-419 |
2.31e-52 |
|
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: 181.24 E-value: 2.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 63 EAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESEVseihisqsEIDLALRNLR------SWMKDEK 136
Cdd:cd07105 11 AAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGF--------NVDLAAGMLReaasliTQIIGGS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 137 VPKNLATQLdsAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEV-----LPryldQS 211
Cdd:cd07105 83 IPSDKPGTL--AMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVfheagLP----KG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 212 CFAVVLGGPQE----TGQLLEHK-FDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFR 286
Cdd:cd07105 157 VLNVVTHSPEDapevVEALIAHPaVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 287 YFNCGQTCVAPDYVLCSPHTRERLLPALQSAITRFYGEDPRrspsLGRVVSDKHFRRLRGL----LGCG-RVAIGGQSDE 361
Cdd:cd07105 237 FLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVV----LGSLVSAAAADRVKELvddaLSKGaKLVVGGLADE 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 362 DER--YIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSR 419
Cdd:cd07105 313 SPSgtSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTR 372
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
150-419 |
2.55e-51 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 179.33 E-value: 2.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 150 IRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRYLDQSCFAVVLGGPQETGQ-LLE 228
Cdd:PRK13473 134 IRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDaLVG 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 229 H-KFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTCVAPDYVLCSPHTR 307
Cdd:PRK13473 214 HpKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIY 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 308 ERLLPALQSAITRFYGEDPRRSPS-LGRVVSDKHFRRLRGL------LGCGRVAIGGQ-SDEDERYIAPTVLVDVQETEP 379
Cdd:PRK13473 294 DDLVAKLAAAVATLKVGDPDDEDTeLGPLISAAHRDRVAGFverakaLGHIRVVTGGEaPDGKGYYYEPTLLAGARQDDE 373
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1886245108 380 VMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSR 419
Cdd:PRK13473 374 IVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTR 413
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
62-419 |
2.63e-51 |
|
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: 179.09 E-value: 2.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESEVSEIHISqseIDLaLR---NLRSWMKDEKVP 138
Cdd:cd07108 29 KAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPEAAVL---ADL-FRyfgGLAGELKGETLP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 139 KNlATQLdsAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRYLDQSCFAVVLG 218
Cdd:cd07108 105 FG-PDVL--TYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQVLPAGVLNVITG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 219 GPQETGQ-LLEH-KFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYV--DDDCDpQTVANRVAWFRYFNCGQTC 294
Cdd:cd07108 182 YGEECGAaLVDHpDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVfpDADLD-DAVDGAIAGMRFTRQGQSC 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 295 VAPDYVLCSPHTRERLLPALQSAITRFYGEDPRRSPS-LGRVVSDKHFRRLRGLLGCG------RVAIGGQSDEDER--- 364
Cdd:cd07108 261 TAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATdIGAIISEKQFAKVCGYIDLGlstsgaTVLRGGPLPGEGPlad 340
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1886245108 365 --YIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSR 419
Cdd:cd07108 341 gfFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTR 397
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
62-402 |
2.73e-51 |
|
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: 178.95 E-value: 2.73e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAGR--TRSPEFRAAQLKGLGRFLQENKQLLQ--EALaqDLHKstfesevsEIHISQS-EIDLALRNLRsW----- 131
Cdd:cd07112 34 RRAFESGVwsRLSPAERKAVLLRLADLIEAHRDELAllETL--DMGK--------PISDALAvDVPSAANTFR-Wyaeai 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 132 --MKDEKVPknlaTQLDS-AFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEV----- 203
Cdd:cd07112 103 dkVYGEVAP----TGPDAlALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELaleag 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 204 LPRyldqSCFAVVLGGPQETGQLL-EHK-FDYIFFTGSPRVGRIVMTAAAK-HLTPVTLELGGKNPCYVDDDC-DPQTVA 279
Cdd:cd07112 179 LPA----GVLNVVPGFGHTAGEALgLHMdVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADApDLDAAA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 280 NRVAWFRYFNCGQTCVAPDYVLCSPHTRERLLPALQSAITRFYGEDPRR-SPSLGRVVSDKHFRRLRGLLGCG-----RV 353
Cdd:cd07112 255 EAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDpATRMGALVSEAHFDKVLGYIESGkaegaRL 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1886245108 354 AIGGQSDEDER---YIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAI 402
Cdd:cd07112 335 VAGGKRVLTETggfFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAV 386
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
62-420 |
1.88e-49 |
|
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: 174.06 E-value: 1.88e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAGRTR--SPEFRAAQLKGLGRFLQENkqllQEALAQdlhkstFESEVSEIHISQS--EIDLALRNLRswmkdekV 137
Cdd:cd07118 29 RKAFDKGPWPrmSGAERAAVLLKVADLIRAR----RERLAL------IETLESGKPISQArgEIEGAADLWR-------Y 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 138 PKNLATQL--DS---------AFIRKEPFGLVLIIAPWNYPVnLTL---VPLvgALAAGNCVVLKPSEFSRSTEKVLAEV 203
Cdd:cd07118 92 AASLARTLhgDSynnlgddmlGLVLREPIGVVGIITPWNFPF-LILsqkLPF--ALAAGCTVVVKPSEFTSGTTLMLAEL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 204 LPRY-LDQSCFAVVLGGPQETGQ-LLEHK-FDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVAN 280
Cdd:cd07118 169 LIEAgLPAGVVNIVTGYGATVGQaMTEHPdVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAAD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 281 RVAWFRYFNCGQTCVAPDYVLCSPHTRERLLPALQSAITRFYGEDP-RRSPSLGRVVSDKHFRRLRGLLGCGR-----VA 354
Cdd:cd07118 249 AVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPlDPETKVGAIINEAQLAKITDYVDAGRaegatLL 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1886245108 355 IGGQSDEDE--RYIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRS 420
Cdd:cd07118 329 LGGERLASAagLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKD 396
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
62-420 |
3.22e-49 |
|
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: 173.13 E-value: 3.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKStfesevseIHISQS-EIDLALRNLRSWmkdekvpKN 140
Cdd:cd07093 29 KEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKP--------ITLARTrDIPRAAANFRFF-------AD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 141 LATQLDSAFI----------RKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEV-----LP 205
Cdd:cd07093 94 YILQLDGESYpqdggalnyvLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELaneagLP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 206 RyldqSCFAVVLG-GPqETGQLL-EHK-FDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRV 282
Cdd:cd07093 174 P----GVVNVVHGfGP-EAGAALvAHPdVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 283 AWFRYFNCGQTCvapdyvLCSphtrERLLpaLQSAI-----TRFYGE-------DPrRSPS--LGRVVSDKHFRRLRGLL 348
Cdd:cd07093 249 VRSSFSNNGEVC------LAG----SRIL--VQRSIydeflERFVERakalkvgDP-LDPDteVGPLISKEHLEKVLGYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 349 GCGR-----VAIGGQSDEDER-----YIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFS 418
Cdd:cd07093 316 ELARaegatILTGGGRPELPDleggyFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWT 395
|
..
gi 1886245108 419 RS 420
Cdd:cd07093 396 RD 397
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
150-409 |
1.19e-47 |
|
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: 169.05 E-value: 1.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 150 IRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRY-LDQSCFAVVLGGPQETGQLL- 227
Cdd:cd07150 115 SVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAgLPKGVFNVVTGGGAEVGDELv 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 228 -EHKFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTCVAPDYVLCSPHT 306
Cdd:cd07150 195 dDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPV 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 307 RERLLPALQSAITRFYGEDPR-RSPSLGRVVSDKHFRRLRGLL------GcGRVAIGGQsdEDERYIAPTVLVDVQETEP 379
Cdd:cd07150 275 YDEFVKKFVARASKLKVGDPRdPDTVIGPLISPRQVERIKRQVedavakG-AKLLTGGK--YDGNFYQPTVLTDVTPDMR 351
|
250 260 270
....*....|....*....|....*....|
gi 1886245108 380 VMQEEIFGPILPIVNVGSLDEAIDFINRRE 409
Cdd:cd07150 352 IFREETFGPVTSVIPAKDAEEALELANDTE 381
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
59-420 |
3.72e-47 |
|
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: 167.47 E-value: 3.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 59 QRLREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQD----LHKSTFESEVSEIHISQSeidlalrnlrswmkd 134
Cdd:cd07152 20 ARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVREsgsiRPKAGFEVGAAIGELHEA--------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 135 ekvpKNLATQ-----LDSA-----FIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSR-STEKVLAEV 203
Cdd:cd07152 85 ----AGLPTQpqgeiLPSApgrlsLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPvSGGVVIARL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 204 -----LPRYLDQscfavVLGGPQETGQ-LLEH-KFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQ 276
Cdd:cd07152 161 feeagLPAGVLH-----VLPGGADAGEaLVEDpNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 277 TVANRVAWFRYFNCGQTCVAPDYVLCSPHTRERLLPALQSAITRFYGEDPRRSP-SLGRVVSDKHFRRLRGL------LG 349
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQvALGPLINARQLDRVHAIvddsvaAG 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1886245108 350 cGRVAIGGQSdeDERYIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRS 420
Cdd:cd07152 316 -ARLEAGGTY--DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRD 383
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
149-419 |
4.54e-47 |
|
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: 167.62 E-value: 4.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 149 FIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRY-LDQSCFAVVLGGPQETGQ-L 226
Cdd:cd07115 112 YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAgFPAGVLNVVTGFGEVAGAaL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 227 LEH-KFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTCVAPDYVLCSPH 305
Cdd:cd07115 192 VEHpDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHES 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 306 TRERLLPALQSAITRFYGEDP-RRSPSLGRVVSDKHFRRLRGLLGCG-----RVAIGGQSDeDER--YIAPTVLVDVQET 377
Cdd:cd07115 272 IYDEFLERFTSLARSLRPGDPlDPKTQMGPLVSQAQFDRVLDYVDVGreegaRLLTGGKRP-GARgfFVEPTIFAAVPPE 350
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1886245108 378 EPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSR 419
Cdd:cd07115 351 MRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTR 392
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
62-419 |
1.72e-46 |
|
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: 165.98 E-value: 1.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESEVseihisqsEIDLALRNLRSWMKDEKVPKNL 141
Cdd:cd07145 31 EKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV--------EVERTIRLFKLAAEEAKVLRGE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 142 ATQLDS--------AFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRY-LDQSC 212
Cdd:cd07145 103 TIPVDAyeynerriAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPGV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 213 FAVVLGGPQETG-QLLEH-KFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNC 290
Cdd:cd07145 183 INVVTGYGSEVGdEIVTNpKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 291 GQTCVAPDYVLCSPHTRERLLPALQSAITRFYGEDP-RRSPSLGRVVSDKHFRRLRGLL------GcGRVAIGGQSDEDE 363
Cdd:cd07145 263 GQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPlDESTDLGPLISPEAVERMENLVndavekG-GKILYGGKRDEGS 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1886245108 364 rYIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSR 419
Cdd:cd07145 342 -FFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTN 396
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
58-419 |
1.78e-46 |
|
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: 166.37 E-value: 1.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 58 LQRLREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESevseihiSQSEIDLALRNLRSWMKDEKV 137
Cdd:cd07559 44 VDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRET-------LAADIPLAIDHFRYFAGVIRA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 138 PKNLATQLDS---AFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRYLDQSCFA 214
Cdd:cd07559 117 QEGSLSEIDEdtlSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 215 VVLGGPQETGQ-LLEHK-FDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDcdpqTVANRVAWFR------ 286
Cdd:cd07559 197 VVTGFGSEAGKpLASHPrIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFFDD----AMDADDDFDDkaeegq 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 287 ---YFNCGQTCVAPDYVLCSPHTRERLLPALQSAITRFYGEDPRRSPS-LGRVVSDKHFRRLRGLLGCGR-----VAIGG 357
Cdd:cd07559 273 lgfAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETmMGAQVSKDQLEKILSYVDIGKeegaeVLTGG 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1886245108 358 Q-----SDEDERYIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSR 419
Cdd:cd07559 353 ErltlgGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTR 419
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
62-413 |
2.55e-46 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 166.45 E-value: 2.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAGRTR-----SPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESE-----VS---EIHISQSEiDLALRNl 128
Cdd:PLN02467 55 RKAFKRNKGKdwartTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAwdmddVAgcfEYYADLAE-ALDAKQ- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 129 rswmkdeKVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEV----- 203
Cdd:PLN02467 133 -------KAPVSLPMETFKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADIcrevg 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 204 LPRyldqSCFAVVLGGPQETGQ-LLEHK-FDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDpqtVANR 281
Cdd:PLN02467 206 LPP----GVLNVVTGLGTEAGApLASHPgVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVD---LDKA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 282 VAWfRYFNC----GQTCVAPDYVLCSPHTRERLLPALQSAITRFYGEDPRRSP-SLGRVVSDKHFRRLRGLLGCGR---- 352
Cdd:PLN02467 279 VEW-AMFGCfwtnGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGcRLGPVVSEGQYEKVLKFISTAKsega 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1886245108 353 -VAIGGQSDEDER---YIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLA 413
Cdd:PLN02467 358 tILCGGKRPEHLKkgfFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLA 422
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
62-406 |
5.73e-46 |
|
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: 165.06 E-value: 5.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAG--RTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESEVSEIHISQSEIDLALRNLRSWMKDEKVPk 139
Cdd:cd07139 46 RRAFDNGpwPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEERRP- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 140 nlATQLDSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEV-----LPryldQSCFA 214
Cdd:cd07139 125 --GSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAaeeagLP----PGVVN 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 215 VVLGGPQETGQLLEHK-FDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQT 293
Cdd:cd07139 199 VVPADREVGEYLVRHPgVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 294 CVAPDYVLCSPHTRERLLPALQSAITRFYGEDP-RRSPSLGRVVSDKHFRRLRGLLGCGR------VAIGGQSDEDER-- 364
Cdd:cd07139 279 CVALTRILVPRSRYDEVVEALAAAVAALKVGDPlDPATQIGPLASARQRERVEGYIAKGRaegarlVTGGGRPAGLDRgw 358
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1886245108 365 YIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFIN 406
Cdd:cd07139 359 FVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIAN 400
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
62-420 |
7.31e-46 |
|
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: 164.83 E-value: 7.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFES--EVSE-IHISQSEIDLALRnlrswMKDEKVP 138
Cdd:cd07131 47 REAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGrgDVQEaIDMAQYAAGEGRR-----LFGETVP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 139 KNLATQLdsAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRY-LDQSCFAVVL 217
Cdd:cd07131 122 SELPNKD--AMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAgLPPGVVNVVH 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 218 GGPQETGQ-LLEH-KFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTCV 295
Cdd:cd07131 200 GRGEEVGEaLVEHpDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCT 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 296 APDYVLCSPHTRERLLPALQSAITRFYGEDPRRSPSL-GRVVSDKHFRR------------LRGLLGCGRVAIGGQsdED 362
Cdd:cd07131 280 ATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDmGPLINEAQLEKvlnyneigkeegATLLLGGERLTGGGY--EK 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1886245108 363 ERYIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRS 420
Cdd:cd07131 358 GYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTED 415
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
146-418 |
8.45e-46 |
|
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: 164.60 E-value: 8.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 146 DSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRY-LDQSCFAVVLGGPQETG 224
Cdd:TIGR01804 125 SFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAgLPKGVFNVVQGDGAEVG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 225 QLL-EHK-FDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTCVAPDYVLC 302
Cdd:TIGR01804 205 PLLvNHPdVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFV 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 303 SPHTRERLLPALQSAITRFYGEDP-RRSPSLGRVVSDKHFRRLRGLLGCG-----RVAIGGQSDEDER-----YIAPTVL 371
Cdd:TIGR01804 285 HKKIKERFLARLVERTERIKLGDPfDEATEMGPLISAAHRDKVLSYIEKGkaegaTLATGGGRPENVGlqngfFVEPTVF 364
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1886245108 372 VDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFS 418
Cdd:TIGR01804 365 ADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFT 411
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
62-406 |
1.09e-45 |
|
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: 164.34 E-value: 1.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFES--EVSE-IHISQSEIDLALR----NLRSWMKD 134
Cdd:cd07097 47 AAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEArgEVTRaGQIFRYYAGEALRlsgeTLPSTRPG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 135 EKVpknlatqldsaFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRY-LDQSCF 213
Cdd:cd07097 127 VEV-----------ETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAgLPAGVF 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 214 AVVLGGPQETGQ-LLEHK-FDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCG 291
Cdd:cd07097 196 NLVMGSGSEVGQaLVEHPdVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 292 QTCVAPDYVLCSP--HTR--ERLLPALQSAITrfyGEDPRRSPSLGRVVSDKHFRRLRGLLG-----CGRVAIGGQ---S 359
Cdd:cd07097 276 QRCTASSRLIVTEgiHDRfvEALVERTKALKV---GDALDEGVDIGPVVSERQLEKDLRYIEiarseGAKLVYGGErlkR 352
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1886245108 360 DEDERYIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFIN 406
Cdd:cd07097 353 PDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIAN 399
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
148-406 |
3.91e-45 |
|
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: 162.34 E-value: 3.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 148 AFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEV-----LPRYLdqscFAVVLGGPQE 222
Cdd:cd07114 113 NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLaeeagFPPGV----VNVVTGFGPE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 223 TGQLL-EH-KFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTCVAPDYV 300
Cdd:cd07114 189 TGEALvEHpLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 301 LCSPHTRERLLPALQSAITRFYGEDPRR-SPSLGRVVSDKHFRRLRGLLGC-----GRVAIGG-QSDEDER----YIAPT 369
Cdd:cd07114 269 LVQRSIYDEFVERLVARARAIRVGDPLDpETQMGPLATERQLEKVERYVARareegARVLTGGeRPSGADLgagyFFEPT 348
|
250 260 270
....*....|....*....|....*....|....*..
gi 1886245108 370 VLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFIN 406
Cdd:cd07114 349 ILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALAN 385
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
54-406 |
1.60e-44 |
|
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: 159.93 E-value: 1.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 54 LADTLQRLREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESevseihisQSEIDLALRNLR---- 129
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA--------RAEVEKCAWICRyyae 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 130 ---SWMKDEKVPknlaTQLDSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEF----SRSTEKVLAE 202
Cdd:cd07100 73 naeAFLADEPIE----TDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNvpgcALAIEELFRE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 203 V-LPryldQSCFAVVLGGPQETGQLLEHkfDYI---FFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTV 278
Cdd:cd07100 149 AgFP----EGVFQNLLIDSDQVEAIIAD--PRVrgvTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 279 ANRVAWFRYFNCGQTCVAP------DYVlcsphtRERLLPALQSAITRFYGEDPRRSPS-LGRVVSDKHFRRLRGLL--- 348
Cdd:cd07100 223 VKTAVKGRLQNAGQSCIAAkrfivhEDV------YDEFLEKFVEAMAALKVGDPMDEDTdLGPLARKDLRDELHEQVeea 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1886245108 349 ---GCgRVAIGGQ-SDEDERYIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFIN 406
Cdd:cd07100 297 vaaGA-TLLLGGKrPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALAN 357
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
62-419 |
3.90e-44 |
|
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: 159.93 E-value: 3.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESevseihiSQSEIDLALRNLRSWMKDEKVPKNL 141
Cdd:cd07117 48 QEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRET-------RAVDIPLAADHFRYFAGVIRAEEGS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 142 ATQLDSAF---IRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRYLDQSCFAVVLG 218
Cdd:cd07117 121 ANMIDEDTlsiVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNIVTG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 219 GPQETGQ-LLEHK-FDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTCVA 296
Cdd:cd07117 201 KGSKSGEyLLNHPgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 297 PDYVLCSPHTRERLLPALQSAITRFYGEDP-RRSPSLGRVVSDKHFRRLRGLLGCG-----RVAIGGQ----SDED-ERY 365
Cdd:cd07117 281 GSRIFVQEGIYDEFVAKLKEKFENVKVGNPlDPDTQMGAQVNKDQLDKILSYVDIAkeegaKILTGGHrlteNGLDkGFF 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1886245108 366 IAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSR 419
Cdd:cd07117 361 IEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTK 414
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
62-409 |
4.52e-44 |
|
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: 159.46 E-value: 4.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLhKSTFESEVSEIHISQSEIDLaLRNLRSWMKDEKVPknl 141
Cdd:cd07107 29 RAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDC-GNPVSAMLGDVMVAAALLDY-FAGLVTELKGETIP--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 142 ATQLDSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRYLDQSCFAVVLGGPQ 221
Cdd:cd07107 104 VGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREVLPPGVFNILPGDGA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 222 ETGQ-LLEHK-FDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANR-VAWFRYFNCGQTCVAPD 298
Cdd:cd07107 184 TAGAaLVRHPdVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAaVAGMNFTWCGQSCGSTS 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 299 YVLCSPHTRERLLPALQSAITRFYGEDPRR-SPSLGRVVSDKHFRRLRGLLGCG-----RVAIGGQSDEDER-----YIA 367
Cdd:cd07107 264 RLFVHESIYDEVLARVVERVAAIKVGDPTDpATTMGPLVSRQQYDRVMHYIDSAkregaRLVTGGGRPEGPAleggfYVE 343
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1886245108 368 PTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRRE 409
Cdd:cd07107 344 PTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVE 385
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
62-420 |
4.71e-44 |
|
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: 160.47 E-value: 4.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFES--EVSEihisqsEIDLALRNLRSWMKDEKVPK 139
Cdd:cd07124 79 RAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEAdaDVAE------AIDFLEYYAREMLRLRGFPV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 140 NLATQLDSaFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRY-LDQSCFAVVLG 218
Cdd:cd07124 153 EMVPGEDN-RYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAgLPPGVVNFLPG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 219 GPQETGQ-LLEH-KFDYIFFTGSPRVGRIVMTAAAK------HLTPVTLELGGKNPCYVDDDCDPQTVANRV--AWFRYf 288
Cdd:cd07124 232 PGEEVGDyLVEHpDVRFIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGKNAIIVDEDADLDEAAEGIvrSAFGF- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 289 nCGQTCVAPD--YVLCSPHTR--ERLLPALQSAITrfyGEDPRRSPSLGRVVSDKHFRRLRGLL----GCGRVAIGGQSD 360
Cdd:cd07124 311 -QGQKCSACSrvIVHESVYDEflERLVERTKALKV---GDPEDPEVYMGPVIDKGARDRIRRYIeigkSEGRLLLGGEVL 386
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1886245108 361 EDER---YIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRS 420
Cdd:cd07124 387 ELAAegyFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRS 449
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
62-420 |
5.27e-44 |
|
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: 159.78 E-value: 5.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAG--RTRSPEFRAAQLKGLGRFLQENKqllqEALAQdlhkstFESEVSEIHISQSEIDLA--------LRNLRSW 131
Cdd:cd07119 45 RRAFDSGewPHLPAQERAALLFRIADKIREDA----EELAR------LETLNTGKTLRESEIDIDdvancfryYAGLATK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 132 MKDEKVPKNLATQldsAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTE----KVLAEV-LPR 206
Cdd:cd07119 115 ETGEVYDVPPHVI---SRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTialfELIEEAgLPA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 207 yldqSCFAVVLGGPQETGQ-LLEHK-FDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAW 284
Cdd:cd07119 192 ----GVVNLVTGSGATVGAeLAESPdVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALN 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 285 FRYFNCGQTCVAPDYVLCSPHTRERLLPAL---QSAITRFYGEDPRrsPSLGRVVSDKHFRRLRGLLGCG-----RVAIG 356
Cdd:cd07119 268 GVFFNAGQVCSAGSRLLVEESIHDKFVAALaerAKKIKLGNGLDAD--TEMGPLVSAEHREKVLSYIQLGkeegaRLVCG 345
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1886245108 357 GQSDEDER-----YIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRS 420
Cdd:cd07119 346 GKRPTGDElakgyFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKD 414
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
62-420 |
9.05e-44 |
|
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: 158.91 E-value: 9.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAG--RTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESevseihiSQSEIDLALRNLRS---WMK--D 134
Cdd:cd07091 51 RAAFETGwwRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEES-------AKGDVALSIKCLRYyagWADkiQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 135 EKVPKNLATQLdsAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPryldQSCFA 214
Cdd:cd07091 124 GKTIPIDGNFL--AYTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIK----EAGFP 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 215 -----VVLG-GPQETGQLLEH-KFDYIFFTGSPRVGRIVMTAAAK-HLTPVTLELGGKNPCYVDDDCDPQTVANrVAWFR 286
Cdd:cd07091 198 pgvvnIVPGfGPTAGAAISSHmDVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVE-WAAFG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 287 -YFNCGQTCVAPDYVLCSPHTRERLLPALQSAITRFYGEDP-RRSPSLGRVVSDKHFRRLRGLLGCG-----RVAIGGQS 359
Cdd:cd07091 277 iFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPfDPDTFQGPQVSKAQFDKILSYIESGkkegaTLLTGGER 356
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1886245108 360 DEDERY-IAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRS 420
Cdd:cd07091 357 HGSKGYfIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKD 418
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
49-409 |
2.48e-43 |
|
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: 157.73 E-value: 2.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 49 PRMDPLaDTLQRLREAFSAGR----TRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESEvSEIHISQSEID-- 122
Cdd:cd07082 33 PALSAL-EILEAAETAYDAGRgwwpTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDAL-KEVDRTIDYIRdt 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 123 -LALRNL-RSWMKDEKVPKNLATQldsAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSrsteKVL 200
Cdd:cd07082 111 iEELKRLdGDSLPGDWFPGTKGKI---AQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQG----VLL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 201 AEVLPRYLDQSCF-----AVVLGGPQETGQ-LLEH-KFDYIFFTGSPRVGRIVMTAAAKhlTPVTLELGGKNPCYVDDDC 273
Cdd:cd07082 184 GIPLAEAFHDAGFpkgvvNVVTGRGREIGDpLVTHgRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 274 DPQTVANRVAWFRY-FNcGQTCVAPDYVLCSPHTRERLLPALQSAITRFYGEDPRR-SPSLGRVVSDKHFRRLRGLL--- 348
Cdd:cd07082 262 DLELAAKEIVKGALsYS-GQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDnGVDITPLIDPKSADFVEGLIdda 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1886245108 349 ---GcGRVAIGGQSdEDERYIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRRE 409
Cdd:cd07082 341 vakG-ATVLNGGGR-EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSN 402
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
58-406 |
2.50e-43 |
|
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: 157.37 E-value: 2.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 58 LQRLREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKStfesevseIHISQSEIDLALRNLR------SW 131
Cdd:cd07149 27 IAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKP--------IKDARKEVDRAIETLRlsaeeaKR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 132 MKDEKVPknlatqLDS--------AFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEV 203
Cdd:cd07149 99 LAGETIP------FDAspggegriGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 204 LPR-YLDQSCFAVVLGGPQETG-QLLEHK-FDYIFFTGSPRVGRIVMTAAAkhLTPVTLELGGKNPCYVDDDCDPQTVAN 280
Cdd:cd07149 173 LLEaGLPKGALNVVTGSGETVGdALVTDPrVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEKAVE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 281 RVAWFRYFNCGQTCVAPDYVLCSPHTRERLLPALQSAITRFYGEDPR-RSPSLGRVVSDKHFRRLRGLL-----GCGRVA 354
Cdd:cd07149 251 RCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLdEDTDVGPMISEAEAERIEEWVeeaveGGARLL 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1886245108 355 IGGQsdEDERYIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFIN 406
Cdd:cd07149 331 TGGK--RDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMAN 380
|
|
| ABALDH |
TIGR03374 |
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1. ... |
64-419 |
3.23e-43 |
|
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1.35), also called gamma-aminobutyraldehyde dehydrogenase. This enzyme can follow putrescine transaminase (EC 2.6.1.82) for a two-step conversion of putrescine to gamma-aminobutyric acid (GABA). The member from Escherichia coli is characterized as a homotetramer that binds one NADH per momomer. This enzyme belongs to the medium-chain aldehyde dehydrogenases, and is quite similar in sequence to the betaine aldehyde dehydrogenase (EC 1.2.1.8) family.
Pssm-ID: 132417 Cd Length: 472 Bit Score: 157.47 E-value: 3.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 64 AFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHK---STFESEVSEIhisqseIDL------ALRNLRSWMKD 134
Cdd:TIGR03374 50 AFAEWGQTTPKARAECLLKLADVIEENAQVFAELESRNCGKplhSVFNDEIPAI------VDVfrffagAARCLSGLAAG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 135 EKVPKNlatqldSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRYLDQSCFA 214
Cdd:TIGR03374 124 EYLEGH------TSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVVN 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 215 VVLGGPQETGQLL--EHKFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQ 292
Cdd:TIGR03374 198 ILFGRGKTVGDPLtgHEKVRMVSLTGSIATGEHILSHTAPSIKRTHMELGGKAPVIVFDDADIDAVVEGVRTFGFYNAGQ 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 293 TCVAPDYVLCSPHTRERLLPALQSAITRFYGEDPR-RSPSLGRVVSDKHFRRLRGL------LGCGRVAIGGQSDEDE-R 364
Cdd:TIGR03374 278 DCTAACRIYAQRGIYDTLVEKLGAAVATLKSGAPDdESTELGPLSSLAHLERVMKAveeakaLGHIKVITGGEKRKGNgY 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1886245108 365 YIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSR 419
Cdd:TIGR03374 358 YFAPTLLAGAKQDDAIVQKEVFGPVVSITSFDDEEQVVNWANDSQYGLASSVWTK 412
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
62-406 |
7.05e-43 |
|
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: 156.05 E-value: 7.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESEVsEIHISQSEIDLALRNLRSwMKDEKVPKNL 141
Cdd:cd07094 31 RAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV-EVDRAIDTLRLAAEEAER-IRGEEIPLDA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 142 ATQLDS--AFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVL-PRYLDQSCFAVVLG 218
Cdd:cd07094 109 TQGSDNrlAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILvEAGVPEGVLQVVTG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 219 GPQETGQLL--EHKFDYIFFTGSPRVGRIVMTAAAKhlTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTCVA 296
Cdd:cd07094 189 EREVLGDAFaaDERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCIS 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 297 PDYVLCSPHTRERLLPALQSAITRFYGEDPRRSPS-LGRVVSDKHFRRL-----RGLLGCGRVAIGGQsdEDERYIAPTV 370
Cdd:cd07094 267 VQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTdVGPLISEEAAERVerwveEAVEAGARLLCGGE--RDGALFKPTV 344
|
330 340 350
....*....|....*....|....*....|....*.
gi 1886245108 371 LVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFIN 406
Cdd:cd07094 345 LEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIAN 380
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
62-409 |
2.03e-42 |
|
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: 155.37 E-value: 2.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKsTFESEVSEIHISQSEIDLALrNLRSWMKDEKVPkNL 141
Cdd:cd07085 48 KAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGK-TLADARGDVLRGLEVVEFAC-SIPHLLKGEYLE-NV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 142 ATQLDSAFIRkEPFGLVLIIAPWNYPVnltLVPL---VGALAAGNCVVLKPSEFSRSTEKVLAEV-----LPRyldqSCF 213
Cdd:cd07085 125 ARGIDTYSYR-QPLGVVAGITPFNFPA---MIPLwmfPMAIACGNTFVLKPSERVPGAAMRLAELlqeagLPD----GVL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 214 AVVLGGPQETGQLLEH-KFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQ 292
Cdd:cd07085 197 NVVHGGKEAVNALLDHpDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 293 TCVAPDYVLCSPHTRERLLPALQSAITRF---YGEDPRrsPSLGRVVSDKHFRRLRGLLGCG-----RVAIGGQSD---- 360
Cdd:cd07085 277 RCMALSVAVAVGDEADEWIPKLVERAKKLkvgAGDDPG--ADMGPVISPAAKERIEGLIESGveegaKLVLDGRGVkvpg 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1886245108 361 -EDERYIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRRE 409
Cdd:cd07085 355 yENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANP 404
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
149-409 |
4.33e-42 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 152.97 E-value: 4.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 149 FIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRY-LDQSCFAVVLGGPQETGQLL 227
Cdd:PRK10090 66 LLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQEL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 228 --EHKFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTCVAPD--YVLCS 303
Cdd:PRK10090 146 agNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAErvYVQKG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 304 PHTR--ERLLPALqSAITrfYGeDP--RRSPSLGRVVSDKHFRRLRGLLG-----CGRVAIGGQSDEDERYI-APTVLVD 373
Cdd:PRK10090 226 IYDQfvNRLGEAM-QAVQ--FG-NPaeRNDIAMGPLINAAALERVEQKVAraveeGARVALGGKAVEGKGYYyPPTLLLD 301
|
250 260 270
....*....|....*....|....*....|....*.
gi 1886245108 374 VQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRRE 409
Cdd:PRK10090 302 VRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSD 337
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
55-406 |
5.38e-42 |
|
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: 153.67 E-value: 5.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 55 ADTLQRLREAF-SAGRTRSP---EFRAAQLKGLGRFLQENKqllqEALAQDLhksTFESEVSEIHiSQSEIDLALRNLRS 130
Cdd:cd07146 17 AGTEEALREALaLAASYRSTltrYQRSAILNKAAALLEARR----EEFARLI---TLESGLCLKD-TRYEVGRAADVLRF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 131 WMKD------EKVPKNLATQLDS--AFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAE 202
Cdd:cd07146 89 AAAEalrddgESFSCDLTANGKArkIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLAD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 203 VLPRY-LDQSCFAVVLGGPQETGQLLEH--KFDYIFFTGSPRVG-RIVMTAAAKHLtpvTLELGGKNPCYVDDDCDPQTV 278
Cdd:cd07146 169 LLYEAgLPPDMLSVVTGEPGEIGDELIThpDVDLVTFTGGVAVGkAIAATAGYKRQ---LLELGGNDPLIVMDDADLERA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 279 ANRVAWFRYFNCGQTCVAPDYVLCSPHTRERLLPALQSAITRFYGEDPRRSPS-LGRVVSDKHFRRLRGL----LGCG-R 352
Cdd:cd07146 246 ATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATdMGTVIDEEAAIQIENRveeaIAQGaR 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1886245108 353 VAIGGQsdEDERYIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFIN 406
Cdd:cd07146 326 VLLGNQ--RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISN 377
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
62-416 |
6.19e-42 |
|
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: 154.14 E-value: 6.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAF-SAGRTRSPEFRAAQLKGLGRFLQENKqllqEALAQdlhKSTFESEVSeIHISQS-EIDLALRNLR---SWMKdeK 136
Cdd:cd07113 47 WRAFvSAWAKTTPAERGRILLRLADLIEQHG----EELAQ---LETLCSGKS-IHLSRAfEVGQSANFLRyfaGWAT--K 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 137 VP-KNLATQLDS-------AFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEV----- 203
Cdd:cd07113 117 INgETLAPSIPSmqgerytAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELakeag 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 204 LPryldQSCFAVVLGGPQETGQLLEH-KFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRV 282
Cdd:cd07113 197 IP----DGVLNVVNGKGAVGAQLISHpDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 283 AWFRYFNCGQTCVAPDYVLCSPHTRERLLPALQSAITRFYGEDP-RRSPSLGRVVSDKHFRRLRGLLGCGR------VAI 355
Cdd:cd07113 273 LTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPmDESVMFGPLANQPHFDKVCSYLDDARaegdeiVRG 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1886245108 356 GGQSDEDERYIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINrrEKPLALYA 416
Cdd:cd07113 353 GEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLIN--DTPFGLTA 411
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
148-419 |
1.02e-41 |
|
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: 153.72 E-value: 1.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 148 AFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRY-LDQSCFAVVLGGPQETGQ- 225
Cdd:cd07144 138 AYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVNIIPGYGAVAGSa 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 226 LLEH-KFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTCVAPDYVLCSP 304
Cdd:cd07144 218 LAEHpDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 305 HTRERLLPALQSAITRFY--GEDPRRSPSLGRVVSDKHFRRLRGLLGCGR------VAIG---GQSDEDERYIAPTVLVD 373
Cdd:cd07144 298 SIYDKFVEKFVEHVKQNYkvGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKkegaklVYGGekaPEGLGKGYFIPPTIFTD 377
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1886245108 374 VQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSR 419
Cdd:cd07144 378 VPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTK 423
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
49-420 |
4.17e-41 |
|
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: 151.31 E-value: 4.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 49 PRMDP--LADTLQRLREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEaLAQdlhkstFESEVSEIHISQSEIDLAL- 125
Cdd:cd07101 13 PQSTPadVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLD-LIQ------LETGKARRHAFEEVLDVAIv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 126 -----RNLRSWMKDEKVPKNLATqLDSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVL 200
Cdd:cd07101 86 aryyaRRAERLLKPRRRRGAIPV-LTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 201 AEV-----LPRYLdqscFAVVLGGPQETGQLLEHKFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDP 275
Cdd:cd07101 165 VELlieagLPRDL----WQVVTGPGSEVGGAIVDNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 276 QTVAnRVAWFRYF-NCGQTCVAPD--YVLCSPHTR--ERLLPALQSAITrfyGEDPRRSPSLGRVVSDKHFRRLRGLLGC 350
Cdd:cd07101 241 DKAA-AGAVRACFsNAGQLCVSIEriYVHESVYDEfvRRFVARTRALRL---GAALDYGPDMGSLISQAQLDRVTAHVDD 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1886245108 351 GR-----VAIGGQSDED--ERYIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRS 420
Cdd:cd07101 317 AVakgatVLAGGRARPDlgPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRD 393
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
148-419 |
4.89e-41 |
|
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: 151.91 E-value: 4.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 148 AFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRY-LDQSCFAVVLGGPQETGQL 226
Cdd:cd07143 138 TYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGYGRTCGNA 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 227 LE-H-KFDYIFFTGSPRVGRIVMTAAAK-HLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTCVAPDYVLCS 303
Cdd:cd07143 218 ISsHmDIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQ 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 304 PHTRERLLPALQSAITRF-----YGEDPRRSPSlgrvVSDKHFRRLRGLLGCGR-----VAIGGQSDEDERY-IAPTVLV 372
Cdd:cd07143 298 EGIYDKFVKRFKEKAKKLkvgdpFAEDTFQGPQ----VSQIQYERIMSYIESGKaegatVETGGKRHGNEGYfIEPTIFT 373
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1886245108 373 DVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSR 419
Cdd:cd07143 374 DVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTN 420
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
57-406 |
1.07e-39 |
|
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: 148.10 E-value: 1.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 57 TLQRLREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFES--EVSE-IHISqseiDLALRNLRSwMK 133
Cdd:cd07086 40 AVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGlgEVQEmIDIC----DYAVGLSRM-LY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 134 DEKVPKNLATQldSAFIRKEPFGLVLIIAPWNYPV-----NLTLvplvgALAAGNCVVLKPSE----FSRSTEKVLAEVL 204
Cdd:cd07086 115 GLTIPSERPGH--RLMEQWNPLGVVGVITAFNFPVavpgwNAAI-----ALVCGNTVVWKPSEttplTAIAVTKILAEVL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 205 PRY-LDQSCFAVVLGGpQETGQLLEH--KFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANR 281
Cdd:cd07086 188 EKNgLPPGVVNLVTGG-GDGGELLVHdpRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 282 VAWFRYFNCGQTCVApdyvlcsphTR-----ERLLPALQSAITRFYGE----DPRRSPSL-GRVVSDKHFRR-LRGL--- 347
Cdd:cd07086 267 VLFAAVGTAGQRCTT---------TRrlivhESVYDEFLERLVKAYKQvrigDPLDEGTLvGPLINQAAVEKyLNAIeia 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1886245108 348 --LGcGRVAIGG---QSDEDERYIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFIN 406
Cdd:cd07086 338 ksQG-GTVLTGGkriDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINN 400
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
149-422 |
9.06e-39 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 145.99 E-value: 9.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 149 FIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRY-LDQSCFAVVLGGPQETGQLL 227
Cdd:PLN02278 155 LVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAgIPPGVLNVVMGDAPEIGDAL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 228 --EHKFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTCVAPDYVLCSPH 305
Cdd:PLN02278 235 laSPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEG 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 306 TRERLLPALQSAITRF-YGEDPRRSPSLGRVVSDKHFRRLRG------------LLGCGRVAIGGQsdederYIAPTVLV 372
Cdd:PLN02278 315 IYDKFAEAFSKAVQKLvVGDGFEEGVTQGPLINEAAVQKVEShvqdavskgakvLLGGKRHSLGGT------FYEPTVLG 388
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1886245108 373 DVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRSSQ 422
Cdd:PLN02278 389 DVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQ 438
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
148-419 |
9.22e-39 |
|
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: 145.14 E-value: 9.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 148 AFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRY-LDQSCFAVVLGGpQETGQL 226
Cdd:cd07090 110 AYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAgLPDGVFNVVQGG-GETGQL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 227 LEHKFDY--IFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTCVAPDYVL--- 301
Cdd:cd07090 189 LCEHPDVakVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFvqr 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 302 -CSPHTRERLLPALQS-AITRFYGEDPRrspsLGRVVSDKHFRRLRGLLGCG-----RVAIGGQSDEDER------YIAP 368
Cdd:cd07090 269 sIKDEFTERLVERTKKiRIGDPLDEDTQ----MGALISEEHLEKVLGYIESAkqegaKVLCGGERVVPEDglengfYVSP 344
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1886245108 369 TVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSR 419
Cdd:cd07090 345 CVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTR 395
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
62-406 |
3.41e-38 |
|
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: 143.18 E-value: 3.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESEvSEIHISQSEIDLALRNLrswmkDEKV-PKN 140
Cdd:cd07095 10 RAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQ-TEVAAMAGKIDISIKAY-----HERTgERA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 141 LATQLDSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVL-PRYLDQSCFAVVLGG 219
Cdd:cd07095 84 TPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWeEAGLPPGVLNLVQGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 220 PQETGQLLEHK-FDYIFFTGSPRVGRIVMTAAAKHltP---VTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTCV 295
Cdd:cd07095 164 RETGEALAAHEgIDGLLFTGSAATGLLLHRQFAGR--PgkiLALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 296 APDYVLCSPHTR-ERLLPALQSAITRFYGEDPRRSPS-LGRVVSDKHFRRlrGLLGCGR-VAIGGQS-------DEDERY 365
Cdd:cd07095 242 CARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPfMGPLIIAAAAAR--YLLAQQDlLALGGEPllamerlVAGTAF 319
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1886245108 366 IAPTvLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFIN 406
Cdd:cd07095 320 LSPG-IIDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALAN 359
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
58-419 |
5.75e-38 |
|
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: 143.85 E-value: 5.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 58 LQRLREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFES--EVSEihisqsEIDLALRNLRSWMKDE 135
Cdd:TIGR01237 75 LQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEAdaEVAE------AIDFMEYYARQMIELA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 136 KVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRY-LDQSCFA 214
Cdd:TIGR01237 149 KGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAgLPKGVVQ 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 215 VVLGGPQETGQ-LLEH-KFDYIFFTGSPRVG-RIVMTAA-----AKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFR 286
Cdd:TIGR01237 229 FVPGSGSEVGDyLVDHpKTSLITFTGSREVGtRIFERAAkvqpgQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 287 YFNCGQTCVAPD--YVLCSPHTR--ERLLPALQSAITrfyGEDPRRSPSLGRVVSDKHFRRLRGLLGCG----RVAIGGQ 358
Cdd:TIGR01237 309 FGFAGQKCSAGSraVVHEKVYDEvvERFVEITESLKV---GPPDSADVYVGPVIDQKSFNKIMEYIEIGkaegRLVSGGC 385
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1886245108 359 SDEDERY-IAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPL--ALYAFSR 419
Cdd:TIGR01237 386 GDDSKGYfIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLtgGVISNNR 449
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
153-419 |
1.48e-37 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 142.77 E-value: 1.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 153 EPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRY-LDQSCFAVVLGGPQETGQ-LLEH- 229
Cdd:PRK03137 170 IPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAgLPAGVVNFVPGSGSEVGDyLVDHp 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 230 KFDYIFFTGSPRVGRIVMTAAAK------HLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTCVAP------ 297
Cdd:PRK03137 250 KTRFITFTGSREVGLRIYERAAKvqpgqiWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACsraivh 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 298 ----DYVLcsphtrERLLpALQSAITRFYGEDPrrsPSLGRVVSDKHFRRLRGLL----GCGRVAIGGQSDEDERY-IAP 368
Cdd:PRK03137 330 edvyDEVL------EKVV-ELTKELTVGNPEDN---AYMGPVINQASFDKIMSYIeigkEEGRLVLGGEGDDSKGYfIQP 399
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1886245108 369 TVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPL--ALYAFSR 419
Cdd:PRK03137 400 TIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLtgAVISNNR 452
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
53-420 |
7.07e-37 |
|
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: 140.13 E-value: 7.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 53 PLAdTLQRLREAFSAGR-------TRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLH----KSTFESEVSeIHISQSEI 121
Cdd:cd07151 27 PAA-SKEDVDEAYRAAAaaqkewaATLPQERAEILEKAAQILEERRDEIVEWLIRESGstriKANIEWGAA-MAITREAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 122 DLALRnlrswMKDEKVPKNLATQldSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVL- 200
Cdd:cd07151 105 TFPLR-----MEGRILPSDVPGK--ENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGLLl 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 201 AEVLPRY-LDQSCFAVVLGGPQETG-QLLEHKF-DYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQT 277
Cdd:cd07151 178 AKIFEEAgLPKGVLNVVVGAGSEIGdAFVEHPVpRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 278 VANRVAWFRYFNCGQTCVAPDYVLCSPHTRERLLPALQSAITRF-YGeDPRRSPSL-GRVVSDKHFRRLRGLL------G 349
Cdd:cd07151 258 AVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALpYG-DPSDPDTVvGPLINESQVDGLLDKIeqaveeG 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1886245108 350 cGRVAIGGqsDEDERYIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRS 420
Cdd:cd07151 337 -ATLLVGG--EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSD 404
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
148-419 |
3.94e-36 |
|
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: 138.25 E-value: 3.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 148 AFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAE-------------VLPRYldqscfa 214
Cdd:cd07141 139 TYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASlikeagfppgvvnVVPGY------- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 215 vvlgGPQETGQLLEH-KFDYIFFTGSPRVGRIVMTAAAK-HLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQ 292
Cdd:cd07141 212 ----GPTAGAAISSHpDIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQ 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 293 TCVAPDYVLC-SPHTRERLLPALQSAITRFYGeDPRRSPSL-GRVVSDKHFRRLRGLLGCG-----RVAIGGQSDEDERY 365
Cdd:cd07141 288 CCCAGSRTFVqESIYDEFVKRSVERAKKRVVG-NPFDPKTEqGPQIDEEQFKKILELIESGkkegaKLECGGKRHGDKGY 366
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1886245108 366 -IAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSR 419
Cdd:cd07141 367 fIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTK 421
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
152-419 |
2.18e-35 |
|
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: 136.08 E-value: 2.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 152 KEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTE----KVLAEV-LPryldQSCFAVVLG-GPQETGQ 225
Cdd:cd07142 139 HEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSAllaaKLAAEAgLP----DGVLNIVTGfGPTAGAA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 226 LLEHK-FDYIFFTGSPRVGRIVMTAAAK-HLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTCVAPDYVLCs 303
Cdd:cd07142 215 IASHMdVDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFV- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 304 pHTR---ERLLPALQSAITRFYGEDPRRSPSLGRVVSDKHFRRLRGLLGCGR------VAIGGQSDEDERYIAPTVLVDV 374
Cdd:cd07142 294 -HESiydEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGKeegatlITGGDRIGSKGYYIQPTIFSDV 372
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1886245108 375 QETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSR 419
Cdd:cd07142 373 KDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSK 417
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
48-413 |
2.22e-35 |
|
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: 135.99 E-value: 2.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 48 PPRMDPLADTLQ----RLREAFSAGRTRSPEF-------RAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESEvseihi 116
Cdd:cd07111 44 PATGEVLASVLQaeeeDVDAAVAAARTAFESWsalpghvRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESR------ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 117 sQSEIDLALRNLR---SWmkdekvpknlATQLDSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFS 193
Cdd:cd07111 118 -DCDIPLVARHFYhhaGW----------AQLLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 194 RSTEKVLAEVLPRY-LDQSCFAVVLGGPQETGQLLEH-KFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDD 271
Cdd:cd07111 187 PLTALLFAEICAEAgLPPGVLNIVTGNGSFGSALANHpGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 272 DCDPQTVANRVAWFRYFNCGQTCVAPDYVLCSPHTRERLLPALQSAITRFYGEDP-RRSPSLGRVVSDKHFRRLRGLLGC 350
Cdd:cd07111 267 DADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPlDKAIDMGAIVDPAQLKRIRELVEE 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1886245108 351 GRV--AIGGQSD----EDERYIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLA 413
Cdd:cd07111 347 GRAegADVFQPGadlpSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLA 415
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
62-419 |
6.98e-35 |
|
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: 134.39 E-value: 6.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAGR-TRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESEVsEIHISQSEID----LAlRNLRSWMKDEK 136
Cdd:cd07120 29 RRAFDETDwAHDPRLRARVLLELADAFEANAERLARLLALENGKILGEARF-EISGAISELRyyagLA-RTEAGRMIEPE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 137 vPKNLATQLdsafirKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPR--YLDQSCFA 214
Cdd:cd07120 107 -PGSFSLVL------REPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEipSLPAGVVN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 215 VVLGGPQETGQLL--EHKFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQ 292
Cdd:cd07120 180 LFTESGSEGAAHLvaSPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 293 TCVAPDYVLC----SPHTRERLLPALQsAITRFYGEDPrrSPSLGRVVSDKHFRRLRGLLG-----CGRVAI-GGQSDED 362
Cdd:cd07120 260 FCMAGSRVLVqrsiADEVRDRLAARLA-AVKVGPGLDP--ASDMGPLIDRANVDRVDRMVEraiaaGAEVVLrGGPVTEG 336
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 363 ER---YIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSR 419
Cdd:cd07120 337 LAkgaFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTR 396
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
154-406 |
7.57e-35 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 135.39 E-value: 7.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 154 PFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSefSRSTEKVLAEV-------LPRYLdqscFAVVLGGPQETGQL 226
Cdd:PRK09407 154 PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPD--SQTPLTALAAVellyeagLPRDL----WQVVTGPGPVVGTA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 227 LEHKFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTCVAPD--YVLCSp 304
Cdd:PRK09407 228 LVDNADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIEriYVHES- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 305 hTRERLLPALQSAITRF-YGEDPRRSPSLGRVVSDKHFRRLRGLLGCGR-----VAIGGQSDED--ERYIAPTVLVDVQE 376
Cdd:PRK09407 307 -IYDEFVRAFVAAVRAMrLGAGYDYSADMGSLISEAQLETVSAHVDDAVakgatVLAGGKARPDlgPLFYEPTVLTGVTP 385
|
250 260 270
....*....|....*....|....*....|
gi 1886245108 377 TEPVMQEEIFGPILPIVNVGSLDEAIDFIN 406
Cdd:PRK09407 386 DMELAREETFGPVVSVYPVADVDEAVERAN 415
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
152-413 |
1.56e-34 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 134.18 E-value: 1.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 152 KEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRY-LDQSCFAVVLG-GPQETGQLLEH 229
Cdd:PLN02766 156 KEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAgVPDGVINVVTGfGPTAGAAIASH 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 230 -KFDYIFFTGSPRVGRIVMTAAAK-HLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTCVAPDYVLCSPHTR 307
Cdd:PLN02766 236 mDVDKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIY 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 308 ERLLPALQSAITRFYGEDPRRSPS-LGRVVSDKHFRRLRGLLGCGR-----VAIGGQSDEDERY-IAPTVLVDVQETEPV 380
Cdd:PLN02766 316 DEFVKKLVEKAKDWVVGDPFDPRArQGPQVDKQQFEKILSYIEHGKregatLLTGGKPCGDKGYyIEPTIFTDVTEDMKI 395
|
250 260 270
....*....|....*....|....*....|...
gi 1886245108 381 MQEEIFGPILPIVNVGSLDEAIDFINRREKPLA 413
Cdd:PLN02766 396 AQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLA 428
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
63-417 |
4.24e-34 |
|
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: 131.98 E-value: 4.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 63 EAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHK--STFESEV----SEIHISQSEidlALRNLRSWMKDEK 136
Cdd:cd07147 32 KAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKpiKDARGEVaraiDTFRIAAEE---ATRIYGEVLPLDI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 137 VPKNLATQldsAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRY-LDQSCFAV 215
Cdd:cd07147 109 SARGEGRQ---GLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETgLPKGAFSV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 216 VLGGPQETGQLLEHK-FDYIFFTGSPRVGRIVMTAAAKHltPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTC 294
Cdd:cd07147 186 LPCSRDDADLLVTDErIKLLSFTGSPAVGWDLKARAGKK--KVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSC 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 295 VAPDYVLCSPHTRERLLPALQSAITRFYGEDPRRSPS-LGRVVSDKHFRRLRGLL-----GCGRVAIGGQSDEDerYIAP 368
Cdd:cd07147 264 ISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATdVGPMISESEAERVEGWVneavdAGAKLLTGGKRDGA--LLEP 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 369 TVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINR-----------REKPLALYAF 417
Cdd:cd07147 342 TILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDskfglqagvftRDLEKALRAW 401
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
62-420 |
9.74e-34 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 131.94 E-value: 9.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAG--RTRSPEFRAAQLKGLGRFLQENKQLLqeALAQdlhksTFESEVSEIHISQSEIDLALRNLRsWMKD--EKV 137
Cdd:PRK09847 67 RGVFERGdwSLSSPAKRKAVLNKLADLMEAHAEEL--ALLE-----TLDTGKPIRHSLRDDIPGAARAIR-WYAEaiDKV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 138 PKNLATQLDS--AFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRY-LDQSCFA 214
Cdd:PRK09847 139 YGEVATTSSHelAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLN 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 215 VVLGGPQETGQLL--EHKFDYIFFTGSPRVGRIVMT-AAAKHLTPVTLELGGKNPCYVDDDC-DPQTVANRVAWFRYFNC 290
Cdd:PRK09847 219 VVTGFGHEAGQALsrHNDIDAIAFTGSTRTGKQLLKdAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 291 GQTCVAPDYVLCSPHTRERLLPALQSAITRFYGEDP-RRSPSLGRVVSDKH----FRRLRGLLGCGRVAIGGQSDEDERY 365
Cdd:PRK09847 299 GQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPlDPATTMGTLIDCAHadsvHSFIREGESKGQLLLDGRNAGLAAA 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1886245108 366 IAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRS 420
Cdd:PRK09847 379 IGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRD 433
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
58-406 |
1.57e-31 |
|
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: 125.26 E-value: 1.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 58 LQRLREAFSA-GRTrSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESevseihiSQSEIDLALRNLRSWMKDEK 136
Cdd:cd07116 44 LDAAHAAKEAwGKT-SVAERANILNKIADRMEANLEMLAVAETWDNGKPVRET-------LAADIPLAIDHFRYFAGCIR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 137 VPKNLATQLDS---AFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRYLDQSCF 213
Cdd:cd07116 116 AQEGSISEIDEntvAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 214 AVVLGGPQETGQLL--EHKFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNP-CYVDD--DCDPQTVANRVAWFRYF 288
Cdd:cd07116 196 NVVNGFGLEAGKPLasSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPnIFFADvmDADDAFFDKALEGFVMF 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 289 --NCGQTCVAPDYVLCSPHTRERLLP-ALQ--SAITRFYGEDPrrSPSLGRVVSDKHFRRLRGLLGCGR-----VAIGGQ 358
Cdd:cd07116 276 alNQGEVCTCPSRALIQESIYDRFMErALErvKAIKQGNPLDT--ETMIGAQASLEQLEKILSYIDIGKeegaeVLTGGE 353
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1886245108 359 -----SDEDERYIAPTVLVDVQETEpVMQEEIFGPILPIVNVGSLDEAIDFIN 406
Cdd:cd07116 354 rnelgGLLGGGYYVPTTFKGGNKMR-IFQEEIFGPVLAVTTFKDEEEALEIAN 405
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
49-419 |
4.80e-31 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 124.25 E-value: 4.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 49 PRM--DPLADTLQRLREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESEvSEIHISQSEIDlalr 126
Cdd:PRK11241 43 PKMgaDETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAK-GEISYAASFIE---- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 127 nlrsWMKDEK-------VPKNlatQLDSAFIR-KEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEK 198
Cdd:PRK11241 118 ----WFAEEGkriygdtIPGH---QADKRLIViKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSAL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 199 VLAEVLPRY-LDQSCFAVVLG-----GPQETGQLLEHKFDyifFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDD 272
Cdd:PRK11241 191 ALAELAIRAgIPAGVFNVVTGsagavGGELTSNPLVRKLS---FTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 273 CDPQTVANRVAWFRYFNCGQTCVAPDYVLCSPHTRERLLPALQSAITRFY-GEDPRRSPSLGRVVSDKHFRRLR-----G 346
Cdd:PRK11241 268 ADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHiGDGLEKGVTIGPLIDEKAVAKVEehiadA 347
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1886245108 347 LLGCGRVAIGGQSDEDE-RYIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSR 419
Cdd:PRK11241 348 LEKGARVVCGGKAHELGgNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYAR 421
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
146-420 |
9.66e-31 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 123.07 E-value: 9.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 146 DSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEV-----LPRYLdqscFAVVlGGP 220
Cdd:PRK13252 134 SFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIyteagLPDGV----FNVV-QGD 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 221 QETGQLL-EH-KFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQT------VANrvawfrYFNCGQ 292
Cdd:PRK13252 209 GRVGAWLtEHpDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRaadiamLAN------FYSSGQ 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 293 TCVAPDYVLCSPHTRERLLPALQSAITRFYGEDPR-RSPSLGRVVSDKHFRRLRGLLGCG-----RVAIGGQSDEDER-- 364
Cdd:PRK13252 283 VCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMdPATNFGPLVSFAHRDKVLGYIEKGkaegaRLLCGGERLTEGGfa 362
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1886245108 365 ---YIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRS 420
Cdd:PRK13252 363 ngaFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTAD 421
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
70-419 |
3.78e-30 |
|
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: 121.92 E-value: 3.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 70 TRSP-EFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTfeseVSEIHISQSEIDLALRNLRSWMKDEKVPKNLAT---QL 145
Cdd:cd07083 72 KDWPqEDRARLLLKAADLLRRRRRELIATLTYEVGKNW----VEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPypgED 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 146 DSAFIRkePFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSE----FSRSTEKVLAEV-LPRYLDQSCFAVvlgGP 220
Cdd:cd07083 148 NESFYV--GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEdavvVGYKVFEIFHEAgFPPGVVQFLPGV---GE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 221 QETGQLLEH-KFDYIFFTGSPRVGRIVMTAAAKHLT------PVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQT 293
Cdd:cd07083 223 EVGAYLTEHeRIRGINFTGSLETGKKIYEAAARLAPgqtwfkRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 294 CVAPDYVLCSPHTRERLLPALQSAITRFYGEDPRR-SPSLGRVVSDKHFRRLRGLLGCGR----VAIGGQSDEDERY-IA 367
Cdd:cd07083 303 CSAASRLILTQGAYEPVLERLLKRAERLSVGPPEEnGTDLGPVIDAEQEAKVLSYIEHGKnegqLVLGGKRLEGEGYfVA 382
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1886245108 368 PTVLVDVQETEPVMQEEIFGPILPIVNVGSLD--EAIDFINRREKPLALYAFSR 419
Cdd:cd07083 383 PTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSR 436
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
153-419 |
4.05e-30 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 122.22 E-value: 4.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 153 EPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRY-LDQSCFAVVLG-GPQETGQLLEH- 229
Cdd:PLN02466 194 EPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAgLPPGVLNVVSGfGPTAGAALASHm 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 230 KFDYIFFTGSPRVGRIVMTAAAK-HLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTCVAPD--YVlcspHT 306
Cdd:PLN02466 274 DVDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSrtFV----HE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 307 R---ERLLPALQSAITRFYGEDPRRSPSLGRVVSDKHFRRLRGLL------GCGRVAIGGQSDEDERYIAPTVLVDVQET 377
Cdd:PLN02466 350 RvydEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIksgvesGATLECGGDRFGSKGYYIQPTVFSNVQDD 429
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1886245108 378 EPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSR 419
Cdd:PLN02466 430 MLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQ 471
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
62-419 |
6.59e-30 |
|
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: 121.06 E-value: 6.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAG--RTRSPEFRAAQLKGLGRFLQENKQLLqeALAQDLHKSTFESEVSEIHISQSeIDlALRNLRSW---MKDEK 136
Cdd:cd07140 53 KEAFENGewGKMNARDRGRLMYRLADLMEEHQEEL--ATIESLDSGAVYTLALKTHVGMS-IQ-TFRYFAGWcdkIQGKT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 137 VPKNLA-TQLDSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLPRY-LDQSCFA 214
Cdd:cd07140 129 IPINQArPNRNLTLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAgFPKGVIN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 215 VVLGGPQETGQLLEHKFDY--IFFTGSPRVGRIVMTAAAK-HLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCG 291
Cdd:cd07140 209 ILPGSGSLVGQRLSDHPDVrkLGFTGSTPIGKHIMKSCAVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 292 QTCVAPDYVLCSPHTRERLLPALQSAITRFYGEDP-RRSPSLGRVVSDKHFRRL-----RGLLGCGRVAIGG-QSDEDER 364
Cdd:cd07140 289 ENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPlDRSTDHGPQNHKAHLDKLveyceRGVKEGATLVYGGkQVDRPGF 368
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1886245108 365 YIAPTVLVDVQETEPVMQEEIFGPILPI--VNVGSLDEAIDFINRREKPLALYAFSR 419
Cdd:cd07140 369 FFEPTVFTDVEDHMFIAKEESFGPIMIIskFDDGDVDGVLQRANDTEYGLASGVFTK 425
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
62-406 |
1.90e-25 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 108.12 E-value: 1.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 62 REAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFES--EVSEIhISQSEIDLALRNLRSWMKDEKVPK 139
Cdd:PRK09457 47 RAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAatEVTAM-INKIAISIQAYHERTGEKRSEMAD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 140 NlatqldSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFsrsTEKVLAEVLPRYLDQSCFAVVLG- 218
Cdd:PRK09457 126 G------AAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSEL---TPWVAELTVKLWQQAGLPAGVLNl 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 219 --GPQETGQ-LLEHK-FDYIFFTGSPRVGRIVMTAAAKHltP---VTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCG 291
Cdd:PRK09457 197 vqGGRETGKaLAAHPdIDGLLFTGSANTGYLLHRQFAGQ--PekiLALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 292 Q--TCVAPDYVLCSPHTrERLLPALQSAITRF----YGEDPrrSPSLGRVVSDKHFRRL----RGLLGCGRVAI--GGQS 359
Cdd:PRK09457 275 QrcTCARRLLVPQGAQG-DAFLARLVAVAKRLtvgrWDAEP--QPFMGAVISEQAAQGLvaaqAQLLALGGKSLleMTQL 351
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1886245108 360 DEDERYIAPTvLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFIN 406
Cdd:PRK09457 352 QAGTGLLTPG-IIDVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLAN 397
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
54-406 |
4.80e-25 |
|
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: 106.90 E-value: 4.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 54 LADTLQRLREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKsTFE---SEVSEihisqsEIDLA---LRN 127
Cdd:cd07125 71 VDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGK-TLAdadAEVRE------AIDFCryyAAQ 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 128 LRSWMKDEKVPKNLAtQLDsaFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVL--- 204
Cdd:cd07125 144 ARELFSDPELPGPTG-ELN--GLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLhea 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 205 --PRYLDQscfaVVLGGPQETGQ-LLEHK-FDYIFFTGSPRVGRIVMTAAAKH---LTPVTLELGGKNPCYVDDDCDP-Q 276
Cdd:cd07125 221 gvPRDVLQ----LVPGDGEEIGEaLVAHPrIDGVIFTGSTETAKLINRALAERdgpILPLIAETGGKNAMIVDSTALPeQ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 277 TVANRVA-WFRyfNCGQTCVAPDyVLC-----SPHTRERLLPALQSAITrfyGeDPR-RSPSLGRVVSDKHFRRLRGLLG 349
Cdd:cd07125 297 AVKDVVQsAFG--SAGQRCSALR-LLYlqeeiAERFIEMLKGAMASLKV---G-DPWdLSTDVGPLIDKPAGKLLRAHTE 369
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1886245108 350 CGR-----VAIGGQSDEDERYIAPTVLVDVqeTEPVMQEEIFGPILPIV--NVGSLDEAIDFIN 406
Cdd:cd07125 370 LMRgeawlIAPAPLDDGNGYFVAPGIIEIV--GIFDLTTEVFGPILHVIrfKAEDLDEAIEDIN 431
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
154-406 |
2.47e-23 |
|
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: 101.51 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 154 PFGLVLIIAPWNYPV-----NLTLvplvgALAAGNCVVLKPSE----FSRSTEKVLAEVLPRY-LDQSCFAVVLGGPQET 223
Cdd:cd07130 132 PLGVVGVITAFNFPVavwgwNAAI-----ALVCGNVVVWKPSPttplTAIAVTKIVARVLEKNgLPGAIASLVCGGADVG 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 224 GQLLEHK-FDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTCVApdyvlc 302
Cdd:cd07130 207 EALVKDPrVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTT------ 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 303 sphTR-----ERLLPALQSAITRFYGE----DPRRSPSL-GRVVSDKHFRRLRGLL------GcGRVAIGGQS-DEDERY 365
Cdd:cd07130 281 ---TRrlivhESIYDEVLERLKKAYKQvrigDPLDDGTLvGPLHTKAAVDNYLAAIeeaksqG-GTVLFGGKViDGPGNY 356
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1886245108 366 IAPTVlVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFIN 406
Cdd:cd07130 357 VEPTI-VEGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNN 396
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
76-406 |
8.97e-22 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 97.13 E-value: 8.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 76 RAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESeVSEIHISQSEIDLA----LRNLRS--WMKDEKVPKNLATQLdsAF 149
Cdd:PLN00412 77 RAELLHKAAAILKEHKAPIAECLVKEIAKPAKDA-VTEVVRSGDLISYTaeegVRILGEgkFLVSDSFPGNERNKY--CL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 150 IRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPsefsrsteKVLAEVLPRYLDQsCF----------AVVLGG 219
Cdd:PLN00412 154 TSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKP--------PTQGAVAALHMVH-CFhlagfpkgliSCVTGK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 220 PQETGQLL-EHK-FDYIFFTGSPRVGRIVMTAAakhLTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTCVAP 297
Cdd:PLN00412 225 GSEIGDFLtMHPgVNCISFTGGDTGIAISKKAG---MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAV 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 298 DYVLCSPHTRERLLPALQSAITRFYGEDPRRSPSLGRVVSDKHFRRLRGLLGCGRVAIGGQSDEDER---YIAPTVLVDV 374
Cdd:PLN00412 302 KVVLVMESVADALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKRegnLIWPLLLDNV 381
|
330 340 350
....*....|....*....|....*....|..
gi 1886245108 375 QETEPVMQEEIFGPILPIVNVGSLDEAIDFIN 406
Cdd:PLN00412 382 RPDMRIAWEEPFGPVLPVIRINSVEEGIHHCN 413
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
76-406 |
1.73e-20 |
|
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: 93.25 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 76 RAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESEVsEIHISQSEIDLALRNLRSwMKDEKVPKNLaTQLDS---AFIRK 152
Cdd:cd07148 46 RIAILERLADLMEERADELALLIAREGGKPLVDAKV-EVTRAIDGVELAADELGQ-LGGREIPMGL-TPASAgriAFTTR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 153 EPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFS----RSTEKVLAEV-LPrylDQSCFAVVLGGPQETGQLL 227
Cdd:cd07148 123 EPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATplscLAFVDLLHEAgLP---EGWCQAVPCENAVAEKLVT 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 228 EHKFDYIFFTGSPRVGRIVMTAAAKHlTPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTCVAPDYVLCSPHTR 307
Cdd:cd07148 200 DPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 308 ERLLPALQSAITRFYGEDP-RRSPSLGRVVSDKHFRRLR-----GLLGCGRVAIGGQSDEDERYiAPTVLVDVQETEPVM 381
Cdd:cd07148 279 DDFAQRLAAAAEKLVVGDPtDPDTEVGPLIRPREVDRVEewvneAVAAGARLLCGGKRLSDTTY-APTVLLDPPRDAKVS 357
|
330 340
....*....|....*....|....*
gi 1886245108 382 QEEIFGPILPIVNVGSLDEAIDFIN 406
Cdd:cd07148 358 TQEIFGPVVCVYSYDDLDEAIAQAN 382
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
61-395 |
5.72e-20 |
|
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: 91.53 E-value: 5.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 61 LREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFESEVSEIHISQSEIDLALRNLRS------WMKD 134
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAfviysyRIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 135 EKV-PKNLATQLDSAFIRKePFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLpRY---LDQ 210
Cdd:cd07084 81 EPGnHLGQGLKQQSHGYRW-PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLL-HYaglLPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 211 SCFAVVLGGPQETGQLLEH-KFDYIFFTGSPRVGRIVMTAAakHLTPVTLELGGKNPCYVDDDCDP-QTVANRVAWFRYF 288
Cdd:cd07084 159 EDVTLINGDGKTMQALLLHpNPKMVLFTGSSRVAEKLALDA--KQARIYLELAGFNWKVLGPDAQAvDYVAWQCVQDMTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 289 NCGQTCVAPD--YVLCSPHTReRLLPALQSAITrfygedpRRSPS---LGRVVSDKHFRRL--RGLLGCGRVAIGGQ--- 358
Cdd:cd07084 237 CSGQKCTAQSmlFVPENWSKT-PLVEKLKALLA-------RRKLEdllLGPVQTFTTLAMIahMENLLGSVLLFSGKelk 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1886245108 359 -SDEDERY---IAPTVLVDVQE---TEPVMQEEIFGPILPIVNV 395
Cdd:cd07084 309 nHSIPSIYgacVASALFVPIDEilkTYELVTEEIFGPFAIVVEY 352
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
52-418 |
3.90e-19 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 89.15 E-value: 3.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 52 DPLADTLQRLREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKStfesevseihISQSEIDLALR-NLRS 130
Cdd:PRK13968 29 DDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKP----------INQARAEVAKSaNLCD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 131 WMKdEKVPKNLATQL-----DSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLP 205
Cdd:PRK13968 99 WYA-EHGPAMLKAEPtlvenQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 206 RY-LDQSCFAVVLGGPQETGQLL-EHKFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVA 283
Cdd:PRK13968 178 DAgIPQGVYGWLNADNDGVSQMInDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 284 WFRYFNCGQTCVAPDYVLCSPHTRERLLPALQSAITRFYGEDPRRSPS-LGRV----VSDKHFRRLRGLLGCG-RVAIGG 357
Cdd:PRK13968 258 AGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENaLGPMarfdLRDELHHQVEATLAEGaRLLLGG 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1886245108 358 QSDEDE-RYIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFS 418
Cdd:PRK13968 338 EKIAGAgNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFT 399
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
141-420 |
4.77e-19 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 89.12 E-value: 4.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 141 LATQLDSAFIRKE-----------PFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLK--PSE--FSRSTEKVLAEVLP 205
Cdd:PLN02315 130 LSRQLNGSIIPSErpnhmmmevwnPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKgaPTTplITIAMTKLVAEVLE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 206 RY-LDQSCFAVVLGGpQETGQLL--EHKFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRV 282
Cdd:PLN02315 210 KNnLPGAIFTSFCGG-AEIGEAIakDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSV 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 283 AWFRYFNCGQTCVAPDYVLCSPHTRERLLPALQSAITRFYGEDPRRSPSLGRVVSDKHFRR--LRGLLGC----GRVAIG 356
Cdd:PLN02315 289 LFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKnfEKGIEIIksqgGKILTG 368
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1886245108 357 GQS-DEDERYIAPTVlVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRREKPLALYAFSRS 420
Cdd:PLN02315 369 GSAiESEGNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRN 432
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
52-406 |
7.90e-18 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 85.17 E-value: 7.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 52 DPLAD-----TLQRLREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKsTFESEVSEIHISQSEIDLALR 126
Cdd:PRK09406 18 TALTDdevdaAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGK-TLASAKAEALKCAKGFRYYAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 127 NLRSWMKDE--KVPKNLATQldsAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVL 204
Cdd:PRK09406 97 HAEALLADEpaDAAAVGASR---AYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 205 PRY-LDQSCFAVVL-GGPQETGQLLEHKFDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRV 282
Cdd:PRK09406 174 RRAgFPDGCFQTLLvGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 283 AWFRYFNCGQTCVAPDYVLCSPHTRERLLPALQSAITRFYGEDP-RRSPSLGRVVS----DKHFRRLRGLLGCG-RVAIG 356
Cdd:PRK09406 254 VTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPtDPDTDVGPLATeqgrDEVEKQVDDAVAAGaTILCG 333
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1886245108 357 GQS-DEDERYIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFIN 406
Cdd:PRK09406 334 GKRpDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIAN 384
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
153-419 |
2.68e-16 |
|
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: 80.72 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 153 EPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFS-----RSTEKVLAEVLPryldQSCFAVVLGGPQETGQLL 227
Cdd:TIGR01238 159 ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTsliayRAVELMQEAGFP----AGTIQLLPGRGADVGAAL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 228 --EHKFDYIFFTGSPRVGRIVMTAAAKHL---TPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTCVAPDYVLC 302
Cdd:TIGR01238 235 tsDPRIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCV 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 303 SPHTRERLLPALQSAITRFYGEDP-RRSPSLGRVVSDK-------HFRRLRGLLGCGRVAIGGQSDEDER--YIAPTV-- 370
Cdd:TIGR01238 315 QEDVADRVLTMIQGAMQELKVGVPhLLTTDVGPVIDAEakqnllaHIEHMSQTQKKIAQLTLDDSRACQHgtFVAPTLfe 394
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1886245108 371 LVDVQEtepvMQEEIFGPILPIV--NVGSLDEAIDFINRREKPLALYAFSR 419
Cdd:TIGR01238 395 LDDIAE----LSEEVFGPVLHVVryKARELDQIVDQINQTGYGLTMGVHSR 441
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
53-409 |
3.18e-16 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 80.56 E-value: 3.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 53 PLAdTLQRLREAFSAGRTRSPEFRAAQLKGLGRFLQENKQLLQEALAQDLHKSTFEsEVSEIHISQSEIDLALR------ 126
Cdd:PLN02419 146 PLT-TNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTE-QGKTLKDSHGDIFRGLEvvehac 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 127 NLRSWMKDEKVPkNLATQLDSAFIRkEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEV-LP 205
Cdd:PLN02419 224 GMATLQMGEYLP-NVSNGVDTYSIR-EPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELaME 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 206 RYLDQSCFAVVLGGPQETGQLLEHK-FDYIFFTGSPRVGRIVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQTVANRVAW 284
Cdd:PLN02419 302 AGLPDGVLNIVHGTNDTVNAICDDEdIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLA 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 285 FRYFNCGQTCVAPDYVLCSPHTR--ERLLPALQSAITRFYGEDPrrSPSLGRVVSDKHFRRLRGLLGCG-----RVAIGG 357
Cdd:PLN02419 382 AGFGAAGQRCMALSTVVFVGDAKswEDKLVERAKALKVTCGSEP--DADLGPVISKQAKERICRLIQSGvddgaKLLLDG 459
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1886245108 358 QS-----DEDERYIAPTVLVDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINRRE 409
Cdd:PLN02419 460 RDivvpgYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNK 516
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
154-406 |
7.43e-13 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 70.77 E-value: 7.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 154 PFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEfsrSTEKVLAEVLpRYLDQScfavvlGGPQETGQLL------ 227
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAE---QTPLIAAQAV-RILLEA------GVPAGVVQLLpgrget 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 228 -------EHKFDYIFFTGSPRVGRIVMTAAAKHL------TPVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTC 294
Cdd:PRK11809 838 vgaalvaDARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRC 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 295 VAPDyVLC-SPHTRERLLPALQSAITRFYGEDPRR-SPSLGRVVS-------DKHFRRLRgllGCGRV---AIGGQSDED 362
Cdd:PRK11809 918 SALR-VLClQDDVADRTLKMLRGAMAECRMGNPDRlSTDIGPVIDaeakaniERHIQAMR---AKGRPvfqAARENSEDW 993
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1886245108 363 ER--YIAPTV--LVDVQEtepvMQEEIFGPILPIV--NVGSLDEAIDFIN 406
Cdd:PRK11809 994 QSgtFVPPTLieLDSFDE----LKREVFGPVLHVVryNRNQLDELIEQIN 1039
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
150-407 |
6.06e-12 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 67.53 E-value: 6.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 150 IRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEfsrSTEKVLAEVLpRYLDQ-----SCFAVVLGGPQETG 224
Cdd:PRK11904 680 LRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAE---QTPLIAAEAV-KLLHEagipkDVLQLLPGDGATVG 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 225 Q-LLEH-KFDYIFFTGSPRVGRIV-MTAAAKHLTPVTL--ELGGKNPCYVDDDCDPQTVANRV---AwFRyfNCGQTCVA 296
Cdd:PRK11904 756 AaLTADpRIAGVAFTGSTETARIInRTLAARDGPIVPLiaETGGQNAMIVDSTALPEQVVDDVvtsA-FR--SAGQRCSA 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 297 PDyVLCSPH-TRERLLPALQSAItrfyGE----DPRR-SPSLGRVVS-------DKHFRRLRGLlgcGRVAIGGQSDEDE 363
Cdd:PRK11904 833 LR-VLFVQEdIADRVIEMLKGAM----AElkvgDPRLlSTDVGPVIDaeakanlDAHIERMKRE---ARLLAQLPLPAGT 904
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1886245108 364 R---YIAPTvLVDVQETEpVMQEEIFGPILPIV--NVGSLDEAIDFINR 407
Cdd:PRK11904 905 EnghFVAPT-AFEIDSIS-QLEREVFGPILHVIryKASDLDKVIDAINA 951
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
178-409 |
1.29e-11 |
|
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: 66.03 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 178 ALAAGNCVVLK--PS--EFSRSTEKVLAEVLPRY-LDQSCFAVVLGGPQETGQ-LLEH-KFDYIFFTGSPRVGRIVMTAA 250
Cdd:cd07129 131 ALAAGCPVVVKahPAhpGTSELVARAIRAALRATgLPAGVFSLLQGGGREVGVaLVKHpAIKAVGFTGSRRGGRALFDAA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 251 AKHLT--PVTLELGGKNPCYVdddcDPQTVANR--------VAWFRyFNCGQTCVAPDYVLcSPHTRErlLPALQSAITR 320
Cdd:cd07129 211 AARPEpiPFYAELGSVNPVFI----LPGALAERgeaiaqgfVGSLT-LGAGQFCTNPGLVL-VPAGPA--GDAFIAALAE 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 321 FYGEDPRR---SPSLGRVVsDKHFRRLRGLLGcGRVAIGGQSDEDERYIAPTVL-VDVQE--TEPVMQEEIFGPILPIVN 394
Cdd:cd07129 283 ALAAAPAQtmlTPGIAEAY-RQGVEALAAAPG-VRVLAGGAAAEGGNQAAPTLFkVDAAAflADPALQEEVFGPASLVVR 360
|
250
....*....|....*
gi 1886245108 395 VGSLDEAIDFINRRE 409
Cdd:cd07129 361 YDDAAELLAVAEALE 375
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
156-390 |
2.13e-11 |
|
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: 65.69 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 156 GLVLIIAPWNYPV---NLTLVPlvgALAaGNCVVLKPSEF----SRSTEKVLAEV-LPRYLDQscFavVLGGPQETGQ-L 226
Cdd:cd07123 172 GFVYAVSPFNFTAiggNLAGAP---ALM-GNVVLWKPSDTavlsNYLVYKILEEAgLPPGVIN--F--VPGDGPVVGDtV 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 227 LEHK-FDYIFFTGSPRVGRIVMTAAAKHLT-----P-VTLELGGKNPCYVDDDCDPQTVAN---RVAwFRYfnCGQTCVA 296
Cdd:cd07123 244 LASPhLAGLHFTGSTPTFKSLWKQIGENLDryrtyPrIVGETGGKNFHLVHPSADVDSLVTatvRGA-FEY--QGQKCSA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 297 pdyvlCS----PHTRE-RLLPALQSAITRFYGEDPRR-SPSLGRVVSDKHFRRLRGLLGCGR------VAIGGQSDEDER 364
Cdd:cd07123 321 -----ASrayvPESLWpEVKERLLEELKEIKMGDPDDfSNFMGAVIDEKAFDRIKGYIDHAKsdpeaeIIAGGKCDDSVG 395
|
250 260
....*....|....*....|....*..
gi 1886245108 365 Y-IAPTVLVDVQETEPVMQEEIFGPIL 390
Cdd:cd07123 396 YfVEPTVIETTDPKHKLMTEEIFGPVL 422
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
154-418 |
4.22e-10 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 61.34 E-value: 4.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 154 PFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFS----RSTEKVLAEVLPRY-LDQSCFAVVLGGPQE--TGQL 226
Cdd:cd07127 193 PRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAAilplAITVQVAREVLAEAgFDPNLVTLAADTPEEpiAQTL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 227 LEH-KFDYIFFTGSPRVGRIVMTAAAKHLtpVTLELGGKNPCYVDDDCDPQTVANRVAWFRYFNCGQTCVAPDYVLCSP- 304
Cdd:cd07127 273 ATRpEVRIIDFTGSNAFGDWLEANARQAQ--VYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRd 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 305 --HTRERLL------PALQSAITRFYGEDPRRSPSLGRVVSDKHFRRLRGLLGCGRVAIGGQSDE-----DERYIAPTVL 371
Cdd:cd07127 351 giQTDDGRKsfdevaADLAAAIDGLLADPARAAALLGAIQSPDTLARIAEARQLGEVLLASEAVAhpefpDARVRTPLLL 430
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1886245108 372 VDVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINR--REK-PLALYAFS 418
Cdd:cd07127 431 KLDASDEAAYAEERFGPIAFVVATDSTDHSIELAREsvREHgAMTVGVYS 480
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
153-406 |
1.01e-09 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 60.65 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 153 EPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEfsrSTEKVLAEvlpryldqscfAVVL----GGPQETGQLLE 228
Cdd:PRK11905 675 KPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAE---QTPLIAAR-----------AVRLlheaGVPKDALQLLP 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 229 HKFDYI-------------FFTGSPRVGRIVMTAAAKHLT-PVTL--ELGGKNPCYVDDDCDP-QTVANRVA-WFRyfNC 290
Cdd:PRK11905 741 GDGRTVgaalvadpriagvMFTGSTEVARLIQRTLAKRSGpPVPLiaETGGQNAMIVDSSALPeQVVADVIAsAFD--SA 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 291 GQTCVAPDyVLC-----SPHTRERLLPALQSAITrfyGeDPRR-SPSLGRVVSDK-------HFRRLRGlLGCG--RVAI 355
Cdd:PRK11905 819 GQRCSALR-VLClqedvADRVLTMLKGAMDELRI---G-DPWRlSTDVGPVIDAEaqanieaHIEAMRA-AGRLvhQLPL 892
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1886245108 356 GGQSdEDERYIAPTVLvdvqETE--PVMQEEIFGPILPIV--NVGSLDEAIDFIN 406
Cdd:PRK11905 893 PAET-EKGTFVAPTLI----EIDsiSDLEREVFGPVLHVVrfKADELDRVIDDIN 942
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
140-406 |
6.12e-08 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 54.94 E-value: 6.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 140 NLATQLDSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEfsrSTEKVLAEV--------LPRyldqS 211
Cdd:COG4230 666 AQARRLFAAPTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAE---QTPLIAARAvrllheagVPA----D 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 212 CFAVVLGGPQETGQLL--EHKFDYIFFTGSPRVGRIV-MTAAAKHLTPVTL--ELGGKNPCYVDDDCDPQTVANRV---A 283
Cdd:COG4230 739 VLQLLPGDGETVGAALvaDPRIAGVAFTGSTETARLInRTLAARDGPIVPLiaETGGQNAMIVDSSALPEQVVDDVlasA 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 284 wFRyfNCGQTCVAPDyVLCSPH-TRERLLPALQSAItrfyGE----DPRR-SPSLGRVVSDK-------HFRRLRGLlgc 350
Cdd:COG4230 819 -FD--SAGQRCSALR-VLCVQEdIADRVLEMLKGAM----AElrvgDPADlSTDVGPVIDAEaranleaHIERMRAE--- 887
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1886245108 351 GR-VAIGGQSDEDER--YIAPTV--LVDVQEtepvMQEEIFGPILPIV--NVGSLDEAIDFIN 406
Cdd:COG4230 888 GRlVHQLPLPEECANgtFVAPTLieIDSISD----LEREVFGPVLHVVryKADELDKVIDAIN 946
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
156-407 |
8.22e-07 |
|
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: 51.12 E-value: 8.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 156 GLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKP-SEFSRSTEKVLAEVLPR-YLDQSCFAVVLGGpqeTGQLLEH--KF 231
Cdd:cd07128 146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPaTATAYLTEAVVKDIVESgLLPEGALQLICGS---VGDLLDHlgEQ 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 232 DYIFFTGSPRVGRIVMT--AAAKHLTPVTLELGGKNPCYVDDDCDPQT-----VANRVAWFRYFNCGQTCVAPDYVLCSP 304
Cdd:cd07128 223 DVVAFTGSAATAAKLRAhpNIVARSIRFNAEADSLNAAILGPDATPGTpefdlFVKEVAREMTVKAGQKCTAIRRAFVPE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 305 HTRERLLPALQSAITRFYGEDPRR-SPSLGRVVSDKHFRRLRG----LLGCGRVAIGGQSDEDER--------YIAPTVL 371
Cdd:cd07128 303 ARVDAVIEALKARLAKVVVGDPRLeGVRMGPLVSREQREDVRAavatLLAEAEVVFGGPDRFEVVgadaekgaFFPPTLL 382
|
250 260 270
....*....|....*....|....*....|....*...
gi 1886245108 372 V--DVQETEPVMQEEIFGPILPIVNVGSLDEAIDFINR 407
Cdd:cd07128 383 LcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAAR 420
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
137-242 |
3.31e-06 |
|
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: 49.03 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 137 VPKNLATQLDSAFirKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKpsefSRSTEKVLAEVLPRYL------DQ 210
Cdd:cd07126 127 VPGDHQGQQSSGY--RWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLK----VDSKVSVVMEQFLRLLhlcgmpAT 200
|
90 100 110
....*....|....*....|....*....|..
gi 1886245108 211 SCFAVVLGGPQETGQLLEHKFDYIFFTGSPRV 242
Cdd:cd07126 201 DVDLIHSDGPTMNKILLEANPRMTLFTGSSKV 232
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
66-282 |
2.35e-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: 46.45 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 66 SAGR---TRSPEFRAAQLKGLGRFLQENKQLLQEALAQDL---HKSTFESEVSEIHISQSE-IDLALRNLRSWMKDEKVP 138
Cdd:cd07077 5 NAQRtlaVNHDEQRDLIINAIANALYDTRQRLASEAVSERgayIRSLIANWIAMMGCSESKlYKNIDTERGITASVGHIQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 139 KNLATQLDSAFIRKEPFGLVLIIAPWNYPVNLTLVPLVGaLAAGNCVVLKPSEFSRSTEKVLAEVLPRyldqscfAVVLG 218
Cdd:cd07077 85 DVLLPDNGETYVRAFPIGVTMHILPSTNPLSGITSALRG-IATRNQCIFRPHPSAPFTNRALALLFQA-------ADAAH 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1886245108 219 GPQETGQLLEH-------------KFDYIFFTGSPRVGRivmtAAAKH--LTPVTLELGGKNPCYVDDDCDPQTVANRV 282
Cdd:cd07077 157 GPKILVLYVPHpsdelaeellshpKIDLIVATGGRDAVD----AAVKHspHIPVIGFGAGNSPVVVDETADEERASGSV 231
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
133-294 |
1.39e-03 |
|
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: 40.71 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 133 KDEKVPKNLATqlDSAF---IRKEPFGLVLIIAPWNYPVNLTLVPLVGALAAGNCVVLKPSEFSRSTEKVLAEVLpryLD 209
Cdd:cd07081 73 KDEKTCGVLTG--DENGgtlIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLL---LQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886245108 210 QscfAVVLGGPQ-----------ETGQLLEHK--FDYIFFTGSPRvgriVMTAAAKHLTPVTLELGGKNPCYVDDDCDPQ 276
Cdd:cd07081 148 A---AVAAGAPEnligwidnpsiELAQRLMKFpgIGLLLATGGPA----VVKAAYSSGKPAIGVGAGNTPVVIDETADIK 220
|
170
....*....|....*...
gi 1886245108 277 TVANRVAWFRYFNCGQTC 294
Cdd:cd07081 221 RAVQSIVKSKTFDNGVIC 238
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
354-403 |
1.77e-03 |
|
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: 40.30 E-value: 1.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1886245108 354 AIGGQSDEDERYIaptvLVDVQETEPVMQEEIFGPILPIVNVGSLDEAID 403
Cdd:cd07121 304 AAGIEVPADIRLI----IVETDKDHPFVVEEQMMPILPVVRVKNFDEAIE 349
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
354-403 |
6.62e-03 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 38.73 E-value: 6.62e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1886245108 354 AIGGQSDEDERYIaptvLVDVQETEPVMQEEIFGPILPIVNVGSLDEAID 403
Cdd:PRK15398 334 AAGINVPKDTRLL----IVETDANHPFVVTELMMPVLPVVRVKDVDEAIA 379
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