|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
1-366 |
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: 676.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 1 MKDEPRSTNLFMKLDSVFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQYLDQS 80
Cdd:cd07132 78 MKPEPVKKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 81 CFAVVLGGPQETGQLLEHKLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAG 160
Cdd:cd07132 158 CYPVVLGGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 161 QTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGHIINQKQFQRLRALLGCSRVAIGGQSNESDRYIAPTVL 240
Cdd:cd07132 238 QTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 241 VDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYISLLSVP 320
Cdd:cd07132 318 TDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLP 397
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2217281694 321 FGGVGHSGMGRYHGKFTFDTFSHHRTCLLAPSGLEKLKEIHYPPYT 366
Cdd:cd07132 398 FGGVGNSGMGAYHGKYSFDTFSHKRSCLVKSLNMEKLNSLRYPPYS 443
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
1-348 |
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: 542.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 1 MKDEPRSTNLFMKLDSVFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQYLDQS 80
Cdd:cd07087 78 MKPRRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 81 CFAVVLGGPQETGQLLEHKLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAG 160
Cdd:cd07087 158 AVAVVEGGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 161 QTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGHIINQKQFQRLRALLGCSRVAIGGQSNESDRYIAPTVL 240
Cdd:cd07087 238 QTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGKVVIGGQVDKEERYIAPTIL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 241 VDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYISLLSVP 320
Cdd:cd07087 318 DDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLP 397
|
330 340
....*....|....*....|....*...
gi 2217281694 321 FGGVGHSGMGRYHGKFTFDTFSHHRTCL 348
Cdd:cd07087 398 FGGVGNSGMGAYHGKAGFDTFSHLKSVL 425
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
1-374 |
4.27e-177 |
|
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: 500.11 E-value: 4.27e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 1 MKDEPRSTNLFMKLDSVFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQYLDQS 80
Cdd:cd07136 78 MKPKRVKTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 81 CFAVVLGGPQETGQLLEHKLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAG 160
Cdd:cd07136 158 YVAVVEGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 161 QTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGHIINQKQFQRLRALLGCSRVAIGGQSNESDRYIAPTVL 240
Cdd:cd07136 238 QTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGKIVFGGNTDRETLYIEPTIL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 241 VDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGsfGG--NEGFTYISLLS 318
Cdd:cd07136 318 DNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFG--GGciNDTIMHLANPY 395
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217281694 319 VPFGGVGHSGMGRYHGKFTFDTFSHHRTCLLAPSGLEkLKeIHYPPYTDWNQQLLR 374
Cdd:cd07136 396 LPFGGVGNSGMGSYHGKYSFDTFSHKKSILKKSTWFD-LP-LRYPPYKGKKKKLKK 449
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
1-374 |
7.49e-173 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 491.08 E-value: 7.49e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 1 MKDEPRSTNLFMKLDSVFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQYLDQS 80
Cdd:PTZ00381 87 LKPEKVDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 81 CFAVVLGGPQETGQLLEHKLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAG 160
Cdd:PTZ00381 167 YVRVIEGGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 161 QTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGHIINQKQFQRLRALLGC--SRVAIGGQSNESDRYIAPT 238
Cdd:PTZ00381 247 QTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKDhgGKVVYGGEVDIENKYVAPT 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 239 VLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYISLLS 318
Cdd:PTZ00381 327 IIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPN 406
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217281694 319 VPFGGVGHSGMGRYHGKFTFDTFSHHRTCLLAPSGLEKLKEIHYPPYTDWNQQLLR 374
Cdd:PTZ00381 407 LPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNKSTGNSFDLSLRYPPYTSFKSWVLS 462
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
1-346 |
8.10e-166 |
|
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: 470.93 E-value: 8.10e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 1 MKDEPRSTN-LFMKLDSVFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQYLDQ 79
Cdd:cd07135 85 AKDEKVKDGpLAFMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLDP 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 80 SCFAVVLGGPQETGQLLEHKLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNA 159
Cdd:cd07135 165 DAFQVVQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 160 GQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGHIINQKQFQRLRALLGCSR--VAIGGQSNESDRYIAP 237
Cdd:cd07135 245 GQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDTTKgkVVIGGEMDEATRFIPP 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 238 TVLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYISLL 317
Cdd:cd07135 325 TIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVD 404
|
330 340
....*....|....*....|....*....
gi 2217281694 318 SVPFGGVGHSGMGRYHGKFTFDTFSHHRT 346
Cdd:cd07135 405 NAPFGGVGDSGYGAYHGKYGFDTFTHERT 433
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
1-348 |
1.53e-146 |
|
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: 422.02 E-value: 1.53e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 1 MKDEPRSTNLFMKLDSVFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQYLDQS 80
Cdd:cd07134 78 MKPKRVRTPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDED 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 81 CFAVVLGGPQETGQLLEHKLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAG 160
Cdd:cd07134 158 EVAVFEGDAEVAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 161 QTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDP--QSSPNLGHIINQKQFQRLRALL-----GCSRVAIGGQSNESDR 233
Cdd:cd07134 238 QTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAarKASPDLARIVNDRHFDRLKGLLddavaKGAKVEFGGQFDAAQR 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 234 YIAPTVLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTY 313
Cdd:cd07134 318 YIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLH 397
|
330 340 350
....*....|....*....|....*....|....*
gi 2217281694 314 ISLLSVPFGGVGHSGMGRYHGKFTFDTFSHHRTCL 348
Cdd:cd07134 398 FLNPNLPFGGVNNSGIGSYHGVYGFKAFSHERAVL 432
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
19-348 |
1.21e-140 |
|
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: 407.18 E-value: 1.21e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 19 IWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQYLDQSCFAVVLGGPQETGQLLEH 98
Cdd:cd07137 97 IVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIKVIEGGVPETTALLEQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 99 KLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVA---WFCyfNAGQTCVAPDYVLCSPEM 175
Cdd:cd07137 177 KWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAggkWGC--NNGQACIAPDYVLVEESF 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 176 QERLLPALQSTITRFYGDDPQSSPNLGHIINQKQFQRLRALLGCSRVAI----GGQSNESDRYIAPTVLVDVQETEPVMQ 251
Cdd:cd07137 255 APTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADkivhGGERDEKNLYIEPTILLDPPLDSSIMT 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 252 EEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYISLLSVPFGGVGHSGMGR 331
Cdd:cd07137 335 EEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTLPFGGVGESGFGA 414
|
330
....*....|....*..
gi 2217281694 332 YHGKFTFDTFSHHRTCL 348
Cdd:cd07137 415 YHGKFSFDAFSHKKAVL 431
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
1-346 |
4.51e-136 |
|
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: 395.31 E-value: 4.51e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 1 MKDEPRSTNLFMKLDSVFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQYLDQS 80
Cdd:cd07133 79 MKPSRRHVGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDED 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 81 CFAVVLGGPQETGQLLEHKLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAG 160
Cdd:cd07133 159 EVAVVTGGADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 161 QTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPqSSPNLGHIINQKQFQRLRALL------GCSRVAIGGQSNE--SD 232
Cdd:cd07133 239 QTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYPTLA-DNPDYTSIINERHYARLQGLLedarakGARVIELNPAGEDfaAT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 233 RYIAPTVLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFT 312
Cdd:cd07133 318 RKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLL 397
|
330 340 350
....*....|....*....|....*....|....
gi 2217281694 313 YISLLSVPFGGVGHSGMGRYHGKFTFDTFSHHRT 346
Cdd:cd07133 398 HVAQDDLPFGGVGASGMGAYHGKEGFLTFSHAKP 431
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
22-374 |
1.57e-128 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 377.92 E-value: 1.57e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 22 EPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQYLDQSCFAVVLGGPQETGQLLEHKLD 101
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAVKVIEGGPAVGEQLLQHKWD 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 102 YIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVD---DNCDPQTVANRVA---W-FCyfnAGQTCVAPDYVLCSPE 174
Cdd:PLN02203 187 KIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVggkWgSC---AGQACIAIDYVLVEER 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 175 MQERLLPALQSTITRFYGDDPQSSPNLGHIINQKQFQRLRALLGCSRVAI----GGQSNESDRYIAPTVLVDVQETEPVM 250
Cdd:PLN02203 264 FAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAAsivhGGSIDEKKLFIEPTILLNPPLDSDIM 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 251 QEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYISLLSVPFGGVGHSGMG 330
Cdd:PLN02203 344 TEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYACDSLPFGGVGESGFG 423
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2217281694 331 RYHGKFTFDTFSHHRTCLLAPSGLEklKEIHYPPYTDWNQQLLR 374
Cdd:PLN02203 424 RYHGKYSFDTFSHEKAVLRRSLLTE--FEFRYPPWNDFKLGFLR 465
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
4-349 |
8.71e-113 |
|
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: 336.10 E-value: 8.71e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 4 EPRSTNLFMKLDSVFIWkEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCF 82
Cdd:cd07078 78 GEVIPSPDPGELAIVRR-EPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLPPGVL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 83 AVVLGGPQETGQ-LLEH-KLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAG 160
Cdd:cd07078 157 NVVTGDGDEVGAaLASHpRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAG 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 161 QTCVAPDYVLCSPEMQERLLPALQSTITRFY-GDDPQSSPNLGHIINQKQFQRLRALL-----GCSRVAIGGQSNESD-- 232
Cdd:cd07078 237 QVCTAASRLLVHESIYDEFVERLVERVKALKvGNPLDPDTDMGPLISAAQLDRVLAYIedakaEGAKLLCGGKRLEGGkg 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 233 RYIAPTVLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFT 312
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSV 396
|
330 340 350
....*....|....*....|....*....|....*..
gi 2217281694 313 YISlLSVPFGGVGHSGMGRYHGKFTFDTFSHHRTCLL 349
Cdd:cd07078 397 GAE-PSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
1-374 |
6.23e-99 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 302.35 E-value: 6.23e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 1 MKDEPRSTNLFMKLDSVFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQYLDQS 80
Cdd:PLN02174 90 MAPEKAKTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 81 CFAVVLGGPQETGQLLEHKLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRV---AWFCyf 157
Cdd:PLN02174 170 AVRVVEGAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIiagKWGC-- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 158 NAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGHIINQKQFQRLRALLG----CSRVAIGGQSNESDR 233
Cdd:PLN02174 248 NNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDekevSDKIVYGGEKDRENL 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 234 YIAPTVLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTY 313
Cdd:PLN02174 328 KIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVH 407
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217281694 314 ISLLSVPFGGVGHSGMGRYHGKFTFDTFSHHRTCLLapSGLEKLKEIHYPPYTDWNQQLLR 374
Cdd:PLN02174 408 LALHTLPFGGVGESGMGAYHGKFSFDAFSHKKAVLY--RSLFGDSAVRYPPYSRGKLRLLK 466
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
4-349 |
7.74e-90 |
|
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: 275.26 E-value: 7.74e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 4 EPRSTNLFMKLDSVFIWkEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCF 82
Cdd:cd06534 74 GPELPSPDPGGEAYVRR-EPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 83 AVVLGGPQETGQ-LLEH-KLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAG 160
Cdd:cd06534 153 NVVPGGGDEVGAaLLSHpRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 161 QTCVAPDYVLCSPEMQERLLPALQstitrfygddpqsspnlghiinqkqfqrlrallgcsrvaiggqsnesdryiapTVL 240
Cdd:cd06534 233 QICTAASRLLVHESIYDEFVEKLV-----------------------------------------------------TVL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 241 VDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYISlLSVP 320
Cdd:cd06534 260 VDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVG-PEAP 338
|
330 340
....*....|....*....|....*....
gi 2217281694 321 FGGVGHSGMGRYHGKFTFDTFSHHRTCLL 349
Cdd:cd06534 339 FGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
17-346 |
3.81e-89 |
|
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: 277.01 E-value: 3.81e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 17 VFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGPQETGQ- 94
Cdd:COG1012 135 AYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAgLPAGVLNVVTGDGSEVGAa 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 95 LLEH-KLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLC-- 171
Cdd:COG1012 215 LVAHpDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVhe 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 172 --SPEMQERLLPALQSTItrfYGDDPQSSPNLGHIINQKQFQRLRALL------GCsRVAIGGQSNESDR--YIAPTVLV 241
Cdd:COG1012 295 siYDEFVERLVAAAKALK---VGDPLDPGTDMGPLISEAQLERVLAYIedavaeGA-ELLTGGRRPDGEGgyFVEPTVLA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 242 DVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYISlLSVPF 321
Cdd:COG1012 371 DVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAV-PQAPF 449
|
330 340
....*....|....*....|....*
gi 2217281694 322 GGVGHSGMGRYHGKFTFDTFSHHRT 346
Cdd:COG1012 450 GGVKQSGIGREGGREGLEEYTETKT 474
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
18-342 |
5.93e-81 |
|
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: 255.15 E-value: 5.93e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 18 FIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGPQETGQ-L 95
Cdd:pfam00171 121 YTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAgLPAGVLNVVTGSGAEVGEaL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 96 LEHK-LDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSPE 174
Cdd:pfam00171 201 VEHPdVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHES 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 175 MQERLLPALQSTITRF-YGDDPQSSPNLGHIINQKQFQRLRALL------GCsRVAIGGQSNESD-RYIAPTVLVDVQET 246
Cdd:pfam00171 281 IYDEFVEKLVEAAKKLkVGDPLDPDTDMGPLISKAQLERVLKYVedakeeGA-KLLTGGEAGLDNgYFVEPTVLANVTPD 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 247 EPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYiSLLSVPFGGVGH 326
Cdd:pfam00171 360 MRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTG-DADGLPFGGFKQ 438
|
330
....*....|....*.
gi 2217281694 327 SGMGRYHGKFTFDTFS 342
Cdd:pfam00171 439 SGFGREGGPYGLEEYT 454
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
1-334 |
1.12e-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: 249.06 E-value: 1.12e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 1 MKDEPRSTNLFMKLDSVFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGT----EKVLAEVLPqy 76
Cdd:cd07099 97 LAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVgellAEAWAAAGP-- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 77 lDQSCFAVVLGGpQETGQ-LLEHKLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFC 155
Cdd:cd07099 175 -PQGVLQVVTGD-GATGAaLIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 156 YFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGDDPQSSPNLGHIINQKQFQRLR-----ALLGCSRVAIGG-QS 228
Cdd:cd07099 253 MVNAGQTCISVERVYVHESVYDEFVARLVAKARALrPGADDIGDADIGPMTTARQLDIVRrhvddAVAKGAKALTGGaRS 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 229 NESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGN 308
Cdd:cd07099 333 NGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSIN 412
|
330 340
....*....|....*....|....*.
gi 2217281694 309 EGFTYISLLSVPFGGVGHSGMGRYHG 334
Cdd:cd07099 413 DVLLTAGIPALPFGGVKDSGGGRRHG 438
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
17-341 |
1.84e-66 |
|
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: 217.30 E-value: 1.84e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 17 VFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGPQETGQ- 94
Cdd:cd07103 111 ILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEAgLPAGVLNVVTGSPAEIGEa 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 95 LLEH----KldyIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPD--Y 168
Cdd:cd07103 191 LCASprvrK---ISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANriY 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 169 VLCS--PEMQERLLPALQSTITrfyGDDPQSSPNLGHIINQKQFQRLRALL------GcSRVAIGGQSNESD-RYIAPTV 239
Cdd:cd07103 268 VHESiyDEFVEKLVERVKKLKV---GNGLDEGTDMGPLINERAVEKVEALVedavakG-AKVLTGGKRLGLGgYFYEPTV 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 240 LVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFtyISLLSV 319
Cdd:cd07103 344 LTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGL--ISDAEA 421
|
330 340
....*....|....*....|..
gi 2217281694 320 PFGGVGHSGMGRYHGKFTFDTF 341
Cdd:cd07103 422 PFGGVKESGLGREGGKEGLEEY 443
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
19-343 |
5.24e-62 |
|
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: 205.07 E-value: 5.24e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 19 IWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSE---ISQGTekVLAEV-----LPQYLdqscFAVVLGGPQ 90
Cdd:cd07104 94 VRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSrtpVTGGL--LIAEIfeeagLPKGV----LNVVPGGGS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 91 ETGQ-LLEHKL-DYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDY 168
Cdd:cd07104 168 EIGDaLVEHPRvRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGR 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 169 VLCSPEMQERLLPALQSTITRF-YGD--DPQSSpnLGHIINQKQFQRLRALLGCS-----RVAIGGQSNesDRYIAPTVL 240
Cdd:cd07104 248 ILVHESVYDEFVEKLVAKAKALpVGDprDPDTV--IGPLINERQVDRVHAIVEDAvaagaRLLTGGTYE--GLFYQPTVL 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 241 VDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSgsfggneGFTYISLLSV- 319
Cdd:cd07104 324 SDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLET-------GMVHINDQTVn 396
|
330 340
....*....|....*....|....*....
gi 2217281694 320 -----PFGGVGHSGMGRYHGKFTFDTFSH 343
Cdd:cd07104 397 dephvPFGGVKASGGGRFGGPASLEEFTE 425
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
18-346 |
5.31e-61 |
|
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: 203.24 E-value: 5.31e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 18 FIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEV-----LPQyldqSCFAVVLGGPQET 92
Cdd:cd07089 118 VVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIiaetdLPA----GVVNVVTGSDNAV 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 93 GQLL--EHKLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVL 170
Cdd:cd07089 194 GEALttDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLL 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 171 CSPEMQERLLPALQSTITRF-YGD--DPqsSPNLGHIINQKQFQRLRALL------GcSRVAIGGQSNES-DR--YIAPT 238
Cdd:cd07089 274 VPRSRYDEVVEALAAAFEALpVGDpaDP--GTVMGPLISAAQRDRVEGYIargrdeG-ARLVTGGGRPAGlDKgfYVEPT 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 239 VLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYISllS 318
Cdd:cd07089 351 LFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINGGGGYGP--D 428
|
330 340
....*....|....*....|....*...
gi 2217281694 319 VPFGGVGHSGMGRYHGKFTFDTFSHHRT 346
Cdd:cd07089 429 APFGGYKQSGLGRENGIEGLEEFLETKS 456
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
1-335 |
2.02e-60 |
|
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: 202.14 E-value: 2.02e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 1 MKDEPRSTNLFMKLDSVFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEIS--------QGTEKVLAEV 72
Cdd:cd07098 98 LRPESRPGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVawssgfflSIIRECLAAC 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 73 -LPQYLDQS--CFAvvlggpqETGQ-LLEH-KLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTV 147
Cdd:cd07098 178 gHDPDLVQLvtCLP-------ETAEaLTSHpVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQI 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 148 ANRVAWFCYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGDDPQSSPNLGHIINQKQFQRLRALLGCS-----R 221
Cdd:cd07098 251 ASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALrQGPPLDGDVDVGAMISPARFDRLEELVADAvekgaR 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 222 VAIGGQSNE-----SDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQM 296
Cdd:cd07098 331 LLAGGKRYPhpeypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRI 410
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2217281694 297 LERTSSGSFGGNE-GFTYIsLLSVPFGGVGHSGMGRYHGK 335
Cdd:cd07098 411 ASQLETGMVAINDfGVNYY-VQQLPFGGVKGSGFGRFAGE 449
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
18-344 |
8.44e-60 |
|
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: 200.16 E-value: 8.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 18 FIWKEPFGLVLIIAPWNYPLnLTLV-LLVGALAAGSCVVLKPSEISQGTEKVLAEV-----LPQYLdqscFAVVLGGPQE 91
Cdd:cd07102 111 YIRREPLGVVLIIAPWNYPY-LTAVnAVIPALLAGNAVILKHSPQTPLCGERFAAAfaeagLPEGV----FQVLHLSHET 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 92 TGQLL-EHKLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCvapdyvl 170
Cdd:cd07102 186 SAALIaDPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSC------- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 171 CSPE-------MQERLLPALQSTITRF-YGDDPQSSPNLGHIINQKQFQRLR-----ALLGCSRVAIGGQ----SNESDR 233
Cdd:cd07102 259 CSIEriyvhesIYDAFVEAFVAVVKGYkLGDPLDPSTTLGPVVSARAADFVRaqiadAIAKGARALIDGAlfpeDKAGGA 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 234 YIAPTVLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGfTY 313
Cdd:cd07102 339 YLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNRC-DY 417
|
330 340 350
....*....|....*....|....*....|....*
gi 2217281694 314 ISlLSVPFGGVGHSGMGRYHGKFTFDTF----SHH 344
Cdd:cd07102 418 LD-PALAWTGVKDSGRGVTLSRLGYDQLtrpkSYH 451
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
18-331 |
1.19e-59 |
|
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: 199.48 E-value: 1.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 18 FIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQYLDQSCFAVVLGGPQETGQLL- 96
Cdd:cd07092 113 MIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGVVNVVCGGGASAGDALv 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 97 -EHKLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSPEM 175
Cdd:cd07092 193 aHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 176 QERLLPALQSTITRF-YGDDPQSSPNLGHIINQKQFQRLRALL----GCSRVAIGGQSNESDRY-IAPTVLVDVQETEPV 249
Cdd:cd07092 273 YDEFVAALVEAVSAIrVGDPDDEDTEMGPLNSAAQRERVAGFVerapAHARVLTGGRRAEGPGYfYEPTVVAGVAQDDEI 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 250 MQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYISllSVPFGGVGHSGM 329
Cdd:cd07092 353 VQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNTHIPLAA--EMPHGGFKQSGY 430
|
..
gi 2217281694 330 GR 331
Cdd:cd07092 431 GK 432
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
21-349 |
2.95e-59 |
|
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: 198.72 E-value: 2.95e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 21 KEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGPQETGQ-LLEH 98
Cdd:cd07118 117 REPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAgLPAGVVNIVTGYGATVGQaMTEH 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 99 KL-DYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSPEMQE 177
Cdd:cd07118 197 PDvDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIAD 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 178 RLLPAL--QSTITRFyGD--DPQSspNLGHIINQKQFQRLRALLGCSR-----VAIGGQSNESD--RYIAPTVLVDVQET 246
Cdd:cd07118 277 AFVAAVvaRSRKVRV-GDplDPET--KVGAIINEAQLAKITDYVDAGRaegatLLLGGERLASAagLFYQPTIFTDVTPD 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 247 EPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGN---EGFTyisllSVPFGG 323
Cdd:cd07118 354 MAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNtflDGSP-----ELPFGG 428
|
330 340
....*....|....*....|....*.
gi 2217281694 324 VGHSGMGRYHGKFTFDTFSHHRTCLL 349
Cdd:cd07118 429 FKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
23-335 |
1.10e-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: 196.98 E-value: 1.10e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 23 PFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQYLDQSCFAVVLGGpQETGQLL-EH-KL 100
Cdd:cd07106 114 PLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEVLPPGVLNVVSGG-DELGPALtSHpDI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 101 DYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPD--YVlcsPEMQ-E 177
Cdd:cd07106 193 RKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKrlYV---HESIyD 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 178 RLLPALQSTITRFY-GDDPQSSPNLGHIINQKQFQRLRALL-----GCSRVAIGGQSNESDRY-IAPTVLVDVQETEPVM 250
Cdd:cd07106 270 EFCEALVALAKAAVvGDGLDPGTTLGPVQNKMQYDKVKELVedakaKGAKVLAGGEPLDGPGYfIPPTIVDDPPEGSRIV 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 251 QEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYisLLSVPFGGVGHSGMG 330
Cdd:cd07106 350 DEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWINTHGAL--DPDAPFGGHKQSGIG 427
|
....*
gi 2217281694 331 RYHGK 335
Cdd:cd07106 428 VEFGI 432
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
17-342 |
3.07e-58 |
|
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: 195.92 E-value: 3.07e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 17 VFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGPQETGQ- 94
Cdd:cd07109 111 VYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAgLPAGALNVVTGLGAEAGAa 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 95 LLEHK-LDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSP 173
Cdd:cd07109 191 LVAHPgVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHR 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 174 EMQERLLPALQSTITRFYGDDPQSSPNLGHIINQKQFQRLRALLGCS-----RVAIGGQ----SNESDRYIAPTVLVDVQ 244
Cdd:cd07109 271 SIYDEVLERLVERFRALRVGPGLEDPDLGPLISAKQLDRVEGFVARArargaRIVAGGRiaegAPAGGYFVAPTLLDDVP 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 245 ETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTY--ISLlsvPFG 322
Cdd:cd07109 351 PDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNYGAGggIEL---PFG 427
|
330 340
....*....|....*....|
gi 2217281694 323 GVGHSGMGRYHGKFTFDTFS 342
Cdd:cd07109 428 GVKKSGHGREKGLEALYNYT 447
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
21-342 |
2.31e-57 |
|
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: 193.70 E-value: 2.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 21 KEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGPQETGQLL--E 97
Cdd:cd07150 117 RRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAgLPKGVFNVVTGGGAEVGDELvdD 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 98 HKLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSPEMQE 177
Cdd:cd07150 197 PRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYD 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 178 RLLPALQSTITRF-YGDDPQSSPNLGHIINQKQFQRLR-----ALLGCSRVAIGGQSNesDRYIAPTVLVDVQETEPVMQ 251
Cdd:cd07150 277 EFVKKFVARASKLkVGDPRDPDTVIGPLISPRQVERIKrqvedAVAKGAKLLTGGKYD--GNFYQPTVLTDVTPDMRIFR 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 252 EEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNeGFTYISLLSVPFGGVGHSGMGR 331
Cdd:cd07150 355 EETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHIN-DPTILDEAHVPFGGVKASGFGR 433
|
330
....*....|.
gi 2217281694 332 YHGKFTFDTFS 342
Cdd:cd07150 434 EGGEWSMEEFT 444
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
16-343 |
9.90e-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: 192.18 E-value: 9.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 16 SVFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEV-----LPQyldqSCFAVVLGGPQ 90
Cdd:cd07110 113 KARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIaaeagLPP----GVLNVVTGTGD 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 91 ETGQ-LLEHK-LDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDY 168
Cdd:cd07110 189 EAGApLAAHPgIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSR 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 169 VLCSPEMQERLLPALQSTITRFYGDDPQSSP-NLGHIINQKQFQRLRALLGC-----SRVAIGGQSNESDR---YIAPTV 239
Cdd:cd07110 269 LLVHESIADAFLERLATAAEAIRVGDPLEEGvRLGPLVSQAQYEKVLSFIARgkeegARLLCGGRRPAHLEkgyFIAPTV 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 240 LVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEG---FTYisl 316
Cdd:cd07110 349 FADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVWINCSqpcFPQ--- 425
|
330 340
....*....|....*....|....*..
gi 2217281694 317 lsVPFGGVGHSGMGRYHGKFTFDTFSH 343
Cdd:cd07110 426 --APWGGYKRSGIGRELGEWGLDNYLE 450
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
21-342 |
2.80e-56 |
|
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: 190.73 E-value: 2.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 21 KEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGPQETGQ-LLEH 98
Cdd:cd07115 115 REPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAgFPAGVLNVVTGFGEVAGAaLVEH 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 99 K-LDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSPEMQE 177
Cdd:cd07115 195 PdVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYD 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 178 RLLPALQSTITRFYGDDP-QSSPNLGHIINQKQFQRLRALL------GCSRVAIGGQSNESDRYIAPTVLVDVQETEPVM 250
Cdd:cd07115 275 EFLERFTSLARSLRPGDPlDPKTQMGPLVSQAQFDRVLDYVdvgreeGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIA 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 251 QEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNegfTYISLLS-VPFGGVGHSGM 329
Cdd:cd07115 355 QEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWIN---TYNRFDPgSPFGGYKQSGF 431
|
330
....*....|...
gi 2217281694 330 GRYHGKFTFDTFS 342
Cdd:cd07115 432 GREMGREALDEYT 444
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
17-341 |
2.13e-54 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 186.82 E-value: 2.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 17 VFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGPQETGQL 95
Cdd:PLN02278 154 LLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAgIPPGVLNVVMGDAPEIGDA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 96 L--EHKLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSP 173
Cdd:PLN02278 234 LlaSPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 174 EMQERLLPALQSTITRF-YGDDPQSSPNLGHIINQKQFQRLRA------------LLGCSRVAIGGQsnesdrYIAPTVL 240
Cdd:PLN02278 314 GIYDKFAEAFSKAVQKLvVGDGFEEGVTQGPLINEAAVQKVEShvqdavskgakvLLGGKRHSLGGT------FYEPTVL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 241 VDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFtyISLLSVP 320
Cdd:PLN02278 388 GDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGL--ISTEVAP 465
|
330 340
....*....|....*....|.
gi 2217281694 321 FGGVGHSGMGRYHGKFTFDTF 341
Cdd:PLN02278 466 FGGVKQSGLGREGSKYGIDEY 486
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
20-345 |
3.49e-54 |
|
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: 185.19 E-value: 3.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 20 WKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKP---SEISQGTekVLAEVLPQY-LDQSCFAVVLGGPqETGQ- 94
Cdd:cd07152 107 RRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPdprTPVSGGV--VIARLFEEAgLPAGVLHVLPGGA-DAGEa 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 95 LLEH-KLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSP 173
Cdd:cd07152 184 LVEDpNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHE 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 174 EMQERLLPALQSTITRFYGDDPQSSP-NLGHIINQKQFQRLRALLGCS-----RVAIGGQSNesDRYIAPTVLVDVQETE 247
Cdd:cd07152 264 SVADAYTAKLAAKAKHLPVGDPATGQvALGPLINARQLDRVHAIVDDSvaagaRLEAGGTYD--GLFYRPTVLSGVKPGM 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 248 PVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGfTYISLLSVPFGGVGHS 327
Cdd:cd07152 342 PAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQ-TVNDEPHNPFGGMGAS 420
|
330
....*....|....*....
gi 2217281694 328 GMG-RYHGKFTFDTFSHHR 345
Cdd:cd07152 421 GNGsRFGGPANWEEFTQWQ 439
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
21-341 |
5.31e-54 |
|
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: 185.01 E-value: 5.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 21 KEPFGLVLIIAPWNYPLNlTLVLLVG-ALAAGSCVVLKPSEISQGTEKVLAEV-----LPQyldqSCFAVVLGGPQETGQ 94
Cdd:cd07138 128 REPIGVCGLITPWNWPLN-QIVLKVApALAAGCTVVLKPSEVAPLSAIILAEIldeagLPA----GVFNLVNGDGPVVGE 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 95 LL-EH-KLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCD-----PQTVANrvawfCYFNAGQTCVAPD 167
Cdd:cd07138 203 ALsAHpDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADlekavPRGVAA-----CFANSGQSCNAPT 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 168 YVL----CSPEMQERLLPALQSTITrfyGDDPQSSPNLGHIINQKQFQRLRALLGC-----SRVAIGG----QSNESDRY 234
Cdd:cd07138 278 RMLvprsRYAEAEEIAAAAAEAYVV---GDPRDPATTLGPLASAAQFDRVQGYIQKgieegARLVAGGpgrpEGLERGYF 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 235 IAPTVLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNS----SQVVNQMleRTSSGSFGGneg 310
Cdd:cd07138 355 VKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADperaRAVARRL--RAGQVHING--- 429
|
330 340 350
....*....|....*....|....*....|.
gi 2217281694 311 fTYISLLSvPFGGVGHSGMGRYHGKFTFDTF 341
Cdd:cd07138 430 -AAFNPGA-PFGGYKQSGNGREWGRYGLEEF 458
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
21-331 |
1.06e-52 |
|
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: 181.40 E-value: 1.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 21 KEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQYLDQSCFAVVLGGPQETGQ-LLEH- 98
Cdd:cd07108 115 REPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQVLPAGVLNVITGYGEECGAaLVDHp 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 99 KLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYV--DDNCDpQTVANRVAWFCYFNAGQTCVAPDYVLCSPEMQ 176
Cdd:cd07108 195 DVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVfpDADLD-DAVDGAIAGMRFTRQGQSCTAGSRLFVHEDIY 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 177 ERLLPALQSTITRFYGDDP-QSSPNLGHIINQKQFQRLRALLGC------SRVAIGGQSNESDR-----YIAPTVLVDVQ 244
Cdd:cd07108 274 DAFLEKLVAKLSKLKIGDPlDEATDIGAIISEKQFAKVCGYIDLglstsgATVLRGGPLPGEGPladgfFVQPTIFSGVD 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 245 ETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTyiSLLSVPFGGV 324
Cdd:cd07108 354 NEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQGGG--QQPGQSYGGF 431
|
....*..
gi 2217281694 325 GHSGMGR 331
Cdd:cd07108 432 KQSGLGR 438
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
19-331 |
1.75e-52 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 181.26 E-value: 1.75e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 19 IWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQYLDQSCFAVVLGGPQETGQ-LLE 97
Cdd:PRK13473 134 IRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDaLVG 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 98 H-KLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSPEMQ 176
Cdd:PRK13473 214 HpKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIY 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 177 ERL---LPALQSTITrfYGDDPQSSPNLGHIINQKQFQRL-----RAL-LGCSRVAIGGQSNESD-RYIAPTVLVDVQET 246
Cdd:PRK13473 294 DDLvakLAAAVATLK--VGDPDDEDTELGPLISAAHRDRVagfveRAKaLGHIRVVTGGEAPDGKgYYYEPTLLAGARQD 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 247 EPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYISllSVPFGGVGH 326
Cdd:PRK13473 372 DEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVS--EMPHGGQKQ 449
|
....*
gi 2217281694 327 SGMGR 331
Cdd:PRK13473 450 SGYGK 454
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
18-342 |
2.52e-52 |
|
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: 180.49 E-value: 2.52e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 18 FIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEV-----LPqyldQSCFAVVLGGPQET 92
Cdd:cd07112 119 LITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELaleagLP----AGVLNVVPGFGHTA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 93 GQLL-EHK-LDYIFFTGSPRVGKIVMT-AATKHLTPVTLELGGKNPCYVDDNC-DPQTVANRVAWFCYFNAGQTCVAPDY 168
Cdd:cd07112 195 GEALgLHMdVDALAFTGSTEVGRRFLEySGQSNLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSR 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 169 VLCSPEMQERLLPALQSTITRFY-GD--DPQSSpnLGHIINQKQFQRLRALLGCS-----RVAIGGQSNESDR---YIAP 237
Cdd:cd07112 275 LLVHESIKDEFLEKVVAAAREWKpGDplDPATR--MGALVSEAHFDKVLGYIESGkaegaRLVAGGKRVLTETggfFVEP 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 238 TVLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNeGFTYISlL 317
Cdd:cd07112 353 TVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVN-CFDEGD-I 430
|
330 340
....*....|....*....|....*
gi 2217281694 318 SVPFGGVGHSGMGRYHGKFTFDTFS 342
Cdd:cd07112 431 TTPFGGFKQSGNGRDKSLHALDKYT 455
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
22-342 |
5.97e-52 |
|
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: 179.30 E-value: 5.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 22 EPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLG-GPqETGQLL-EH 98
Cdd:cd07093 116 QPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAgLPPGVVNVVHGfGP-EAGAALvAH 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 99 K-LDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCvapdyvLCSpemqE 177
Cdd:cd07093 195 PdVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVC------LAG----S 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 178 RLLpaLQSTI-----TRF--------YGDDPQSSPNLGHIINQKQFQRLRALLGCSR-----VAIGGQSNESDR-----Y 234
Cdd:cd07093 265 RIL--VQRSIydeflERFverakalkVGDPLDPDTEVGPLISKEHLEKVLGYVELARaegatILTGGGRPELPDleggyF 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 235 IAPTVLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSG-----SFggne 309
Cdd:cd07093 343 VEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGtvwvnCW---- 418
|
330 340 350
....*....|....*....|....*....|...
gi 2217281694 310 gftYISLLSVPFGGVGHSGMGRYHGKFTFDTFS 342
Cdd:cd07093 419 ---LVRDLRTPFGGVKASGIGREGGDYSLEFYT 448
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
21-331 |
1.10e-51 |
|
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: 179.33 E-value: 1.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 21 KEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLG-GPQETGQLLEH 98
Cdd:cd07091 139 REPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAgFPPGVVNIVPGfGPTAGAAISSH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 99 -KLDYIFFTGSPRVGKIVMTAATK-HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSPEMQ 176
Cdd:cd07091 219 mDVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIY 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 177 ERLLPALQSTITRFY-GDDPQSSPNLGHIINQKQFQRLRALL------GCSRVAIGGQSNESDRYIAPTVLVDVQETEPV 249
Cdd:cd07091 299 DEFVEKFKARAEKRVvGDPFDPDTFQGPQVSKAQFDKILSYIesgkkeGATLLTGGERHGSKGYFIQPTVFTDVKDDMKI 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 250 MQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNegfTY-ISLLSVPFGGVGHSG 328
Cdd:cd07091 379 AKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVN---TYnVFDAAVPFGGFKQSG 455
|
...
gi 2217281694 329 MGR 331
Cdd:cd07091 456 FGR 458
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
23-337 |
2.39e-51 |
|
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: 177.89 E-value: 2.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 23 PFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSeiSQGTEKVLAEV-------LPQYLdqscFAVVLGGPQETGQL 95
Cdd:cd07101 118 PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPD--SQTALTALWAVellieagLPRDL----WQVVTGPGSEVGGA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 96 LEHKLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPD--YVLCS- 172
Cdd:cd07101 192 IVDNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIEriYVHESv 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 173 -PEMQERLLPALQSTITrfyGDDPQSSPNLGHIINQKQFQRLRALLGCSR-----VAIGGQSnesdR------YIAPTVL 240
Cdd:cd07101 272 yDEFVRRFVARTRALRL---GAALDYGPDMGSLISQAQLDRVTAHVDDAVakgatVLAGGRA----RpdlgpyFYEPTVL 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 241 VDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGF--TYISlLS 318
Cdd:cd07101 345 TGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEGYaaAWAS-ID 423
|
330 340
....*....|....*....|....
gi 2217281694 319 VPFGGVGHSGMGRYHG-----KFT 337
Cdd:cd07101 424 APMGGMKDSGLGRRHGaegllKYT 447
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
21-341 |
2.68e-51 |
|
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: 178.37 E-value: 2.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 21 KEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGPQETGQ-LLEH 98
Cdd:cd07144 142 HEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVNIIPGYGAVAGSaLAEH 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 99 -KLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSPEMQE 177
Cdd:cd07144 222 pDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYD 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 178 RLLPALQSTITRFY--GDDPQSSPNLGHIINQKQFQRLRALL------GCSRVAIG---GQSNESDRYIAPTVLVDVQET 246
Cdd:cd07144 302 KFVEKFVEHVKQNYkvGSPFDDDTVVGPQVSKTQYDRVLSYIekgkkeGAKLVYGGekaPEGLGKGYFIPPTIFTDVPQD 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 247 EPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEgfTYISLLSVPFGGVGH 326
Cdd:cd07144 382 MRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINS--SNDSDVGVPFGGFKM 459
|
330
....*....|....*
gi 2217281694 327 SGMGRYHGKFTFDTF 341
Cdd:cd07144 460 SGIGRELGEYGLETY 474
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
4-349 |
5.98e-51 |
|
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: 177.00 E-value: 5.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 4 EPRSTnlfMKLDSVFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCF 82
Cdd:cd07139 121 ERRPG---SGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAgLPPGVV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 83 AVVLGGPQETGQLLEHK-LDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQ 161
Cdd:cd07139 198 NVVPADREVGEYLVRHPgVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQ 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 162 TCVAPDYVLCSPEMQERLLPALQSTITRF-YGD--DPqsSPNLGHIINQKQFQRL-----RALLGCSRVAIGGQSNES-D 232
Cdd:cd07139 278 VCVALTRILVPRSRYDEVVEALAAAVAALkVGDplDP--ATQIGPLASARQRERVegyiaKGRAEGARLVTGGGRPAGlD 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 233 R--YIAPTVLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNeg 310
Cdd:cd07139 356 RgwFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-- 433
|
330 340 350
....*....|....*....|....*....|....*....
gi 2217281694 311 fTYISLLSVPFGGVGHSGMGRYHGKFTFDTFSHHRTCLL 349
Cdd:cd07139 434 -GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
16-314 |
1.13e-50 |
|
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: 176.30 E-value: 1.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 16 SVFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEV-----LPQYLdqscFAVVLGGPQ 90
Cdd:cd07088 126 NIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELvdeagLPAGV----LNIVTGRGS 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 91 ETGQLL-EH-KLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPD- 167
Cdd:cd07088 202 VVGDALvAHpKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAEr 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 168 -YVLCS--PEMQERLLPALQSTItrfYGDDPQSSPNLGHIINQKQFQRL-----RALLGCSRVAIGGQSNESDR--YIAP 237
Cdd:cd07088 282 vYVHEDiyDEFMEKLVEKMKAVK---VGDPFDAATDMGPLVNEAALDKVeemveRAVEAGATLLTGGKRPEGEKgyFYEP 358
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217281694 238 TVLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSsqvVNQMLERTSSGSFGgnEgfTYI 314
Cdd:cd07088 359 TVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTEN---LNTAMRATNELEFG--E--TYI 428
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
15-346 |
2.01e-50 |
|
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: 174.69 E-value: 2.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 15 DSVFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGPQE-- 91
Cdd:cd07105 90 TLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAgLPKGVLNVVTHSPEDap 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 92 --TGQLLEHKL-DYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDY 168
Cdd:cd07105 170 evVEALIAHPAvRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTER 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 169 VLCSPEMQERLLPALQSTITRFYGDDPQsspnLGHIINQKQFQRLRALL------GcSRVAIGGQSNESDR--YIAPTVL 240
Cdd:cd07105 250 IIVHESIADEFVEKLKAAAEKLFAGPVV----LGSLVSAAAADRVKELVddalskG-AKLVVGGLADESPSgtSMPPTIL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 241 VDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEkplalYAFSNS--SQVVNQMLE---RTSSGSfggnegfTYIS 315
Cdd:cd07105 325 DNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSE-----YGLSAAvfTRDLARALAvakRIESGA-------VHIN 392
|
330 340 350
....*....|....*....|....*....|....*..
gi 2217281694 316 LLSV------PFGGVGHSGMGRYHGKFTFDTFSHHRT 346
Cdd:cd07105 393 GMTVhdeptlPHGGVKSSGYGRFNGKWGIDEFTETKW 429
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
15-342 |
3.26e-50 |
|
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: 175.00 E-value: 3.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 15 DSVFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGPQETG 93
Cdd:TIGR01804 125 SFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAgLPKGVFNVVQGDGAEVG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 94 QLL-EHKL-DYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLC 171
Cdd:TIGR01804 205 PLLvNHPDvAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFV 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 172 SPEMQERLLPALQSTITRFYGDDP-QSSPNLGHIINQKQFQRLRALLGC-----SRVAIGGQSNESDR-----YIAPTVL 240
Cdd:TIGR01804 285 HKKIKERFLARLVERTERIKLGDPfDEATEMGPLISAAHRDKVLSYIEKgkaegATLATGGGRPENVGlqngfFVEPTVF 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 241 VDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNegfTY-ISLLSV 319
Cdd:TIGR01804 365 ADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWIN---TYnLYPAEA 441
|
330 340
....*....|....*....|...
gi 2217281694 320 PFGGVGHSGMGRYHGKFTFDTFS 342
Cdd:TIGR01804 442 PFGGYKQSGIGRENGKAALAHYT 464
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
17-330 |
1.25e-49 |
|
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: 173.31 E-value: 1.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 17 VFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGPQETGQL 95
Cdd:cd07146 114 IFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAgLPPDMLSVVTGEPGEIGDE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 96 LEH--KLDYIFFTGSPRVGKIVmtAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSP 173
Cdd:cd07146 194 LIThpDVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 174 EMQERLLPALQSTITRF-YGDDPQSSPNLGHIINQK---QFQR--LRALLGCSRVAIGGQSNESdrYIAPTVLVDVQETE 247
Cdd:cd07146 272 SVADEFVDLLVEKSAALvVGDPMDPATDMGTVIDEEaaiQIENrvEEAIAQGARVLLGNQRQGA--LYAPTVLDHVPPDA 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 248 PVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYISLLSvPFGGVGHS 327
Cdd:cd07146 350 ELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEVPGFRSELS-PFGGVKDS 428
|
...
gi 2217281694 328 GMG 330
Cdd:cd07146 429 GLG 431
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
17-331 |
1.47e-49 |
|
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: 173.12 E-value: 1.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 17 VFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEV-----LPQYLdqscFAVVLGGPQE 91
Cdd:cd07114 113 NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLaeeagFPPGV----VNVVTGFGPE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 92 TGQLL-EHKL-DYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYV 169
Cdd:cd07114 189 TGEALvEHPLvAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 170 LCSPEMQERLLPALqSTITRF--YGDDPQSSPNLGHIINQKQFQRLRALLGCS-----RVAIGGQSNESDR-----YIAP 237
Cdd:cd07114 269 LVQRSIYDEFVERL-VARARAirVGDPLDPETQMGPLATERQLEKVERYVARAreegaRVLTGGERPSGADlgagyFFEP 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 238 TVLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNegfTYISL- 316
Cdd:cd07114 348 TILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVN---TYRALs 424
|
330
....*....|....*
gi 2217281694 317 LSVPFGGVGHSGMGR 331
Cdd:cd07114 425 PSSPFGGFKDSGIGR 439
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
18-331 |
9.81e-49 |
|
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: 170.85 E-value: 9.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 18 FIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQ-YLDQSCFAVVLGGPQETG-QL 95
Cdd:cd07149 118 FTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEaGLPKGALNVVTGSGETVGdAL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 96 LEHK-LDYIFFTGSPRVGKIVMTAATkhLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSPE 174
Cdd:cd07149 198 VTDPrVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHED 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 175 MQERLLPALQSTITRF-YGDDPQSSPNLGHIINQKQFQRLR-----ALLGCSRVAIGGQSNEsdRYIAPTVLVDVQETEP 248
Cdd:cd07149 276 IYDEFLERFVAATKKLvVGDPLDEDTDVGPMISEAEAERIEewveeAVEGGARLLTGGKRDG--AILEPTVLTDVPPDMK 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 249 VMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYiSLLSVPFGGVGHSG 328
Cdd:cd07149 354 VVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINDSSTF-RVDHMPYGGVKESG 432
|
...
gi 2217281694 329 MGR 331
Cdd:cd07149 433 TGR 435
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
17-346 |
1.81e-47 |
|
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: 167.81 E-value: 1.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 17 VFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGPQETGQ- 94
Cdd:cd07097 129 VETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAgLPAGVFNLVMGSGSEVGQa 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 95 LLEHK-LDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSP 173
Cdd:cd07097 209 LVEHPdVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTE 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 174 EMQERLLPAL-QSTITRFYGDDPQSSPNLGHIINQKQFQR-LRAL-LG---CSRVAIGGQSNESDR---YIAPTVLVDVQ 244
Cdd:cd07097 289 GIHDRFVEALvERTKALKVGDALDEGVDIGPVVSERQLEKdLRYIeIArseGAKLVYGGERLKRPDegyYLAPALFAGVT 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 245 ETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSG------SFGGNEgftyislLS 318
Cdd:cd07097 369 NDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGvvmvnlPTAGVD-------YH 441
|
330 340
....*....|....*....|....*....
gi 2217281694 319 VPFGGVGHSGMG-RYHGKFTFDTFSHHRT 346
Cdd:cd07097 442 VPFGGRKGSSYGpREQGEAALEFYTTIKT 470
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
17-343 |
6.94e-47 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 166.83 E-value: 6.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 17 VFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGPQETGQ- 94
Cdd:PLN02467 145 GYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVgLPPGVLNVVTGLGTEAGAp 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 95 LLEHK-LDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDpqtVANRVAW--F-CYFNAGQTCVAPDYVL 170
Cdd:PLN02467 225 LASHPgVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVD---LDKAVEWamFgCFWTNGQICSATSRLL 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 171 C----SPEMQERLLPALQStITrfYGDDPQSSPNLGHIINQKQFQRLRALLGCSR-----VAIGG---QSNESDRYIAPT 238
Cdd:PLN02467 302 VheriASEFLEKLVKWAKN-IK--ISDPLEEGCRLGPVVSEGQYEKVLKFISTAKsegatILCGGkrpEHLKKGFFIEPT 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 239 VLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGN---EGFTYis 315
Cdd:PLN02467 379 IITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINcsqPCFCQ-- 456
|
330 340
....*....|....*....|....*...
gi 2217281694 316 llsVPFGGVGHSGMGRYHGKFTFDTFSH 343
Cdd:PLN02467 457 ---APWGGIKRSGFGRELGEWGLENYLS 481
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
19-342 |
1.70e-46 |
|
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: 165.17 E-value: 1.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 19 IWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSE---ISQGTekVLAEVLPQY-LDQSCFAVVLGGPQETG- 93
Cdd:cd07151 126 VYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASdtpITGGL--LLAKIFEEAgLPKGVLNVVVGAGSEIGd 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 94 QLLEHKL-DYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCS 172
Cdd:cd07151 204 AFVEHPVpRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVH 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 173 PEMQERLLPALQSTITRF-YGDDPQSSPNLGHIINQKQFQRL-----RALLGCSRVAIGGQSNesDRYIAPTVLVDVQET 246
Cdd:cd07151 284 EDVYDEFVEKFVERVKALpYGDPSDPDTVVGPLINESQVDGLldkieQAVEEGATLLVGGEAE--GNVLEPTVLSDVTND 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 247 EPVMQEEIFGPILPIVNVQSVDEAIKFINRQEkplalyaFSNSSQVVNQMLERTSSGSFGGNEGFTYISLLSV------P 320
Cdd:cd07151 362 MEIAREEIFGPVAPIIKADDEEEALELANDTE-------YGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVndephvP 434
|
330 340
....*....|....*....|..
gi 2217281694 321 FGGVGHSGMGRYHGKFTFDTFS 342
Cdd:cd07151 435 FGGEKNSGLGRFNGEWALEEFT 456
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
21-360 |
2.53e-46 |
|
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: 165.18 E-value: 2.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 21 KEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGPQETGQ-LLEH 98
Cdd:cd07119 132 REPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAgLPAGVVNLVTGSGATVGAeLAES 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 99 K-LDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSPEMQE 177
Cdd:cd07119 212 PdVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHD 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 178 RLLPALQSTITRF---YGDDPqsSPNLGHIINQKQFQRLRALLGC-----SRVAIGGQSNESDR-----YIAPTVLVDVQ 244
Cdd:cd07119 292 KFVAALAERAKKIklgNGLDA--DTEMGPLVSAEHREKVLSYIQLgkeegARLVCGGKRPTGDElakgyFVEPTIFDDVD 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 245 ETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNE-GFTYIsllSVPFGG 323
Cdd:cd07119 370 RTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDyHPYFA---EAPWGG 446
|
330 340 350
....*....|....*....|....*....|....*..
gi 2217281694 324 VGHSGMGRYhgkftfdtfshhrtclLAPSGLEKLKEI 360
Cdd:cd07119 447 YKQSGIGRE----------------LGPTGLEEYQET 467
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
17-346 |
5.52e-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: 163.67 E-value: 5.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 17 VFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGPQETG-Q 94
Cdd:cd07145 117 AFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPGVINVVTGYGSEVGdE 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 95 LLEH-KLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSP 173
Cdd:cd07145 197 IVTNpKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 174 EMQERLLPALQSTITRFYGDDP-QSSPNLGHIINQKQFQRLRALLGCS-----RVAIGGQSNESDrYIAPTVLVDVQETE 247
Cdd:cd07145 277 EVYDKFLKLLVEKVKKLKVGDPlDESTDLGPLISPEAVERMENLVNDAvekggKILYGGKRDEGS-FFPPTVLENDTPDM 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 248 PVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSsqvVNQMLERTSSGSFGG---NEGfTYISLLSVPFGGV 324
Cdd:cd07145 356 IVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTND---INRALKVARELEAGGvviNDS-TRFRWDNLPFGGF 431
|
330 340
....*....|....*....|..
gi 2217281694 325 GHSGMGRYHGKFTFDTFSHHRT 346
Cdd:cd07145 432 KKSGIGREGVRYTMLEMTEEKT 453
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
21-346 |
6.44e-46 |
|
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: 163.37 E-value: 6.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 21 KEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVL-PQYLDQSCFAVVLGGPQETGQLL--E 97
Cdd:cd07094 121 REPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILvEAGVPEGVLQVVTGEREVLGDAFaaD 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 98 HKLDYIFFTGSPRVGKIVMTAATKhlTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSPEMQE 177
Cdd:cd07094 201 ERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYD 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 178 RLLPALQSTITRFYGDDP-QSSPNLGHIINQKQFQRL-----RALLGCSRVAIGGQsnESDRYIAPTVLVDVQETEPVMQ 251
Cdd:cd07094 279 EFIEAFVAAVKKLKVGDPlDEDTDVGPLISEEAAERVerwveEAVEAGARLLCGGE--RDGALFKPTVLEDVPRDTKLST 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 252 EEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYISlLSVPFGGVGHSGMGR 331
Cdd:cd07094 357 EETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDSSAFRT-DWMPFGGVKESGVGR 435
|
330
....*....|....*
gi 2217281694 332 YHGKFTFDTFSHHRT 346
Cdd:cd07094 436 EGVPYAMEEMTEEKT 450
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
17-341 |
2.70e-45 |
|
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: 162.28 E-value: 2.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 17 VFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTE----KVLAEV-LPQyldqSCFAVVLG-GPQ 90
Cdd:cd07142 135 VYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSAllaaKLAAEAgLPD----GVLNIVTGfGPT 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 91 ETGQLLEHK-LDYIFFTGSPRVGKIVMTAATK-HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDY 168
Cdd:cd07142 211 AGAAIASHMdVDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSR 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 169 VLCSPEMQERLLP-ALQSTITRFYGDDPQSSPNLGHIINQKQFQRLRALL------GCSRVAIGGQSNESDRYIAPTVLV 241
Cdd:cd07142 291 TFVHESIYDEFVEkAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIehgkeeGATLITGGDRIGSKGYYIQPTIFS 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 242 DVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGN--EGFTyislLSV 319
Cdd:cd07142 371 DVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcyDVFD----ASI 446
|
330 340
....*....|....*....|..
gi 2217281694 320 PFGGVGHSGMGRYHGKFTFDTF 341
Cdd:cd07142 447 PFGGYKMSGIGREKGIYALNNY 468
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
23-337 |
4.19e-45 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 162.74 E-value: 4.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 23 PFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSeiSQGTEKVLAEV-------LPQYLdqscFAVVLGGPQETGQL 95
Cdd:PRK09407 154 PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPD--SQTPLTALAAVellyeagLPRDL----WQVVTGPGPVVGTA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 96 LEHKLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPD--YVLCS- 172
Cdd:PRK09407 228 LVDNADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIEriYVHESi 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 173 -PEMQERLLPALQS-TITRFYGDDPQsspnLGHIINQKQFQRLRALLGCSR-----VAIGGQSnesdR------YIAPTV 239
Cdd:PRK09407 308 yDEFVRAFVAAVRAmRLGAGYDYSAD----MGSLISEAQLETVSAHVDDAVakgatVLAGGKA----RpdlgplFYEPTV 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 240 LVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINrqEKPLALYA--FSNSSQVVNQMLERTSSGSFGGNEGF--TYIS 315
Cdd:PRK09407 380 LTGVTPDMELAREETFGPVVSVYPVADVDEAVERAN--DTPYGLNAsvWTGDTARGRAIAARIRAGTVNVNEGYaaAWGS 457
|
330 340
....*....|....*....|....*..
gi 2217281694 316 lLSVPFGGVGHSGMGRYHG-----KFT 337
Cdd:PRK09407 458 -VDAPMGGMKDSGLGRRHGaegllKYT 483
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
22-346 |
5.73e-45 |
|
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: 161.54 E-value: 5.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 22 EPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGPQETGQLLE-H- 98
Cdd:cd07143 143 EPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGYGRTCGNAISsHm 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 99 KLDYIFFTGSPRVGKIVMTAATK-HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSPEMQE 177
Cdd:cd07143 223 DIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYD 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 178 RLLPALQSTITRFYGDDP-QSSPNLGHIINQKQFQRLRALLGCSR-----VAIGGQSNESDRY-IAPTVLVDVQETEPVM 250
Cdd:cd07143 303 KFVKRFKEKAKKLKVGDPfAEDTFQGPQVSQIQYERIMSYIESGKaegatVETGGKRHGNEGYfIEPTIFTDVTEDMKIV 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 251 QEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSsqvVNQMLeRTSSGSFGGNEGFTYISLLS--VPFGGVGHSG 328
Cdd:cd07143 383 KEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNN---INNAI-RVANALKAGTVWVNCYNLLHhqVPFGGYKQSG 458
|
330
....*....|....*...
gi 2217281694 329 MGRYHGKFTFDTFSHHRT 346
Cdd:cd07143 459 IGRELGEYALENYTQIKA 476
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
21-346 |
8.63e-45 |
|
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: 160.55 E-value: 8.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 21 KEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGpQETGQLLEHK 99
Cdd:cd07090 114 REPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAgLPDGVFNVVQGG-GETGQLLCEH 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 100 LDY--IFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSPEMQE 177
Cdd:cd07090 193 PDVakVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKD 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 178 RLLPALQSTITRFYGDDP-QSSPNLGHIINQKQFQRLRALLGC-----SRVAIGGQSNESDR------YIAPTVLVDVQE 245
Cdd:cd07090 273 EFTERLVERTKKIRIGDPlDEDTQMGALISEEHLEKVLGYIESakqegAKVLCGGERVVPEDglengfYVSPCVLTDCTD 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 246 TEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNegfTY-ISLLSVPFGGV 324
Cdd:cd07090 353 DMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWIN---TYnISPVEVPFGGY 429
|
330 340
....*....|....*....|..
gi 2217281694 325 GHSGMGRYHGKFTFDTFSHHRT 346
Cdd:cd07090 430 KQSGFGRENGTAALEHYTQLKT 451
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
18-343 |
2.32e-44 |
|
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: 159.82 E-value: 2.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 18 FIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQYLDQSCFAVVLGGPQETGQ-LL 96
Cdd:cd07559 131 YHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVNVVTGFGSEAGKpLA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 97 EHK-LDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNP-------CYVDDNCDPQTVANRVAWFcyFNAGQTCVAPDY 168
Cdd:cd07559 211 SHPrIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPniffddaMDADDDFDDKAEEGQLGFA--FNQGEVCTCPSR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 169 VLCSPEMQERLLPALQSTITRFYGDDPQ-SSPNLGHIINQKQFQRLRALL------GCsRVAIGGQSNESDR-----YIA 236
Cdd:cd07559 289 ALVQESIYDEFIERAVERFEAIKVGNPLdPETMMGAQVSKDQLEKILSYVdigkeeGA-EVLTGGERLTLGGldkgyFYE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 237 PTVLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNegfTYISL 316
Cdd:cd07559 368 PTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVN---CYHQY 444
|
330 340
....*....|....*....|....*...
gi 2217281694 317 LS-VPFGGVGHSGMGRYHGKFTFDTFSH 343
Cdd:cd07559 445 PAhAPFGGYKKSGIGRETHKMMLDHYQQ 472
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
18-346 |
2.72e-44 |
|
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: 159.44 E-value: 2.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 18 FIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGPQETGQ-L 95
Cdd:cd07131 130 MTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAgLPPGVVNVVHGRGEEVGEaL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 96 LEH-KLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSPE 174
Cdd:cd07131 210 VEHpDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHES 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 175 MQERLLPALQSTITRFYGDDPQSSPNL-GHIINQKQFQR------------LRALLGCSRVAIGGQsnESDRYIAPTVLV 241
Cdd:cd07131 290 VYDEFLKRFVERAKRLRVGDGLDEETDmGPLINEAQLEKvlnyneigkeegATLLLGGERLTGGGY--EKGYFVEPTVFT 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 242 DVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSgsfggneGFTYISLLSV-- 319
Cdd:cd07131 368 DVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEA-------GITYVNAPTIga 440
|
330 340 350
....*....|....*....|....*....|..
gi 2217281694 320 ----PFGGVGHSGMG-RYHGKFTFDTFSHHRT 346
Cdd:cd07131 441 evhlPFGGVKKSGNGhREAGTTALDAFTEWKA 472
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
21-346 |
4.63e-44 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 159.22 E-value: 4.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 21 KEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLG-GPQETGQLLEH 98
Cdd:PLN02766 156 KEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAgVPDGVINVVTGfGPTAGAAIASH 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 99 -KLDYIFFTGSPRVGKIVM-TAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSPEMQ 176
Cdd:PLN02766 236 mDVDKVSFTGSTEVGRKIMqAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIY 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 177 ERLLPALQSTITRFYGDDP-QSSPNLGHIINQKQFQRLRALL------GCSRVAIGGQSNESDRYIAPTVLVDVQETEPV 249
Cdd:PLN02766 316 DEFVKKLVEKAKDWVVGDPfDPRARQGPQVDKQQFEKILSYIehgkreGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKI 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 250 MQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYISllSVPFGGVGHSGM 329
Cdd:PLN02766 396 AQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDP--DCPFGGYKMSGF 473
|
330
....*....|....*..
gi 2217281694 330 GRYHGKFTFDTFSHHRT 346
Cdd:PLN02766 474 GRDQGMDALDKYLQVKS 490
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
22-330 |
7.77e-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: 158.93 E-value: 7.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 22 EPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGPQETGQ-LLEH- 98
Cdd:cd07124 165 RPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAgLPPGVVNFLPGPGEEVGDyLVEHp 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 99 KLDYIFFTGSPRVGKIVMTAATK------HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVApdyvlCS 172
Cdd:cd07124 245 DVRFIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSA-----CS 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 173 ---------PEMQERLLPALQSTITrfyGDDPQSSPNLGHIINQKQFQRLR----ALLGCSRVAIGGQSNESDR---YIA 236
Cdd:cd07124 320 rvivhesvyDEFLERLVERTKALKV---GDPEDPEVYMGPVIDKGARDRIRryieIGKSEGRLLLGGEVLELAAegyFVQ 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 237 PTVLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYISL 316
Cdd:cd07124 397 PTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALV 476
|
330
....*....|....
gi 2217281694 317 LSVPFGGVGHSGMG 330
Cdd:cd07124 477 GRQPFGGFKMSGTG 490
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
16-334 |
1.10e-43 |
|
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: 157.99 E-value: 1.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 16 SVFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGPQETGQ 94
Cdd:cd07113 135 TAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAgIPDGVLNVVNGKGAVGAQ 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 95 LLEH-KLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSP 173
Cdd:cd07113 215 LISHpDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHR 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 174 EMQERLLPALQSTITRFYGDDPQS-SPNLGHIINQKQFQRLRALLGCSR-----VAIGGQSNESDRY-IAPTVLVDVQET 246
Cdd:cd07113 295 SKFDELVTKLKQALSSFQVGSPMDeSVMFGPLANQPHFDKVCSYLDDARaegdeIVRGGEALAGEGYfVQPTLVLARSAD 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 247 EPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEgFTYISlLSVPFGGVGH 326
Cdd:cd07113 375 SRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNM-HTFLD-PAVPFGGMKQ 452
|
....*...
gi 2217281694 327 SGMGRYHG 334
Cdd:cd07113 453 SGIGREFG 460
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
21-334 |
2.25e-42 |
|
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: 154.07 E-value: 2.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 21 KEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQYLDQSCFAVVLGGPQETGQ-LLEHK 99
Cdd:cd07107 114 REPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREVLPPGVFNILPGDGATAGAaLVRHP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 100 L-DYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANR-VAWFCYFNAGQTCVAPDYVLCSPEMQE 177
Cdd:cd07107 194 DvKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAaVAGMNFTWCGQSCGSTSRLFVHESIYD 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 178 RLLPALQSTITRFYGDDPqSSPN--LGHIINQKQFQRLRALLGCSR------VAIGGQSN----ESDRYIAPTVLVDVQE 245
Cdd:cd07107 274 EVLARVVERVAAIKVGDP-TDPAttMGPLVSRQQYDRVMHYIDSAKregarlVTGGGRPEgpalEGGFYVEPTVFADVTP 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 246 TEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYisLLSVPFGGVG 325
Cdd:cd07107 353 GMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVWINGSSRH--FLGAPFGGVK 430
|
....*....
gi 2217281694 326 HSGMGRYHG 334
Cdd:cd07107 431 NSGIGREEC 439
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
15-314 |
5.71e-42 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 151.81 E-value: 5.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 15 DSVFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGPQETG 93
Cdd:PRK10090 63 ENILLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 94 QLL--EHKLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCD-----PQTVANRVawfcyFNAGQTCVAP 166
Cdd:PRK10090 143 QELagNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADldlavKAIVDSRV-----INSGQVCNCA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 167 D--YVLCS--PEMQERLLPALQSTItrfYGDDPQ-SSPNLGHIINQKQFQRL-----RALLGCSRVAIGGQSNESDRYI- 235
Cdd:PRK10090 218 ErvYVQKGiyDQFVNRLGEAMQAVQ---FGNPAErNDIAMGPLINAAALERVeqkvaRAVEEGARVALGGKAVEGKGYYy 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 236 APTVLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEkplalYAFSNS--SQVVNQMLERTSSGSFGGnegfTY 313
Cdd:PRK10090 295 PPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSD-----YGLTSSiyTQNLNVAMKAIKGLKFGE----TY 365
|
.
gi 2217281694 314 I 314
Cdd:PRK10090 366 I 366
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
19-342 |
2.20e-41 |
|
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: 151.45 E-value: 2.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 19 IWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQYLDQSCFAVVLGGPQETGQ-LLE 97
Cdd:cd07117 132 VLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNIVTGKGSKSGEyLLN 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 98 HK-LDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSPEMQ 176
Cdd:cd07117 212 HPgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 177 ERLLPALQSTITRFYGDDPQS-SPNLGHIINQKQFQRLRALL------GCsRVAIGGQ---SNESDR--YIAPTVLVDVQ 244
Cdd:cd07117 292 DEFVAKLKEKFENVKVGNPLDpDTQMGAQVNKDQLDKILSYVdiakeeGA-KILTGGHrltENGLDKgfFIEPTLIVNVT 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 245 ETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFsnsSQVVNQMLeRTSSGSFGG----NegfTYISLLS-V 319
Cdd:cd07117 371 NDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVF---TKDINRAL-RVARAVETGrvwvN---TYNQIPAgA 443
|
330 340
....*....|....*....|...
gi 2217281694 320 PFGGVGHSGMGRYHGKFTFDTFS 342
Cdd:cd07117 444 PFGGYKKSGIGRETHKSMLDAYT 466
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
1-346 |
5.00e-41 |
|
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: 149.53 E-value: 5.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 1 MKDEPRSTnlfmKLDSVFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQ 79
Cdd:cd07100 78 LADEPIET----DAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAgFPE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 80 SCFAVVLGGPQETGQLLEHKL-DYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFN 158
Cdd:cd07100 154 GVFQNLLIDSDQVEAIIADPRvRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQN 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 159 AGQTCVAP----------DyvlcspEMQERLLPALQSTITrfyGDD--------PQSSPNLGHIInQKQFQRLRA----- 215
Cdd:cd07100 234 AGQSCIAAkrfivhedvyD------EFLEKFVEAMAALKV---GDPmdedtdlgPLARKDLRDEL-HEQVEEAVAagatl 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 216 LLGCSRVAIGGQsnesdrYIAPTVLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQ 295
Cdd:cd07100 304 LLGGKRPDGPGA------FYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAER 377
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217281694 296 MLERTSSGSfggnegfTYI-----SLLSVPFGGVGHSGMGRYHGKFTFDTFSHHRT 346
Cdd:cd07100 378 VARRLEAGM-------VFIngmvkSDPRLPFGGVKRSGYGRELGRFGIREFVNIKT 426
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
21-346 |
5.44e-41 |
|
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: 150.58 E-value: 5.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 21 KEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAE-------------VLPQYldqscfavvlg 87
Cdd:cd07141 143 HEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASlikeagfppgvvnVVPGY----------- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 88 GPQETGQLLEH-KLDYIFFTGSPRVGKIVMTAATK-HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVA 165
Cdd:cd07141 212 GPTAGAAISSHpDIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 166 PDYVLC-SPEMQERLLPALQSTITRFYGDDPQSSPNLGHIINQKQFQRLRALL------GCSRVAIGGQSNESDRYIAPT 238
Cdd:cd07141 292 GSRTFVqESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIesgkkeGAKLECGGKRHGDKGYFIQPT 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 239 VLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNegfTYiSLLS 318
Cdd:cd07141 372 VFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVN---CY-NVVS 447
|
330 340 350
....*....|....*....|....*....|
gi 2217281694 319 V--PFGGVGHSGMGRYHGKFTFDTFSHHRT 346
Cdd:cd07141 448 PqaPFGGYKMSGNGRELGEYGLQEYTEVKT 477
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
19-331 |
2.66e-40 |
|
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: 148.49 E-value: 2.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 19 IWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSeiSQGTekVLAEVLPQYLDQSCF-----AVVLGGPQETG 93
Cdd:cd07082 137 VRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPA--TQGV--LLGIPLAEAFHDAGFpkgvvNVVTGRGREIG 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 94 Q-LLEH-KLDYIFFTGSPRVGKIVMTAAtkHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLC 171
Cdd:cd07082 213 DpLVTHgRIDVISFTGSTEVGNRLKKQH--PMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLV 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 172 SPEMQERLLPALQSTITRFYGDDP-QSSPNLGHIINQKQFQRLRALL------GcSRVAIGGQsNESDRYIAPTVLVDVQ 244
Cdd:cd07082 291 HESVADELVELLKEEVAKLKVGMPwDNGVDITPLIDPKSADFVEGLIddavakG-ATVLNGGG-REGGNLIYPTLLDPVT 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 245 ETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNS----SQVVNQML-------ERTSSG--SFggnegf 311
Cdd:cd07082 369 PDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDinkaRKLADALEvgtvninSKCQRGpdHF------ 442
|
330 340
....*....|....*....|
gi 2217281694 312 tyisllsvPFGGVGHSGMGR 331
Cdd:cd07082 443 --------PFLGRKDSGIGT 454
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
22-328 |
3.66e-40 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 148.93 E-value: 3.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 22 EPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGPQETGQ-LLEH- 98
Cdd:PRK03137 170 IPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAgLPAGVVNFVPGSGSEVGDyLVDHp 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 99 KLDYIFFTGSPRVGKIVMTAATK------HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVApdyvlCS 172
Cdd:PRK03137 250 KTRFITFTGSREVGLRIYERAAKvqpgqiWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSA-----CS 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 173 ---------PEMQERLLpALQSTITrfYGDdPQSSPNLGHIINQKQFQRLRALL----GCSRVAIGGQSNESDRY-IAPT 238
Cdd:PRK03137 325 raivhedvyDEVLEKVV-ELTKELT--VGN-PEDNAYMGPVINQASFDKIMSYIeigkEEGRLVLGGEGDDSKGYfIQPT 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 239 VLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYISLLS 318
Cdd:PRK03137 401 IFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGY 480
|
330
....*....|
gi 2217281694 319 VPFGGVGHSG 328
Cdd:PRK03137 481 HPFGGFNMSG 490
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
19-350 |
5.76e-40 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 148.12 E-value: 5.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 19 IWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGPQETGQLL- 96
Cdd:PRK09847 153 IVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGFGHEAGQALs 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 97 -EHKLDYIFFTGSPRVGKIVMT-AATKHLTPVTLELGGKNPCYVDDNC-DPQTVANRVAWFCYFNAGQTCVAPDYVLCSP 173
Cdd:PRK09847 233 rHNDIDAIAFTGSTRTGKQLLKdAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 174 EMQERLLPALQSTITRFYGDDP-QSSPNLGHIINQKQFQRLRALL--GCSR--VAIGGQSNESDRYIAPTVLVDVQETEP 248
Cdd:PRK09847 313 SIADEFLALLKQQAQNWQPGHPlDPATTMGTLIDCAHADSVHSFIreGESKgqLLLDGRNAGLAAAIGPTIFVDVDPNAS 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 249 VMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSF---GGNEGFtyislLSVPFGGVG 325
Cdd:PRK09847 393 LSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVfvnNYNDGD-----MTVPFGGYK 467
|
330 340
....*....|....*....|....*
gi 2217281694 326 HSGMGRYHGKFTFDTFSHHRTCLLA 350
Cdd:PRK09847 468 QSGNGRDKSLHALEKFTELKTIWIS 492
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
19-347 |
1.75e-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: 146.55 E-value: 1.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 19 IWKePFGLVLIIAPWNYPL-----NLTLvllvgALAAGSCVVLKPSE----ISQGTEKVLAEVLPQY-LDQSCFAVVLGG 88
Cdd:cd07086 130 QWN-PLGVVGVITAFNFPVavpgwNAAI-----ALVCGNTVVWKPSEttplTAIAVTKILAEVLEKNgLPPGVVNLVTGG 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 89 pQETGQLLEH--KLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAP 166
Cdd:cd07086 204 -GDGGELLVHdpRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTT 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 167 DYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNL-GHIINQKQFQR-LRA-----------LLGCSRVAIGGQSNesdr 233
Cdd:cd07086 283 RRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLvGPLINQAAVEKyLNAieiaksqggtvLTGGKRIDGGEPGN---- 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 234 YIAPTVLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSfggneGFTY 313
Cdd:cd07086 359 YVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKGSDC-----GIVN 433
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2217281694 314 ISLLSV------PFGGVGHSGMGRYHGKFTFDTFSHHRTC 347
Cdd:cd07086 434 VNIPTSgaeiggAFGGEKETGGGRESGSDAWKQYMRRSTC 473
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
17-333 |
1.02e-38 |
|
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: 144.20 E-value: 1.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 17 VFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGPQETGQL 95
Cdd:cd07085 130 TYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAgLPDGVLNVVHGGKEAVNAL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 96 LEHKL-DYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSPE 174
Cdd:cd07085 210 LDHPDiKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGD 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 175 MQERLLPALQSTITRF---YGDDPqsSPNLGHIINQKQFQRLRALLGCS-----RVAIGGQSNESDRY-----IAPTVLV 241
Cdd:cd07085 290 EADEWIPKLVERAKKLkvgAGDDP--GADMGPVISPAAKERIEGLIESGveegaKLVLDGRGVKVPGYengnfVGPTILD 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 242 DVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEkplalYA-----FSNSSQVVNQMLERTSSGSFGGNEGftyisl 316
Cdd:cd07085 368 NVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANP-----YGngaaiFTRSGAAARKFQREVDAGMVGINVP------ 436
|
330 340
....*....|....*....|..
gi 2217281694 317 LSVP-----FGGVGHSGMGRYH 333
Cdd:cd07085 437 IPVPlaffsFGGWKGSFFGDLH 458
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
17-341 |
1.01e-37 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 141.97 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 17 VFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLG-----GPQ 90
Cdd:PRK11241 140 LIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAgIPAGVFNVVTGsagavGGE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 91 ETGQLLEHKLDyifFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVL 170
Cdd:PRK11241 220 LTSNPLVRKLS---FTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLY 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 171 CSPEMQERLLPALQSTITRFY-GDDPQSSPNLGHIINQKQFQRLR-----ALLGCSRVAIGGQSNE-SDRYIAPTVLVDV 243
Cdd:PRK11241 297 VQDGVYDRFAEKLQQAVSKLHiGDGLEKGVTIGPLIDEKAVAKVEehiadALEKGARVVCGGKAHElGGNFFQPTILVDV 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 244 QETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFtyISLLSVPFGG 323
Cdd:PRK11241 377 PANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGI--ISNEVAPFGG 454
|
330
....*....|....*...
gi 2217281694 324 VGHSGMGRYHGKFTFDTF 341
Cdd:PRK11241 455 IKASGLGREGSKYGIEDY 472
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
22-341 |
1.69e-37 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 141.87 E-value: 1.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 22 EPFGLVLIIAPWNYPLnLTLVLLVG-ALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLG-GPQETGQLLEH 98
Cdd:PLN02466 194 EPIGVAGQIIPWNFPL-LMFAWKVGpALACGNTIVLKTAEQTPLSALYAAKLLHEAgLPPGVLNVVSGfGPTAGAALASH 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 99 -KLDYIFFTGSPRVGKIVMTAATK-HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSPEM- 175
Cdd:PLN02466 273 mDVDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVy 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 176 QERLLPALQSTITRFYGDDPQSSPNLGHIINQKQFQRLRALL------GCSRVAIGGQSNESDRYIAPTVLVDVQETEPV 249
Cdd:PLN02466 353 DEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIksgvesGATLECGGDRFGSKGYYIQPTVFSNVQDDMLI 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 250 MQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYISllSVPFGGVGHSGM 329
Cdd:PLN02466 433 AQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDA--AIPFGGYKMSGI 510
|
330
....*....|..
gi 2217281694 330 GRYHGKFTFDTF 341
Cdd:PLN02466 511 GREKGIYSLNNY 522
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
19-334 |
5.42e-37 |
|
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: 139.40 E-value: 5.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 19 IWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQ--YLDQSCFAVVLGGPQETGQLL 96
Cdd:cd07120 113 VLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEipSLPAGVVNLFTESGSEGAAHL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 97 --EHKLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLC--- 171
Cdd:cd07120 193 vaSPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVqrs 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 172 -SPEMQERLLPALQStITRFYGDDPQSspNLGHIINQKQFQRL-----RALLGCSRVAI-GGQSNESDR---YIAPTVLV 241
Cdd:cd07120 273 iADEVRDRLAARLAA-VKVGPGLDPAS--DMGPLIDRANVDRVdrmveRAIAAGAEVVLrGGPVTEGLAkgaFLRPTLLE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 242 DVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNegfTYISLLS-VP 320
Cdd:cd07120 350 VDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWIN---DWNKLFAeAE 426
|
330
....*....|....
gi 2217281694 321 FGGVGHSGMGRYHG 334
Cdd:cd07120 427 EGGYRQSGLGRLHG 440
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
23-331 |
3.54e-36 |
|
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: 136.99 E-value: 3.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 23 PFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVL-PQYLDQSCFAVVLGGPQETGQLLEHK-L 100
Cdd:cd07147 123 PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLaETGLPKGAFSVLPCSRDDADLLVTDErI 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 101 DYIFFTGSPRVG-KIVMTAATKHltpVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCS----PEM 175
Cdd:cd07147 203 KLLSFTGSPAVGwDLKARAGKKK---VVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHrsvyDEF 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 176 QERLLPALQSTITrfyGDDPQSSPNLGHIINQKQFQRLR-----ALLGCSRVAIGGQSNESdrYIAPTVLVDVQETEPVM 250
Cdd:cd07147 280 KSRLVARVKALKT---GDPKDDATDVGPMISESEAERVEgwvneAVDAGAKLLTGGKRDGA--LLEPTILEDVPPDMEVN 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 251 QEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYiSLLSVPFGGVGHSGMG 330
Cdd:cd07147 355 CEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINDVPTF-RVDHMPYGGVKDSGIG 433
|
.
gi 2217281694 331 R 331
Cdd:cd07147 434 R 434
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
13-335 |
5.28e-36 |
|
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: 137.14 E-value: 5.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 13 KLDSVFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGPQE 91
Cdd:cd07111 137 LLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAgLPPGVLNIVTGNGSF 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 92 TGQLLEH-KLDYIFFTGSPRVGKIV--MTAATKhlTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDY 168
Cdd:cd07111 217 GSALANHpGVDKVAFTGSTEVGRALrrATAGTG--KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSR 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 169 VLCSPEMQERLLPALQSTITRF-YGDDPQSSPNLGHIINQKQFQRLRALL------GCSRVAIGGQSNESDRYIAPTVLV 241
Cdd:cd07111 295 LLVQESVAEELIRKLKERMSHLrVGDPLDKAIDMGAIVDPAQLKRIRELVeegraeGADVFQPGADLPSKGPFYPPTLFT 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 242 DVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALyafSNSSQVVNQMLE---RTSSGSFGGNeGFTYISlLS 318
Cdd:cd07111 375 NVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAA---SVWSENLSLALEvalSLKAGVVWIN-GHNLFD-AA 449
|
330
....*....|....*..
gi 2217281694 319 VPFGGVGHSGMGRYHGK 335
Cdd:cd07111 450 AGFGGYRESGFGREGGK 466
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
23-330 |
1.37e-34 |
|
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: 133.47 E-value: 1.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 23 PFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSE----ISQGTEKVLAEV-LPQYLDQSCFAVvlgGPQETGQLLE 97
Cdd:cd07083 154 GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEdavvVGYKVFEIFHEAgFPPGVVQFLPGV---GEEVGAYLTE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 98 H-KLDYIFFTGSPRVGKIVMTAATKHLT------PVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVL 170
Cdd:cd07083 231 HeRIRGINFTGSLETGKKIYEAAARLAPgqtwfkRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 171 CSPEMQERLLPALQSTITRFYGDDPQS-SPNLGHIINQKQFQRLRALLGCSR----VAIGGQSNESDRY-IAPTVLVDVQ 244
Cdd:cd07083 311 LTQGAYEPVLERLLKRAERLSVGPPEEnGTDLGPVIDAEQEAKVLSYIEHGKnegqLVLGGKRLEGEGYfVAPTVVEEVP 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 245 ETEPVMQEEIFGPILPIVNVQSVD--EAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYiSLLSV-PF 321
Cdd:cd07083 391 PKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITG-ALVGVqPF 469
|
....*....
gi 2217281694 322 GGVGHSGMG 330
Cdd:cd07083 470 GGFKLSGTN 478
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
21-342 |
4.66e-34 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 131.54 E-value: 4.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 21 KEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVlGGPQETGQLL-EH 98
Cdd:PRK13252 140 REPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAgLPDGVFNVV-QGDGRVGAWLtEH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 99 -KLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQT------VANrvawfcYFNAGQTCVAPDYVLC 171
Cdd:PRK13252 219 pDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRaadiamLAN------FYSSGQVCTNGTRVFV 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 172 SPEMQERLLPALQSTITRFYGDDPQS-SPNLGHIINQKQFQRL------------RALLGCSRVAIGGQSNesDRYIAPT 238
Cdd:PRK13252 293 QKSIKAAFEARLLERVERIRIGDPMDpATNFGPLVSFAHRDKVlgyiekgkaegaRLLCGGERLTEGGFAN--GAFVAPT 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 239 VLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNS----SQVVNQMlertssgsfggNEGFTYI 314
Cdd:PRK13252 371 VFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADlsraHRVIHQL-----------EAGICWI 439
|
330 340 350
....*....|....*....|....*....|...
gi 2217281694 315 -----SLLSVPFGGVGHSGMGRYHGKFTFDTFS 342
Cdd:PRK13252 440 ntwgeSPAEMPVGGYKQSGIGRENGIATLEHYT 472
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
22-350 |
7.14e-34 |
|
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: 131.04 E-value: 7.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 22 EPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQYLDQSCFAVVLGGPQETGQLL--EHK 99
Cdd:cd07116 135 EPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGFGLEAGKPLasSKR 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 100 LDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNP-CYVDD--NCDPQTVANRVAWFCYF--NAGQTCVAPDYVLCSPE 174
Cdd:cd07116 215 IAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPnIFFADvmDADDAFFDKALEGFVMFalNQGEVCTCPSRALIQES 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 175 MQERLLP-ALQSTITRFYGDDPQSSPNLGHIINQKQFQRLRALLGCSR-----VAIGGQSNE-----SDRYIAPTVLVDV 243
Cdd:cd07116 295 IYDRFMErALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKeegaeVLTGGERNElggllGGGYYVPTTFKGG 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 244 QETEpVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYISllSVPFGG 323
Cdd:cd07116 375 NKMR-IFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPA--HAAFGG 451
|
330 340
....*....|....*....|....*..
gi 2217281694 324 VGHSGMGRYHGKFTFDTFSHHRTCLLA 350
Cdd:cd07116 452 YKQSGIGRENHKMMLDHYQQTKNLLVS 478
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
18-331 |
1.18e-31 |
|
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: 124.31 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 18 FIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVL-PQYLDQSCFAVVLGGPQETGQLL 96
Cdd:cd07095 92 VLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWeEAGLPPGVLNLVQGGRETGEALA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 97 EHK-LDYIFFTGSPRVGKIVMTAATKHltP---VTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCS 172
Cdd:cd07095 172 AHEgIDGLLFTGSAATGLLLHRQFAGR--PgkiLALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVP 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 173 PEMQ-ERLLPALQSTITRFYGDDPQSSPN-LGHIINQKQFQRlrALLGCSR-VAIGGQS-------NESDRYIAPTvLVD 242
Cdd:cd07095 250 DGAVgDAFLERLVEAAKRLRIGAPDAEPPfMGPLIIAAAAAR--YLLAQQDlLALGGEPllamerlVAGTAFLSPG-IID 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 243 VQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYISlLSVPFG 322
Cdd:cd07095 327 VTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTTGAS-STAPFG 405
|
....*....
gi 2217281694 323 GVGHSGMGR 331
Cdd:cd07095 406 GVGLSGNHR 414
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
18-331 |
5.35e-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: 120.29 E-value: 5.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 18 FIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAE-VLPQYLDQSCFAVVLGGPQETGQLL 96
Cdd:cd07140 142 LTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAElTVKAGFPKGVINILPGSGSLVGQRL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 97 EHKLDY--IFFTGSPRVGKIVM-TAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSP 173
Cdd:cd07140 222 SDHPDVrkLGFTGSTPIGKHIMkSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 174 EMQERLLPALQSTITRFYGDDP-QSSPNLGHIINQKQFQRL-----RALLGCSRVAIGG-QSNESDRYIAPTVLVDVQET 246
Cdd:cd07140 302 SIHDEFVRRVVEEVKKMKIGDPlDRSTDHGPQNHKAHLDKLveyceRGVKEGATLVYGGkQVDRPGFFFEPTVFTDVEDH 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 247 EPVMQEEIFGPILPIVNVQS--VDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNegfTYISL-LSVPFGG 323
Cdd:cd07140 382 MFIAKEESFGPIMIISKFDDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVN---TYNKTdVAAPFGG 458
|
....*...
gi 2217281694 324 VGHSGMGR 331
Cdd:cd07140 459 FKQSGFGK 466
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
22-330 |
1.82e-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: 107.67 E-value: 1.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 22 EPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVL-----PQYLDQscfaVVLGGPQETGQ-L 95
Cdd:cd07125 166 HGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLheagvPRDVLQ----LVPGDGEEIGEaL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 96 LEHK-LDYIFFTGSPRVGKIV--MTAATKH-LTPVTLELGGKNPCYVDDNCDP-QTVANRV--AwfcYFNAGQTCVAPDy 168
Cdd:cd07125 242 VAHPrIDGVIFTGSTETAKLInrALAERDGpILPLIAETGGKNAMIVDSTALPeQAVKDVVqsA---FGSAGQRCSALR- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 169 VLC-----SPEMQERLLPALQSTITrfygDDPQ-SSPNLGHIINQKQFQRLRALL----GCSRVAIGGQSNESD-RYIAP 237
Cdd:cd07125 318 LLYlqeeiAERFIEMLKGAMASLKV----GDPWdLSTDVGPLIDKPAGKLLRAHTelmrGEAWLIAPAPLDDGNgYFVAP 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 238 TVLVDVqeTEPVMQEEIFGPILPIV--NVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYIS 315
Cdd:cd07125 394 GIIEIV--GIFDLTTEVFGPILHVIrfKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAI 471
|
330
....*....|....*
gi 2217281694 316 LLSVPFGGVGHSGMG 330
Cdd:cd07125 472 VGRQPFGGWGLSGTG 486
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
18-330 |
7.69e-24 |
|
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: 102.50 E-value: 7.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 18 FIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEIS----QGTEKVLAEV-LPQyldQSCFAVVLGGPQET 92
Cdd:cd07148 119 FTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATplscLAFVDLLHEAgLPE---GWCQAVPCENAVAE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 93 GQLLEHKLDYIFFTGSPRVGKIVMTAATKHlTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCS 172
Cdd:cd07148 196 KLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVP 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 173 PEMQERLLPALQSTITRF-YGDDPQSSPNLGHIINQKQFQRLR-----ALLGCSRVAIGGQsNESDRYIAPTVLVDVQET 246
Cdd:cd07148 275 AEIADDFAQRLAAAAEKLvVGDPTDPDTEVGPLIRPREVDRVEewvneAVAAGARLLCGGK-RLSDTTYAPTVLLDPPRD 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 247 EPVMQEEIFGPILPIVNVQSVDEAIKFINrqEKPLALYA--FSNSSQVVNQMLERTSSGSFGGNEgFTYISLLSVPFGGV 324
Cdd:cd07148 354 AKVSTQEIFGPVVCVYSYDDLDEAIAQAN--SLPVAFQAavFTKDLDVALKAVRRLDATAVMVND-HTAFRVDWMPFAGR 430
|
....*.
gi 2217281694 325 GHSGMG 330
Cdd:cd07148 431 RQSGYG 436
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
23-328 |
3.69e-23 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 100.80 E-value: 3.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 23 PFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGPqETGQ-LLEHK- 99
Cdd:PRK09457 134 PHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAgLPAGVLNLVQGGR-ETGKaLAAHPd 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 100 LDYIFFTGSPRVG------------KIVmtaatkhltpvTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPD 167
Cdd:PRK09457 213 IDGLLFTGSANTGyllhrqfagqpeKIL-----------ALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCAR 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 168 YVLCSPEMQ-ERLLPALQSTITRF----YGDDPQssPNLGHIINQKQFQRL----RALLgcsrvAIGGQS-NESDRYIAP 237
Cdd:PRK09457 282 RLLVPQGAQgDAFLARLVAVAKRLtvgrWDAEPQ--PFMGAVISEQAAQGLvaaqAQLL-----ALGGKSlLEMTQLQAG 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 238 TVLV-----DVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFT 312
Cdd:PRK09457 355 TGLLtpgiiDVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLT 434
|
330
....*....|....*.
gi 2217281694 313 YISlLSVPFGGVGHSG 328
Cdd:PRK09457 435 GAS-SAAPFGGVGASG 449
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
23-346 |
1.02e-21 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 96.08 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 23 PFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQY-LDQSCFAVVLGGPQETGQLL-EHKL 100
Cdd:PRK13968 126 PLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDAgIPQGVYGWLNADNDGVSQMInDSRI 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 101 DYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCD-----PQTVANRvawfcYFNAGQTCVAPDYVLCSPEM 175
Cdd:PRK13968 206 AAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADlelavKAAVAGR-----YQNTGQVCAAAKRFIIEEGI 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 176 QERLLPALQSTITRFYGDDPQSSPN-------------LGHIINQKQFQRLRALLGCSRVAigGQSNesdrYIAPTVLVD 242
Cdd:PRK13968 281 ASAFTERFVAAAAALKMGDPRDEENalgpmarfdlrdeLHHQVEATLAEGARLLLGGEKIA--GAGN----YYAPTVLAN 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 243 VQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNeGFTyISLLSVPFG 322
Cdd:PRK13968 355 VTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFIN-GYC-ASDARVAFG 432
|
330 340
....*....|....*....|....
gi 2217281694 323 GVGHSGMGRYHGKFTFDTFSHHRT 346
Cdd:PRK13968 433 GVKKSGFGRELSHFGLHEFCNIQT 456
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
23-275 |
1.54e-21 |
|
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: 95.74 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 23 PFGLVLIIAPWNYPL-----NLTLvllvgALAAGSCVVLKPSE----ISQGTEKVLAEVLPQY-LDQSCFAVVLGGPQET 92
Cdd:cd07130 132 PLGVVGVITAFNFPVavwgwNAAI-----ALVCGNVVVWKPSPttplTAIAVTKIVARVLEKNgLPGAIASLVCGGADVG 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 93 GQLLEHK-LDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLc 171
Cdd:cd07130 207 EALVKDPrVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLI- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 172 speMQERLLPALQSTITRFYGD----DPQSSPNL-GHIINQKQFQRLRALLGCSR-----VAIGGQSNESD-RYIAPTVl 240
Cdd:cd07130 286 ---VHESIYDEVLERLKKAYKQvrigDPLDDGTLvGPLHTKAAVDNYLAAIEEAKsqggtVLFGGKVIDGPgNYVEPTI- 361
|
250 260 270
....*....|....*....|....*....|....*
gi 2217281694 241 VDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFIN 275
Cdd:cd07130 362 VEGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNN 396
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
21-275 |
2.76e-20 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 92.13 E-value: 2.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 21 KEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSeiSQGTEKVLAEVlpqyldqSCF----------AVVLGGPQ 90
Cdd:PLN00412 156 KIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPP--TQGAVAALHMV-------HCFhlagfpkgliSCVTGKGS 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 91 ETGQLL-EHK-LDYIFFTGsprvGKIVMTAATK-HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPD 167
Cdd:PLN00412 227 EIGDFLtMHPgVNCISFTG----GDTGIAISKKaGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVK 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 168 YVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGHIINQKQFQRLRALLGCSRVAIGGQSNESDR---YIAPTVLVDVQ 244
Cdd:PLN00412 303 VVLVMESVADALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKRegnLIWPLLLDNVR 382
|
250 260 270
....*....|....*....|....*....|.
gi 2217281694 245 ETEPVMQEEIFGPILPIVNVQSVDEAIKFIN 275
Cdd:PLN00412 383 PDMRIAWEEPFGPVLPVIRINSVEEGIHHCN 413
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
19-347 |
4.42e-20 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 91.82 E-value: 4.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 19 IWKePFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLK--PSE--ISQGTEKVLAEVLPQY-LDQSCFAVVLGGpQETG 93
Cdd:PLN02315 151 VWN-PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKgaPTTplITIAMTKLVAEVLEKNnLPGAIFTSFCGG-AEIG 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 94 QLL--EHKLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLC 171
Cdd:PLN02315 229 EAIakDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 172 SPEMQERLLPALQSTITRFYGDDP-QSSPNLG--HIINQKQ-----FQRLRALLGcsRVAIGGQSNESD-RYIAPTVlVD 242
Cdd:PLN02315 309 HESIYDDVLEQLLTVYKQVKIGDPlEKGTLLGplHTPESKKnfekgIEIIKSQGG--KILTGGSAIESEgNFVQPTI-VE 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 243 VQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLertssGSFGGNEGFTYISL------ 316
Cdd:PLN02315 386 ISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWI-----GPLGSDCGIVNVNIptngae 460
|
330 340 350
....*....|....*....|....*....|.
gi 2217281694 317 LSVPFGGVGHSGMGRYHGKFTFDTFSHHRTC 347
Cdd:PLN02315 461 IGGAFGGEKATGGGREAGSDSWKQYMRRSTC 491
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
22-330 |
5.64e-20 |
|
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: 91.51 E-value: 5.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 22 EPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSE-----ISQGTEKVLAEVLPqyldQSCFAVVLGGPQETGQLL 96
Cdd:TIGR01238 159 ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEqtsliAYRAVELMQEAGFP----AGTIQLLPGRGADVGAAL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 97 --EHKLDYIFFTGSPRVGKIVMTAATKHL---TPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLC 171
Cdd:TIGR01238 235 tsDPRIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCV 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 172 SPEMQERLLPALQSTITRFYGDDP-QSSPNLGHIINQKQFQRL----RALLGCSRvAIGGQSNESDR------YIAPTV- 239
Cdd:TIGR01238 315 QEDVADRVLTMIQGAMQELKVGVPhLLTTDVGPVIDAEAKQNLlahiEHMSQTQK-KIAQLTLDDSRacqhgtFVAPTLf 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 240 -LVDVQEtepvMQEEIFGPILPIV--NVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYISL 316
Cdd:TIGR01238 394 eLDDIAE----LSEEVFGPVLHVVryKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVV 469
|
330
....*....|....
gi 2217281694 317 LSVPFGGVGHSGMG 330
Cdd:TIGR01238 470 GVQPFGGQGLSGTG 483
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
23-334 |
6.21e-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: 90.76 E-value: 6.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 23 PFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQ--YLDQSCFAVVLGGPQETGQLLEH-K 99
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYagLLPPEDVTLINGDGKTMQALLLHpN 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 100 LDYIFFTGSPRVGKIVmtAATKHLTPVTLELGGKNPCYVDDncDPQTVANrVAWFCYFNA----GQTCVAPD--YVLCSP 173
Cdd:cd07084 180 PKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGP--DAQAVDY-VAWQCVQDMtacsGQKCTAQSmlFVPENW 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 174 EMQeRLLPALQSTITRFYGDD----PQSSPNLghiinQKQFQRLRALLGcsRVAIGGQSNESDRYI--------APTVLV 241
Cdd:cd07084 255 SKT-PLVEKLKALLARRKLEDlllgPVQTFTT-----LAMIAHMENLLG--SVLLFSGKELKNHSIpsiygacvASALFV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 242 DVQE---TEPVMQEEIFGPILPIVNVQSVDEA--IKFINRQEKPLALYAFSNSSQVVNQMLERTSSGsfggneGFTYisl 316
Cdd:cd07084 327 PIDEilkTYELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQELIGNLWVA------GRTY--- 397
|
330 340
....*....|....*....|
gi 2217281694 317 lsvpFGGVGHSGM--GRYHG 334
Cdd:cd07084 398 ----AILRGRTGVapNQNHG 413
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
21-346 |
5.41e-18 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 85.57 E-value: 5.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 21 KEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEV-LPQYLDQSCFAVVLGGPQETGQLLEHK 99
Cdd:PLN02419 247 REPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELaMEAGLPDGVLNIVHGTNDTVNAICDDE 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 100 -LDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLC---SPEM 175
Cdd:PLN02419 327 dIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFvgdAKSW 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 176 QERLL---PALQSTItrfyGDDPQSspNLGHIINQKQFQRL------------RALLGCSRVAIGGQsnESDRYIAPTVL 240
Cdd:PLN02419 407 EDKLVeraKALKVTC----GSEPDA--DLGPVISKQAKERIcrliqsgvddgaKLLLDGRDIVVPGY--EKGNFIGPTIL 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 241 VDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTyISLLSVP 320
Cdd:PLN02419 479 SGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIP-VPLPFFS 557
|
330 340
....*....|....*....|....*...
gi 2217281694 321 FGGVGHSGMG--RYHGKFTFDTFSHHRT 346
Cdd:PLN02419 558 FTGNKASFAGdlNFYGKAGVDFFTQIKL 585
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
22-331 |
8.66e-18 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 84.40 E-value: 8.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 22 EPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLK-PSEISQgTEKVLAEVLPQY-LDQSCFAVVL-GGPQETGQLLEH 98
Cdd:PRK09406 122 QPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKhASNVPQ-TALYLADLFRRAgFPDGCFQTLLvGSGAVEAILRDP 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 99 KLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCD-PQTVANRVAWFCYfNAGQTCVAPDYVLCSPEMQE 177
Cdd:PRK09406 201 RVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADlDRAAETAVTARVQ-NNGQSCIAAKRFIVHADVYD 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 178 ---RLLPALQSTITrfYGDDPQSSPNLGHIINQKQFQRLRALL-----GCSRVAIGGQSNESDR-YIAPTVLVDVQETEP 248
Cdd:PRK09406 280 afaEKFVARMAALR--VGDPTDPDTDVGPLATEQGRDEVEKQVddavaAGATILCGGKRPDGPGwFYPPTVITDITPDMR 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 249 VMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNeGFTyISLLSVPFGGVGHSG 328
Cdd:PRK09406 358 LYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFIN-GMT-VSYPELPFGGVKRSG 435
|
...
gi 2217281694 329 MGR 331
Cdd:PRK09406 436 YGR 438
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
23-278 |
5.69e-13 |
|
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: 69.88 E-value: 5.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 23 PFGLVLIIAPWNYPLNLTLVllvG-----ALAAGSCVVLKPSEISQGTEKVLAEVLPQYLDQS-----CFAVVLGGPQET 92
Cdd:cd07129 105 PLGPVAVFGASNFPLAFSVA---GgdtasALAAGCPVVVKAHPAHPGTSELVARAIRAALRATglpagVFSLLQGGGREV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 93 GQ-LLEHKL-DYIFFTGSPRVGKIVMTAATKHLT--PVTLELGGKNPCYVDdncdPQTVANR--------VAWFCyFNAG 160
Cdd:cd07129 182 GVaLVKHPAiKAVGFTGSRRGGRALFDAAAARPEpiPFYAELGSVNPVFIL----PGALAERgeaiaqgfVGSLT-LGAG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 161 QTCVAPDYVLC--SPEmQERLLPALQSTITRFygddpQSSPNLGHIIN---QKQFQRLRALLGcSRVAIGGQSNESDRYI 235
Cdd:cd07129 257 QFCTNPGLVLVpaGPA-GDAFIAALAEALAAA-----PAQTMLTPGIAeayRQGVEALAAAPG-VRVLAGGAAAEGGNQA 329
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2217281694 236 APTVL-VDVQE--TEPVMQEEIFGPILPIVNVQSVDEAIKFINRQE 278
Cdd:cd07129 330 APTLFkVDAAAflADPALQEEVFGPASLVVRYDDAAELLAVAEALE 375
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
23-298 |
6.99e-13 |
|
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: 69.81 E-value: 6.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 23 PFGLVLIIA-----PWN-YPLnltlvlLVGALAAGSCVVLKPSEIS----QGTEKVLAEVLPQY-LDQSCFAVVLGGPQE 91
Cdd:cd07127 193 PRGVALVIGcstfpTWNgYPG------LFASLATGNPVIVKPHPAAilplAITVQVAREVLAEAgFDPNLVTLAADTPEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 92 --TGQLLEH-KLDYIFFTGSPRVGKIVMTAATKHLtpVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDY 168
Cdd:cd07127 267 piAQTLATRpEVRIIDFTGSNAFGDWLEANARQAQ--VYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQN 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 169 VLCSPE----MQERLLP-----ALQSTITRFYGDDPQSSPNLGHIINQKQFQRLRALLGCSRVAIGGQSNESDRYI---- 235
Cdd:cd07127 345 IYVPRDgiqtDDGRKSFdevaaDLAAAIDGLLADPARAAALLGAIQSPDTLARIAEARQLGEVLLASEAVAHPEFPdarv 424
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217281694 236 -APTVLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKF---INRQEKPLALYAFSNSSQVVNQMLE 298
Cdd:cd07127 425 rTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELareSVREHGAMTVGVYSTDPEVVERVQE 491
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
23-330 |
1.17e-11 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 66.54 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 23 PFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEisQgTEKVLAEvlpqyldqscfAVVL----GGPQETGQLL-- 96
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAE--Q-TPLIAAQ-----------AVRIlleaGVPAGVVQLLpg 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 97 -----------EHKLDYIFFTGSPRVGKIVM-TAATK-----HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNA 159
Cdd:PRK11809 834 rgetvgaalvaDARVRGVMFTGSTEVARLLQrNLAGRldpqgRPIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSA 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 160 GQTCVAPDyVLCSPE-MQERLLPALQSTITRF-YGDDPQSSPNLGHIIN-------QKQFQRLRALLGCSRVAIGGQSNE 230
Cdd:PRK11809 914 GQRCSALR-VLCLQDdVADRTLKMLRGAMAECrMGNPDRLSTDIGPVIDaeakaniERHIQAMRAKGRPVFQAARENSED 992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 231 SDR--YIAPTV--LVDVQEtepvMQEEIFGPILPIV--NVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGS 304
Cdd:PRK11809 993 WQSgtFVPPTLieLDSFDE----LKREVFGPVLHVVryNRNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGN 1068
|
330 340 350
....*....|....*....|....*....|...
gi 2217281694 305 FggnegftYISLLSV-------PFGGVGHSGMG 330
Cdd:PRK11809 1069 L-------YVNRNMVgavvgvqPFGGEGLSGTG 1094
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
25-328 |
2.06e-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: 65.30 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 25 GLVLIIAPWNYP---LNLtlvllVGALA-AGSCVVLKPSEI----SQGTEKVLAEV-LP----QYL--DQSCF-AVVLGG 88
Cdd:cd07123 172 GFVYAVSPFNFTaigGNL-----AGAPAlMGNVVLWKPSDTavlsNYLVYKILEEAgLPpgviNFVpgDGPVVgDTVLAS 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 89 PQETGqllehkldyIFFTGSprvgkivmTAATKHLT-------------P-VTLELGGKNPCYVDDNCDPQTVAN---RV 151
Cdd:cd07123 247 PHLAG---------LHFTGS--------TPTFKSLWkqigenldryrtyPrIVGETGGKNFHLVHPSADVDSLVTatvRG 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 152 AwFCYfnAGQTCVAPD--YVLCS--PEMQERLLPALqSTITrfYGDDPQSSPNLGHIINQKQFQRLRALLGCSR------ 221
Cdd:cd07123 310 A-FEY--QGQKCSAASraYVPESlwPEVKERLLEEL-KEIK--MGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKsdpeae 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 222 VAIGGQSNESDRY-IAPTVLVDVQETEPVMQEEIFGPILpIVNV---QSVDEAIKFINrQEKPLALYA--FSNSSQVVNQ 295
Cdd:cd07123 384 IIAGGKCDDSVGYfVEPTVIETTDPKHKLMTEEIFGPVL-TVYVypdSDFEETLELVD-TTSPYALTGaiFAQDRKAIRE 461
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2217281694 296 MLE--RTSSGSFggnegftYI---SLLSV----PFGGVGHSG 328
Cdd:cd07123 462 ATDalRNAAGNF-------YIndkPTGAVvgqqPFGGARASG 496
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
25-262 |
1.21e-09 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 60.21 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 25 GLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEisQgTEKVLAEVLpQYLDQ-----SCFAVVLGGPQETGQ-LLEH 98
Cdd:PRK11904 686 GVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAE--Q-TPLIAAEAV-KLLHEagipkDVLQLLPGDGATVGAaLTAD 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 99 -KLDYIFFTGSPRVGKIV-MTAATKHLTPVTL--ELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDyVLCSPE 174
Cdd:PRK11904 762 pRIAGVAFTGSTETARIInRTLAARDGPIVPLiaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALR-VLFVQE 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 175 -MQERLLPALQSTITRFYGDDPQS-SPNLGHIINQKQFQRLRA----------LLGcsRVAIGGQSNESDrYIAPTvLVD 242
Cdd:PRK11904 841 dIADRVIEMLKGAMAELKVGDPRLlSTDVGPVIDAEAKANLDAhiermkrearLLA--QLPLPAGTENGH-FVAPT-AFE 916
|
250 260
....*....|....*....|
gi 2217281694 243 VQETEpVMQEEIFGPILPIV 262
Cdd:PRK11904 917 IDSIS-QLEREVFGPILHVI 935
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
22-275 |
2.87e-09 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 59.11 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 22 EPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEisQgTEKVLAEvlpqyldqscfAVVL----GGPQETGQLL- 96
Cdd:PRK11905 675 KPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAE--Q-TPLIAAR-----------AVRLlheaGVPKDALQLLp 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 97 ------------EHKLDYIFFTGSPRVGKIVMTAATKHLT-PVTL--ELGGKNPCYVDDNCDP-QTVANRVAwfCYFN-A 159
Cdd:PRK11905 741 gdgrtvgaalvaDPRIAGVMFTGSTEVARLIQRTLAKRSGpPVPLiaETGGQNAMIVDSSALPeQVVADVIA--SAFDsA 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 160 GQTCVAPDyVLC-----SPEMQERLLPALQS-TItrfyGDDPQSSPNLGHIINQKQFQRLRA------LLGCS--RVAIG 225
Cdd:PRK11905 819 GQRCSALR-VLClqedvADRVLTMLKGAMDElRI----GDPWRLSTDVGPVIDAEAQANIEAhieamrAAGRLvhQLPLP 893
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2217281694 226 GQSNESdRYIAPTVLvdvqETE--PVMQEEIFGPILPIVNVQS--VDEAIKFIN 275
Cdd:PRK11905 894 AETEKG-TFVAPTLI----EIDsiSDLEREVFGPVLHVVRFKAdeLDRVIDDIN 942
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
47-297 |
1.77e-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: 53.04 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 47 ALAAGSCVVLKP-SEISQGTEKVLAE-----VLPQyldqSCFAVVLGGpqeTGQLLEHKL--DYIFFTGSPRVGKIVMT- 117
Cdd:cd07128 168 ALLAGVPVIVKPaTATAYLTEAVVKDivesgLLPE----GALQLICGS---VGDLLDHLGeqDVVAFTGSAATAAKLRAh 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 118 -AATKHLTPVTLELGGKNPCYVDDNCDPQT-----VANRVAWFCYFNAGQTCVAPDYVLCsPE-----MQERLLPALQST 186
Cdd:cd07128 241 pNIVARSIRFNAEADSLNAAILGPDATPGTpefdlFVKEVAREMTVKAGQKCTAIRRAFV-PEarvdaVIEALKARLAKV 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 187 ITrfyGDDPQSSPNLGHIINQKQFQRLRA----LLGCSRVAIGGQSNESDR--------YIAPTVLV--DVQETEPVMQE 252
Cdd:cd07128 320 VV---GDPRLEGVRMGPLVSREQREDVRAavatLLAEAEVVFGGPDRFEVVgadaekgaFFPPTLLLcdDPDAATAVHDV 396
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2217281694 253 EIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQML 297
Cdd:cd07128 397 EAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELV 441
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
23-303 |
2.36e-05 |
|
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: 46.33 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 23 PFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKpseisqGTEKVlAEVLPQYLD---------QSCFAVVLGGPQETG 93
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLK------VDSKV-SVVMEQFLRllhlcgmpaTDVDLIHSDGPTMNK 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 94 QLLEHKLDYIFFTGSPRV---------GKIVMTAAT---KHLTPvtlelggknpcyvddncDPQTVaNRVAWFC----YF 157
Cdd:cd07126 215 ILLEANPRMTLFTGSSKVaerlalelhGKVKLEDAGfdwKILGP-----------------DVSDV-DYVAWQCdqdaYA 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 158 NAGQTCVAPDyVLCSPE--MQERLLPALQSTITRFYGDDPQSSPNLGhIINQKQFQRLRALLGC--SRVAIGGQS----N 229
Cdd:cd07126 277 CSGQKCSAQS-ILFAHEnwVQAGILDKLKALAEQRKLEDLTIGPVLT-WTTERILDHVDKLLAIpgAKVLFGGKPltnhS 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 230 ESDRY--IAPT-VLVDVQ-----ETEPVMQEEIFGP--ILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLER 299
Cdd:cd07126 355 IPSIYgaYEPTaVFVPLEeiaieENFELVTTEVFGPfqVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVLAN 434
|
....
gi 2217281694 300 TSSG 303
Cdd:cd07126 435 TVNG 438
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
22-262 |
2.84e-05 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 46.47 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 22 EPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEisQ---------------GtekVLAEVLpQYLdqscfavvL 86
Cdd:COG4230 679 RGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAE--QtpliaaravrllheaG---VPADVL-QLL--------P 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 87 GGPQETGQLL--EHKLDYIFFTGSPRVGKIV-MTAATKHLTPVTL--ELGGKNPCYVDDNCDPQTVANRV---AwfcyFN 158
Cdd:COG4230 745 GDGETVGAALvaDPRIAGVAFTGSTETARLInRTLAARDGPIVPLiaETGGQNAMIVDSSALPEQVVDDVlasA----FD 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 159 -AGQTCVAPDyVLCSPE-------------MQERLL--PALQST-----ItrfygdDPQSSPNL-GHIINQKQFQRLRAL 216
Cdd:COG4230 821 sAGQRCSALR-VLCVQEdiadrvlemlkgaMAELRVgdPADLSTdvgpvI------DAEARANLeAHIERMRAEGRLVHQ 893
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2217281694 217 LGCSRVAIGGqsnesdRYIAPTV--LVDVQEtepvMQEEIFGPILPIV 262
Cdd:COG4230 894 LPLPEECANG------TFVAPTLieIDSISD----LEREVFGPVLHVV 931
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
23-272 |
6.51e-05 |
|
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: 44.54 E-value: 6.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 23 PFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQYLDQSC----FAVVLGGP--QETGQLL 96
Cdd:cd07121 97 PFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAIAEAGgpdnLVVTVEEPtiETTNELM 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 97 EH-KLDYIFFTGSPRVGKIVMTAATKhltpvTLELGGKNP-CYVDDNCDPQTVANRVAWFCYFNAGQTC----------- 163
Cdd:cd07121 177 AHpDINLLVVTGGPAVVKAALSSGKK-----AIGAGAGNPpVVVDETADIEKAARDIVQGASFDNNLPCiaekeviavds 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 164 VAPD----------YVLCSPEMQERLLPALQstitrfygDDPQSSPNlghiinqkqfqrlRALLGCSRVAIGGQSN-ESD 232
Cdd:cd07121 252 VADYliaamqrngaYVLNDEQAEQLLEVVLL--------TNKGATPN-------------KKWVGKDASKILKAAGiEVP 310
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2217281694 233 RYIaPTVLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIK 272
Cdd:cd07121 311 ADI-RLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIE 349
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
22-272 |
6.80e-05 |
|
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: 44.56 E-value: 6.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 22 EPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQYldqscfAVVLGGPQ----------- 90
Cdd:cd07081 94 EPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQA------AVAAGAPEnligwidnpsi 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 91 ETGQLLEHK--LDYIFFTGSPRVGKivmtAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGqtcvapdy 168
Cdd:cd07081 168 ELAQRLMKFpgIGLLLATGGPAVVK----AAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNG-------- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217281694 169 VLCSPEMQERLLPALQSTITRFYGDDPqsspnlGHIINQKQFQRLRALL---GCSRVAIGGQS-------------NESD 232
Cdd:cd07081 236 VICASEQSVIVVDSVYDEVMRLFEGQG------AYKLTAEELQQVQPVIlknGDVNRDIVGQDaykiaaaaglkvpQETR 309
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2217281694 233 RYIAPTVLVDvqETEPVMQEEIfGPILPIVNVQSVDEAIK 272
Cdd:cd07081 310 ILIGEVTSLA--EHEPFAHEKL-SPVLAMYRAANFADADA 346
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
223-272 |
7.15e-03 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 38.34 E-value: 7.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2217281694 223 AIGGQSNESDRYIaptvLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIK 272
Cdd:PRK15398 334 AAGINVPKDTRLL----IVETDANHPFVVTELMMPVLPVVRVKDVDEAIA 379
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