|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
75-506 |
0e+00 |
|
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: 792.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 75 AALLVDELRSNFNSGRTKSYEWRISQLQNIARMIDEKEKCITEALYQDLSKPELEAFLAEISNTKSSCMLAIKELKNWMA 154
Cdd:cd07137 1 APRLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 155 PETVKTSVTTFPSSAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEYLDNTTI 234
Cdd:cd07137 81 PEKVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 235 RVIEGGVPETTALLDQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWACNSGQ 314
Cdd:cd07137 161 KVIEGGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCNNGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 315 ACIGVDYVITTKDFASKLIDALKTELETFFGQNALESKDLSRIVNSFHFKRLESMLKENGVANKIVHGGRITEDKLKISP 394
Cdd:cd07137 241 ACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDEKNLYIEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 395 TILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVLHVTVK 474
Cdd:cd07137 321 TILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAID 400
|
410 420 430
....*....|....*....|....*....|..
gi 1032283529 475 DLPFGGVGESGIGAYHGKFSYETFSHKKGVLY 506
Cdd:cd07137 401 TLPFGGVGESGFGAYHGKFSFDAFSHKKAVLY 432
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
78-506 |
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: 623.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 78 LVDELRSNFNSGRTKSYEWRISQLQNIARMIDEKEKCITEALYQDLSKPELEAFLAEISNTKSSCMLAIKELKNWMAPET 157
Cdd:cd07087 3 LVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKPRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 158 VKTSVTTFPSSAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEYLDNTTIRVI 237
Cdd:cd07087 83 VSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVAVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 238 EGGVPETTALLDQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACI 317
Cdd:cd07087 163 EGGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFL-NAGQTCI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 318 GVDYVITTKDFASKLIDALKTELETFFGQNALESKDLSRIVNSFHFKRLESMLkENGvanKIVHGGRITEDKLKISPTIL 397
Cdd:cd07087 242 APDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLL-DDG---KVVIGGQVDKEERYIAPTIL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 398 LDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVLHVTVKDLP 477
Cdd:cd07087 318 DDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLP 397
|
410 420
....*....|....*....|....*....
gi 1032283529 478 FGGVGESGIGAYHGKFSYETFSHKKGVLY 506
Cdd:cd07087 398 FGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
78-529 |
0e+00 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 605.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 78 LVDELRSNFNSGRTKSYEWRISQLQNIARMIDEKEKCITEALYQDLSKPELEAFLAEISNTKSSCMLAIKELKNWMAPET 157
Cdd:cd07136 3 LVEKQRAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKPKR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 158 VKTSVTTFPSSAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEYLDNTTIRVI 237
Cdd:cd07136 83 VKTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVAVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 238 EGGVPETTALLDQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACI 317
Cdd:cd07136 163 EGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFL-NAGQTCV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 318 GVDYVITTKDFASKLIDALKTELETFFGQNALESKDLSRIVNSFHFKRLESMLKEngvaNKIVHGGRITEDKLKISPTIL 397
Cdd:cd07136 242 APDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDN----GKIVFGGNTDRETLYIEPTIL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 398 LDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVLHVTVKDLP 477
Cdd:cd07136 318 DNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYLP 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1032283529 478 FGGVGESGIGAYHGKFSYETFSHKKGVLYRSFSGDADLRYPPYTPKKKMVLK 529
Cdd:cd07136 398 FGGVGNSGMGSYHGKYSFDTFSHKKSILKKSTWFDLPLRYPPYKGKKKKLKK 449
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
70-547 |
0e+00 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 596.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 70 FSGKEAALLVDELRSNFNSGRTKSYEWRISQLQNIARMIDEKEKCITEALYQDLSKPELEAFLAEISNTKSSCMLAIKEL 149
Cdd:PLN02174 7 FGAADASILVTELRRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 150 KNWMAPETVKTSVTTFPSSAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEYL 229
Cdd:PLN02174 87 KNWMAPEKAKTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 230 DNTTIRVIEGGVPETTALLDQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWA 309
Cdd:PLN02174 167 DSSAVRVVEGAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 310 CNSGQACIGVDYVITTKDFASKLIDALKTELETFFGQNALESKDLSRIVNSFHFKRLESMLKENGVANKIVHGGRITEDK 389
Cdd:PLN02174 247 CNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEKDREN 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 390 LKISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVL 469
Cdd:PLN02174 327 LKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAV 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032283529 470 HVTVKDLPFGGVGESGIGAYHGKFSYETFSHKKGVLYRSFSGDADLRYPPYTPKKKMVLKALLSSNIFAAILAFFGFS 547
Cdd:PLN02174 407 HLALHTLPFGGVGESGMGAYHGKFSFDAFSHKKAVLYRSLFGDSAVRYPPYSRGKLRLLKALVDSNIFDIFKVLLGLS 484
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
76-521 |
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: 577.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 76 ALLVDELRSNFNSGRTKSYEWRISQLQNIARMIDEKEKCITEALYQDLSKPELEAFLAEISNTKSSCMLAIKELKNWMAP 155
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 156 ETVKTSVTTFPSSAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEYLDNTTIR 235
Cdd:cd07132 81 EPVKKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 236 VIEGGVPETTALLDQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQA 315
Cdd:cd07132 161 VVLGGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFI-NAGQT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 316 CIGVDYVITTKDFASKLIDALKTELETFFGQNALESKDLSRIVNSFHFKRLESMLKengvANKIVHGGRITEDKLKISPT 395
Cdd:cd07132 240 CIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLS----GGKVAIGGQTDEKERYIAPT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 396 ILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVLHVTVKD 475
Cdd:cd07132 316 VLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDS 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1032283529 476 LPFGGVGESGIGAYHGKFSYETFSHKKGVLYRSFSGD--ADLRYPPYT 521
Cdd:cd07132 396 LPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVKSLNMEklNSLRYPPYS 443
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
78-548 |
0e+00 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 574.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 78 LVDELRSNFNSGRTKSYEWRISQLQNIARMIDEKEKCITEALYQDLSKPELEAFLAEISNTKSSCMLAIKELKNWMAPET 157
Cdd:PLN02203 11 SVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSNLKKWMAPKK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 158 VKTSVTTFPSSAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEYLDNTTIRVI 237
Cdd:PLN02203 91 AKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAVKVI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 238 EGGVPETTALLDQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVD---SDVNLQVAARRIIAGKWACNSGQ 314
Cdd:PLN02203 171 EGGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGSCAGQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 315 ACIGVDYVITTKDFASKLIDALKTELETFFGQNALESKDLSRIVNSFHFKRLESMLKENGVANKIVHGGRITEDKLKISP 394
Cdd:PLN02203 251 ACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAASIVHGGSIDEKKLFIEP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 395 TILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVLHVTVK 474
Cdd:PLN02203 331 TILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYACD 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032283529 475 DLPFGGVGESGIGAYHGKFSYETFSHKKGVLYRSFSGDADLRYPPYTPKKKMVLKALLSSNIFAAILAFFGFSK 548
Cdd:PLN02203 411 SLPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSLLTEFEFRYPPWNDFKLGFLRLVYRFDYFGLLLLLLGLKR 484
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
76-537 |
0e+00 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 553.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 76 ALLVDELRSNFNSGRTKSYEWRISQLQNIARMIDEKEKCITEALYQDLSKPELEAFLAEISNTKSSCMLAIKELKNWMAP 155
Cdd:PTZ00381 10 PPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEYLKP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 156 ETVKTSVTTFPSSAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEYLDNTTIR 235
Cdd:PTZ00381 90 EKVDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPSYVR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 236 VIEGGVPETTALLDQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKwACNSGQA 315
Cdd:PTZ00381 170 VIEGGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGK-FLNAGQT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 316 CIGVDYVITTKDFASKLIDALKTELETFFGQNALESKDLSRIVNSFHFKRLESMLKENGvaNKIVHGGRITEDKLKISPT 395
Cdd:PTZ00381 249 CVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKDHG--GKVVYGGEVDIENKYVAPT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 396 ILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVLHVTVKD 475
Cdd:PTZ00381 327 IIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPN 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032283529 476 LPFGGVGESGIGAYHGKFSYETFSHKKGVLYRSF--SGDADLRYPPYTPKKKMVLKALLSSNIF 537
Cdd:PTZ00381 407 LPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNKSTgnSFDLSLRYPPYTSFKSWVLSFLLKLSIP 470
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
78-505 |
0e+00 |
|
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: 529.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 78 LVDELRSNFNSGRTKSYEWRISQLQNIARMIDEKEKCITEALYQDLSKPELEAFLAEISNTKSSCMLAIKELKNWMAPET 157
Cdd:cd07135 10 IHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKKWAKDEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 158 VK-TSVTTFPSSAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEYLDNTTIRV 236
Cdd:cd07135 90 VKdGPLAFMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLDPDAFQV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 237 IEGGVPETTALLDQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKwACNSGQAC 316
Cdd:cd07135 170 VQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGK-FGNAGQIC 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 317 IGVDYVITTKDFASKLIDALKTELETFFGQNALESKDLSRIVNSFHFKRLESMLKENGvaNKIVHGGRITEDKLKISPTI 396
Cdd:cd07135 249 VAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDTTK--GKVVIGGEMDEATRFIPPTI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 397 LLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKElEKQFVQD-VSAGGITINDTVLHVTVKD 475
Cdd:cd07135 327 VSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKS-EIDHILTrTRSGGVVINDTLIHVGVDN 405
|
410 420 430
....*....|....*....|....*....|
gi 1032283529 476 LPFGGVGESGIGAYHGKFSYETFSHKKGVL 505
Cdd:cd07135 406 APFGGVGDSGYGAYHGKYGFDTFTHERTVV 435
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
82-505 |
3.36e-151 |
|
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: 440.51 E-value: 3.36e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 82 LRSNFNSGRTKSYEWRISQLQNIARMIDEKEKCITEALYQDLSKPELEAFLAEISNTKSSCMLAIKELKNWMAPETVKTS 161
Cdd:cd07134 7 QQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKPKRVRTP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 162 VTTFPSSAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEYLDNTTIRVIEGGV 241
Cdd:cd07134 87 LLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFEGDA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 242 PETTALLDQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACIGVDY 321
Cdd:cd07134 167 EVAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFL-NAGQTCIAPDY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 322 VITTKDFASKLIDALKTELETFFGQNA--LESKDLSRIVNSFHFKRLESMLKEnGVAN--KIVHGGRITEDKLKISPTIL 397
Cdd:cd07134 246 VFVHESVKDAFVEHLKAEIEKFYGKDAarKASPDLARIVNDRHFDRLKGLLDD-AVAKgaKVEFGGQFDAAQRYIAPTVL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 398 LDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVLHVTVKDLP 477
Cdd:cd07134 325 TNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNPNLP 404
|
410 420
....*....|....*....|....*...
gi 1032283529 478 FGGVGESGIGAYHGKFSYETFSHKKGVL 505
Cdd:cd07134 405 FGGVNNSGIGSYHGVYGFKAFSHERAVL 432
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
80-506 |
4.85e-147 |
|
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: 429.60 E-value: 4.85e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 80 DELRSNFNSGRTKSYEWRISQLQNIARMIDEKEKCITEALYQDLS-KPELEAFLAEISNTKSSCMLAIKELKNWMAPETV 158
Cdd:cd07133 5 ERQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFGhRSRHETLLAEILPSIAGIKHARKHLKKWMKPSRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 159 KTSVTTFPSSAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEYLDNTTIRVIE 238
Cdd:cd07133 85 HVGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEVAVVT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 239 GGVPETTALLDQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACIG 318
Cdd:cd07133 165 GGADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLL-NAGQTCVA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 319 VDYVITTKDFASKLIDALKTELETFFGQNAlESKDLSRIVNSFHFKRLESML---KENGV-ANKIVHGGRITEDKLKISP 394
Cdd:cd07133 244 PDYVLVPEDKLEEFVAAAKAAVAKMYPTLA-DNPDYTSIINERHYARLQGLLedaRAKGArVIELNPAGEDFAATRKLPP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 395 TILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVLHVTVK 474
Cdd:cd07133 323 TLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHVAQD 402
|
410 420 430
....*....|....*....|....*....|..
gi 1032283529 475 DLPFGGVGESGIGAYHGKFSYETFSHKKGVLY 506
Cdd:cd07133 403 DLPFGGVGASGMGAYHGKEGFLTFSHAKPVFK 434
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
86-505 |
8.48e-109 |
|
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: 331.87 E-value: 8.48e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 86 FNSGRTKSYEWRISQLQNIARMIDEKEKCITEALYQDLSKPeLEAFLAEISNTKSSCMLAIKELKNWMAPETVKTSVTTF 165
Cdd:cd07078 11 FKAWAALPPAERAAILRKLADLLEERREELAALETLETGKP-IEEALGEVARAADTFRYYAGLARRLHGEVIPSPDPGEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 166 pssAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPET 244
Cdd:cd07078 90 ---AIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLPPGVLNVVTGDGDEV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 245 -TALLDQKW-DKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWaCNSGQACIGVDYV 322
Cdd:cd07078 167 gAALASHPRvDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAF-GNAGQVCTAASRL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 323 ITTKDFASKLIDALKTELETFFGQNALESK-DLSRIVNSFHFKRLESMLkENGVAN--KIVHGGRI--TEDKLKISPTIL 397
Cdd:cd07078 246 LVHESIYDEFVERLVERVKALKVGNPLDPDtDMGPLISAAQLDRVLAYI-EDAKAEgaKLLCGGKRleGGKGYFVPPTVL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 398 LDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVLHVTVkDLP 477
Cdd:cd07078 325 TDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAEP-SAP 403
|
410 420
....*....|....*....|....*...
gi 1032283529 478 FGGVGESGIGAYHGKFSYETFSHKKGVL 505
Cdd:cd07078 404 FGGVKQSGIGREGGPYGLEEYTEPKTVT 431
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
86-505 |
2.72e-89 |
|
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: 279.11 E-value: 2.72e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 86 FNSGRTKSYEWRISQLQNIARMIDEKEKCITEALYQDLSKPeLEAFLAEISNTKSSCMLAIKELKNWMAPETVKTSVTTF 165
Cdd:cd06534 7 FKAWAALPPAERAAILRKIADLLEERREELAALETLETGKP-IEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPGGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 166 pssAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPET 244
Cdd:cd06534 86 ---AYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVVNVVPGGGDEV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 245 TALL--DQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWaCNSGQACIGVDYV 322
Cdd:cd06534 163 GAALlsHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAF-FNAGQICTAASRL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 323 ITTKDFASKLIDALKteletffgqnaleskdlsrivnsfhfkrlesmlkengvankivhggritedklkispTILLDVPE 402
Cdd:cd06534 242 LVHESIYDEFVEKLV---------------------------------------------------------TVLVDVDP 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 403 ASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVLHVTVkDLPFGGVG 482
Cdd:cd06534 265 DMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGP-EAPFGGVK 343
|
410 420
....*....|....*....|...
gi 1032283529 483 ESGIGAYHGKFSYETFSHKKGVL 505
Cdd:cd06534 344 NSGIGREGGPYGLEEYTRTKTVV 366
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
97-507 |
4.88e-80 |
|
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: 258.90 E-value: 4.88e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 97 RISQLQNIARMIDEKEKCITEALYQDLSKPELEAfLAEISNTKSSCMLAIKELKNwMAPETVKTSVTtfPSSAQIVSEPL 176
Cdd:COG1012 67 RAAILLRAADLLEERREELAALLTLETGKPLAEA-RGEVDRAADFLRYYAGEARR-LYGETIPSDAP--GTRAYVRREPL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 177 GVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPETTALL--DQKWD 253
Cdd:COG1012 143 GVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAgLPAGVLNVVTGDGSEVGAALvaHPDVD 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 254 KIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACIGVDYVITTKDFASKLI 333
Cdd:COG1012 223 KISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFG-NAGQRCTAASRLLVHESIYDEFV 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 334 DALKTELETF-FGQNALESKDLSRIVNSFHFKRLESMLKEnGVAN--KIVHGGRITEDK--LKISPTILLDVPEASSMMQ 408
Cdd:COG1012 302 ERLVAAAKALkVGDPLDPGTDMGPLISEAQLERVLAYIED-AVAEgaELLTGGRRPDGEggYFVEPTVLADVTPDMRIAR 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 409 EEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVLHVTVkDLPFGGVGESGIGA 488
Cdd:COG1012 381 EEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVP-QAPFGGVKQSGIGR 459
|
410
....*....|....*....
gi 1032283529 489 YHGKFSYETFSHKKGVLYR 507
Cdd:COG1012 460 EGGREGLEEYTETKTVTIR 478
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
74-505 |
7.78e-77 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 249.83 E-value: 7.78e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 74 EAALLVDELRSNFNSGRTKSYEWRISQLQNIARMIDEKEKCITEALYQDLSKPELEAfLAEISNTKSSCMLAIKELKNWM 153
Cdd:cd07099 19 EVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADA-GLEVLLALEAIDWAARNAPRVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 154 APETVKTSVTTFPSSAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNT 232
Cdd:cd07099 98 APRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAgPPQG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 233 TIRVIEGGVPETTALLDQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWaCNS 312
Cdd:cd07099 178 VLQVVTGDGATGAALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAM-VNA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 313 GQACIGVDYVITTKDFASKLIDALKTELETF-FGQNALESKDLSRIVNSFHFKRLESMLKEnGVAN--KIVHGG-RITED 388
Cdd:cd07099 257 GQTCISVERVYVHESVYDEFVARLVAKARALrPGADDIGDADIGPMTTARQLDIVRRHVDD-AVAKgaKALTGGaRSNGG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 389 KLKISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTV 468
Cdd:cd07099 336 GPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVL 415
|
410 420 430
....*....|....*....|....*....|....*..
gi 1032283529 469 LHVTVKDLPFGGVGESGIGAYHGKFSYETFSHKKGVL 505
Cdd:cd07099 416 LTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIA 452
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
97-504 |
8.62e-76 |
|
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: 247.06 E-value: 8.62e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 97 RISQLQNIARMIDEKEKCITEALYQDLSKPELEAfLAEISNTKSSCMLAIKELKNwMAPETVKTSVTTFpssAQIVSEPL 176
Cdd:pfam00171 53 RAAILRKAADLLEERKDELAELETLENGKPLAEA-RGEVDRAIDVLRYYAGLARR-LDGETLPSDPGRL---AYTRREPL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 177 GVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPETTALL--DQKWD 253
Cdd:pfam00171 128 GVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAgLPAGVLNVVTGSGAEVGEALveHPDVR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 254 KIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWaCNSGQACIGVDYVITTKDFASKLI 333
Cdd:pfam00171 208 KVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAF-GNAGQVCTATSRLLVHESIYDEFV 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 334 DALKTELETFFGQNALESK-DLSRIVNSFHFKRLESMLkENGVAN--KIVHGGRITEDK-LKISPTILLDVPEASSMMQE 409
Cdd:pfam00171 287 EKLVEAAKKLKVGDPLDPDtDMGPLISKAQLERVLKYV-EDAKEEgaKLLTGGEAGLDNgYFVEPTVLANVTPDMRIAQE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 410 EIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITIND-TVLHVTVkdLPFGGVGESGIGA 488
Cdd:pfam00171 366 EIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDyTTGDADG--LPFGGFKQSGFGR 443
|
410
....*....|....*.
gi 1032283529 489 YHGKFSYETFSHKKGV 504
Cdd:pfam00171 444 EGGPYGLEEYTEVKTV 459
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
167-504 |
1.90e-56 |
|
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: 195.10 E-value: 1.90e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 167 SSAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFseyldnttirvIEGGVPE--- 243
Cdd:cd07105 90 TLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVF-----------HEAGLPKgvl 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 244 -------------TTALLDQKW-DKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWa 309
Cdd:cd07105 159 nvvthspedapevVEALIAHPAvRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAF- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 310 CNSGQACIGVDYVITTKDFASKLIDALKTELETFFGQNAleskDLSRIVNSFHFKRLESMLkENGVAN--KIVHGG--RI 385
Cdd:cd07105 238 LNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPV----VLGSLVSAAAADRVKELV-DDALSKgaKLVVGGlaDE 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 386 TEDKLKISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITIN 465
Cdd:cd07105 313 SPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHIN 392
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1032283529 466 DTvlhvTVKD---LPFGGVGESGIGAYHGKFSYETFSHKKGV 504
Cdd:cd07105 393 GM----TVHDeptLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
93-492 |
2.86e-55 |
|
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: 192.90 E-value: 2.86e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 93 SYEWRISQLQNIARMIDEKEKCITEALYQDLSKPELEAFLAEISNTKSSCMLAIKELKNWMAPETVKTSVTTFPSSAQIV 172
Cdd:cd07098 38 SFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEILVTCEKIRWTLKHGEKALRPESRPGGLLMFYKRARVE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 173 SEPLGVVLVISAWNFPF--LLSvePVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEYLDN-----TTIRVIEGgVPETT 245
Cdd:cd07098 118 YEPLGVVGAIVSWNYPFhnLLG--PIIAALFAGNAIVVKVSEQVAWSSGFFLSIIRECLAAcghdpDLVQLVTC-LPETA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 246 ALLDQ--KWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACIGVDYVI 323
Cdd:cd07098 195 EALTShpVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQ-SSGQNCIGIERVI 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 324 TTKDFASKLIDALKTELETF-FGQNALESKDLSRIVNSFHFKRLESMLKENGVAN-KIVHGG-RITEDKLK----ISPTI 396
Cdd:cd07098 274 VHEKIYDKLLEILTDRVQALrQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGaRLLAGGkRYPHPEYPqghyFPPTL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 397 LLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVLHVTVKDL 476
Cdd:cd07098 354 LVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQL 433
|
410
....*....|....*.
gi 1032283529 477 PFGGVGESGIGAYHGK 492
Cdd:cd07098 434 PFGGVKGSGFGRFAGE 449
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
58-504 |
3.26e-53 |
|
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: 187.26 E-value: 3.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 58 TLSAVVKEQASDFSGKEAALlvDELRSNFNSGRTKSYEWRISQLQNIARMIDEKEKCITEALYQDLSKPELEAfLAEISN 137
Cdd:cd07094 8 DGEVIGKVPADDRADAEEAL--ATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDA-RVEVDR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 138 TKSSCMLAIKELKNwMAPETVKTSVTTFPSSAQIVS--EPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAP 215
Cdd:cd07094 85 AIDTLRLAAEEAER-IRGEEIPLDATQGSDNRLAWTirEPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 216 AASSLLAKLFSEY---LDNTTIRVIEGGVPETTALLDQKWDKIFFTGGARVARIIMAAAArnLTPVVLELGGKCPALVDS 292
Cdd:cd07094 164 LSALELAKILVEAgvpEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVIVDR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 293 DVNLQVAARRIIAGKWAcNSGQACIGVDYVITTKDFASKLIDALKTELETFFGQNALESK-DLSRIVNSFHFKRLESMLK 371
Cdd:cd07094 242 DADLDAAIEALAKGGFY-HAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDtDVGPLISEEAAERVERWVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 372 ENGVAN-KIVHGGRitEDKLKISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELE 450
Cdd:cd07094 321 EAVEAGaRLLCGGE--RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1032283529 451 KQFVQDVSAGGITINDTVlHVTVKDLPFGGVGESGIGAYHGKFSYETFSHKKGV 504
Cdd:cd07094 399 FKAAEKLEVGGVMVNDSS-AFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTV 451
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
71-496 |
1.07e-51 |
|
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: 183.18 E-value: 1.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 71 SGKEAALLVDELRSNFNSGRTKSYEWRISQLQNIARMIDEKEKCITEALYQDLSKPELEAfLAEISNTKSSCMLAIKELK 150
Cdd:cd07149 19 SEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDA-RKEVDRAIETLRLSAEEAK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 151 NwMAPETVKTSVTtfPSSAQ----IVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFS 226
Cdd:cd07149 98 R-LAGETIPFDAS--PGGEGrigfTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 227 E-YLDNTTIRVIEGGVPET-TALL-DQKWDKIFFTGGARVarIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRI 303
Cdd:cd07149 175 EaGLPKGALNVVTGSGETVgDALVtDPRVRMISFTGSPAV--GEAIARKAGLKKVTLELGSNAAVIVDADADLEKAVERC 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 304 IAGKWAcNSGQACIGVDYVITTKDFASKLIDALKTELETF-FGQNALESKDLSRIVNSFHFKRLESMLKEnGVAN--KIV 380
Cdd:cd07149 253 VSGAFA-NAGQVCISVQRIFVHEDIYDEFLERFVAATKKLvVGDPLDEDTDVGPMISEAEAERIEEWVEE-AVEGgaRLL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 381 HGGRITEDKLkiSPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAG 460
Cdd:cd07149 331 TGGKRDGAIL--EPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVG 408
|
410 420 430
....*....|....*....|....*....|....*.
gi 1032283529 461 GITINDTVlHVTVKDLPFGGVGESGIGAYHGKFSYE 496
Cdd:cd07149 409 GVMINDSS-TFRVDHMPYGGVKESGTGREGPRYAIE 443
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
163-504 |
8.95e-51 |
|
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: 180.60 E-value: 8.95e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 163 TTFPS-----SAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRV 236
Cdd:cd07150 102 ETLPSdspgtVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAgLPKGVFNV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 237 IEGGVPETTALL--DQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARriIAGKWA-CNSG 313
Cdd:cd07150 182 VTGGGAEVGDELvdDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVR--AAAFGAfMHQG 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 314 QACIGVDYVITTKDFASKLIDALKTELETF-FGQNALESKDLSRIVNSFHFKRLESMLkENGVAN--KIVHGGriTEDKL 390
Cdd:cd07150 260 QICMSASRIIVEEPVYDEFVKKFVARASKLkVGDPRDPDTVIGPLISPRQVERIKRQV-EDAVAKgaKLLTGG--KYDGN 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 391 KISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVLH 470
Cdd:cd07150 337 FYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHINDPTIL 416
|
330 340 350
....*....|....*....|....*....|....*.
gi 1032283529 471 --VTVkdlPFGGVGESGIGAYHGKFSYETFSHKKGV 504
Cdd:cd07150 417 deAHV---PFGGVKASGFGREGGEWSMEEFTELKWI 449
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
171-502 |
1.80e-50 |
|
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: 179.26 E-value: 1.80e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 171 IVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLL-AKLFSEY-LDNTTIRVIEGGVPETTALL 248
Cdd:cd07104 94 VRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLiAEIFEEAgLPKGVLNVVPGGGSEIGDAL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 249 --DQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWaCNSGQACIGVDYVITTK 326
Cdd:cd07104 174 veHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAF-LHQGQICMAAGRILVHE 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 327 DFASKLIDALKTELETF-FGQNALESKDLSRIVNSFHFKRLESMLkENGVAN--KIVHGGriTEDKLKISPTILLDVPEA 403
Cdd:cd07104 253 SVYDEFVEKLVAKAKALpVGDPRDPDTVIGPLINERQVDRVHAIV-EDAVAAgaRLLTGG--TYEGLFYQPTVLSDVTPD 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 404 SSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDtvlhVTVKD---LPFGG 480
Cdd:cd07104 330 MPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIND----QTVNDephVPFGG 405
|
330 340
....*....|....*....|..
gi 1032283529 481 VGESGIGAYHGKFSYETFSHKK 502
Cdd:cd07104 406 VKASGGGRFGGPASLEEFTEWQ 427
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
57-504 |
6.02e-50 |
|
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: 179.14 E-value: 6.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 57 ATLSAVVKEQASdfSGKEAALLVDELRSNFNSGRTK-SYEWRISQLQNIARMIDEKEKCIT--EALyqDLSKPELEAFLA 133
Cdd:cd07144 31 STGEVIASVYAA--GEEDVDKAVKAARKAFESWWSKvTGEERGELLDKLADLVEKNRDLLAaiEAL--DSGKPYHSNALG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 134 EISntksSCMLAIKELKNWMAPETVKTSVTTFPSSAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEI 213
Cdd:cd07144 107 DLD----EIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAEN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 214 APAASSLLAKLFSEY-LDNTTIRVIEGGVPETTALLDQ--KWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALV 290
Cdd:cd07144 183 TPLSLLYFANLVKEAgFPPGVVNIIPGYGAVAGSALAEhpDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 291 DSDVNLQVAArriiagKWAC-----NSGQACIGVDYVITTKDFASKLIDALKTELETFFGQNALESKDLSR--IVNSFHF 363
Cdd:cd07144 263 FEDADLDQAV------KWAAagimyNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYKVGSPFDDDTVVgpQVSKTQY 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 364 KRLESMLkENGVAN--KIVHGGRITEDKLK----ISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKP 437
Cdd:cd07144 337 DRVLSYI-EKGKKEgaKLVYGGEKAPEGLGkgyfIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYG 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 438 LAAYLFTNNKELEKQFVQDVSAGGITIN---DTVLHVtvkdlPFGGVGESGIGAYHGKFSYETFSHKKGV 504
Cdd:cd07144 416 LAAAVFTKDIRRAHRVARELEAGMVWINssnDSDVGV-----PFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
174-505 |
1.27e-48 |
|
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: 174.82 E-value: 1.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 174 EPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEYLDNTTIRVIEGGVPETTALL--DQK 251
Cdd:cd07092 117 EPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGVVNVVCGGGASAGDALvaHPR 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 252 WDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWaCNSGQACIGVDYVITTKDFASK 331
Cdd:cd07092 197 VRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGY-YNAGQDCTAACRVYVHESVYDE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 332 LIDALKTELETF-FGQNALESKDLSRIVNSFHFKRLESMLKENGVANKIVHGGRITEDK-LKISPTILLDVPEASSMMQE 409
Cdd:cd07092 276 FVAALVEAVSAIrVGDPDDEDTEMGPLNSAAQRERVAGFVERAPAHARVLTGGRRAEGPgYFYEPTVVAGVAQDDEIVQE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 410 EIFGpllPIITVQKIEDGFQVIR---SKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTvlHVTVKDLPFGGVGESGI 486
Cdd:cd07092 356 EIFG---PVVTVQPFDDEDEAIElanDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNTH--IPLAAEMPHGGFKQSGY 430
|
330
....*....|....*....
gi 1032283529 487 GAYHGKFSYETFSHKKGVL 505
Cdd:cd07092 431 GKDLSIYALEDYTRIKHVM 449
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
152-487 |
5.10e-48 |
|
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: 173.00 E-value: 5.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 152 WMAPETVKTSVTTFPSSAQ-----IVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFS 226
Cdd:cd07103 89 WFAEEARRIYGRTIPSPAPgkrilVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 227 EY-LDNTTIRVIEGGVPETTALL--DQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRI 303
Cdd:cd07103 169 EAgLPAGVLNVVTGSPAEIGEALcaSPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 304 IAGKWAcNSGQACIGVDYVITTKDFASKLIDALKTELETFFGQNALESK-DLSRIVNSfhfKRLESM--LKENGVAN--K 378
Cdd:cd07103 249 IASKFR-NAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGtDMGPLINE---RAVEKVeaLVEDAVAKgaK 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 379 IVHGG-RITEDKLKISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDgfqVIR---SKPKPLAAYLFTNNKELEKQFV 454
Cdd:cd07103 325 VLTGGkRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDE---VIAranDTPYGLAAYVFTRDLARAWRVA 401
|
330 340 350
....*....|....*....|....*....|...
gi 1032283529 455 QDVSAGGITINDTVlhVTVKDLPFGGVGESGIG 487
Cdd:cd07103 402 EALEAGMVGINTGL--ISDAEAPFGGVKESGLG 432
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
171-504 |
6.93e-48 |
|
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: 172.91 E-value: 6.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 171 IVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEG-GVPETTALL 248
Cdd:cd07118 115 VLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAgLPAGVVNIVTGyGATVGQAMT 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 249 -DQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACIGVDYVITTKD 327
Cdd:cd07118 195 eHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYF-NAGECCNSGSRLLVHES 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 328 FASKLIDALKTELETF-FGQNALESKDLSRIVNSFHFKRLESMLKEnGVAN--KIVHGGRITE--DKLKISPTILLDVPE 402
Cdd:cd07118 274 IADAFVAAVVARSRKVrVGDPLDPETKVGAIINEAQLAKITDYVDA-GRAEgaTLLLGGERLAsaAGLFYQPTIFTDVTP 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 403 ASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINdTVLHVTVkDLPFGGVG 482
Cdd:cd07118 353 DMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVN-TFLDGSP-ELPFGGFK 430
|
330 340
....*....|....*....|..
gi 1032283529 483 ESGIGAYHGKFSYETFSHKKGV 504
Cdd:cd07118 431 QSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
172-505 |
9.83e-48 |
|
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: 172.55 E-value: 9.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 172 VSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEYLDNTTIRVIEGGVPETTALLDQ- 250
Cdd:cd07108 114 VREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQVLPAGVLNVITGYGEECGAALVDh 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 251 -KWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWACNSGQACIGVDYVITTKDFA 329
Cdd:cd07108 194 pDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGAIAGMRFTRQGQSCTAGSRLFVHEDIY 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 330 SKLIDALKTELETFFGQNAL-ESKDLSRIVNSFHFKRLESMLKEnGVAN---KIVHGGRI-TEDKLK----ISPTILLDV 400
Cdd:cd07108 274 DAFLEKLVAKLSKLKIGDPLdEATDIGAIISEKQFAKVCGYIDL-GLSTsgaTVLRGGPLpGEGPLAdgffVQPTIFSGV 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 401 PEASSMMQEEIFGPLLPIItvqKIEDGFQVIRS---KPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTvlHVTVKDLP 477
Cdd:cd07108 353 DNEWRLAREEIFGPVLCAI---PWKDEDEVIAMandSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQG--GGQQPGQS 427
|
330 340 350
....*....|....*....|....*....|..
gi 1032283529 478 FGGVGESGIGAyhgKFSYET----FSHKKGVL 505
Cdd:cd07108 428 YGGFKQSGLGR---EASLEGmlehFTQKKTVN 456
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
174-504 |
1.40e-46 |
|
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: 169.28 E-value: 1.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 174 EPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPETTALL--DQ 250
Cdd:cd07093 116 QPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAgLPPGVVNVVHGFGPEAGAALvaHP 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 251 KWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACIGVDYVITTK---- 326
Cdd:cd07093 196 DVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFS-NNGEVCLAGSRILVQRsiyd 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 327 DFASKLIDALK-------TELETFFGqnALESKDlsrivnsfHFKRLESML---KENGVanKIVHGGRITEDKLK----- 391
Cdd:cd07093 275 EFLERFVERAKalkvgdpLDPDTEVG--PLISKE--------HLEKVLGYVelaRAEGA--TILTGGGRPELPDLeggyf 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 392 ISPTILLDVPEASSMMQEEIFGpllPIITVQKIEDGFQVIR---SKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTV 468
Cdd:cd07093 343 VEPTVITGLDNDSRVAQEEIFG---PVVTVIPFDDEEEAIElanDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNCWL 419
|
330 340 350
....*....|....*....|....*....|....*...
gi 1032283529 469 lhvtVKDL--PFGGVGESGIGAYHGKFSYETFSHKKGV 504
Cdd:cd07093 420 ----VRDLrtPFGGVKASGIGREGGDYSLEFYTELKNV 453
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
80-504 |
7.80e-46 |
|
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: 167.04 E-value: 7.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 80 DELRSNFNSGRTKSYEWRisqlqniARMIDEKEKCITEALyqdlskPELEAFLAEISNTKSSCM-----LAIKELK---- 150
Cdd:cd07102 18 EAVRAALERARAAQKGWR-------AVPLEERKAIVTRAV------ELLAANTDEIAEELTWQMgrpiaQAGGEIRgmle 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 151 --NWM---APETVKTSVTTFPSSAQ--IVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAK 223
Cdd:cd07102 85 raRYMisiAEEALADIRVPEKDGFEryIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 224 LFSEY-LDNTTIRVIEGGVPETTALLDQK-WDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAAR 301
Cdd:cd07102 165 AFAEAgLPEGVFQVLHLSHETSAALIADPrIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 302 RIIAGKWAcNSGQACIGVDYVITTKDFASKLIDALKTELETF-FGQNALESKDLSRIVNSFHFKRLESMLKE---NGvAN 377
Cdd:cd07102 245 SLVDGAFF-NSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYkLGDPLDPSTTLGPVVSARAADFVRAQIADaiaKG-AR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 378 KIVHGGRITEDKLK---ISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFV 454
Cdd:cd07102 323 ALIDGALFPEDKAGgayLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALG 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1032283529 455 QDVSAGGITIN--DTVlhvtVKDLPFGGVGESGIGAYHGKFSYETFSHKKGV 504
Cdd:cd07102 403 EQLETGTVFMNrcDYL----DPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
174-504 |
2.19e-45 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 165.80 E-value: 2.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 174 EPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPETTALLDQ-- 250
Cdd:cd07114 118 EPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAgFPPGVVNVVTGFGPETGEALVEhp 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 251 KWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACIGVDYVITTKDFAS 330
Cdd:cd07114 198 LVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFA-AAGQTCVAGSRLLVQRSIYD 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 331 KLIDALKTELETF-FGQNALESKDLSRIVNSFHFKRLESML---KENGVanKIVHGG-RITEDKLK----ISPTILLDVP 401
Cdd:cd07114 277 EFVERLVARARAIrVGDPLDPETQMGPLATERQLEKVERYVaraREEGA--RVLTGGeRPSGADLGagyfFEPTILADVT 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 402 EASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDtvLHVTVKDLPFGGV 481
Cdd:cd07114 355 NDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNT--YRALSPSSPFGGF 432
|
330 340
....*....|....*....|...
gi 1032283529 482 GESGIGAYHGKFSYETFSHKKGV 504
Cdd:cd07114 433 KDSGIGRENGIEAIREYTQTKSV 455
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
83-505 |
6.89e-45 |
|
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: 164.45 E-value: 6.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 83 RSNFNSGRTKSYEWRISQLQNIARMIDEKEKCITEALYQDLSKPELEAfLAEISNTkSSCM-----LAiKELKNWmAPET 157
Cdd:cd07110 29 RRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA-AWDVDDV-AGCFeyyadLA-EQLDAK-AERA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 158 VKTSVTTFpsSAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRV 236
Cdd:cd07110 105 VPLPSEDF--KARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIAAEAgLPPGVLNV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 237 IEGGVPETTALL--DQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGK-WacNSG 313
Cdd:cd07110 183 VTGTGDEAGAPLaaHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCfW--NNG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 314 QACIGVDYVITTKDFASKLIDALKTELETFFGQNALESK-DLSRIVNSFHFKRLESML---KENGVanKIVHGGRITEDK 389
Cdd:cd07110 261 QICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGvRLGPLVSQAQYEKVLSFIargKEEGA--RLLCGGRRPAHL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 390 LK---ISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITIND 466
Cdd:cd07110 339 EKgyfIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVWINC 418
|
410 420 430
....*....|....*....|....*....|....*....
gi 1032283529 467 TvlHVTVKDLPFGGVGESGIGAYHGKFSYETFSHKKGVL 505
Cdd:cd07110 419 S--QPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
169-487 |
1.32e-44 |
|
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: 1.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 169 AQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPETTAL 247
Cdd:cd07145 117 AFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPGVINVVTGYGSEVGDE 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 248 L--DQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACIGVDYVITT 325
Cdd:cd07145 197 IvtNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFE-NAGQVCNAVKRILVE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 326 KDFASKLIDALKTELETF-FGQNALESKDLSRIVNSFHFKRLESMLKEN-GVANKIVHGGRITEDKLkISPTILLDVPEA 403
Cdd:cd07145 276 EEVYDKFLKLLVEKVKKLkVGDPLDESTDLGPLISPEAVERMENLVNDAvEKGGKILYGGKRDEGSF-FPPTVLENDTPD 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 404 SSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVLhVTVKDLPFGGVGE 483
Cdd:cd07145 355 MIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDSTR-FRWDNLPFGGFKK 433
|
....
gi 1032283529 484 SGIG 487
Cdd:cd07145 434 SGIG 437
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
86-504 |
1.32e-44 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 163.01 E-value: 1.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 86 FNSGRTKSYEWRISQLQNIARMIDE-KE---KCITealyQDLSKPELEAfLAEISNTKSSCMLAIKELKNWMAPETVKTS 161
Cdd:cd07100 12 FLAWRKTSFAERAALLRKLADLLRErKDelaRLIT----LEMGKPIAEA-RAEVEKCAWICRYYAENAEAFLADEPIETD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 162 vttfPSSAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFseyldnttirvIEGGV 241
Cdd:cd07100 87 ----AGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELF-----------REAGF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 242 PE---TTALLDQKW-DKIF---------FTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKW 308
Cdd:cd07100 152 PEgvfQNLLIDSDQvEAIIadprvrgvtLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 309 AcNSGQACIGVDYVITTKD----FASKLIDALK-------TELETFFGqnALESKDLsrivnsfhFKRLESMLKEnGVAN 377
Cdd:cd07100 232 Q-NAGQSCIAAKRFIVHEDvydeFLEKFVEAMAalkvgdpMDEDTDLG--PLARKDL--------RDELHEQVEE-AVAA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 378 --KIVHGGRITEDK-LKISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFV 454
Cdd:cd07100 300 gaTLLLGGKRPDGPgAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVA 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1032283529 455 QDVSAGGITINDTVLhvTVKDLPFGGVGESGIGAYHGKFSYETFSHKKGV 504
Cdd:cd07100 380 RRLEAGMVFINGMVK--SDPRLPFGGVKRSGYGRELGRFGIREFVNIKTV 427
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
172-504 |
7.31e-44 |
|
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: 161.84 E-value: 7.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 172 VSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPETTALL-- 248
Cdd:cd07115 114 VREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAgFPAGVLNVVTGFGEVAGAALve 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 249 DQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARriiAGKWAC--NSGQACIGVDYVITTK 326
Cdd:cd07115 194 HPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVR---AAATGIfyNQGQMCTAGSRLLVHE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 327 DFASKLIDALKTELETFFGQNALESK-DLSRIVNSFHFKRLESML---KENGVanKIVHGG-RITEDKLKISPTILLDVP 401
Cdd:cd07115 271 SIYDEFLERFTSLARSLRPGDPLDPKtQMGPLVSQAQFDRVLDYVdvgREEGA--RLLTGGkRPGARGFFVEPTIFAAVP 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 402 EASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINdTVLHVTVKdLPFGGV 481
Cdd:cd07115 349 PEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWIN-TYNRFDPG-SPFGGY 426
|
330 340
....*....|....*....|...
gi 1032283529 482 GESGIGAYHGKFSYETFSHKKGV 504
Cdd:cd07115 427 KQSGFGREMGREALDEYTEVKSV 449
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
74-505 |
1.68e-43 |
|
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: 161.32 E-value: 1.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 74 EAALLVDELRSNFNSG--RTKSYEWRISQLQNIARMIDEKEKCITEALYQDLSKP--ELEAFLAEISNT-KSSCMLAIKE 148
Cdd:cd07119 36 DAKRAIAAARRAFDSGewPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTlrESEIDIDDVANCfRYYAGLATKE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 149 LKNWM-APETVKTsvttfpssaQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSE 227
Cdd:cd07119 116 TGEVYdVPPHVIS---------RTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 228 Y-LDNTTIRVIEGGVPETTALL--DQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRII 304
Cdd:cd07119 187 AgLPAGVVNLVTGSGATVGAELaeSPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQAL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 305 AGKWAcNSGQACIGVDYVITTKDFASKLIDALKTELETFFGQNAL-ESKDLSRIVNSFHFKRLESML---KENGVanKIV 380
Cdd:cd07119 267 NGVFF-NAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLdADTEMGPLVSAEHREKVLSYIqlgKEEGA--RLV 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 381 HGG-RITEDKLK----ISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQ 455
Cdd:cd07119 344 CGGkRPTGDELAkgyfVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVAR 423
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1032283529 456 DVSAGGITINDtvLHVTVKDLPFGGVGESGIGAYHGKFSYETFSHKKGVL 505
Cdd:cd07119 424 RLRAGTVWIND--YHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHIN 471
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
160-506 |
7.50e-43 |
|
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: 158.95 E-value: 7.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 160 TSVTTFPSSAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIE 238
Cdd:cd07089 108 PALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAETdLPAGVVNVVT 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 239 GGVPETTALL--DQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGkWACNSGQAC 316
Cdd:cd07089 188 GSDNAVGEALttDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGV-CMHNAGQGC 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 317 igvdyVITTKDFA-----SKLIDALKTELETF-FGQNALESKDLSRIVNSFHFKRLESMLKEnGVAN--KIVHGGRITED 388
Cdd:cd07089 267 -----ALTTRLLVprsryDEVVEALAAAFEALpVGDPADPGTVMGPLISAAQRDRVEGYIAR-GRDEgaRLVTGGGRPAG 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 389 KLK---ISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITIN 465
Cdd:cd07089 341 LDKgfyVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGIN 420
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1032283529 466 DTVLHVTvkDLPFGGVGESGIGAYHGKFSYETFSHKKGVLY 506
Cdd:cd07089 421 GGGGYGP--DAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
101-504 |
1.01e-42 |
|
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: 159.01 E-value: 1.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 101 LQNIARMIDEKEKCITEALYQDL----SKPELEAFLAeisntksscMLAIKELKNWMAPETVKTSVTTFPS-SAQIVSEP 175
Cdd:cd07151 60 LEKAAQILEERRDEIVEWLIRESgstrIKANIEWGAA---------MAITREAATFPLRMEGRILPSDVPGkENRVYREP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 176 LGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLL-AKLFSEY-LDNTTIRVIEGGVPET-TALLDQKW 252
Cdd:cd07151 131 LGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGLLlAKIFEEAgLPKGVLNVVVGAGSEIgDAFVEHPV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 253 DK-IFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACIGVDYVITTKDFASK 331
Cdd:cd07151 211 PRlISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFL-HQGQICMAINRIIVHEDVYDE 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 332 LIDALKTELETF-FGQNALESKDLSRIVNSFHFKRLESML---KENGVanKIVHGGRIteDKLKISPTILLDVPEASSMM 407
Cdd:cd07151 290 FVEKFVERVKALpYGDPSDPDTVVGPLINESQVDGLLDKIeqaVEEGA--TLLVGGEA--EGNVLEPTVLSDVTNDMEIA 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 408 QEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTvlhvTVKD---LPFGGVGES 484
Cdd:cd07151 366 REEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQ----PVNDephVPFGGEKNS 441
|
410 420
....*....|....*....|
gi 1032283529 485 GIGAYHGKFSYETFSHKKGV 504
Cdd:cd07151 442 GLGRFNGEWALEEFTTDKWI 461
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
172-487 |
2.23e-42 |
|
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: 157.78 E-value: 2.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 172 VSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPETTALL-- 248
Cdd:cd07109 114 VREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAgLPAGALNVVTGLGAEAGAALva 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 249 DQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIagkWAC--NSGQACIGVDYVITTK 326
Cdd:cd07109 194 HPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVV---NAIiqNAGQTCSAGSRLLVHR 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 327 DFASKLIDALKTELETFFGQNALESKDLSRIVNSFHFKRLESML---KENGVAnkIVHGGRITEDKLK----ISPTILLD 399
Cdd:cd07109 271 SIYDEVLERLVERFRALRVGPGLEDPDLGPLISAKQLDRVEGFVaraRARGAR--IVAGGRIAEGAPAggyfVAPTLLDD 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 400 VPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVLHVTVkDLPFG 479
Cdd:cd07109 349 VPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNYGAGGGI-ELPFG 427
|
....*...
gi 1032283529 480 GVGESGIG 487
Cdd:cd07109 428 GVKKSGHG 435
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
175-492 |
3.66e-42 |
|
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: 156.92 E-value: 3.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 175 PLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEYLDNTTIRVIEGGV---PETTALLDqk 251
Cdd:cd07106 114 PLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEVLPPGVLNVVSGGDelgPALTSHPD-- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 252 WDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACIGVD--YVITT--KD 327
Cdd:cd07106 192 IRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFI-NSGQVCAAIKrlYVHESiyDE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 328 FASKLIDALKTeleTFFGQNALESKDLSRIVNSFHFKRLESML---KENGVanKIVHGGRITEDK-LKISPTILLDVPEA 403
Cdd:cd07106 271 FCEALVALAKA---AVVGDGLDPGTTLGPVQNKMQYDKVKELVedaKAKGA--KVLAGGEPLDGPgYFIPPTIVDDPPEG 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 404 SSMMQEEIFGPLLPIITVQKIEDgfqVIR---SKPKPLAAYLFTNNKELEKQFVQDVSAGGITINdTVLHVTVkDLPFGG 480
Cdd:cd07106 346 SRIVDEEQFGPVLPVLKYSDEDE---VIAranDSEYGLGASVWSSDLERAEAVARRLEAGTVWIN-THGALDP-DAPFGG 420
|
330
....*....|..
gi 1032283529 481 VGESGIGAYHGK 492
Cdd:cd07106 421 HKQSGIGVEFGI 432
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
152-498 |
1.97e-41 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 156.00 E-value: 1.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 152 WMAPETVKTSVTTFPSSAQ-----IVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFS 226
Cdd:PLN02278 132 YFAEEAKRVYGDIIPSPFPdrrllVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELAL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 227 EY-LDNTTIRVIEGGVPET-TALLDQ-KWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRI 303
Cdd:PLN02278 212 QAgIPPGVLNVVMGDAPEIgDALLASpKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 304 IAGKWAcNSGQACIGVDYVITTKD----FASKLIDALKtELETffGQNALESKDLSRIVNSFHFKRLESMLKEnGVAN-- 377
Cdd:PLN02278 292 LASKFR-NSGQTCVCANRILVQEGiydkFAEAFSKAVQ-KLVV--GDGFEEGVTQGPLINEAAVQKVESHVQD-AVSKga 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 378 KIVHGG-RITEDKLKISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQD 456
Cdd:PLN02278 367 KVLLGGkRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEA 446
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1032283529 457 VSAGGITINDTVLHVTVKdlPFGGVGESGIGAYHGKFSYETF 498
Cdd:PLN02278 447 LEYGIVGVNEGLISTEVA--PFGGVKQSGLGREGSKYGIDEY 486
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
90-507 |
3.94e-41 |
|
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: 154.65 E-value: 3.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 90 RTKSYEWRISQLQNIARMIDEKEKCITEALYQDLSKPELEAfLAEISNTKSSCMLAIKELKNwMAPETVK--TSVTTFPS 167
Cdd:cd07082 56 PTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDA-LKEVDRTIDYIRDTIEELKR-LDGDSLPgdWFPGTKGK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 168 SAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPETTA 246
Cdd:cd07082 134 IAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAgFPKGVVNVVTGRGREIGD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 247 LL--DQKWDKIFFTGGARVARIIMAAAArnLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACIGVDYVIT 324
Cdd:cd07082 214 PLvtHGRIDVISFTGSTEVGNRLKKQHP--MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALS-YSGQRCTAIKRVLV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 325 TKDFASKLIDALKTELETF-FGQNALESKDLSRIVNSFHFKRLESML---KENGVanKIVHGGRITEDKLkISPTILLDV 400
Cdd:cd07082 291 HESVADELVELLKEEVAKLkVGMPWDNGVDITPLIDPKSADFVEGLIddaVAKGA--TVLNGGGREGGNL-IYPTLLDPV 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 401 PEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVLHVTvkD-LPFG 479
Cdd:cd07082 368 TPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGP--DhFPFL 445
|
410 420
....*....|....*....|....*...
gi 1032283529 480 GVGESGIGAYHGKFSYETFSHKKGVLYR 507
Cdd:cd07082 446 GRKDSGIGTQGIGDALRSMTRRKGIVIN 473
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
83-487 |
6.89e-41 |
|
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: 153.53 E-value: 6.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 83 RSNFNSGR--TKSYEWRISQLQNIARMIDE--KEKCITEALyqDLSKPELEAFLAEISNTKSSCmlaikelkNWMAPETV 158
Cdd:cd07112 34 RRAFESGVwsRLSPAERKAVLLRLADLIEAhrDELALLETL--DMGKPISDALAVDVPSAANTF--------RWYAEAID 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 159 KTSVTTFPSSAQ----IVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTT 233
Cdd:cd07112 104 KVYGEVAPTGPDalalITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAgLPAGV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 234 IRVIEGGVPET-TAL-LDQKWDKIFFTGGARV-ARIIMAAAARNLTPVVLELGGKCPALVDSDV-NLQVAARRIIAGKWA 309
Cdd:cd07112 184 LNVVPGFGHTAgEALgLHMDVDALAFTGSTEVgRRFLEYSGQSNLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFW 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 310 cNSGQACIGVDYVITTKDFASKLIDALKTELETFFGQNALE-SKDLSRIVNSFHFKRLESMLkENGVAN--KIVHGGRIT 386
Cdd:cd07112 264 -NQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDpATRMGALVSEAHFDKVLGYI-ESGKAEgaRLVAGGKRV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 387 EDKLK---ISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGIT 463
Cdd:cd07112 342 LTETGgffVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVW 421
|
410 420
....*....|....*....|....
gi 1032283529 464 INdTVLHVTVKdLPFGGVGESGIG 487
Cdd:cd07112 422 VN-CFDEGDIT-TPFGGFKQSGNG 443
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
156-507 |
8.42e-41 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 153.84 E-value: 8.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 156 ETVKTSVTTFPSSAQivsEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTI 234
Cdd:cd07143 128 QVIETDIKKLTYTRH---EPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVI 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 235 RVIEGGVPETTALLDQ--KWDKIFFTGGARV-ARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAArriiagKWAC- 310
Cdd:cd07143 205 NVVSGYGRTCGNAISShmDIDKVAFTGSTLVgRKVMEAAAKSNLKKVTLELGGKSPNIVFDDADLESAV------VWTAy 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 311 ----NSGQACIGVDYVITTKDFASKLIDALKTELETF-----FGQNALESKDLSRIvnsfHFKRLESMLkENGV---ANK 378
Cdd:cd07143 279 giffNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLkvgdpFAEDTFQGPQVSQI----QYERIMSYI-ESGKaegATV 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 379 IVHGGRITEDKLKISPTILLDVPEASSMMQEEIFGpllPIITVQKIEDGFQVIR---SKPKPLAAYLFTNNKELEKQFVQ 455
Cdd:cd07143 354 ETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFG---PVVAVIKFKTEEEAIKranDSTYGLAAAVFTNNINNAIRVAN 430
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1032283529 456 DVSAGGITIND-TVLHVTVkdlPFGGVGESGIGAYHGKFSYETFSHKKGVLYR 507
Cdd:cd07143 431 ALKAGTVWVNCyNLLHHQV---PFGGYKQSGIGRELGEYALENYTQIKAVHIN 480
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
168-498 |
8.73e-41 |
|
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: 153.43 E-value: 8.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 168 SAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPETTA 246
Cdd:cd07138 123 NSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAgLPAGVFNLVNGDGPVVGE 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 247 LL--DQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACIGVDYVIT 324
Cdd:cd07138 203 ALsaHPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFA-NSGQSCNAPTRMLV 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 325 TKDFASKLIDALKTELETF-FGQNALESKDLSRIVNSFHFKRLESMLKEnGVAN--KIVHGGRITEDKLK----ISPTIL 397
Cdd:cd07138 282 PRSRYAEAEEIAAAAAEAYvVGDPRDPATTLGPLASAAQFDRVQGYIQK-GIEEgaRLVAGGPGRPEGLErgyfVKPTVF 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 398 LDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVLHvtvKDLP 477
Cdd:cd07138 361 ADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFN---PGAP 437
|
330 340
....*....|....*....|.
gi 1032283529 478 FGGVGESGIGAYHGKFSYETF 498
Cdd:cd07138 438 FGGYKQSGNGREWGRYGLEEF 458
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
154-488 |
1.87e-40 |
|
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: 152.79 E-value: 1.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 154 APETVKTSVTTFPSS-----AQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSey 228
Cdd:cd07097 109 AGEALRLSGETLPSTrpgveVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILE-- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 229 ldnttirviEGGVPETT-------------ALL-DQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDV 294
Cdd:cd07097 187 ---------EAGLPAGVfnlvmgsgsevgqALVeHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 295 NLQVAARRIIAGKWAcNSGQACIGVDYVITTKDFASKLIDALKTELETFFGQNALESK-DLSRIVNSFHFKRLESMLkEN 373
Cdd:cd07097 258 DLDLAVECAVQGAFF-STGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGvDIGPVVSERQLEKDLRYI-EI 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 374 GVAN--KIVHGGRITEDKLK---ISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKE 448
Cdd:cd07097 336 ARSEgaKLVYGGERLKRPDEgyyLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLK 415
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1032283529 449 LEKQFVQDVSAGGITINDTVLHVTVKdLPFGGVGESGIGA 488
Cdd:cd07097 416 HATHFKRRVEAGVVMVNLPTAGVDYH-VPFGGRKGSSYGP 454
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
168-504 |
2.91e-40 |
|
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: 152.03 E-value: 2.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 168 SAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPETTA 246
Cdd:cd07088 126 NIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAgLPAGVLNIVTGRGSVVGD 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 247 LL--DQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACIGVDYVIT 324
Cdd:cd07088 206 ALvaHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRII-NCGQVCTCAERVYV 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 325 TKD----FASKLIDALKtelETFFGQNALESKDLSRIVNSFHFKRLESML---KENGVanKIVHGGRI--TEDKLKISPT 395
Cdd:cd07088 285 HEDiydeFMEKLVEKMK---AVKVGDPFDAATDMGPLVNEAALDKVEEMVeraVEAGA--TLLTGGKRpeGEKGYFYEPT 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 396 ILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTvlhvtvkd 475
Cdd:cd07088 360 VLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRE-------- 431
|
330 340 350
....*....|....*....|....*....|....*.
gi 1032283529 476 lPF-------GGVGESGIGAYHGKFSYETFSHKKGV 504
Cdd:cd07088 432 -NFeamqgfhAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
163-491 |
2.93e-40 |
|
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: 151.68 E-value: 2.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 163 TTFPSSAQIVS----EPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASS-LLAKLFSEY-LDNTTIRV 236
Cdd:cd07152 94 EILPSAPGRLSlarrVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGvVIARLFEEAgLPAGVLHV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 237 IEGGVPETTAL-LDQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQA 315
Cdd:cd07152 174 LPGGADAGEALvEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFL-HQGQI 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 316 CIGVDYVITTKDFASKLIDALKTELETF-FGQNALESKDLSRIVNSFHFKRLESMLKENGVAN-KIVHGGriTEDKLKIS 393
Cdd:cd07152 253 CMAAGRHLVHESVADAYTAKLAAKAKHLpVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGaRLEAGG--TYDGLFYR 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 394 PTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITIND-TVLHVT 472
Cdd:cd07152 331 PTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDqTVNDEP 410
|
330
....*....|....*....
gi 1032283529 473 VkdLPFGGVGESGIGAYHG 491
Cdd:cd07152 411 H--NPFGGMGASGNGSRFG 427
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
57-510 |
8.89e-40 |
|
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: 150.96 E-value: 8.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 57 ATLSAVVKEQ-ASDFSGKEAAllVDELRSNFNSGRTKSYEWRISQLQNIARMIDEKekciTEALYQDLSKpELEAFLAEi 135
Cdd:cd07131 22 ADLEEVVGTFpLSTASDVDAA--VEAAREAFPEWRKVPAPRRAEYLFRAAELLKKR----KEELARLVTR-EMGKPLAE- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 136 snTKSSCMLAIkELKNWMAPETVKTSVTTFPSS-----AQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKP 210
Cdd:cd07131 94 --GRGDVQEAI-DMAQYAAGEGRRLFGETVPSElpnkdAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 211 SEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPET-TALLDQ-KWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCP 287
Cdd:cd07131 171 AEDTPACALKLVELFAEAgLPPGVVNVVHGRGEEVgEALVEHpDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 288 ALVDSDVNLQVAARRIIAGKWAcNSGQACIGVDYVITTKD----FASKLIDALK-------TELETFFGQnALESKDLSR 356
Cdd:cd07131 251 IIVMDDADLDLALEGALWSAFG-TTGQRCTATSRLIVHESvydeFLKRFVERAKrlrvgdgLDEETDMGP-LINEAQLEK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 357 IVNSFHFKRLESMlkengvanKIVHGG-RITEDKLK----ISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVI 431
Cdd:cd07131 329 VLNYNEIGKEEGA--------TLLLGGeRLTGGGYEkgyfVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 432 RSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVLHVTVKdLPFGGVGESGIGayH---GKFSYETFSHKKGVlYRS 508
Cdd:cd07131 401 NDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVH-LPFGGVKKSGNG--HreaGTTALDAFTEWKAV-YVD 476
|
..
gi 1032283529 509 FS 510
Cdd:cd07131 477 YS 478
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
104-491 |
4.07e-39 |
|
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: 148.66 E-value: 4.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 104 IARMID-EKEKCITEALYqdlskpeleaflaEISNTKSSCMLAIKELKNwMAPETVKTSVTTFPSSAQIVS--EPLGVVL 180
Cdd:cd07146 60 FARLITlESGLCLKDTRY-------------EVGRAADVLRFAAAEALR-DDGESFSCDLTANGKARKIFTlrEPLGVVL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 181 VISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPETTALL--DQKWDKIFF 257
Cdd:cd07146 126 AITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAgLPPDMLSVVTGEPGEIGDELitHPDVDLVTF 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 258 TGGARVARIIMAAAARNLTpvVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACIGVDYVITTKDFASKLIDALK 337
Cdd:cd07146 206 TGGVAVGKAIAATAGYKRQ--LLELGGNDPLIVMDDADLERAATLAVAGSYA-NSGQRCTAVKRILVHESVADEFVDLLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 338 TELETF-FGQNALESKDLSRIVNSFHFKRLesmlkENGVANKIVHGGRI----TEDKLKISPTILLDVPEASSMMQEEIF 412
Cdd:cd07146 283 EKSAALvVGDPMDPATDMGTVIDEEAAIQI-----ENRVEEAIAQGARVllgnQRQGALYAPTVLDHVPPDAELVTEETF 357
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032283529 413 GPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDtVLHVTVKDLPFGGVGESGIGAYHG 491
Cdd:cd07146 358 GPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNE-VPGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
174-506 |
6.39e-39 |
|
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: 148.51 E-value: 6.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 174 EPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPETTALL--DQ 250
Cdd:cd07091 140 EPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAgFPPGVVNIVPGFGPTAGAAIssHM 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 251 KWDKIFFTGGARV-ARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACIGVDYVITTKDFA 329
Cdd:cd07091 220 DVDKIAFTGSTAVgRTIMEAAAKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFF-NQGQCCCAGSRIFVQESIY 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 330 SKLIDALKTELETF-FGQNALESKDLSRIVNSFHFKRLESML---KENGVanKIVHGGRITEDK-LKISPTILLDVPEAS 404
Cdd:cd07091 299 DEFVEKFKARAEKRvVGDPFDPDTFQGPQVSKAQFDKILSYIesgKKEGA--TLLTGGERHGSKgYFIQPTVFTDVKDDM 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 405 SMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITIND-TVLHVTVkdlPFGGVGE 483
Cdd:cd07091 377 KIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTyNVFDAAV---PFGGFKQ 453
|
330 340
....*....|....*....|...
gi 1032283529 484 SGIGAYHGKFSYETFSHKKGVLY 506
Cdd:cd07091 454 SGFGRELGEEGLEEYTQVKAVTI 476
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
77-505 |
9.38e-39 |
|
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: 148.26 E-value: 9.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 77 LLVDELRSNFNSGRTKSYEWRISQLQNIARMIDEKEKCITEALYQDLSKPELEAFLAEISntksscmLAIKELKNWMAP- 155
Cdd:cd07559 42 LAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRETLAADIP-------LAIDHFRYFAGVi 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 156 ETVKTSVTTFPSS--AQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEYLDNTT 233
Cdd:cd07559 115 RAQEGSLSEIDEDtlSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLLPKGV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 234 IRVIEG-GVPETTALLDQK-WDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDV-----NLQVAARRIIAG 306
Cdd:cd07559 195 VNVVTGfGSEAGKPLASHPrIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 307 kWACNSGQACIGVDYVITTKDFASKLIDALKTELETFFGQNALESKD-LSRIVNSFHFKRLESML---KENGvANKIVHG 382
Cdd:cd07559 275 -FAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETmMGAQVSKDQLEKILSYVdigKEEG-AEVLTGG 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 383 GRITEDKLK----ISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVS 458
Cdd:cd07559 353 ERLTLGGLDkgyfYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQ 432
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1032283529 459 AGGITINdtVLHVTVKDLPFGGVGESGIGAYHGKFSYETFSHKKGVL 505
Cdd:cd07559 433 TGRVWVN--CYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNIL 477
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
174-504 |
2.26e-38 |
|
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: 146.68 E-value: 2.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 174 EPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGvPETTALLDQKW 252
Cdd:cd07090 115 EPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAgLPDGVFNVVQGG-GETGQLLCEHP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 253 D--KIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACIGVDYVITTKD--- 327
Cdd:cd07090 194 DvaKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFL-SQGQVCSNGTRVFVQRSikd 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 328 -FASKLIDALKtelETFFGQNALESKDLSRIVNSFHFKRLESML---KENGVanKIVHGG-RIT-EDKLK----ISPTIL 397
Cdd:cd07090 273 eFTERLVERTK---KIRIGDPLDEDTQMGALISEEHLEKVLGYIesaKQEGA--KVLCGGeRVVpEDGLEngfyVSPCVL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 398 LDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDtvLHVTVKDLP 477
Cdd:cd07090 348 TDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINT--YNISPVEVP 425
|
330 340
....*....|....*....|....*..
gi 1032283529 478 FGGVGESGIGAYHGKFSYETFSHKKGV 504
Cdd:cd07090 426 FGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
172-488 |
3.70e-38 |
|
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: 146.98 E-value: 3.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 172 VSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFseyldnttirvIEGGVPETT------ 245
Cdd:cd07124 163 VYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEIL-----------EEAGLPPGVvnflpg 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 246 -------ALLDQ-KWDKIFFTG----GARV--ARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWACn 311
Cdd:cd07124 232 pgeevgdYLVEHpDVRFIAFTGsrevGLRIyeRAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGF- 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 312 SGQACIGVDYVITTKDFASKLIDALKTELETF-FGQNALESKDLSRIVNSFHFKRLESMLKENGVANKIVHGGRITEDKL 390
Cdd:cd07124 311 QGQKCSACSRVIVHESVYDEFLERLVERTKALkVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVLELAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 391 K---ISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDT 467
Cdd:cd07124 391 EgyfVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRK 470
|
330 340
....*....|....*....|.
gi 1032283529 468 VLHVTVKDLPFGGVGESGIGA 488
Cdd:cd07124 471 ITGALVGRQPFGGFKMSGTGS 491
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
166-502 |
7.24e-38 |
|
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: 145.34 E-value: 7.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 166 PSSAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPET 244
Cdd:TIGR01804 124 PSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAgLPKGVFNVVQGDGAEV 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 245 TALL--DQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACIGVDYV 322
Cdd:TIGR01804 204 GPLLvnHPDVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFF-SAGQVCSNGTRV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 323 ITTKDFASKLIDALKTELETFFGQNAL-ESKDLSRIVNSFHFKRLESML---KENGVanKIVHGGRITEDK-----LKIS 393
Cdd:TIGR01804 283 FVHKKIKERFLARLVERTERIKLGDPFdEATEMGPLISAAHRDKVLSYIekgKAEGA--TLATGGGRPENVglqngFFVE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 394 PTILLDVPEASSMMQEEIFGpllPIITVQKIEDGFQVIRSKPKP---LAAYLFTNNKELEKQFVQDVSAGGITINDtvLH 470
Cdd:TIGR01804 361 PTVFADCTDDMTIVREEIFG---PVMTVLTFSDEDEVIARANDTeygLAGGVFTADLGRAHRVADQLEAGTVWINT--YN 435
|
330 340 350
....*....|....*....|....*....|..
gi 1032283529 471 VTVKDLPFGGVGESGIGAYHGKFSYETFSHKK 502
Cdd:TIGR01804 436 LYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
83-505 |
2.26e-37 |
|
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: 144.13 E-value: 2.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 83 RSNFNSGRTKSYEWRISQLQNIARMIDEKEKCITEALYQDLSKPELEAFLAEISNTK------SSCMLAIKELKNWMAPE 156
Cdd:cd07117 48 QEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAVDIPLAAdhfryfAGVIRAEEGSANMIDED 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 157 TVKTsvttfpssaqIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEYLDNTTIRV 236
Cdd:cd07117 128 TLSI----------VLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 237 IEG-GVPETTALLDQK-WDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGkWACNSGQ 314
Cdd:cd07117 198 VTGkGSKSGEYLLNHPgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLG-ILFNQGQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 315 ACIGVDYVITTKDFASKLIDALKTELETFFGQNALE-SKDLSRIVNSFHFKRLESML---KENGvANKIVHGGRITEDKL 390
Cdd:cd07117 277 VCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDpDTQMGAQVNKDQLDKILSYVdiaKEEG-AKILTGGHRLTENGL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 391 K----ISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINd 466
Cdd:cd07117 356 DkgffIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVN- 434
|
410 420 430
....*....|....*....|....*....|....*....
gi 1032283529 467 tVLHVTVKDLPFGGVGESGIGAYHGKFSYETFSHKKGVL 505
Cdd:cd07117 435 -TYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIY 472
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
172-504 |
5.01e-37 |
|
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: 142.90 E-value: 5.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 172 VSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEYLDNTTIRVIEGGVPETTALL--D 249
Cdd:cd07107 113 LREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREVLPPGVFNILPGDGATAGAALvrH 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 250 QKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWACNSGQACIGVDYVITTKDFA 329
Cdd:cd07107 193 PDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAAVAGMNFTWCGQSCGSTSRLFVHESIY 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 330 SKLIDALKTELETFF-GQNALESKDLSRIVNSFHFKRLESML---KENGVanKIVHGGRITEDKLK-----ISPTILLDV 400
Cdd:cd07107 273 DEVLARVVERVAAIKvGDPTDPATTMGPLVSRQQYDRVMHYIdsaKREGA--RLVTGGGRPEGPALeggfyVEPTVFADV 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 401 PEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVLHvtVKDLPFGG 480
Cdd:cd07107 351 TPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVWINGSSRH--FLGAPFGG 428
|
330 340
....*....|....*....|....
gi 1032283529 481 VGESGIGAYHGKFSYETFSHKKGV 504
Cdd:cd07107 429 VKNSGIGREECLEELLSYTQEKNV 452
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
175-498 |
5.41e-37 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 141.80 E-value: 5.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 175 PLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPETTALL--DQK 251
Cdd:PRK10090 71 ALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQELagNPK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 252 WDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKwACNSGQACIGVDYVITTKDFASK 331
Cdd:PRK10090 151 VAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSR-VINSGQVCNCAERVYVQKGIYDQ 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 332 LIDALKTELE-TFFGQNALESK-DLSRIVNSFHFKRLESMLK---ENGVanKIVHGGRITEDK-LKISPTILLDVPEASS 405
Cdd:PRK10090 230 FVNRLGEAMQaVQFGNPAERNDiAMGPLINAAALERVEQKVAravEEGA--RVALGGKAVEGKgYYYPPTLLLDVRQEMS 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 406 MMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTV------LHvtvkdlpfG 479
Cdd:PRK10090 308 IMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENfeamqgFH--------A 379
|
330
....*....|....*....
gi 1032283529 480 GVGESGIGAYHGKFSYETF 498
Cdd:PRK10090 380 GWRKSGIGGADGKHGLHEY 398
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
159-505 |
1.60e-36 |
|
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: 141.86 E-value: 1.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 159 KTSVTTFPSSAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVI 237
Cdd:cd07142 125 MTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAgLPDGVLNIV 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 238 EGGVPETTALLDQKW--DKIFFTGGARV-ARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARriiAGKWAC--NS 312
Cdd:cd07142 205 TGFGPTAGAAIASHMdvDKVAFTGSTEVgKIIMQLAAKSNLKPVTLELGGKSPFIVCEDADVDKAVE---LAHFALffNQ 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 313 GQACIGVDYVITTKDFASKLIDALKTE-LETFFGQNALESKDLSRIVNSFHFKRLESML---KENGvANKIVHGGRITED 388
Cdd:cd07142 282 GQCCCAGSRTFVHESIYDEFVEKAKARaLKRVVGDPFRKGVEQGPQVDKEQFEKILSYIehgKEEG-ATLITGGDRIGSK 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 389 KLKISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINdtV 468
Cdd:cd07142 361 GYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVN--C 438
|
330 340 350
....*....|....*....|....*....|....*..
gi 1032283529 469 LHVTVKDLPFGGVGESGIGAYHGKFSYETFSHKKGVL 505
Cdd:cd07142 439 YDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVV 475
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
152-507 |
1.80e-36 |
|
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: 141.42 E-value: 1.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 152 WMAPETVKTSVTTFPS------SAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLF 225
Cdd:cd07113 113 WATKINGETLAPSIPSmqgeryTAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 226 SEY-LDNTTIRVIEGGVPETTALLDQ-KWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRI 303
Cdd:cd07113 193 KEAgIPDGVLNVVNGKGAVGAQLISHpDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGL 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 304 IAGKWAcNSGQACIGVDYVITTKDFASKLIDALKTELETFFGQNAL-ESKDLSRIVNSFHFKRLESMLKENGVAN-KIVH 381
Cdd:cd07113 273 LTAGFL-HQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMdESVMFGPLANQPHFDKVCSYLDDARAEGdEIVR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 382 GGR-ITEDKLKISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAG 460
Cdd:cd07113 352 GGEaLAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAG 431
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1032283529 461 GITINdtvLHvTVKD--LPFGGVGESGIGAYHGKFSYETFSHKKGVLYR 507
Cdd:cd07113 432 TVWVN---MH-TFLDpaVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
175-487 |
4.46e-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: 140.07 E-value: 4.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 175 PLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLfseyldnttirVIEGGVPE----------- 243
Cdd:cd07147 123 PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEV-----------LAETGLPKgafsvlpcsrd 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 244 TTALL--DQKWDKIFFTGGARVARIIMAAAARNltPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACIGVDY 321
Cdd:cd07147 192 DADLLvtDERIKLLSFTGSPAVGWDLKARAGKK--KVVLELGGNAAVIVDSDADLDFAAQRIIFGAFY-QAGQSCISVQR 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 322 VITTKD----FASKLIDALKTeLETffGQNALESKDLSRIVNSFHFKRLESMLKEnGVAN--KIVHGGRITEDKLKisPT 395
Cdd:cd07147 269 VLVHRSvydeFKSRLVARVKA-LKT--GDPKDDATDVGPMISESEAERVEGWVNE-AVDAgaKLLTGGKRDGALLE--PT 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 396 ILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDtVLHVTVKD 475
Cdd:cd07147 343 ILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVIND-VPTFRVDH 421
|
330
....*....|..
gi 1032283529 476 LPFGGVGESGIG 487
Cdd:cd07147 422 MPYGGVKDSGIG 433
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
83-485 |
4.82e-36 |
|
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: 139.33 E-value: 4.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 83 RSNFNSGRTKSYEWRISQLQNIARMIDEKEKCITEALYQDLSKPELEAfLAEISNTKSSCMLAIKELKNWMAPETVKTSV 162
Cdd:cd07095 10 RAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEA-QTEVAAMAGKIDISIKAYHERTGERATPMAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 163 TTfpssAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGV 241
Cdd:cd07095 89 GR----AVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAgLPPGVLNLVQGGR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 242 PETTALLDQKW-DKIFFTGGARVARIIMAAAARNltPVV---LELGGKCPALVDSDVNLQVAARRIIAGkwAC-NSGQAC 316
Cdd:cd07095 165 ETGEALAAHEGiDGLLFTGSAATGLLLHRQFAGR--PGKilaLEMGGNNPLVVWDVADIDAAAYLIVQS--AFlTAGQRC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 317 IGVDYVITTKD-FASKLIDALK-----------TELETFFG----QNALEskdlsrivnsfHFKRLESMLKENGvANKIV 380
Cdd:cd07095 241 TCARRLIVPDGaVGDAFLERLVeaakrlrigapDAEPPFMGpliiAAAAA-----------RYLLAQQDLLALG-GEPLL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 381 HGGRITEDKLKISPTIlLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAG 460
Cdd:cd07095 309 AMERLVAGTAFLSPGI-IDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAG 387
|
410 420
....*....|....*....|....*
gi 1032283529 461 GITINDTvLHVTVKDLPFGGVGESG 485
Cdd:cd07095 388 IVNWNRP-TTGASSTAPFGGVGLSG 411
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
174-487 |
6.11e-36 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 140.04 E-value: 6.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 174 EPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEYLDNTTIRVIEGGVPET-TALLDQ-K 251
Cdd:PRK13473 137 DPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVgDALVGHpK 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 252 WDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWaCNSGQACIGVDYVITTK----D 327
Cdd:PRK13473 217 VRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGY-YNAGQDCTAACRIYAQRgiydD 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 328 FASKLIDALKTeleTFFGQNALESKDLSRIVNSFHFKRLESML---KENGVAnKIVHGGRITEDK-LKISPTILLDVPEA 403
Cdd:PRK13473 296 LVAKLAAAVAT---LKVGDPDDEDTELGPLISAAHRDRVAGFVeraKALGHI-RVVTGGEAPDGKgYYYEPTLLAGARQD 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 404 SSMMQEEIFGpllPIITVQKIEDGFQVIR---SKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDtvlHVT-VKDLPFG 479
Cdd:PRK13473 372 DEIVQREVFG---PVVSVTPFDDEDQAVRwanDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNT---HFMlVSEMPHG 445
|
....*...
gi 1032283529 480 GVGESGIG 487
Cdd:PRK13473 446 GQKQSGYG 453
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
174-504 |
1.23e-34 |
|
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: 136.49 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 174 EPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPETTALLDQKW 252
Cdd:cd07085 135 QPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAgLPDGVLNVVHGGKEAVNALLDHPD 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 253 DK-IFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWACnSGQACIGVDYVITTKDFASK 331
Cdd:cd07085 215 IKaVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGA-AGQRCMALSVAVAVGDEADE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 332 LIDALKTELETF-FGQNALESKDLSRIVNSFHFKRLESMLkENGV---ANKIVHGGRITEDKLK----ISPTILLDVPEA 403
Cdd:cd07085 294 WIPKLVERAKKLkVGAGDDPGADMGPVISPAAKERIEGLI-ESGVeegAKLVLDGRGVKVPGYEngnfVGPTILDNVTPD 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 404 SSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVlHVTVKDLPFGGVGE 483
Cdd:cd07085 373 MKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPI-PVPLAFFSFGGWKG 451
|
330 340
....*....|....*....|...
gi 1032283529 484 SGIGAYH--GKFSYETFSHKKGV 504
Cdd:cd07085 452 SFFGDLHfyGKDGVRFYTQTKTV 474
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
175-492 |
7.83e-34 |
|
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: 133.59 E-value: 7.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 175 PLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPET-TALLDQKw 252
Cdd:cd07101 118 PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAgLPRDLWQVVTGPGSEVgGAIVDNA- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 253 DKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACIGVDYVITTKDFASKL 332
Cdd:cd07101 197 DYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFS-NAGQLCVSIERIYVHESVYDEF 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 333 IDALKTELETFFGQNALE-SKDLSRIVNSFHFKRLESMLkENGVAN--KIVHGGRITED--KLKISPTILLDVPEASSMM 407
Cdd:cd07101 276 VRRFVARTRALRLGAALDyGPDMGSLISQAQLDRVTAHV-DDAVAKgaTVLAGGRARPDlgPYFYEPTVLTGVTEDMELF 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 408 QEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDT-VLHVTVKDLPFGGVGESGI 486
Cdd:cd07101 355 AEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEGyAAAWASIDAPMGGMKDSGL 434
|
....*.
gi 1032283529 487 GAYHGK 492
Cdd:cd07101 435 GRRHGA 440
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
169-502 |
3.50e-33 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 132.33 E-value: 3.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 169 AQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEG-GVPETTA 246
Cdd:PRK09847 151 AMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGfGHEAGQA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 247 L-LDQKWDKIFFTGGARVARIIMAAA-ARNLTPVVLELGGKCPALVDSDV-NLQVAARRIIAGKWAcNSGQACIGVDYVI 323
Cdd:PRK09847 231 LsRHNDIDAIAFTGSTRTGKQLLKDAgDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFY-NQGQVCIAGTRLL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 324 TTKDFASKLIDALKTELETFFGQNALE-SKDLSRIVNSFHFKRLESMLKENGVANKIVHGGRITEDKLKISPTILLDVPE 402
Cdd:PRK09847 310 LEESIADEFLALLKQQAQNWQPGHPLDpATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGLAAAIGPTIFVDVDP 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 403 ASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITIND------TVlhvtvkdl 476
Cdd:PRK09847 390 NASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNyndgdmTV-------- 461
|
330 340
....*....|....*....|....*.
gi 1032283529 477 PFGGVGESGIGAYHGKFSYETFSHKK 502
Cdd:PRK09847 462 PFGGYKQSGNGRDKSLHALEKFTELK 487
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
101-504 |
4.89e-33 |
|
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: 131.31 E-value: 4.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 101 LQNIARMIDEKEKCITEALYQDLSKPELEAFLaEISntksscmLAIKELKNW--MAPETVKTSVTTFPSS-AQIVSEPLG 177
Cdd:cd07120 48 LLELADAFEANAERLARLLALENGKILGEARF-EIS-------GAISELRYYagLARTEAGRMIEPEPGSfSLVLREPMG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 178 VVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSE--YLDNTTIRVIEGGVPETTALL--DQKWD 253
Cdd:cd07120 120 VAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEipSLPAGVVNLFTESGSEGAAHLvaSPDVD 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 254 KIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKwACNSGQACIGVDYVITTKDFASKLI 333
Cdd:cd07120 200 VISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERAL-TIFAGQFCMAGSRVLVQRSIADEVR 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 334 DALKTELETF-FGQNALESKDLSRIVNSFHFKRLESMLKENGV--ANKIVHGGRITEDKLK---ISPTILLDVPEASSMM 407
Cdd:cd07120 279 DRLAARLAAVkVGPGLDPASDMGPLIDRANVDRVDRMVERAIAagAEVVLRGGPVTEGLAKgafLRPTLLEVDDPDADIV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 408 QEEIFGpllPIITVQKIEDGFQVIRSKPKP---LAAYLFTNNKELEKQFVQDVSAGGITINDtvlHVTVKD-LPFGGVGE 483
Cdd:cd07120 359 QEEIFG---PVLTLETFDDEAEAVALANDTdygLAASVWTRDLARAMRVARAIRAGTVWIND---WNKLFAeAEEGGYRQ 432
|
410 420
....*....|....*....|.
gi 1032283529 484 SGIGAYHGKFSYETFSHKKGV 504
Cdd:cd07120 433 SGLGRLHGVAALEDFIEYKHI 453
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
89-504 |
5.03e-33 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 132.16 E-value: 5.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 89 GRTKSYEW-------RISQLQNIARMIDEKEKCITEALYQDLSKP---------------ELEAFLAEISNTKSScmlai 146
Cdd:PLN02467 59 KRNKGKDWarttgavRAKYLRAIAAKITERKSELAKLETLDCGKPldeaawdmddvagcfEYYADLAEALDAKQK----- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 147 kelknwmAPetVKTSVTTFPSsaQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFS 226
Cdd:PLN02467 134 -------AP--VSLPMETFKG--YVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 227 EY-LDNTTIRVIEGGVPETTALLDQK--WDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRI 303
Cdd:PLN02467 203 EVgLPPGVLNVVTGLGTEAGAPLASHpgVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 304 IAGKWACNsGQACIGVDYVITTKDFASKLIDALKTELETFFGQNALESK-DLSRIVNSFHFKRLESML---KENGVAnkI 379
Cdd:PLN02467 283 MFGCFWTN-GQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGcRLGPVVSEGQYEKVLKFIstaKSEGAT--I 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 380 VHGGRITEDKLK---ISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQD 456
Cdd:PLN02467 360 LCGGKRPEHLKKgffIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEA 439
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1032283529 457 VSAGGITINDTvlHVTVKDLPFGGVGESGIGAYHGKFSYETFSHKKGV 504
Cdd:PLN02467 440 FQAGIVWINCS--QPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQV 485
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
175-491 |
7.31e-33 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 131.92 E-value: 7.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 175 PLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLfseyldnttirVIEGGVPET---------- 244
Cdd:PRK09407 154 PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVEL-----------LYEAGLPRDlwqvvtgpgp 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 245 ---TALLDQKwDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAgkwAC--NSGQACIGV 319
Cdd:PRK09407 223 vvgTALVDNA-DYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVR---ACfsNAGQLCISI 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 320 D--YVITTK--DFASKLIDALKT-ELETFFGQNAleskDLSRIVNSFHFKRLESMLkENGVAN--KIVHGGRITED--KL 390
Cdd:PRK09407 299 EriYVHESIydEFVRAFVAAVRAmRLGAGYDYSA----DMGSLISEAQLETVSAHV-DDAVAKgaTVLAGGKARPDlgPL 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 391 KISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITIND---- 466
Cdd:PRK09407 374 FYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEgyaa 453
|
330 340
....*....|....*....|....*...
gi 1032283529 467 ---TVlhvtvkDLPFGGVGESGIGAYHG 491
Cdd:PRK09407 454 awgSV------DAPMGGMKDSGLGRRHG 475
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
163-487 |
1.43e-32 |
|
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: 130.39 E-value: 1.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 163 TTFPSSAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGV 241
Cdd:cd07139 125 GSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAgLPPGVVNVVPADR 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 242 pETTALL--DQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACIGV 319
Cdd:cd07139 205 -EVGEYLvrHPGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLM-NNGQVCVAL 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 320 DYVITTKDFASKLIDALKTELETF-FGQNALESKDLSRIVNSFHFKRLESMLkENGVAN--KIVHGGRITEDKLK---IS 393
Cdd:cd07139 283 TRILVPRSRYDEVVEALAAAVAALkVGDPLDPATQIGPLASARQRERVEGYI-AKGRAEgaRLVTGGGRPAGLDRgwfVE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 394 PTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVLHVTv 473
Cdd:cd07139 362 PTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDFG- 440
|
330
....*....|....
gi 1032283529 474 kdLPFGGVGESGIG 487
Cdd:cd07139 441 --APFGGFKQSGIG 452
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
174-492 |
6.18e-32 |
|
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: 128.67 E-value: 6.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 174 EPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPETTALLDQ-K 251
Cdd:cd07111 146 KPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAgLPPGVLNIVTGNGSFGSALANHpG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 252 WDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACIGVDYVITTKDFASK 331
Cdd:cd07111 226 VDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWF-NQGQVCCAGSRLLVQESVAEE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 332 LIDALKTELETFFGQNALE-SKDLSRIVNSFHFKRLESMLKENGV--ANKIVHGGRITEDKLKISPTILLDVPEASSMMQ 408
Cdd:cd07111 305 LIRKLKERMSHLRVGDPLDkAIDMGAIVDPAQLKRIRELVEEGRAegADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQ 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 409 EEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVLhvtvKD--LPFGGVGESGI 486
Cdd:cd07111 385 EEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNL----FDaaAGFGGYRESGF 460
|
....*.
gi 1032283529 487 GAYHGK 492
Cdd:cd07111 461 GREGGK 466
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
54-495 |
7.67e-32 |
|
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: 128.85 E-value: 7.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 54 TCYATLSAVvkEQASdfsgkEAALlvdelrSNFNSGRTKSYEWRISQLQNIARMIDEKEKCITEALYQDLSKPELEAfLA 133
Cdd:cd07083 49 TAKADKAEA--EAAL-----EAAW------AAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEA-ID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 134 EISNTKSSCMLAIKELKNWMAPETVKTSVTtfPSSAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEI 213
Cdd:cd07083 115 DVAEAIDFIRYYARAALRLRYPAVEVVPYP--GEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAED 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 214 APAASSLLAKLFSEY-LDNTTIRVIEGGVPETTALL--DQKWDKIFFTGGARVARIIMAAAARNLT------PVVLELGG 284
Cdd:cd07083 193 AVVVGYKVFEIFHEAgFPPGVVQFLPGVGEEVGAYLteHERIRGINFTGSLETGKKIYEAAARLAPgqtwfkRLYVETGG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 285 KCPALVDSDVNLQVAARRIIAGKWAcNSGQACIGVDYVITTKDFASKLIDALKTELETFFGQNALESK-DLSRIVNSFHF 363
Cdd:cd07083 273 KNAIIVDETADFELVVEGVVVSAFG-FQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGtDLGPVIDAEQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 364 KRLESMLKENGVANKIVHGGRITE-DKLKISPTILLDVPEASSMMQEEIFGPLLPIITVQ--KIEDGFQVIRSKPKPLAA 440
Cdd:cd07083 352 AKVLSYIEHGKNEGQLVLGGKRLEgEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKddDFAEALEVANSTPYGLTG 431
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1032283529 441 YLFTNNKELEKQFVQDVSAGGITINDTVLHVTVKDLPFGGVGESGIGAYHGKFSY 495
Cdd:cd07083 432 GVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHY 486
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
174-507 |
2.09e-31 |
|
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: 127.08 E-value: 2.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 174 EPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPETTALLD--Q 250
Cdd:cd07141 144 EPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAgFPPGVVNVVPGYGPTAGAAISshP 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 251 KWDKIFFTGGARV-ARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACIGVDYVITTKD-- 327
Cdd:cd07141 224 DIDKVAFTGSTEVgKLIQQAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFF-NMGQCCCAGSRTFVQESiy 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 328 --FASKLIDALKT-------ELETFFGQNaleskdlsriVNSFHFKRLESML---KENGVanKIVHGGRITEDK-LKISP 394
Cdd:cd07141 303 deFVKRSVERAKKrvvgnpfDPKTEQGPQ----------IDEEQFKKILELIesgKKEGA--KLECGGKRHGDKgYFIQP 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 395 TILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINdTVLHVTVK 474
Cdd:cd07141 371 TVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVN-CYNVVSPQ 449
|
330 340 350
....*....|....*....|....*....|...
gi 1032283529 475 dLPFGGVGESGIGAYHGKFSYETFSHKKGVLYR 507
Cdd:cd07141 450 -APFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 481
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
166-505 |
9.10e-31 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 126.08 E-value: 9.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 166 PSSAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPET 244
Cdd:PLN02466 186 PHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAgLPPGVLNVVSGFGPTA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 245 TALLDQKW--DKIFFTGGARV-ARIIMAAAARNLTPVVLELGGKCPALV--DSDVN--LQVAARRIIAgkwacNSGQACI 317
Cdd:PLN02466 266 GAALASHMdvDKLAFTGSTDTgKIVLELAAKSNLKPVTLELGGKSPFIVceDADVDkaVELAHFALFF-----NQGQCCC 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 318 GVDYVITTKDFASKLIDALKTE-LETFFGQNALESKDLSRIVNSFHFKRLESMLK---ENGvANKIVHGGRITEDKLKIS 393
Cdd:PLN02466 341 AGSRTFVHERVYDEFVEKAKARaLKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKsgvESG-ATLECGGDRFGSKGYYIQ 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 394 PTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINdtVLHVTV 473
Cdd:PLN02466 420 PTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVN--CFDVFD 497
|
330 340 350
....*....|....*....|....*....|..
gi 1032283529 474 KDLPFGGVGESGIGAYHGKFSYETFSHKKGVL 505
Cdd:PLN02466 498 AAIPFGGYKMSGIGREKGIYSLNNYLQVKAVV 529
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
174-505 |
2.61e-30 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 124.16 E-value: 2.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 174 EPLGVVLVISAWNFP---FLLSVEPvigAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPETTALLD 249
Cdd:PLN02766 157 EPIGVVGHIIPWNFPstmFFMKVAP---ALAAGCTMVVKPAEQTPLSALFYAHLAKLAgVPDGVINVVTGFGPTAGAAIA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 250 QKWD--KIFFTGGARV-ARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACIGVDYVITTK 326
Cdd:PLN02766 234 SHMDvdKVSFTGSTEVgRKIMQAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFY-NKGEICVASSRVYVQE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 327 DFASKLIDALKTELETFFGQNALESK-DLSRIVNSFHFKRLESML---KENGVAnkIVHGGRITEDK-LKISPTILLDVP 401
Cdd:PLN02766 313 GIYDEFVKKLVEKAKDWVVGDPFDPRaRQGPQVDKQQFEKILSYIehgKREGAT--LLTGGKPCGDKgYYIEPTIFTDVT 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 402 EASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINdtVLHVTVKDLPFGGV 481
Cdd:PLN02766 391 EDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN--CYFAFDPDCPFGGY 468
|
330 340
....*....|....*....|....
gi 1032283529 482 GESGIGAYHGKFSYETFSHKKGVL 505
Cdd:PLN02766 469 KMSGFGRDQGMDALDKYLQVKSVV 492
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
170-485 |
2.77e-30 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 124.28 E-value: 2.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 170 QIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPETTA-L 247
Cdd:PRK03137 166 RYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAgLPAGVVNFVPGSGSEVGDyL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 248 LDQKWDK-IFFTG----GARVARIIMAAAARN--LTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWACnSGQACIGVD 320
Cdd:PRK03137 246 VDHPKTRfITFTGsrevGLRIYERAAKVQPGQiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGF-SGQKCSACS 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 321 YVITTKDFASKLIDALKTELETFFGQNALESKDLSRIVNSFHFKRLESML---KENGvanKIVHGGRITEDK-LKISPTI 396
Cdd:PRK03137 325 RAIVHEDVYDEVLEKVVELTKELTVGNPEDNAYMGPVINQASFDKIMSYIeigKEEG---RLVLGGEGDDSKgYFIQPTI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 397 LLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVLHVTVKDL 476
Cdd:PRK03137 402 FADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYH 481
|
....*....
gi 1032283529 477 PFGGVGESG 485
Cdd:PRK03137 482 PFGGFNMSG 490
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
175-487 |
5.31e-30 |
|
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: 123.06 E-value: 5.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 175 PLGVVLVISAWNFPFllsvePVIG-----AIAAGNAVVLKPSEIAPAASSLLAKLFSEYLDNT-----TIRVIEGGVPET 244
Cdd:cd07086 133 PLGVVGVITAFNFPV-----AVPGwnaaiALVCGNTVVWKPSETTPLTAIAVTKILAEVLEKNglppgVVNLVTGGGDGG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 245 TALL-DQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIagkWAC--NSGQACigvdy 321
Cdd:cd07086 208 ELLVhDPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVL---FAAvgTAGQRC----- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 322 viTTkdfASKLI------DALKTELETFFGQ----NALESK-DLSRIVNSFHFKRLESML---KENGVanKIVHGGRITE 387
Cdd:cd07086 280 --TT---TRRLIvhesvyDEFLERLVKAYKQvrigDPLDEGtLVGPLINQAAVEKYLNAIeiaKSQGG--TVLTGGKRID 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 388 DKLK---ISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNN-KELEKQFVQDVSAGGI- 462
Cdd:cd07086 353 GGEPgnyVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDlREAFRWLGPKGSDCGIv 432
|
330 340 350
....*....|....*....|....*....|
gi 1032283529 463 -----TINDTVlhvtvkDLPFGGVGESGIG 487
Cdd:cd07086 433 nvnipTSGAEI------GGAFGGEKETGGG 456
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
97-487 |
1.79e-29 |
|
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: 120.99 E-value: 1.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 97 RISQLQNIARMIDEKEKCITEALYQDLSKPELEAfLAEISNTKSSCMLAIKELKNwMAPETVKTSVTtfPSS----AQIV 172
Cdd:cd07148 46 RIAILERLADLMEERADELALLIAREGGKPLVDA-KVEVTRAIDGVELAADELGQ-LGGREIPMGLT--PASagriAFTT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 173 SEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLfseyldnttirVIEGGVPE--TTALL-- 248
Cdd:cd07148 122 REPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDL-----------LHEAGLPEgwCQAVPce 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 249 ---------DQKWDKIFFTGGARVariiMAAAARNLTP---VVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQAC 316
Cdd:cd07148 191 navaeklvtDPRVAFFSFIGSARV----GWMLRSKLAPgtrCALEHGGAAPVIVDRSADLDAMIPPLVKGGFY-HAGQVC 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 317 IGVDYVITTKDFASKLIDALKTELETF-FGQNALESKDLSRIVNSFHFKRLESMLKE--NGVANKIVHGGRITEDKLkiS 393
Cdd:cd07148 266 VSVQRVFVPAEIADDFAQRLAAAAEKLvVGDPTDPDTEVGPLIRPREVDRVEEWVNEavAAGARLLCGGKRLSDTTY--A 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 394 PTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITIND-TVLHVt 472
Cdd:cd07148 344 PTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDhTAFRV- 422
|
410
....*....|....*.
gi 1032283529 473 vkD-LPFGGVGESGIG 487
Cdd:cd07148 423 --DwMPFAGRRQSGYG 436
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
169-505 |
2.62e-25 |
|
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: 109.08 E-value: 2.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 169 AQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEYLDNTTIRVIEGGVPETTALL 248
Cdd:cd07116 130 AYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGFGLEAGKPL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 249 --DQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAA--RRIIAG--KWACNSGQACIGVDYV 322
Cdd:cd07116 210 asSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPNIFFADVMDADDAffDKALEGfvMFALNQGEVCTCPSRA 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 323 ITTKDFASKLIDALKTELETFFGQNALESKDLsrIVNSFHFKRLESML------KENGvANKIVHGGRITEDKLK----I 392
Cdd:cd07116 290 LIQESIYDRFMERALERVKAIKQGNPLDTETM--IGAQASLEQLEKILsyidigKEEG-AEVLTGGERNELGGLLgggyY 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 393 SPTILLdvpEASSM--MQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINdtVLH 470
Cdd:cd07116 367 VPTTFK---GGNKMriFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN--CYH 441
|
330 340 350
....*....|....*....|....*....|....*
gi 1032283529 471 VTVKDLPFGGVGESGIGAYHGKFSYETFSHKKGVL 505
Cdd:cd07116 442 LYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLL 476
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
74-491 |
9.65e-25 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 107.13 E-value: 9.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 74 EAALLVDELRsnFNSGRTKSYEWRISQLQNIARMIDEKEKCITEALYQDLSKPeLEAFLAEISNTKSSCMLAIKELKNWM 153
Cdd:PRK09406 26 DAAIARAHAR--FRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKT-LASAKAEALKCAKGFRYYAEHAEALL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 154 APETVKTSVTTfPSSAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSeyldntt 233
Cdd:PRK09406 103 ADEPADAAAVG-ASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFR------- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 234 irviEGGVPE---TTALL----------DQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAA 300
Cdd:PRK09406 175 ----RAGFPDgcfQTLLVgsgaveailrDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 301 RRIIAGKwaC-NSGQACIGVDYVITTKD----FASKLID---ALK----TELETFFGQNALES--KDLSRIVnsfhfkrl 366
Cdd:PRK09406 251 ETAVTAR--VqNNGQSCIAAKRFIVHADvydaFAEKFVArmaALRvgdpTDPDTDVGPLATEQgrDEVEKQV-------- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 367 esmlkENGVAN--KIVHGG-RITEDKLKISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLF 443
Cdd:PRK09406 321 -----DDAVAAgaTILCGGkRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAW 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1032283529 444 TNNKELEKQFVQDVSAGGITINDTVlhVTVKDLPFGGVGESGIG---AYHG 491
Cdd:PRK09406 396 TRDEAEQERFIDDLEAGQVFINGMT--VSYPELPFGGVKRSGYGrelSAHG 444
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
84-498 |
3.05e-24 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 105.71 E-value: 3.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 84 SNFNSGRTKSYEWRISQLQNIARMI----DEKEKCITealyQDLSKPELEAfLAEISNTKSSCmlaikelkNWMA---PE 156
Cdd:PRK13968 40 AGFRDWRETNIDYRAQKLRDIGKALrarsEEMAQMIT----REMGKPINQA-RAEVAKSANLC--------DWYAehgPA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 157 TVKTSVTTFPSS-AQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEyldnttir 235
Cdd:PRK13968 107 MLKAEPTLVENQqAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKD-------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 236 vieGGVPE-------------TTALLDQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARR 302
Cdd:PRK13968 179 ---AGIPQgvygwlnadndgvSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 303 IIAGKWAcNSGQACIGVDYVITTKDFASKLID-------ALK----TELETFFGQNAleSKDLSrivNSFHfKRLESMLK 371
Cdd:PRK13968 256 AVAGRYQ-NTGQVCAAAKRFIIEEGIASAFTErfvaaaaALKmgdpRDEENALGPMA--RFDLR---DELH-HQVEATLA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 372 ENgvANKIVHGGRITEDKLKISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEK 451
Cdd:PRK13968 329 EG--ARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQAR 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1032283529 452 QFVQDVSAGGITINDtvlhVTVKD--LPFGGVGESGIGAYHGKFSYETF 498
Cdd:PRK13968 407 QMAARLECGGVFING----YCASDarVAFGGVKKSGFGRELSHFGLHEF 451
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
174-505 |
1.50e-23 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 103.81 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 174 EPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFseyldnttirvIEGGVP----------- 242
Cdd:PRK13252 141 EPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIY-----------TEAGLPdgvfnvvqgdg 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 243 ETTALLDQKWD--KIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACIGVD 320
Cdd:PRK13252 210 RVGAWLTEHPDiaKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFY-SSGQVCTNGT 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 321 YVITTKDFASKLIDALKTELE-----------TFFGqnALESKDLSRIVNSFhfkrLESMLKENGvanKIVHGG-RITED 388
Cdd:PRK13252 289 RVFVQKSIKAAFEARLLERVEririgdpmdpaTNFG--PLVSFAHRDKVLGY----IEKGKAEGA---RLLCGGeRLTEG 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 389 KLK----ISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDgfqVIR---SKPKPLAAYLFTNNKELEKQFVQDVSAGG 461
Cdd:PRK13252 360 GFAngafVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDE---VIAranDTEYGLAAGVFTADLSRAHRVIHQLEAGI 436
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1032283529 462 ITINDTVLhvTVKDLPFGGVGESGIGAYHGKFSYETFSHKKGVL 505
Cdd:PRK13252 437 CWINTWGE--SPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQ 478
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
175-485 |
2.17e-23 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 103.50 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 175 PLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPETTALLDQK-W 252
Cdd:PRK09457 134 PHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAgLPAGVLNLVQGGRETGKALAAHPdI 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 253 DKIFFTGGARVARIIMAAAARNltP---VVLELGGKCPALVDSDVNLQVAARRIIAGKWaCNSGQACIGVDYVITTKD-- 327
Cdd:PRK09457 214 DGLLFTGSANTGYLLHRQFAGQ--PekiLALEMGGNNPLVIDEVADIDAAVHLIIQSAF-ISAGQRCTCARRLLVPQGaq 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 328 ---FASKLIDALKT-ELETFFGQNA------LESKDLSRIVNSFHFkrlesmLKENGvANKIVHGGRITEDKLKISPTIl 397
Cdd:PRK09457 291 gdaFLARLVAVAKRlTVGRWDAEPQpfmgavISEQAAQGLVAAQAQ------LLALG-GKSLLEMTQLQAGTGLLTPGI- 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 398 LDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTvLHVTVKDLP 477
Cdd:PRK09457 363 IDVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKP-LTGASSAAP 441
|
....*...
gi 1032283529 478 FGGVGESG 485
Cdd:PRK09457 442 FGGVGASG 449
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
172-490 |
3.79e-23 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 102.65 E-value: 3.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 172 VSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPETTALLDQ 250
Cdd:TIGR01722 133 IRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEAgAPDGVLNVVHGDKEAVDRLLEH 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 251 KWDK-IFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWACnSGQACIGVDYVITTKDfA 329
Cdd:TIGR01722 213 PDVKaVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGA-AGQRCMAISAAVLVGA-A 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 330 SKLIDALKTELETF-FGQNALESKDLSRIVNSFHFKRLESMLkENGVAN--KIVHGGR-IT----EDKLKISPTILLDVP 401
Cdd:TIGR01722 291 DEWVPEIRERAEKIrIGPGDDPGAEMGPLITPQAKDRVASLI-AGGAAEgaEVLLDGRgYKvdgyEEGNWVGPTLLERVP 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 402 EASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINdTVLHVTVKDLPFGGV 481
Cdd:TIGR01722 370 PTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVN-VPIPVPLPYFSFTGW 448
|
....*....
gi 1032283529 482 GESGIGAYH 490
Cdd:TIGR01722 449 KDSFFGDHH 457
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
152-498 |
3.23e-22 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 99.98 E-value: 3.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 152 WMAPETVKTSVTTFPSSAQ-----IVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFS 226
Cdd:PRK11241 118 WFAEEGKRIYGDTIPGHQAdkrliVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 227 EY-LDNTTIRVIEGGVPETTALLDQK--WDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRI 303
Cdd:PRK11241 198 RAgIPAGVFNVVTGSAGAVGGELTSNplVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 304 IAGKWAcNSGQACIGVDYVITTKDFASKLIDALKTELETFFGQNALESK-DLSRIVNSFHFKRLESMLkENGVAN--KIV 380
Cdd:PRK11241 278 LASKFR-NAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGvTIGPLIDEKAVAKVEEHI-ADALEKgaRVV 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 381 HGGRITE-DKLKISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSA 459
Cdd:PRK11241 356 CGGKAHElGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEY 435
|
330 340 350
....*....|....*....|....*....|....*....
gi 1032283529 460 GGITINDTVLHVTVKdlPFGGVGESGIGAYHGKFSYETF 498
Cdd:PRK11241 436 GIVGINTGIISNEVA--PFGGIKASGLGREGSKYGIEDY 472
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
174-487 |
1.18e-20 |
|
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: 94.87 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 174 EPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPaassLLAKLFSEYldntTIRV-IEGGV----PETTALL 248
Cdd:cd07140 146 EPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTP----LTALKFAEL----TVKAgFPKGVinilPGSGSLV 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 249 DQKWD------KIFFTGGARV-ARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRiiaGKWAC--NSGQACIGV 319
Cdd:cd07140 218 GQRLSdhpdvrKLGFTGSTPIgKHIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRM---GMSSVffNKGENCIAA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 320 DYVITTK----DFASKLIDALKT-------ELETFFG-QNaleskdlsrivnsfHFKRLESMLK--ENGVAN--KIVHGG 383
Cdd:cd07140 295 GRLFVEEsihdEFVRRVVEEVKKmkigdplDRSTDHGpQN--------------HKAHLDKLVEycERGVKEgaTLVYGG 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 384 RITEDK-LKISPTILLDVPEASSMMQEEIFGpllPIITVQKIEDG-----FQVIRSKPKPLAAYLFTNNKELEKQFVQDV 457
Cdd:cd07140 361 KQVDRPgFFFEPTVFTDVEDHMFIAKEESFG---PIMIISKFDDGdvdgvLQRANDTEYGLASGVFTKDINKALYVSDKL 437
|
330 340 350
....*....|....*....|....*....|
gi 1032283529 458 SAGGITINdtVLHVTVKDLPFGGVGESGIG 487
Cdd:cd07140 438 EAGTVFVN--TYNKTDVAAPFGGFKQSGFG 465
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
174-495 |
2.22e-20 |
|
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: 94.57 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 174 EPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSeyldnttirviEGGVPETT-------- 245
Cdd:cd07125 166 HGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLH-----------EAGVPRDVlqlvpgdg 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 246 -----ALL-DQKWDKIFFTGG---ARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQAC 316
Cdd:cd07125 235 eeigeALVaHPRIDGVIFTGStetAKLINRALAERDGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFG-SAGQRC 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 317 IGVDYVITTKDFASKLIDALK---TELETffGQNALESKDLSRIVNSFHFKRLESMLKENGVANKIVHGGRITEDK--Lk 391
Cdd:cd07125 314 SALRLLYLQEEIAERFIEMLKgamASLKV--GDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDGNgyF- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 392 ISPTILLDVpeASSMMQEEIFGPLLPIIT--VQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVL 469
Cdd:cd07125 391 VAPGIIEIV--GIFDLTTEVFGPILHVIRfkAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNIT 468
|
330 340
....*....|....*....|....*.
gi 1032283529 470 HVTVKDLPFGGVGESGIGAYHGKFSY 495
Cdd:cd07125 469 GAIVGRQPFGGWGLSGTGPKAGGPNY 494
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
141-504 |
4.36e-19 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 90.96 E-value: 4.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 141 SCMLAIKELKNWMApeTVKTSVTTFPssaqiVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSL 220
Cdd:PLN02419 222 ACGMATLQMGEYLP--NVSNGVDTYS-----IREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVI 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 221 LAKLFSEY-LDNTTIRVIEGGVPETTALL-DQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQV 298
Cdd:PLN02419 295 LAELAMEAgLPDGVLNIVHGTNDTVNAICdDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDA 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 299 AARRIIAGKWACnSGQACIGVDYVITTKDFAS---KLIDALKTeLETFFGQNAleSKDLSRIVNSFHFKRLESMLkENGV 375
Cdd:PLN02419 375 TLNALLAAGFGA-AGQRCMALSTVVFVGDAKSwedKLVERAKA-LKVTCGSEP--DADLGPVISKQAKERICRLI-QSGV 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 376 AN--KIVHGGRIT-----EDKLKISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKE 448
Cdd:PLN02419 450 DDgaKLLLDGRDIvvpgyEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGA 529
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1032283529 449 LEKQFVQDVSAGGITINdTVLHVTVKDLPFGGVGESGIG--AYHGKFSYETFSHKKGV 504
Cdd:PLN02419 530 AARKFQMDIEAGQIGIN-VPIPVPLPFFSFTGNKASFAGdlNFYGKAGVDFFTQIKLV 586
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
80-488 |
8.35e-18 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 86.35 E-value: 8.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 80 DELRSNFNSGRTKSYEW-------RISQLQNIARMIDEKEKCITEALYQDLSKPELEAfLAEISNTKsscmlaikELKNW 152
Cdd:PLN00412 53 EEVNKAMESAKAAQKAWaktplwkRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDA-VTEVVRSG--------DLISY 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 153 MAPETVKT-------SVTTFPSSAQ----IVSE-PLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSL 220
Cdd:PLN00412 124 TAEEGVRIlgegkflVSDSFPGNERnkycLTSKiPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALH 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 221 LAKLFSEY-LDNTTIRVIEGGVPETTALLDQK--WDKIFFTGGarvARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQ 297
Cdd:PLN00412 204 MVHCFHLAgFPKGLISCVTGKGSEIGDFLTMHpgVNCISFTGG---DTGIAISKKAGMVPLQMELGGKDACIVLEDADLD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 298 VAARRIIAGKWAcNSGQACIGVDYVITTKDFASKLIDALKTELETFFGQNALESKDLSRIVNSFHFKRLESMLKENGVAN 377
Cdd:PLN00412 281 LAAANIIKGGFS-YSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVMDAKEKG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 378 KIVHGGRITEDKLkISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDV 457
Cdd:PLN00412 360 ATFCQEWKREGNL-IWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAM 438
|
410 420 430
....*....|....*....|....*....|....*
gi 1032283529 458 SAGGITINDTVL----HvtvkdLPFGGVGESGIGA 488
Cdd:PLN00412 439 ETGTVQINSAPArgpdH-----FPFQGLKDSGIGS 468
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
170-491 |
1.87e-17 |
|
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: 85.35 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 170 QIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPETTALL 248
Cdd:TIGR01238 155 EFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAgFPAGTIQLLPGRGADVGAAL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 249 --DQKWDKIFFTGG---ARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACIGVDYVI 323
Cdd:TIGR01238 235 tsDPRIAGVAFTGStevAQLINQTLAQREDAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFD-SAGQRCSALRVLC 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 324 TTKDFASKLIDALKTEL-ETFFGQNALESKDLSRIVNSFHFKRLESMLKENGVANKIVHGGRITED----KLKISPTILL 398
Cdd:TIGR01238 314 VQEDVADRVLTMIQGAMqELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDSracqHGTFVAPTLF 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 399 DVPEASSmMQEEIFGPLLPII--TVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVLHVTVKDL 476
Cdd:TIGR01238 394 ELDDIAE-LSEEVFGPVLHVVryKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQ 472
|
330
....*....|....*
gi 1032283529 477 PFGGVGESGIGAYHG 491
Cdd:TIGR01238 473 PFGGQGLSGTGPKAG 487
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
175-451 |
9.00e-17 |
|
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: 83.02 E-value: 9.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 175 PLGVVLVISAWNFPFllsvePVIG---AIAA--GNAVVLKPSEIAP----AASSLLAKLFSEY-LDNTTIRVIEGGVPET 244
Cdd:cd07130 132 PLGVVGVITAFNFPV-----AVWGwnaAIALvcGNVVVWKPSPTTPltaiAVTKIVARVLEKNgLPGAIASLVCGGADVG 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 245 TALL-DQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIagkWAC--NSGQACIGVDY 321
Cdd:cd07130 207 EALVkDPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVL---FAAvgTAGQRCTTTRR 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 322 VITTKDFASKLIDALKTELETFFGQNALESKDL------SRIVNSFHfKRLESMLKENGvanKIVHGG-RITEDKLKISP 394
Cdd:cd07130 284 LIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLvgplhtKAAVDNYL-AAIEEAKSQGG---TVLFGGkVIDGPGNYVEP 359
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1032283529 395 TIlLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNN-KELEK 451
Cdd:cd07130 360 TI-VEGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDlRNAFR 416
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
156-491 |
5.00e-16 |
|
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: 80.36 E-value: 5.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 156 ETVKTSVTTFPSSAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSE--YLDNTT 233
Cdd:cd07084 81 EPGNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYagLLPPED 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 234 IRVIEGGVPETTALLDQ-KWDKIFFTGGARVARIIMAAAARnlTPVVLELGGKCPALVDSDVNlQVA--ARRIIAGKWAC 310
Cdd:cd07084 161 VTLINGDGKTMQALLLHpNPKMVLFTGSSRVAEKLALDAKQ--ARIYLELAGFNWKVLGPDAQ-AVDyvAWQCVQDMTAC 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 311 nSGQAC--IGVDYVITTkDFASKLIDALKTELEtffgQNALESKDLSRIVNSFHFKRLESMLKENGV----ANKIVHGGR 384
Cdd:cd07084 238 -SGQKCtaQSMLFVPEN-WSKTPLVEKLKALLA----RRKLEDLLLGPVQTFTTLAMIAHMENLLGSvllfSGKELKNHS 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 385 ITEDKLKISPTILLDVPEAS----SMMQEEIFGPLLPIITVQK--IEDGFQVIRSKPKPLAAYLFTNNKElekqFVQDVs 458
Cdd:cd07084 312 IPSIYGACVASALFVPIDEIlktyELVTEEIFGPFAIVVEYKKdqLALVLELLERMHGSLTAAIYSNDPI----FLQEL- 386
|
330 340 350
....*....|....*....|....*....|....*
gi 1032283529 459 AGGITINDTVLhvtvkdlpFGGVGESGI--GAYHG 491
Cdd:cd07084 387 IGNLWVAGRTY--------AILRGRTGVapNQNHG 413
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
172-448 |
5.18e-15 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 77.57 E-value: 5.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 172 VSEPLGVVLVISAWNFPFllsvePVIG-----AIAAGNAVVLKPSEIAPAASSLLAKLFSEYLDNTTI-----RVIEGGV 241
Cdd:PLN02315 151 VWNPLGIVGVITAFNFPC-----AVLGwnaciALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLpgaifTSFCGGA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 242 PETTAL-LDQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQACIGVD 320
Cdd:PLN02315 226 EIGEAIaKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVG-TAGQRCTTCR 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 321 YVITTKDFASKLIDALKTELETFFGQNALESKDLSRIVNSFHFKR--LESMLKENGVANKIVHGGRITEDKLK-ISPTIL 397
Cdd:PLN02315 305 RLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKnfEKGIEIIKSQGGKILTGGSAIESEGNfVQPTIV 384
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1032283529 398 LDVPEASsMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKE 448
Cdd:PLN02315 385 EISPDAD-VVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPE 434
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
171-486 |
4.71e-11 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 64.55 E-value: 4.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 171 IVSEPLGVVLVISAWNFPfLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEYLDNTTIRVIEGGVPETTALLDQ 250
Cdd:cd07077 96 VRAFPIGVTMHILPSTNP-LSGITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAADAAHGPKILVLYVPHPSDELAE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 251 ------KWDKIFFTGGARVarIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKwaCNSGQACIGVDYVIT 324
Cdd:cd07077 175 ellshpKIDLIVATGGRDA--VDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSK--FFDQNACASEQNLYV 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 325 TKDFASKLIDALKTELetffgqnaleskdlsrivnsfhfkrlesmlkenGVANKIVHggriTEDKLKISPTILLDVPEAS 404
Cdd:cd07077 251 VDDVLDPLYEEFKLKL---------------------------------VVEGLKVP----QETKPLSKETTPSFDDEAL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 405 SMMqeeifGPLLPIITVQKIEDGFQ----VIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVlhVTVKDLPFGG 480
Cdd:cd07077 294 ESM-----TPLECQFRVLDVISAVEnawmIIESGGGPHTRCVYTHKINKVDDFVQYIDTASFYPNESS--KKGRGAFAGK 366
|
....*.
gi 1032283529 481 VGESGI 486
Cdd:cd07077 367 GVERIV 372
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
173-487 |
9.90e-10 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 61.42 E-value: 9.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 173 SEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSE----IAPAASSLLAklfseyldnttirviEGGVPETT--- 245
Cdd:PRK11905 674 HKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEqtplIAARAVRLLH---------------EAGVPKDAlql 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 246 ----------ALL-DQKWDKIFFTGGARVARIIMAAAARNL---TPVVLELGGKCPALVDSDVNLQVAARRIIAGkwACN 311
Cdd:PRK11905 739 lpgdgrtvgaALVaDPRIAGVMFTGSTEVARLIQRTLAKRSgppVPLIAETGGQNAMIVDSSALPEQVVADVIAS--AFD 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 312 S-GQAC--IGVDYVitTKDFASKLIDALK---TELETffGQNALESKDLSRIVNSFHFKRLESMLKENGVANKIVHGGRI 385
Cdd:PRK11905 817 SaGQRCsaLRVLCL--QEDVADRVLTMLKgamDELRI--GDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHQLPL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 386 TEDKLK---ISPTILldvpEASSM--MQEEIFGPLLPIITvqkiedgFqvirskpkplaaylftNNKELEkQFVQDVSA- 459
Cdd:PRK11905 893 PAETEKgtfVAPTLI----EIDSIsdLEREVFGPVLHVVR-------F----------------KADELD-RVIDDINAt 944
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1032283529 460 G-GIT------INDTVLHVT------------------VKDLPFGGVGESGIG 487
Cdd:PRK11905 945 GyGLTfglhsrIDETIAHVTsriragniyvnrniigavVGVQPFGGEGLSGTG 997
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
175-292 |
2.47e-08 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 56.91 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 175 PLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSE----IAPAASSLLaklfseyldnttirvIEGGVP-------- 242
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEqtplIAAQAVRIL---------------LEAGVPagvvqllp 832
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032283529 243 ---ETT-ALL--DQKWDKIFFTGGARVARIIMAAAARNL------TPVVLELGGKCPALVDS 292
Cdd:PRK11809 833 grgETVgAALvaDARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDS 894
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
175-485 |
6.34e-08 |
|
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: 55.29 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 175 PL-GVVLVISAWNFPfllsvepvigAIAA---------GNAVVLKPSEIAPAASSLLAKLFSEY-LDNTTIRVIEGGVPE 243
Cdd:cd07123 169 PLeGFVYAVSPFNFT----------AIGGnlagapalmGNVVLWKPSDTAVLSNYLVYKILEEAgLPPGVINFVPGDGPV 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 244 T--TALLDQKWDKIFFTGGARVARIIMAAAARNLT-----P-VVLELGGKCPALVDSDVNLQVAARRIIAGKWAcNSGQA 315
Cdd:cd07123 239 VgdTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDryrtyPrIVGETGGKNFHLVHPSADVDSLVTATVRGAFE-YQGQK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 316 CIGVD--YVITT--KDFASKLIDALKT-------ELETFFG----QNAleskdlsrivnsfhFKRLESMLKE--NGVANK 378
Cdd:cd07123 318 CSAASraYVPESlwPEVKERLLEELKEikmgdpdDFSNFMGavidEKA--------------FDRIKGYIDHakSDPEAE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 379 IVHGGriTEDKLK---ISPTILLDVPEASSMMQEEIFGPLLpiiTVQKIEDGF--QVIR----SKPKPLAAYLFTNNKEL 449
Cdd:cd07123 384 IIAGG--KCDDSVgyfVEPTVIETTDPKHKLMTEEIFGPVL---TVYVYPDSDfeETLElvdtTSPYALTGAIFAQDRKA 458
|
330 340 350
....*....|....*....|....*....|....*....
gi 1032283529 450 EKQfVQDV---SAGGITINDTVLHVTVKDLPFGGVGESG 485
Cdd:cd07123 459 IRE-ATDAlrnAAGNFYINDKPTGAVVGQQPFGGARASG 496
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
168-221 |
6.66e-08 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 55.71 E-value: 6.66e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032283529 168 SAQIVSEPLGVVLVISAWNFP---FllsVEPVIGAIAAGNAVVLKPSE----IAPAASSLL 221
Cdd:COG4230 673 AAPTVLRGRGVFVCISPWNFPlaiF---TGQVAAALAAGNTVLAKPAEqtplIAARAVRLL 730
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
175-433 |
1.02e-07 |
|
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: 54.47 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 175 PLGVVLVISAWNFPFLLSvepVIG-----AIAAGNAVVLKPSEIAPAASSLLAKLFSEYLDNT-----TIRVIEGGVPET 244
Cdd:cd07129 105 PLGPVAVFGASNFPLAFS---VAGgdtasALAAGCPVVVKAHPAHPGTSELVARAIRAALRATglpagVFSLLQGGGREV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 245 -TALLDQKWDK-IFFTGGARVARIIMAAAARNLT--PVVLELGGKCPALVdsdvnLQVA-ARRI--IAGKWAC----NSG 313
Cdd:cd07129 182 gVALVKHPAIKaVGFTGSRRGGRALFDAAAARPEpiPFYAELGSVNPVFI-----LPGAlAERGeaIAQGFVGsltlGAG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 314 QACI--GVDYVITTKDFAsKLIDALKTELETFFGQNALEskdlSRIVNSFHfKRLESMLKENGVanKIVHGGRITEDKLK 391
Cdd:cd07129 257 QFCTnpGLVLVPAGPAGD-AFIAALAEALAAAPAQTMLT----PGIAEAYR-QGVEALAAAPGV--RVLAGGAAAEGGNQ 328
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1032283529 392 ISPTILldVPEASSMM-----QEEIFGPLLPIITVQKIEDGFQVIRS 433
Cdd:cd07129 329 AAPTLF--KVDAAAFLadpalQEEVFGPASLVVRYDDAAELLAVAEA 373
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
174-221 |
1.65e-06 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 50.97 E-value: 1.65e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1032283529 174 EPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSE----IAPAASSLL 221
Cdd:PRK11904 683 HGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEqtplIAAEAVKLL 734
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
171-426 |
5.29e-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: 45.72 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 171 IVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEyldnttiRVIEGGVP-------- 242
Cdd:cd07081 91 IIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQ-------AAVAAGAPenligwid 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 243 ----ETTALLDQK--WDKIFFTGGARVARIIMAAAarnlTPVVLELGGKCPALVDSDVNLQVAARRIIAGKwACNSGQAC 316
Cdd:cd07081 164 npsiELAQRLMKFpgIGLLLATGGPAVVKAAYSSG----KPAIGVGAGNTPVVIDETADIKRAVQSIVKSK-TFDNGVIC 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 317 IGVDYVITTKDFASKLIDALKTEletffGQNALESKDLsrivnsfhfKRLESMLKENGVANKIVHGgritEDKLKISPTI 396
Cdd:cd07081 239 ASEQSVIVVDSVYDEVMRLFEGQ-----GAYKLTAEEL---------QQVQPVILKNGDVNRDIVG----QDAYKIAAAA 300
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1032283529 397 LLDVP--------EASSMMQEEIFG-----PLLPIITVQKIED 426
Cdd:cd07081 301 GLKVPqetriligEVTSLAEHEPFAheklsPVLAMYRAANFAD 343
|
|
| P5CS |
TIGR01092 |
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ... |
172-345 |
2.01e-04 |
|
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, EC 2.7.2.11) region followed by a gamma-glutamyl phosphate reductase (ProA, EC 1.2.1.41) region. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 130164 [Multi-domain] Cd Length: 715 Bit Score: 44.13 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 172 VSEPLGVVLVISAWNFPFLLSVEPVigAIAAGNAVVLKPSEIAPAASSLLAKLFSEYLDNTTIRVIEGGVPETTAL---- 247
Cdd:TIGR01092 394 TSVPIGVLLIVFESRPDALVQIASL--AIRSGNGLLLKGGKEAARSNAILHKVITEAIPIHVGKKLIGLVTSREEIpdll 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 248 -LDQKWDKIFFTGGARVARIIMAAAArnlTPVVLELGGKCPALVDSDVNLQVAARRIIAGKwaCNSGQACIGVDYVITTK 326
Cdd:TIGR01092 472 kLDDVIDLVIPRGSNKLVSQIKKSTK---IPVLGHADGICHVYVDKSASVDMAKRIVRDAK--CDYPAACNAMETLLVHK 546
|
170 180
....*....|....*....|....
gi 1032283529 327 DFA-----SKLIDALKTELETFFG 345
Cdd:TIGR01092 547 DLLrngllDDLIDMLRTEGVTIHG 570
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
177-466 |
2.80e-04 |
|
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: 43.41 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 177 GVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPseiAPAASSL---LAKLFSE--YLDNTTIRVIEGGvpeTTALLDQ- 250
Cdd:cd07128 146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKP---ATATAYLteaVVKDIVEsgLLPEGALQLICGS---VGDLLDHl 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 251 -KWDKIFFTGGARVARIIMAAaarnltPVVLELGGKCPALVDSdVNLQVAA-----------------RRIIAGKwacnS 312
Cdd:cd07128 220 gEQDVVAFTGSAATAAKLRAH------PNIVARSIRFNAEADS-LNAAILGpdatpgtpefdlfvkevAREMTVK----A 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 313 GQACIGVDYVITTKDFASKLIDALKTELE-TFFGQNALESKDLSRIVNSFHFKRLESMLKENGVANKIVHGGRITEDKLK 391
Cdd:cd07128 289 GQKCTAIRRAFVPEARVDAVIEALKARLAkVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFEVVG 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 392 I--------SPTILL--DVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSA-- 459
Cdd:cd07128 369 AdaekgaffPPTLLLcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAAPyh 448
|
....*..
gi 1032283529 460 GGITIND 466
Cdd:cd07128 449 GRLLVLN 455
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
175-467 |
5.29e-04 |
|
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: 42.85 E-value: 5.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 175 PLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEYL-------DNTTIRVIEGGVPETTAL 247
Cdd:cd07127 193 PRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAAILPLAITVQVAREVLaeagfdpNLVTLAADTPEEPIAQTL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 248 LDQKWDKIF-FTGGARVARIIMAAAARNLtpVVLELGGKCPALVDSDVNLQVAARRiIAGKWACNSGQACIG--VDYV-- 322
Cdd:cd07127 273 ATRPEVRIIdFTGSNAFGDWLEANARQAQ--VYTEKAGVNTVVVDSTDDLKAMLRN-LAFSLSLYSGQMCTTpqNIYVpr 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 323 --ITTKD---FASKLIDALKTELETFFGQNALESKDLSRIVNSFHFKRLE--SMLKENGVANKIVHGGRItEDKLKISPT 395
Cdd:cd07127 350 dgIQTDDgrkSFDEVAADLAAAIDGLLADPARAAALLGAIQSPDTLARIAeaRQLGEVLLASEAVAHPEF-PDARVRTPL 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 396 ILLDVPEASSMMQEEIFGPLLPIITV----QKIEDGFQVIRSKpKPLAAYLFTNNKELEKQfVQDVSA-----------G 460
Cdd:cd07127 429 LLKLDASDEAAYAEERFGPIAFVVATdstdHSIELARESVREH-GAMTVGVYSTDPEVVER-VQEAALdagvalsinltG 506
|
....*..
gi 1032283529 461 GITINDT 467
Cdd:cd07127 507 GVFVNQS 513
|
|
| LuxC |
pfam05893 |
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ... |
175-433 |
3.35e-03 |
|
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) proteins. The channelling of fatty acids into the fatty aldehyde substrate for the bacterial bioluminescence reaction is catalyzed by a fatty acid reductase multienzyme complex, which channels fatty acids through the thioesterase (LuxD), synthetase (LuxE) and reductase (LuxC) components.
Pssm-ID: 399113 Cd Length: 401 Bit Score: 40.12 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 175 PLGVVLVISAWNFPfLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEyLDNT-----TIRVIEGGVPETT--AL 247
Cdd:pfam05893 88 PPGLVFHVLSGNVP-LLPVMSILMGLLVKNVNLLKVSSSDPFTAAALLASFAD-LDPThpladSLSVVYWDGGSTQleDL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 248 LDQKWDKIFFTGGarvariimaaaARNLTPVVLELGGKCP----------ALVDSDVNLQVAARRiIAGKWACNSGQACI 317
Cdd:pfam05893 166 IVANADVVIAWGG-----------EDAINAIRECLKPGKQwidfgakisfAVVDREAALDKAAER-AADDICVFDQQACL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032283529 318 G-------VDYVITTKDFASKLIDALKTELETF------FGQNALESKDLSRIvnsfhfKRLESMLKENGVANKIVHGGR 384
Cdd:pfam05893 234 SpqtvfveSDDKITPDEFAERLAAALAKRARILpkavldIDEAAKISSDRAEC------KLDYAFAGERGVWSDFHQRWT 307
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1032283529 385 ITEdklkisptilldvpeasSMMQEEIFGPLLPIITVQKIEDGFQVIRS 433
Cdd:pfam05893 308 VIW-----------------SDGQEELNSPLNRTVNVVPVPSLSDVVRY 339
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