|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
3-482 |
0e+00 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 835.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 3 KVFQAADATDLVTELRRSFDDGVTRGYEWRVTQLKKLLLICDNHEPEIVSALHDDLGKPELESSVYEVALLRNSINLAVK 82
Cdd:PLN02174 5 KMFGAADASILVTELRRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 83 QLKDWMAPDKAKTSLTTFPASAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQ 162
Cdd:PLN02174 85 QLKNWMAPEKAKTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 163 YLDSSAVRVVEGAVTETTLLLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGK 242
Cdd:PLN02174 165 YLDSSAVRVVEGAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 243 WGCNNGQACISPDYILTTKEFSPKVIDALKQELEAFYGKNPMESKDMSRIVNSNHFDRLSKMLEEKEVSDKIVYGGQKNR 322
Cdd:PLN02174 245 WGCNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEKDR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 323 DKLKIAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDI 402
Cdd:PLN02174 325 ENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDI 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 403 AVHLAVPTLPFGGVGESGMGSYHGKFSFDAFSHKKAVLYKSFIGDAAIRYPPYSTGKLRLLKALVNSNILEIFRVILGLS 482
Cdd:PLN02174 405 AVHLALHTLPFGGVGESGMGAYHGKFSFDAFSHKKAVLYRSLFGDSAVRYPPYSRGKLRLLKALVDSNIFDIFKVLLGLS 484
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
10-441 |
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: 781.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 10 ATDLVTELRRSFDDGVTRGYEWRVTQLKKLLLICDNHEPEIVSALHDDLGKPELESSVYEVALLRNSINLAVKQLKDWMA 89
Cdd:cd07137 1 APRLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 90 PDKAKTSLTTFPASAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQYLDSSAV 169
Cdd:cd07137 81 PEKVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 170 RVVEGAVTETTLLLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGCNNGQ 249
Cdd:cd07137 161 KVIEGGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCNNGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 250 ACISPDYILTTKEFSPKVIDALKQELEAFYGKNPMESKDMSRIVNSNHFDRLSKMLEEKEVSDKIVYGGQKNRDKLKIAP 329
Cdd:cd07137 241 ACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGGERDEKNLYIEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 330 TILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDIAVHLAVP 409
Cdd:cd07137 321 TILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAID 400
|
410 420 430
....*....|....*....|....*....|..
gi 1824090424 410 TLPFGGVGESGMGSYHGKFSFDAFSHKKAVLY 441
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 ... |
12-441 |
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: 674.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 12 DLVTELRRSFDDGVTRGYEWRVTQLKKLLLICDNHEPEIVSALHDDLGKPELESSVYEVALLRNSINLAVKQLKDWMAPD 91
Cdd:cd07087 2 ELVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 92 KAKTSLTTFPASAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQYLDSSAVRV 171
Cdd:cd07087 82 RVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 172 VEGAVTETTLLLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGcNNGQAC 251
Cdd:cd07087 162 VEGGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFL-NAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 252 ISPDYILTTKEFSPKVIDALKQELEAFYGKNPMESKDMSRIVNSNHFDRLSKMLEekevSDKIVYGGQKNRDKLKIAPTI 331
Cdd:cd07087 241 IAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLD----DGKVVIGGQVDKEERYIAPTI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 332 LVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDIAVHLAVPTL 411
Cdd:cd07087 317 LDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNL 396
|
410 420 430
....*....|....*....|....*....|
gi 1824090424 412 PFGGVGESGMGSYHGKFSFDAFSHKKAVLY 441
Cdd:cd07087 397 PFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
12-464 |
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: 644.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 12 DLVTELRRSFDDGVTRGYEWRVTQLKKLLLICDNHEPEIVSALHDDLGKPELESSVYEVALLRNSINLAVKQLKDWMAPD 91
Cdd:cd07136 2 SLVEKQRAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKPK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 92 KAKTSLTTFPASAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQYLDSSAVRV 171
Cdd:cd07136 82 RVKTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 172 VEGAVTETTLLLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWgCNNGQAC 251
Cdd:cd07136 162 VEGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKF-LNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 252 ISPDYILTTKEFSPKVIDALKQELEAFYGKNPMESKDMSRIVNSNHFDRLSKMLEEkevsDKIVYGGQKNRDKLKIAPTI 331
Cdd:cd07136 241 VAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDN----GKIVFGGNTDRETLYIEPTI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 332 LVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDIAVHLAVPTL 411
Cdd:cd07136 317 LDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYL 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1824090424 412 PFGGVGESGMGSYHGKFSFDAFSHKKAVLYKSFIGDAAIRYPPYSTGKLRLLK 464
Cdd:cd07136 397 PFGGVGNSGMGSYHGKYSFDTFSHKKSILKKSTWFDLPLRYPPYKGKKKKLKK 449
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
12-456 |
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: 609.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 12 DLVTELRRSFDDGVTRGYEWRVTQLKKLLLICDNHEPEIVSALHDDLGKPELESSVYEVALLRNSINLAVKQLKDWMAPD 91
Cdd:cd07132 2 EAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 92 KAKTSLTTFPASAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQYLDSSAVRV 171
Cdd:cd07132 82 PVKKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 172 VEGAVTETTLLLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWgCNNGQAC 251
Cdd:cd07132 162 VLGGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKF-INAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 252 ISPDYILTTKEFSPKVIDALKQELEAFYGKNPMESKDMSRIVNSNHFDRLSKMLEekevSDKIVYGGQKNRDKLKIAPTI 331
Cdd:cd07132 241 IAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLS----GGKVAIGGQTDEKERYIAPTV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 332 LVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDIAVHLAVPTL 411
Cdd:cd07132 317 LTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSL 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1824090424 412 PFGGVGESGMGSYHGKFSFDAFSHKKAVLYKSFIGD--AAIRYPPYS 456
Cdd:cd07132 397 PFGGVGNSGMGAYHGKYSFDTFSHKRSCLVKSLNMEklNSLRYPPYS 443
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
12-481 |
0e+00 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 603.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 12 DLVTELRRSFDDGVTRGYEWRVTQLKKLLLICDNHEPEIVSALHDDLGKPELESSVYEVALLRNSINLAVKQLKDWMAPD 91
Cdd:PLN02203 10 GSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSNLKKWMAPK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 92 KAKTSLTTFPASAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQYLDSSAVRV 171
Cdd:PLN02203 90 KAKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAVKV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 172 VEGAVTETTLLLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVID---SDTNLKITAKRIIAGKWGCNNG 248
Cdd:PLN02203 170 IEGGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGSCAG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 249 QACISPDYILTTKEFSPKVIDALKQELEAFYGKNPMESKDMSRIVNSNHFDRLSKMLEEKEVSDKIVYGGQKNRDKLKIA 328
Cdd:PLN02203 250 QACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAASIVHGGSIDEKKLFIE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 329 PTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDIAVHLAV 408
Cdd:PLN02203 330 PTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYAC 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1824090424 409 PTLPFGGVGESGMGSYHGKFSFDAFSHKKAVLYKSFIGDAAIRYPPYSTGKLRLLKALVNSNILEIFRVILGL 481
Cdd:PLN02203 410 DSLPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSLLTEFEFRYPPWNDFKLGFLRLVYRFDYFGLLLLLLGL 482
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
12-481 |
0e+00 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 592.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 12 DLVTELRRSFDDGVTRGYEWRVTQLKKLLLICDNHEPEIVSALHDDLGKPELESSVYEVALLRNSINLAVKQLKDWMAPD 91
Cdd:PTZ00381 11 PIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEYLKPE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 92 KAKTSLTTFPASAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQYLDSSAVRV 171
Cdd:PTZ00381 91 KVDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPSYVRV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 172 VEGAVTETTLLLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGcNNGQAC 251
Cdd:PTZ00381 171 IEGGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFL-NAGQTC 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 252 ISPDYILTTKEFSPKVIDALKQELEAFYGKNPMESKDMSRIVNSNHFDRLSKMLEEKEvsDKIVYGGQKNRDKLKIAPTI 331
Cdd:PTZ00381 250 VAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKDHG--GKVVYGGEVDIENKYVAPTI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 332 LVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDIAVHLAVPTL 411
Cdd:PTZ00381 328 IVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNL 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1824090424 412 PFGGVGESGMGSYHGKFSFDAFSHKKAVLYKSF--IGDAAIRYPPYSTGKLRLLKALVNSNILEIFRVILGL 481
Cdd:PTZ00381 408 PFGGVGNSGMGAYHGKYGFDTFSHPKPVLNKSTgnSFDLSLRYPPYTSFKSWVLSFLLKLSIPVQSEVLKSR 479
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
13-440 |
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: 566.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 13 LVTELRRSFDDGVTRGYEWRVTQLKKLLLICDNHEPEIVSALHDDLGKPELESSVYEVALLRNSINLAVKQLKDWMAPDK 92
Cdd:cd07135 10 IHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKKWAKDEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 93 AKTSLTTF-PASAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQYLDSSAVRV 171
Cdd:cd07135 90 VKDGPLAFmFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLDPDAFQV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 172 VEGAVTETTLLLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGcNNGQAC 251
Cdd:cd07135 170 VQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFG-NAGQIC 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 252 ISPDYILTTKEFSPKVIDALKQELEAFYGKNPMESKDMSRIVNSNHFDRLSKMLEekEVSDKIVYGGQKNRDKLKIAPTI 331
Cdd:cd07135 249 VAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLD--TTKGKVVIGGEMDEATRFIPPTI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 332 LVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDIAVHLAVPTL 411
Cdd:cd07135 327 VSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNA 406
|
410 420
....*....|....*....|....*....
gi 1824090424 412 PFGGVGESGMGSYHGKFSFDAFSHKKAVL 440
Cdd:cd07135 407 PFGGVGDSGYGAYHGKYGFDTFTHERTVV 435
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
3-440 |
1.14e-178 |
|
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: 507.53 E-value: 1.14e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 3 KVFQAADATDLvtELRRSfddgvtrGYEWRVTQLKKLLLICDNHEPEIVSALHDDLGKPELESSVYEVALLRNSINLAVK 82
Cdd:cd07134 2 RVFAAQQAHAL--ALRAS-------TAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 83 QLKDWMAPDKAKTSLTTFPASAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQ 162
Cdd:cd07134 73 HLKKWMKPKRVRTPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIRE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 163 YLDSSAVRVVEGAVTETTLLLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGK 242
Cdd:cd07134 153 AFDEDEVAVFEGDAEVAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 243 WgCNNGQACISPDYILTTKEFSPKVIDALKQELEAFYGKNPM--ESKDMSRIVNSNHFDRLSKMLEE-KEVSDKIVYGGQ 319
Cdd:cd07134 233 F-LNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAArkASPDLARIVNDRHFDRLKGLLDDaVAKGAKVEFGGQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 320 KNRDKLKIAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVV 399
Cdd:cd07134 312 FDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVV 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1824090424 400 NDIAVHLAVPTLPFGGVGESGMGSYHGKFSFDAFSHKKAVL 440
Cdd:cd07134 392 NDVVLHFLNPNLPFGGVNNSGIGSYHGVYGFKAFSHERAVL 432
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
11-441 |
1.45e-167 |
|
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: 479.29 E-value: 1.45e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 11 TDLVTELRRSFDDGVTRGYEWRVTQLKKLLLICDNHEPEIVSALHDDLG-KPELESSVYEVALLRNSINLAVKQLKDWMA 89
Cdd:cd07133 1 QALLERQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFGhRSRHETLLAEILPSIAGIKHARKHLKKWMK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 90 PDKAKTSLTTFPASAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQYLDSSAV 169
Cdd:cd07133 81 PSRRHVGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 170 RVVEGAVTETTLLLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGcNNGQ 249
Cdd:cd07133 161 AVVTGGADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLL-NAGQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 250 ACISPDYILTTKEFSPKVIDALKQELEAFYGkNPMESKDMSRIVNSNHFDRLSKMLEE-KEVSDKIVYGGQKNRDKL--- 325
Cdd:cd07133 240 TCVAPDYVLVPEDKLEEFVAAAKAAVAKMYP-TLADNPDYTSIINERHYARLQGLLEDaRAKGARVIELNPAGEDFAatr 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 326 KIAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDIAVH 405
Cdd:cd07133 319 KLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLH 398
|
410 420 430
....*....|....*....|....*....|....*.
gi 1824090424 406 LAVPTLPFGGVGESGMGSYHGKFSFDAFSHKKAVLY 441
Cdd:cd07133 399 VAQDDLPFGGVGASGMGAYHGKEGFLTFSHAKPVFK 434
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
14-440 |
1.42e-123 |
|
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: 367.30 E-value: 1.42e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 14 VTELRRSFDDGVTRGYEWRVTQLKKLLLICDNHEPEIVSALHDDLGKPeLESSVYEVALLRNSINLAVKQLKDWMAPdka 93
Cdd:cd07078 4 VAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKP-IEEALGEVARAADTFRYYAGLARRLHGE--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 94 kTSLTTFP-ASAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQY-LDSSAVRV 171
Cdd:cd07078 80 -VIPSPDPgELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLPPGVLNV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 172 VEG--AVTETTLLLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGcNNGQ 249
Cdd:cd07078 159 VTGdgDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFG-NAGQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 250 ACISPDYILTTKEFSPKVIDALKQELEAFYGKNPMESK-DMSRIVNSNHFDRLSKMLEE-KEVSDKIVYGGQ--KNRDKL 325
Cdd:cd07078 238 VCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDtDMGPLISAAQLDRVLAYIEDaKAEGAKLLCGGKrlEGGKGY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 326 KIAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDIAVH 405
Cdd:cd07078 318 FVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVG 397
|
410 420 430
....*....|....*....|....*....|....*
gi 1824090424 406 lAVPTLPFGGVGESGMGSYHGKFSFDAFSHKKAVL 440
Cdd:cd07078 398 -AEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVT 431
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
18-440 |
1.29e-98 |
|
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: 301.07 E-value: 1.29e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 18 RRSFDDGVTRGYEWRVTQLKKLLLICDNHEPEIVSALHDDLGKPeLESSVYEVALLRNSINLAVKQLKDWMAPDKAKTSL 97
Cdd:cd06534 4 RAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKP-IEEALGEVARAIDTFRYAAGLADKLGGPELPSPDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 98 TTFpasAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQY-LDSSAVRVVEG-A 175
Cdd:cd06534 83 GGE---AYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVVNVVPGgG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 176 VTETTLLLEQKW-DKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGcNNGQACISP 254
Cdd:cd06534 160 DEVGAALLSHPRvDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFF-NAGQICTAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 255 DYILTTKEFSPKVIDALKqeleafygknpmeskdmsrivnsnhfdrlskmleekevsdkivyggqknrdklkiapTILVD 334
Cdd:cd06534 239 SRLLVHESIYDEFVEKLV---------------------------------------------------------TVLVD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 335 VPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDIAVHlAVPTLPFG 414
Cdd:cd06534 262 VDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIG-VGPEAPFG 340
|
410 420
....*....|....*....|....*.
gi 1824090424 415 GVGESGMGSYHGKFSFDAFSHKKAVL 440
Cdd:cd06534 341 GVKNSGIGREGGPYGLEEYTRTKTVV 366
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
7-439 |
1.03e-94 |
|
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: 294.73 E-value: 1.03e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 7 AADATDLVTELRRSFDDGVTRGYEWRVTQLKKLLLICDNHEPEIVSALHDDLGKPELESSVyEVAL----LRNSINLAVK 82
Cdd:COG1012 42 AEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARG-EVDRaadfLRYYAGEARR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 83 QLKDWMAPDKAKTSlttfpasAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQ 162
Cdd:COG1012 121 LYGETIPSDAPGTR-------AYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 163 Y-LDSSAVRVV--EGAVTETTLLLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRII 239
Cdd:COG1012 194 AgLPAGVLNVVtgDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 240 AGKWGcNNGQACISPDYILTTKEFSPKVIDALKQELEAF-YGkNPM-ESKDMSRIVNSNHFDRLSKMLEE-KEVSDKIVY 316
Cdd:COG1012 274 RGAFG-NAGQRCTAASRLLVHESIYDEFVERLVAAAKALkVG-DPLdPGTDMGPLISEAQLERVLAYIEDaVAEGAELLT 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 317 GGqKNRDKLK---IAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVS 393
Cdd:COG1012 352 GG-RRPDGEGgyfVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLE 430
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1824090424 394 AGGIVVNDIAVHlAVPTLPFGGVGESGMGSYHGKFSFDAFSHKKAV 439
Cdd:COG1012 431 AGMVWINDGTTG-AVPQAPFGGVKQSGIGREGGREGLEEYTETKTV 475
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
7-440 |
9.67e-91 |
|
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: 283.73 E-value: 9.67e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 7 AADATDLVTELRRSFDDGVTRGYEWRVTQLKKLL-LICDNHEpEIVSALHDDLGKPELESsVYEVALLRNSINLAVKQLK 85
Cdd:cd07099 17 PAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKrALADHAD-ELAELLHAETGKPRADA-GLEVLLALEAIDWAARNAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 86 DWMAPDKAKTSLTTFPASAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQYLD 165
Cdd:cd07099 95 RVLAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAGP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 166 SSAV-RVVEGAVTETTLLLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIagkWG 244
Cdd:cd07099 175 PQGVlQVVTGDGATGAALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAV---WG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 245 --CNNGQACISPDYILTTKEFSPKVIDALKQELEAF-----------YGknPMESKDMSRIVNSNHFDRLSKmleekevS 311
Cdd:cd07099 252 amVNAGQTCISVERVYVHESVYDEFVARLVAKARALrpgaddigdadIG--PMTTARQLDIVRRHVDDAVAK-------G 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 312 DKIVYGGQK-NRDKLKIAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFAL 390
Cdd:cd07099 323 AKALTGGARsNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIAR 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1824090424 391 TVSAGGIVVNDIAVHLAVPTLPFGGVGESGMGSYHGKFSFDAFSHKKAVL 440
Cdd:cd07099 403 RLEAGAVSINDVLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIA 452
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
36-439 |
8.71e-90 |
|
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: 281.34 E-value: 8.71e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 36 LKKLLLICDNHEPEIVSALHDDLGKPELESsVYEVALLRNSINLAVKQLKDwMAPDKAKTSLTTFpasAEIVYEPLGVVL 115
Cdd:pfam00171 57 LRKAADLLEERKDELAELETLENGKPLAEA-RGEVDRAIDVLRYYAGLARR-LDGETLPSDPGRL---AYTRREPLGVVG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 116 VISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQY-LDSSAVRVV--EGAVTETTLLLEQKWDKIFY 192
Cdd:pfam00171 132 AITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAgLPAGVLNVVtgSGAEVGEALVEHPDVRKVSF 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 193 TGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGcNNGQACISPDYILTTKEFSPKVIDALK 272
Cdd:pfam00171 212 TGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFG-NAGQVCTATSRLLVHESIYDEFVEKLV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 273 QELEAFYGKNPMESK-DMSRIVNSNHFDRLSKMLEE-KEVSDKIVYGGQKNRDK-LKIAPTILVDVPLDSQIMSEEIFGP 349
Cdd:pfam00171 291 EAAKKLKVGDPLDPDtDMGPLISKAQLERVLKYVEDaKEEGAKLLTGGEAGLDNgYFVEPTVLANVTPDMRIAQEEIFGP 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 350 LLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDIAVHlAVPTLPFGGVGESGMGSYHGKFS 429
Cdd:pfam00171 371 VLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTG-DADGLPFGGFKQSGFGREGGPYG 449
|
410
....*....|
gi 1824090424 430 FDAFSHKKAV 439
Cdd:pfam00171 450 LEEYTEVKTV 459
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
30-441 |
1.73e-67 |
|
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: 223.72 E-value: 1.73e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 30 EWRVTQ-------LKKLLLICDNHEPEIVSALHDDLGKPELESSVYEVALLRNSINLAVKQLKDWMAPDKAKTSLTTFPA 102
Cdd:cd07098 33 EWAKTSfaerrkvLRSLLKYILENQEEICRVACRDTGKTMVDASLGEILVTCEKIRWTLKHGEKALRPESRPGGLLMFYK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 103 SAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQYL-----DSSAVRVVEG-AV 176
Cdd:cd07098 113 RARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIRECLaacghDPDLVQLVTClPE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 177 TETTLLLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGcNNGQACISPDY 256
Cdd:cd07098 193 TAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQ-SSGQNCIGIER 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 257 ILTTKEFSPKVIDALKQELEAFYGKNPMESK-DMSRIVNSNHFDRLSKMLEEKEVSD-KIVYGGQKNRDKLK-----IAP 329
Cdd:cd07098 272 VIVHEKIYDKLLEILTDRVQALRQGPPLDGDvDVGAMISPARFDRLEELVADAVEKGaRLLAGGKRYPHPEYpqghyFPP 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 330 TILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDIAVHLAVP 409
Cdd:cd07098 352 TLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQ 431
|
410 420 430
....*....|....*....|....*....|..
gi 1824090424 410 TLPFGGVGESGMGSYHGKFSFDAFSHKKAVLY 441
Cdd:cd07098 432 QLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTE 463
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
32-439 |
7.87e-64 |
|
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: 212.82 E-value: 7.87e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 32 RVTQLKKLLLICDNHEPEIVSALHDDLGKPELESSVyevallrnSINLAVKQLKDWMApdkAKTSLT--TFPASAE---- 105
Cdd:cd07105 24 RRDILLKAADLLESRRDEFIEAMMEETGATAAWAGF--------NVDLAAGMLREAAS---LITQIIggSIPSDKPgtla 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 106 -IVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQY-LDSSAVRVV----EGAVTET 179
Cdd:cd07105 93 mVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAgLPKGVLNVVthspEDAPEVV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 180 TLLLEQKW-DKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWgCNNGQACISPDYIL 258
Cdd:cd07105 173 EALIAHPAvRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAF-LNSGQICMSTERII 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 259 TTKEFSPKVIDALKQELEAFYGKnpmeSKDMSRIVNSNHFDRLSKMleekeVSD------KIVYGG--QKNRDKLKIAPT 330
Cdd:cd07105 252 VHESIADEFVEKLKAAAEKLFAG----PVVLGSLVSAAAADRVKEL-----VDDalskgaKLVVGGlaDESPSGTSMPPT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 331 ILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDIAVHLAvPT 410
Cdd:cd07105 323 ILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVHDE-PT 401
|
410 420
....*....|....*....|....*....
gi 1824090424 411 LPFGGVGESGMGSYHGKFSFDAFSHKKAV 439
Cdd:cd07105 402 LPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
46-439 |
7.50e-63 |
|
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: 210.75 E-value: 7.50e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 46 HEPEIVSALHDDLGKPeLESSVYEVALLRNSInlavkqlkDWMAPDKAKTSLTTFPASA-----EIVYEPLGVVLVISAW 120
Cdd:cd07103 57 RAEDLARLLTLEQGKP-LAEARGEVDYAASFL--------EWFAEEARRIYGRTIPSPApgkriLVIKQPVGVVAAITPW 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 121 NYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQY-LDSSAVRVVEG---AVTETtlLLEqkwD----KIFY 192
Cdd:cd07103 128 NFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEAgLPAGVLNVVTGspaEIGEA--LCA---SprvrKISF 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 193 TGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGcNNGQACISPDYILTTKEFSPKVIDALK 272
Cdd:cd07103 203 TGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFR-NAGQTCVCANRIYVHESIYDEFVEKLV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 273 QELEAFYGKNPMESK-DMSRIVNSnhfDRLSKMleEKEVSD------KIVYGGQKNRDK-LKIAPTILVDVPLDSQIMSE 344
Cdd:cd07103 282 ERVKKLKVGNGLDEGtDMGPLINE---RAVEKV--EALVEDavakgaKVLTGGKRLGLGgYFYEPTVLTDVTDDMLIMNE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 345 EIFGPLLPVITLNNLEEcfdVIR---SRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDIAVhlAVPTLPFGGVGESGM 421
Cdd:cd07103 357 ETFGPVAPIIPFDTEDE---VIAranDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLI--SDAEAPFGGVKESGL 431
|
410
....*....|....*...
gi 1824090424 422 GSYHGKFSFDAFSHKKAV 439
Cdd:cd07103 432 GREGGKEGLEEYLETKYV 449
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
107-440 |
8.42e-62 |
|
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: 208.37 E-value: 8.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 107 VYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQYLDSSAVRVVEGAVTE--TTLLLE 184
Cdd:cd07108 114 VREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQVLPAGVLNVITGYGEEcgAALVDH 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 185 QKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGCNNGQACISPDYILTTKEFS 264
Cdd:cd07108 194 PDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGAIAGMRFTRQGQSCTAGSRLFVHEDIY 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 265 PKVIDALKQELEAFYGKNPM-ESKDMSRIVNSNHFDRLSKMLEE--KEVSDKIVYGGQ-----KNRDKLKIAPTILVDVP 336
Cdd:cd07108 274 DAFLEKLVAKLSKLKIGDPLdEATDIGAIISEKQFAKVCGYIDLglSTSGATVLRGGPlpgegPLADGFFVQPTIFSGVD 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 337 LDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNdiAVHLAVPTLPFGGV 416
Cdd:cd07108 354 NEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVN--QGGGQQPGQSYGGF 431
|
330 340
....*....|....*....|....*...
gi 1824090424 417 GESGMGSyhgKFSFDA----FSHKKAVL 440
Cdd:cd07108 432 KQSGLGR---EASLEGmlehFTQKKTVN 456
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
5-439 |
2.52e-61 |
|
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: 208.03 E-value: 2.52e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 5 FQAADATDL---VTELRRSFDD------GVTRGyewrvTQLKKLLLICDNHEpEIVSALHD-DLGKPELESSVYEVAllr 74
Cdd:cd07144 39 VYAAGEEDVdkaVKAARKAFESwwskvtGEERG-----ELLDKLADLVEKNR-DLLAAIEAlDSGKPYHSNALGDLD--- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 75 NSINLaVKQLKDWMAPDKAKTSLTTFPASAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSS 154
Cdd:cd07144 110 EIIAV-IRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 155 LLAKLL-EQYLDSSAVRVVEG--AVTETTLLLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNL 231
Cdd:cd07144 189 YFANLVkEAGFPPGVVNIIPGygAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 232 KITAKRIIAGKWgCNNGQACISPDYILTTKEFSPKVIDALKQELEAFYGKNPMESKD--MSRIVNSNHFDRLSKMLEE-K 308
Cdd:cd07144 269 DQAVKWAAAGIM-YNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYKVGSPFDDDtvVGPQVSKTQYDRVLSYIEKgK 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 309 EVSDKIVYGGQKNRDKLK----IAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKL 384
Cdd:cd07144 348 KEGAKLVYGGEKAPEGLGkgyfIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRR 427
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1824090424 385 KERFALTVSAGGIVVNdiAVHLAVPTLPFGGVGESGMGSYHGKFSFDAFSHKKAV 439
Cdd:cd07144 428 AHRVARELEAGMVWIN--SSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
109-439 |
2.37e-60 |
|
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: 203.92 E-value: 2.37e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 109 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLL-AKLLEQY-LDSSAVRVVEGAVTET--TLLLE 184
Cdd:cd07104 97 VPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLiAEIFEEAgLPKGVLNVVPGGGSEIgdALVEH 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 185 QKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWgCNNGQACISPDYILT----- 259
Cdd:cd07104 177 PRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAF-LHQGQICMAAGRILVhesvy 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 260 ---TKEFSPKViDALKqeleafYGkNPMESK-DMSRIVNSNHFDRLSKMLEEKeVSD--KIVYGGQknRDKLKIAPTILV 333
Cdd:cd07104 256 defVEKLVAKA-KALP------VG-DPRDPDtVIGPLINERQVDRVHAIVEDA-VAAgaRLLTGGT--YEGLFYQPTVLS 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 334 DVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDIAVHlAVPTLPF 413
Cdd:cd07104 325 DVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVN-DEPHVPF 403
|
330 340
....*....|....*....|....*.
gi 1824090424 414 GGVGESGMGSYHGKFSFDAFSHKKAV 439
Cdd:cd07104 404 GGVKASGGGRFGGPASLEEFTEWQWI 429
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
6-439 |
6.17e-60 |
|
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: 203.57 E-value: 6.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 6 QAADATDLVTELRRSFDDGVTRGYEWRVTQLKKLLLICDNHEPEIVSALHDDLGKPELESSVYEVAllRNSINLAvkqlk 85
Cdd:cd07093 17 GAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDIP--RAAANFR----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 86 dwMAPDKAKTSLT-TFPASAE----IVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLL 160
Cdd:cd07093 90 --FFADYILQLDGeSYPQDGGalnyVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 161 EQY-LDSSAVRVV--EGAVTETTLLLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKR 237
Cdd:cd07093 168 NEAgLPPGVVNVVhgFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 238 IIAGKWGcNNGQACISPDYILTTKEFSPKVIDALKQELEAFYGKNPM-ESKDMSRIVNSNHFDRLSKMLE-EKEVSDKIV 315
Cdd:cd07093 248 AVRSSFS-NNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLdPDTEVGPLISKEHLEKVLGYVElARAEGATIL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 316 YGGqkNRDKLK-------IAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEEcfdVIR---SRPKPLAAYLFTQNQKLK 385
Cdd:cd07093 327 TGG--GRPELPdleggyfVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEE---AIElanDTPYGLAAYVWTRDLGRA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1824090424 386 ERFALTVSAGGIVVNDIAV-HLavpTLPFGGVGESGMGSYHGKFSFDAFSHKKAV 439
Cdd:cd07093 402 HRVARRLEAGTVWVNCWLVrDL---RTPFGGVKASGIGREGGDYSLEFYTELKNV 453
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
46-439 |
9.51e-58 |
|
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: 197.55 E-value: 9.51e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 46 HEPEIVSALHDDLGKPELESsVYEVA----LLRNSINLAVKQLKDWMAPDKAKTSLTTfpasaeiVYEPLGVVLVISAWN 121
Cdd:cd07150 59 RADDLIDLLIDEGGSTYGKA-WFETTftpeLLRAAAGECRRVRGETLPSDSPGTVSMS-------VRRPLGVVAGITPFN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 122 YPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQY-LDSSAVRVV--EGAVTETTLLLEQKWDKIFYTGSSRI 198
Cdd:cd07150 131 YPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAgLPKGVFNVVtgGGAEVGDELVDDPRVRMVTFTGSTAV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 199 GRIIMMAAAKHLTPVVLELGGKSPVVI--DSDTNLkitAKRIIAGKWGCNNGQACISPDYILTTKEFSPKVIDALKQELE 276
Cdd:cd07150 211 GREIAEKAGRHLKKITLELGGKNPLIVlaDADLDY---AVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARAS 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 277 AFYGKNPMESKDM-SRIVNSNHFDRLSKMLeEKEVSD--KIVYGGQknRDKLKIAPTILVDVPLDSQIMSEEIFGPLLPV 353
Cdd:cd07150 288 KLKVGDPRDPDTViGPLISPRQVERIKRQV-EDAVAKgaKLLTGGK--YDGNFYQPTVLTDVTPDMRIFREETFGPVTSV 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 354 ITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDIAVHlAVPTLPFGGVGESGMGSYHGKFSFDAF 433
Cdd:cd07150 365 IPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHINDPTIL-DEAHVPFGGVKASGFGREGGEWSMEEF 443
|
....*.
gi 1824090424 434 SHKKAV 439
Cdd:cd07150 444 TELKWI 449
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
7-440 |
1.81e-57 |
|
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: 196.95 E-value: 1.81e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 7 AADATDLVTELRRSFDdgvtrgyEW-------RVTQLKKLLLICDNHEPEIVSALHDDLGKPELESSVYEVALLRNSINL 79
Cdd:cd07138 35 AADVDRAVAAARRAFP-------AWsatsveeRAALLERIAEAYEARADELAQAITLEMGAPITLARAAQVGLGIGHLRA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 80 AVKQLKDWmapdkaktSLTTFPASAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKL 159
Cdd:cd07138 108 AADALKDF--------EFEERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 160 LEQY-LDSSAVRVV--EGAVTETTLLLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAK 236
Cdd:cd07138 180 LDEAgLPAGVFNLVngDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 237 RIIAGKWGcNNGQACISPDYILTTKEFSPKVIDALKQELEAFYGKNPMESKD-MSRIVNSNHFDRLSKMLEE--KEVSdK 313
Cdd:cd07138 260 RGVAACFA-NSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATtLGPLASAAQFDRVQGYIQKgiEEGA-R 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 314 IVYGGQKNRDKLK----IAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFA 389
Cdd:cd07138 338 LVAGGPGRPEGLErgyfVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVA 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1824090424 390 LTVSAGGIVVNDIAVHlavPTLPFGGVGESGMGSYHGKFSFDAFSHKKAVL 440
Cdd:cd07138 418 RRLRAGQVHINGAAFN---PGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
7-440 |
6.67e-57 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 195.26 E-value: 6.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 7 AADATDLVTELRRSFDDGVTRGYEWRVTQLKKLLLICDNHEPEIVSALHDDLGKPELESS--VYEVA-LLRNSINLAvKQ 83
Cdd:cd07110 18 AEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAwdVDDVAgCFEYYADLA-EQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 84 LKDwmapdKAKTSLT----TFpaSAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKL 159
Cdd:cd07110 97 LDA-----KAERAVPlpseDF--KARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 160 -LEQYLDSSAVRVVEGAVTET--TLLLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAK 236
Cdd:cd07110 170 aAEAGLPPGVLNVVTGTGDEAgaPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 237 RIIAGK-WgcNNGQACISPDYILTTKEFSPKVIDALKQELEAFYGKNPMESK-DMSRIVNSNHFDRLSKMLEE-KEVSDK 313
Cdd:cd07110 250 WAMFGCfW--NNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGvRLGPLVSQAQYEKVLSFIARgKEEGAR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 314 IVYGGqKNRDKLK----IAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFA 389
Cdd:cd07110 328 LLCGG-RRPAHLEkgyfIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVA 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1824090424 390 LTVSAGGIVVNdiAVHLAVPTLPFGGVGESGMGSYHGKFSFDAFSHKKAVL 440
Cdd:cd07110 407 EALEAGIVWIN--CSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
109-422 |
3.22e-56 |
|
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: 193.58 E-value: 3.22e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 109 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQ-YLDSSAVRVV--EGAVTETTLLLEQ 185
Cdd:cd07149 122 EPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEaGLPKGALNVVtgSGETVGDALVTDP 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 186 KWDKIFYTGSSRIGRIIMMAAAkhLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWgCNNGQACISPDYILTTKEFSP 265
Cdd:cd07149 202 RVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEKAVERCVSGAF-ANAGQVCISVQRIFVHEDIYD 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 266 KVIDALKQELEAFYGKNPM-ESKDMSRIVNSNHFDRLSKMLEE-KEVSDKIVYGGQknRDKLKIAPTILVDVPLDSQIMS 343
Cdd:cd07149 279 EFLERFVAATKKLVVGDPLdEDTDVGPMISEAEAERIEEWVEEaVEGGARLLTGGK--RDGAILEPTVLTDVPPDMKVVC 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 344 EEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDIavhlavPT-----LPFGGVGE 418
Cdd:cd07149 357 EEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINDS------STfrvdhMPYGGVKE 430
|
....
gi 1824090424 419 SGMG 422
Cdd:cd07149 431 SGTG 434
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
2-439 |
4.30e-56 |
|
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: 193.32 E-value: 4.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 2 VKVFQAADATDL---VTELRRSFDDGvtrgyEWR---VTQLKKLLLicdnHEPEIVSALHDDLGKPELESSVYEVALLRN 75
Cdd:cd07118 10 VARYAEGTVEDVdaaVAAARKAFDKG-----PWPrmsGAERAAVLL----KVADLIRARRERLALIETLESGKPISQARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 76 SINLAVKQLKdwMAPDKAKT----SLTTFPAS--AEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELA 149
Cdd:cd07118 81 EIEGAADLWR--YAASLARTlhgdSYNNLGDDmlGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 150 PASSSLLAKLL-EQYLDSSAVRVVEG--AVTETTLLLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVID 226
Cdd:cd07118 159 SGTTLMLAELLiEAGLPAGVVNIVTGygATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 227 SDTNLKITAKRIIAGKWgCNNGQACISPDYILTTKEFSPKVIDALKQELEAFYGKNPM-ESKDMSRIVNSNHFDRLSKML 305
Cdd:cd07118 239 ADADLDAAADAVVFGVY-FNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLdPETKVGAIINEAQLAKITDYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 306 EE-KEVSDKIVYGGQK--NRDKLKIAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQ 382
Cdd:cd07118 318 DAgRAEGATLLLGGERlaSAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDI 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1824090424 383 KLKERFALTVSAGGIVVNDIAVhlAVPTLPFGGVGESGMGSYHGKFSFDAFSHKKAV 439
Cdd:cd07118 398 DTALTVARRIRAGTVWVNTFLD--GSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
107-439 |
1.47e-55 |
|
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: 192.00 E-value: 1.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 107 VYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQY-LDSSAVRVV--EGAVTETTLLL 183
Cdd:cd07114 116 RREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAgFPPGVVNVVtgFGPETGEALVE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 184 EQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGcNNGQACISPDYILTTKEF 263
Cdd:cd07114 196 HPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFA-AAGQTCVAGSRLLVQRSI 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 264 SPKVIDALKQELEAFYGKNPMESK-DMSRIVNSNHFDRLSKMLEE-KEVSDKIVYGGQ-----KNRDKLKIAPTILVDVP 336
Cdd:cd07114 275 YDEFVERLVARARAIRVGDPLDPEtQMGPLATERQLEKVERYVARaREEGARVLTGGErpsgaDLGAGYFFEPTILADVT 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 337 LDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDiaVHLAVPTLPFGGV 416
Cdd:cd07114 355 NDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNT--YRALSPSSPFGGF 432
|
330 340
....*....|....*....|...
gi 1824090424 417 GESGMGSYHGKFSFDAFSHKKAV 439
Cdd:cd07114 433 KDSGIGRENGIEAIREYTQTKSV 455
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
36-439 |
1.73e-55 |
|
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: 191.75 E-value: 1.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 36 LKKLLLICDNHEPEIVSALHDDLGKPELESSVyEVALLRNSINLAVKqlkdWMAPDKAKTSLTTFPASAEIVY-EPLGVV 114
Cdd:cd07151 60 LEKAAQILEERRDEIVEWLIRESGSTRIKANI-EWGAAMAITREAAT----FPLRMEGRILPSDVPGKENRVYrEPLGVV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 115 LVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLL-AKLLEQY-LDSSAVRVVEGAVTET-TLLLEQKWDK-I 190
Cdd:cd07151 135 GVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGLLlAKIFEEAgLPKGVLNVVVGAGSEIgDAFVEHPVPRlI 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 191 FYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGcNNGQACISPDYILTTK----EFSPK 266
Cdd:cd07151 215 SFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFL-HQGQICMAINRIIVHEdvydEFVEK 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 267 VIDALKQeLEafYGkNPMESKDM-SRIVNSNHFDRLSKMLEE-KEVSDKIVYGGQknRDKLKIAPTILVDVPLDSQIMSE 344
Cdd:cd07151 294 FVERVKA-LP--YG-DPSDPDTVvGPLINESQVDGLLDKIEQaVEEGATLLVGGE--AEGNVLEPTVLSDVTNDMEIARE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 345 EIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDIAVHlAVPTLPFGGVGESGMGSY 424
Cdd:cd07151 368 EIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVN-DEPHVPFGGEKNSGLGRF 446
|
410
....*....|....*
gi 1824090424 425 HGKFSFDAFSHKKAV 439
Cdd:cd07151 447 NGEWALEEFTTDKWI 461
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
46-439 |
2.22e-55 |
|
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: 191.11 E-value: 2.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 46 HEPEIVSALHDDLGKPeLESSVYEVALLRNSINLA---VKQLKDWMAPDKAKTSLTTfpASAEIVYEPLGVVLVISAWNY 122
Cdd:cd07094 59 RAEEFAKIIACEGGKP-IKDARVEVDRAIDTLRLAaeeAERIRGEEIPLDATQGSDN--RLAWTIREPVGVVLAITPFNF 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 123 PFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQY---LDSSAVRVVEGAVTETTLLLEQKWDKIFYTGSSRIG 199
Cdd:cd07094 136 PLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILVEAgvpEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 200 RIIMMAAAKhlTPVVLELGGKSPVVIDSDTNLKITAKRIIAGkwGC-NNGQACISPDYILTTKEFSPKVIDALKQELEAF 278
Cdd:cd07094 216 EALRANAGG--KRIALELGGNAPVIVDRDADLDAAIEALAKG--GFyHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 279 YGKNPMESK-DMSRIVNSNHFDRLSKMLEEK-EVSDKIVYGGQknRDKLKIAPTILVDVPLDSQIMSEEIFGPLLPVITL 356
Cdd:cd07094 292 KVGDPLDEDtDVGPLISEEAAERVERWVEEAvEAGARLLCGGE--RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRY 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 357 NNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDiAVHLAVPTLPFGGVGESGMGSYHGKFSFDAFSHK 436
Cdd:cd07094 370 DDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVND-SSAFRTDWMPFGGVKESGVGREGVPYAMEEMTEE 448
|
...
gi 1824090424 437 KAV 439
Cdd:cd07094 449 KTV 451
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
26-439 |
2.77e-55 |
|
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: 190.36 E-value: 2.77e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 26 TRGYEWRVTQLKKLLLICDNHEPEIVSALHDDLGKPeLESSVYEVALlrnsinlaVKQLKDWMApDKAKTSL-----TTF 100
Cdd:cd07100 17 KTSFAERAALLRKLADLLRERKDELARLITLEMGKP-IAEARAEVEK--------CAWICRYYA-ENAEAFLadepiETD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 101 PASAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQ-----------YLDSSAV 169
Cdd:cd07100 87 AGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREagfpegvfqnlLIDSDQV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 170 -------RVVegAVTettllleqkwdkifYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGK 242
Cdd:cd07100 167 eaiiadpRVR--GVT--------------LTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 243 WGcNNGQACISPDYILTTKEFSPKVIDALKQELEAFYGKNPMESKD----MSRivnSNHFDRLSKMLEE-KEVSDKIVYG 317
Cdd:cd07100 231 LQ-NAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTdlgpLAR---KDLRDELHEQVEEaVAAGATLLLG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 318 GQK-NRDKLKIAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGG 396
Cdd:cd07100 307 GKRpDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGM 386
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1824090424 397 IVVNDIAvhLAVPTLPFGGVGESGMGSYHGKFSFDAFSHKKAV 439
Cdd:cd07100 387 VFINGMV--KSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTV 427
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
107-439 |
4.71e-55 |
|
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: 190.52 E-value: 4.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 107 VYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQY-LDSSAVRVVEGAVTET--TLLL 183
Cdd:cd07109 114 VREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAgLPAGALNVVTGLGAEAgaALVA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 184 EQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIagkWGC--NNGQACISPDYILTTK 261
Cdd:cd07109 194 HPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVV---NAIiqNAGQTCSAGSRLLVHR 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 262 EFSPKVIDALKQELEAFYGKNPMESKDMSRIVNSNHFDRLSKMLEEKEVSD-KIVYGGQKNRDKLK----IAPTILVDVP 336
Cdd:cd07109 271 SIYDEVLERLVERFRALRVGPGLEDPDLGPLISAKQLDRVEGFVARARARGaRIVAGGRIAEGAPAggyfVAPTLLDDVP 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 337 LDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDIAVHLAVpTLPFGGV 416
Cdd:cd07109 351 PDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNYGAGGGI-ELPFGGV 429
|
330 340
....*....|....*....|...
gi 1824090424 417 GESGMGSYHGKFSFDAFSHKKAV 439
Cdd:cd07109 430 KKSGHGREKGLEALYNYTQTKTV 452
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
2-439 |
8.37e-55 |
|
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: 189.57 E-value: 8.37e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 2 VKVFQAADATDLVTELRRSFD-----DGVTRG-YEWRVTQLkkLLLICDnhepEIVSALHDDLGKPelessvyevalLRN 75
Cdd:cd07115 13 VAQASAEDVDAAVAAARAAFEawsamDPAERGrILWRLAEL--ILANAD----ELARLESLDTGKP-----------IRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 76 SINLAVKQLKD---WMAPDKAKTSLTTFPASAE----IVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSEL 148
Cdd:cd07115 76 ARRLDVPRAADtfrYYAGWADKIEGEVIPVRGPflnyTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 149 APASSSLLAKLLEQY-LDSSAVRVVE--GAVTETTLLLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVI 225
Cdd:cd07115 156 TPLSALRIAELMAEAgFPAGVLNVVTgfGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 226 DSDTNLKITAKriiAGKWGC--NNGQACISPDYILTTKEFSPKVIDALKQELEAFYGKNPMESK-DMSRIVNSNHFDRLS 302
Cdd:cd07115 236 FADADLDAAVR---AAATGIfyNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKtQMGPLVSQAQFDRVL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 303 KMLE-EKEVSDKIVYGGQKNRDK-LKIAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQ 380
Cdd:cd07115 313 DYVDvGREEGARLLTGGKRPGARgFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTR 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 381 NQKLKERFALTVSAGGIVVNdiaVHLAV-PTLPFGGVGESGMGSYHGKFSFDAFSHKKAV 439
Cdd:cd07115 393 DLGRAHRVAAALKAGTVWIN---TYNRFdPGSPFGGYKQSGFGREMGREALDEYTEVKSV 449
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
6-441 |
9.92e-55 |
|
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: 190.11 E-value: 9.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 6 QAADATDLVTELRRSFDDGVTRGY--EWRVTQLKKLLLICDNHEPEIVSALHDDLGKPELESSVYEVAL----LRNSINL 79
Cdd:cd07091 39 DEEDVDAAVKAARAAFETGWWRKMdpRERGRLLNKLADLIERDRDELAALESLDNGKPLEESAKGDVALsikcLRYYAGW 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 80 AVKQLKDWMAPDKAKTSLTTfpasaeivYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKL 159
Cdd:cd07091 119 ADKIQGKTIPIDGNFLAYTR--------REPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAEL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 160 -LEQYLDSSAVRVVEG--AVTETTLLLEQKWDKIFYTGSSRIGRIIMMAAAK-HLTPVVLELGGKSPVVIDSDTNLKITA 235
Cdd:cd07091 191 iKEAGFPPGVVNIVPGfgPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAV 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 236 KRIIAGKWgCNNGQACISPDYILTTKEFSPKVIDALKQELEAFYGKNPMESK-DMSRIVNSNHFDRLSKMLEE-KEVSDK 313
Cdd:cd07091 271 EWAAFGIF-FNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDtFQGPQVSKAQFDKILSYIESgKKEGAT 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 314 IVYGGQKNRDK-LKIAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTV 392
Cdd:cd07091 350 LLTGGERHGSKgYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRAL 429
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1824090424 393 SAGGIVVNDIAV-HLAVptlPFGGVGESGMGSYHGKFSFDAFSHKKAVLY 441
Cdd:cd07091 430 KAGTVWVNTYNVfDAAV---PFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
104-440 |
2.63e-54 |
|
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: 189.09 E-value: 2.63e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 104 AEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQYLDSSAVRVVEGAVTET--TL 181
Cdd:cd07559 130 SYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVNVVTGFGSEAgkPL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 182 LLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITA--KRIIAGKWGC--NNGQACISPDYI 257
Cdd:cd07559 210 ASHPRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFFDDAMDADDDfdDKAEEGQLGFafNQGEVCTCPSRA 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 258 LTTKEFSPKVIDALKQELEAFYGKNPMESKD-MSRIVNSNHFDRLSKMLE-EKEVSDKIVYGGQKNR--DKLK---IAPT 330
Cdd:cd07559 290 LVQESIYDEFIERAVERFEAIKVGNPLDPETmMGAQVSKDQLEKILSYVDiGKEEGAEVLTGGERLTlgGLDKgyfYEPT 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 331 ILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNdiAVHLAVPT 410
Cdd:cd07559 370 LIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVN--CYHQYPAH 447
|
330 340 350
....*....|....*....|....*....|
gi 1824090424 411 LPFGGVGESGMGSYHGKFSFDAFSHKKAVL 440
Cdd:cd07559 448 APFGGYKKSGIGRETHKMMLDHYQQTKNIL 477
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
109-440 |
2.77e-54 |
|
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: 188.30 E-value: 2.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 109 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQYLDSSAVRVVEG--AVTETTLLLEQK 186
Cdd:cd07092 117 EPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGVVNVVCGggASAGDALVAHPR 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 187 WDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWgCNNGQACISPDYILTTKEFSPK 266
Cdd:cd07092 197 VRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGY-YNAGQDCTAACRVYVHESVYDE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 267 VIDALKQELEAF-YGKNPMESKDMSRIVNSNHFDRLSKMLEEKEVSDKIVYGGQK-NRDKLKIAPTILVDVPLDSQIMSE 344
Cdd:cd07092 276 FVAALVEAVSAIrVGDPDDEDTEMGPLNSAAQRERVAGFVERAPAHARVLTGGRRaEGPGYFYEPTVVAGVAQDDEIVQE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 345 EIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDiavHLAVPT-LPFGGVGESGMGS 423
Cdd:cd07092 356 EIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNT---HIPLAAeMPHGGFKQSGYGK 432
|
330
....*....|....*..
gi 1824090424 424 YHGKFSFDAFSHKKAVL 440
Cdd:cd07092 433 DLSIYALEDYTRIKHVM 449
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
7-441 |
1.00e-53 |
|
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: 187.06 E-value: 1.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 7 AADATDLVTELRRSFDDGV-TRGYEWRVTQLKKLLLICDNHEPEIVSALHDDLGKPELESSVYEVALLRNSINLAVKQLK 85
Cdd:cd07089 18 AADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQVDGPIGHLRYFADLAD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 86 DWMAP-DKAKTSLTTFPASAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQY- 163
Cdd:cd07089 98 SFPWEfDLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAETd 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 164 LDSSAVRVVEGAVTETTLLL--EQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAG 241
Cdd:cd07089 178 LPAGVVNVVTGSDNAVGEALttDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 242 kWGCNNGQACISPDYILTTKEFSPKVIDALKQELEAFYGKNPMESKD-MSRIVNSNHFDRLSKMLEE-KEVSDKIVYGGQ 319
Cdd:cd07089 258 -CMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTvMGPLISAAQRDRVEGYIARgRDEGARLVTGGG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 320 K--NRDK-LKIAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGG 396
Cdd:cd07089 337 RpaGLDKgFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGS 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1824090424 397 IVVNDiAVHLAvPTLPFGGVGESGMGSYHGKFSFDAFSHKKAVLY 441
Cdd:cd07089 417 VGING-GGGYG-PDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
104-441 |
1.61e-53 |
|
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: 186.40 E-value: 1.61e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 104 AEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQY-LDSSAVRVVEGAVTET--T 180
Cdd:cd07145 117 AFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPGVINVVTGYGSEVgdE 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 181 LLLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWgCNNGQACISPDYILTT 260
Cdd:cd07145 197 IVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRF-ENAGQVCNAVKRILVE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 261 KEFSPKVIDALKQELEAFYGKNPM-ESKDMSRIVNSNHFDRLSKMLEE-KEVSDKIVYGGqKNRDKLKIAPTILVDVPLD 338
Cdd:cd07145 276 EEVYDKFLKLLVEKVKKLKVGDPLdESTDLGPLISPEAVERMENLVNDaVEKGGKILYGG-KRDEGSFFPPTVLENDTPD 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 339 SQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDiAVHLAVPTLPFGGVGE 418
Cdd:cd07145 355 MIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVIND-STRFRWDNLPFGGFKK 433
|
330 340
....*....|....*....|...
gi 1824090424 419 SGMGSYHGKFSFDAFSHKKAVLY 441
Cdd:cd07145 434 SGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
6-439 |
2.27e-53 |
|
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: 186.27 E-value: 2.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 6 QAADATDLVTELRRSFDDGVtrgyeWRVT---QLKKLL-----LICDN-HEPEIVSALhdDLGKPELESSVYEVALLRNS 76
Cdd:cd07112 22 DAADVDRAVAAARRAFESGV-----WSRLspaERKAVLlrladLIEAHrDELALLETL--DMGKPISDALAVDVPSAANT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 77 InlavkqlkDWMAP--DK--AKTSLTTFPASAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPAS 152
Cdd:cd07112 95 F--------RWYAEaiDKvyGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 153 SSLLAKL-LEQYLDSSAVRVVEGA--VTETTLLLEQKWDKIFYTGSSRIGRIIMMAAAK-HLTPVVLELGGKSP-VVIDS 227
Cdd:cd07112 167 ALRLAELaLEAGLPAGVLNVVPGFghTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPnIVFAD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 228 DTNLKITAKRIIAGKWGcNNGQACISPDYILTTKEFSPKVIDALKQELEAFYGKNPME-SKDMSRIVNSNHFDRLSKMLE 306
Cdd:cd07112 247 APDLDAAAEAAAAGIFW-NQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDpATRMGALVSEAHFDKVLGYIE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 307 E-KEVSDKIVYGGQKNRDKLK---IAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQ 382
Cdd:cd07112 326 SgKAEGARLVAGGKRVLTETGgffVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDL 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1824090424 383 KLKERFALTVSAGGIVVN-----DIavhlavpTLPFGGVGESGMGSYHGKFSFDAFSHKKAV 439
Cdd:cd07112 406 SRAHRVARRLRAGTVWVNcfdegDI-------TTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
7-439 |
3.44e-52 |
|
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: 182.96 E-value: 3.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 7 AADATDLVTELRRSFDDGVTRGYEWRVTQLKKLLLICDNHEPEIvsALHD--DLGKPelessvyeVALLRNSINLAVKQL 84
Cdd:cd07107 18 AADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEEL--ALIDalDCGNP--------VSAMLGDVMVAAALL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 85 kDWMAPDKAKTSLTTFPASAE----IVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLL 160
Cdd:cd07107 88 -DYFAGLVTELKGETIPVGGRnlhyTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 161 EQYLDSSAVRVVEG--AVTETTLLLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRI 238
Cdd:cd07107 167 REVLPPGVFNILPGdgATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 239 IAG---KWgcnNGQACISPDYILTTKEFSPKVIDALKQELEAFYGKNPM-ESKDMSRIVNSNHFDRLSKMLEE-KEVSDK 313
Cdd:cd07107 247 VAGmnfTW---CGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTdPATTMGPLVSRQQYDRVMHYIDSaKREGAR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 314 IVYGGQKNRDKLK-----IAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERF 388
Cdd:cd07107 324 LVTGGGRPEGPALeggfyVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRT 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1824090424 389 ALTVSAGGIVVNDIAVHLAvpTLPFGGVGESGMGSYHGKFSFDAFSHKKAV 439
Cdd:cd07107 404 ARRVEAGYVWINGSSRHFL--GAPFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
105-439 |
3.13e-51 |
|
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: 180.52 E-value: 3.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 105 EIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQY-LDSSAVRVVEGAVTET--TL 181
Cdd:cd07097 130 ETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAgLPAGVFNLVMGSGSEVgqAL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 182 LLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGcNNGQACISPDYILTTK 261
Cdd:cd07097 210 VEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFF-STGQRCTASSRLIVTE 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 262 EFSPKVIDALKQELEAFYGKNPMESK-DMSRIVNSNHFDRLSKMLE-EKEVSDKIVYGGQKNRDKLK---IAPTILVDVP 336
Cdd:cd07097 289 GIHDRFVEALVERTKALKVGDALDEGvDIGPVVSERQLEKDLRYIEiARSEGAKLVYGGERLKRPDEgyyLAPALFAGVT 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 337 LDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDIAVHLAvPTLPFGGV 416
Cdd:cd07097 369 NDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVD-YHVPFGGR 447
|
330 340
....*....|....*....|....
gi 1824090424 417 GESGMGSY-HGKFSFDAFSHKKAV 439
Cdd:cd07097 448 KGSSYGPReQGEAALEFYTTIKTV 471
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
32-400 |
1.35e-50 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 179.00 E-value: 1.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 32 RVTQLKKLLLICDNHEPEIVSALHDDLGKPelessvyeVALLRNSINLAVKQLkDWMAPDKAKTSLTTFPASAE-----I 106
Cdd:cd07088 59 RAAYLRKLADLIRENADELAKLIVEEQGKT--------LSLARVEVEFTADYI-DYMAEWARRIEGEIIPSDRPnenifI 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 107 VYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQY-LDSSAVRVV--EGAVTETTLLL 183
Cdd:cd07088 130 FKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAgLPAGVLNIVtgRGSVVGDALVA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 184 EQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGcNNGQACISPDYILTTK-- 261
Cdd:cd07088 210 HPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRII-NCGQVCTCAERVYVHEdi 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 262 --EFSPKVIDALKQeleAFYGkNPMESK-DMSRIVNSNHFDRLSKMLEE-KEVSDKIVYGGqkNRDKLK----IAPTILV 333
Cdd:cd07088 289 ydEFMEKLVEKMKA---VKVG-DPFDAAtDMGPLVNEAALDKVEEMVERaVEAGATLLTGG--KRPEGEkgyfYEPTVLT 362
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1824090424 334 DVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVN 400
Cdd:cd07088 363 NVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYIN 429
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
99-439 |
2.68e-50 |
|
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: 177.34 E-value: 2.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 99 TFPASAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQYLDSSAVRVVEG---- 174
Cdd:cd07106 103 DDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEVLPPGVLNVVSGgdel 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 175 --AVTEttlllEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGcNNGQACI 252
Cdd:cd07106 183 gpALTS-----HPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFI-NSGQVCA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 253 SpdyiltTKE-FSPKVI-DALKQELEAFYGKNPM-----ESKDMSRIVNSNHFDRLSKMLEEKEVSD-KIVYGGQ-KNRD 323
Cdd:cd07106 257 A------IKRlYVHESIyDEFCEALVALAKAAVVgdgldPGTTLGPVQNKMQYDKVKELVEDAKAKGaKVLAGGEpLDGP 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 324 KLKIAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDia 403
Cdd:cd07106 331 GYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWINT-- 408
|
330 340 350
....*....|....*....|....*....|....*..
gi 1824090424 404 vHLAV-PTLPFGGVGESGMGSYHGKFSFDAFSHKKAV 439
Cdd:cd07106 409 -HGALdPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
15-439 |
4.37e-50 |
|
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: 177.05 E-value: 4.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 15 TELRRSFDDGVTRGYEWRVTQLKKLLLIC-------DNHEPEIVSALHDDLGKPelessvyeVALLRNSINlAVKQLKDW 87
Cdd:cd07102 18 EAVRAALERARAAQKGWRAVPLEERKAIVtravellAANTDEIAEELTWQMGRP--------IAQAGGEIR-GMLERARY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 88 MApDKAKTSLTTFPASAE------IVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLE 161
Cdd:cd07102 89 MI-SIAEEALADIRVPEKdgferyIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 162 ---------QYLdssavrVVEGAVTEtTLLLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLK 232
Cdd:cd07102 168 eaglpegvfQVL------HLSHETSA-ALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 233 ITAKRIIAGKWgCNNGQACISPDYILTTKEFSPKVIDALKQELEAFYGKNPMESK-DMSRIVNSNHFDRLSKMLEEkEVS 311
Cdd:cd07102 241 AAAESLVDGAF-FNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPStTLGPVVSARAADFVRAQIAD-AIA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 312 D--KIVYGGQK-NRDKLK---IAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLK 385
Cdd:cd07102 319 KgaRALIDGALfPEDKAGgayLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1824090424 386 ERFALTVSAGGIVVNDiAVHLAvPTLPFGGVGESGMGSYHGKFSFDAFSHKKAV 439
Cdd:cd07102 399 EALGEQLETGTVFMNR-CDYLD-PALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
7-440 |
1.26e-49 |
|
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: 176.73 E-value: 1.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 7 AADATDLVTELRRSFDDGvtrgyEWRVT----QLKKLLLICD---NHEPEIVSALHDDLGKPeLESSVYEVA----LLRN 75
Cdd:cd07119 34 AEDAKRAIAAARRAFDSG-----EWPHLpaqeRAALLFRIADkirEDAEELARLETLNTGKT-LRESEIDIDdvanCFRY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 76 SINLAvkqlkdwmapDKAKTSLTTFPASAE--IVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASS 153
Cdd:cd07119 108 YAGLA----------TKETGEVYDVPPHVIsrTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 154 SLLAKLLEQY-LDSSAVRVVEGAVTET--TLLLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTN 230
Cdd:cd07119 178 IALFELIEEAgLPAGVVNLVTGSGATVgaELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADAD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 231 LKITAKRIIAGKWgCNNGQACISPDYILTTKEFSPKVIDALKQELEAFYGKNPM-ESKDMSRIVNSNHFDRLSKMLEE-K 308
Cdd:cd07119 258 FETAVDQALNGVF-FNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLdADTEMGPLVSAEHREKVLSYIQLgK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 309 EVSDKIVYGGQK-NRDKLK----IAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQK 383
Cdd:cd07119 337 EEGARLVCGGKRpTGDELAkgyfVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIA 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1824090424 384 LKERFALTVSAGGIVVNDIavHLAVPTLPFGGVGESGMGSYHGKFSFDAFSHKKAVL 440
Cdd:cd07119 417 RANRVARRLRAGTVWINDY--HPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHIN 471
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
26-442 |
1.57e-49 |
|
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: 176.22 E-value: 1.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 26 TRGYEWRVTQLKKLLLICDNHEPEIVSALHDDLGKPeLESSVYEV----ALLRNSINLAVKQLKDWMAPDKAKTSLTTFp 101
Cdd:cd07082 57 TMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKT-LKDALKEVdrtiDYIRDTIEELKRLDGDSLPGDWFPGTKGKI- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 102 asAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQY-LDSSAVRVV--EGAVTE 178
Cdd:cd07082 135 --AQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAgFPKGVVNVVtgRGREIG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 179 TTLLLEQKWDKIFYTGSSRIGRIIMMAAAKhlTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGcNNGQACISPDYIL 258
Cdd:cd07082 213 DPLVTHGRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALS-YSGQRCTAIKRVL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 259 TTKEFSPKVIDALKQELEAFYGKNPME-SKDMSRIVNSNHFDRLSKMLEE-KEVSDKIVYGGQKNRDKLkIAPTILVDVP 336
Cdd:cd07082 290 VHESVADELVELLKEEVAKLKVGMPWDnGVDITPLIDPKSADFVEGLIDDaVAKGATVLNGGGREGGNL-IYPTLLDPVT 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 337 LDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDIAVHlAVPTLPFGGV 416
Cdd:cd07082 369 PDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQR-GPDHFPFLGR 447
|
410 420
....*....|....*....|....*.
gi 1824090424 417 GESGMGSYHGKFSFDAFSHKKAVLYK 442
Cdd:cd07082 448 KDSGIGTQGIGDALRSMTRRKGIVIN 473
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
106-439 |
5.34e-49 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 175.26 E-value: 5.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 106 IVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQY-LDSSAVRVVEGAVTET--TLL 182
Cdd:PLN02278 156 VLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAgIPPGVLNVVMGDAPEIgdALL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 183 LEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGcNNGQACISPDYILTTK- 261
Cdd:PLN02278 236 ASPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFR-NSGQTCVCANRILVQEg 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 262 ---EFSPKVIDALkQELEAfyGKNPMESKDMSRIVNSNHFDRLskmleEKEVSD------KIVYGGQKNRDKLKI-APTI 331
Cdd:PLN02278 315 iydKFAEAFSKAV-QKLVV--GDGFEEGVTQGPLINEAAVQKV-----ESHVQDavskgaKVLLGGKRHSLGGTFyEPTV 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 332 LVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDIAVHLAVPtl 411
Cdd:PLN02278 387 LGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA-- 464
|
330 340
....*....|....*....|....*...
gi 1824090424 412 PFGGVGESGMGSYHGKFSFDAFSHKKAV 439
Cdd:PLN02278 465 PFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
7-440 |
1.11e-48 |
|
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: 173.78 E-value: 1.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 7 AADATDLVTELRRSFDD--GVTRGYEwRVTQLKKLLLICDNHEPEIVSALHDDLGKPELESSVYEVA----LLRNSINLA 80
Cdd:cd07113 36 EADVDAAVASAWRAFVSawAKTTPAE-RGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRAFEVGqsanFLRYFAGWA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 81 VKQLKDWMAPdkaktsltTFPASAEIVY------EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSS 154
Cdd:cd07113 115 TKINGETLAP--------SIPSMQGERYtaftrrEPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 155 LLAKL-LEQYLDSSAVRVVEGAVTETTLLLEQ-KWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLK 232
Cdd:cd07113 187 RVAELaKEAGIPDGVLNVVNGKGAVGAQLISHpDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADID 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 233 ITAKRIIAGKWgCNNGQACISPDYILTTKEFSPKVIDALKQELEAFYGKNPM-ESKDMSRIVNSNHFDRLSKMLE-EKEV 310
Cdd:cd07113 267 WVVEGLLTAGF-LHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMdESVMFGPLANQPHFDKVCSYLDdARAE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 311 SDKIVYGGQK-NRDKLKIAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFA 389
Cdd:cd07113 346 GDEIVRGGEAlAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYI 425
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1824090424 390 LTVSAGGIVVNdiaVHLAV-PTLPFGGVGESGMGSYHGKFSFDAFSHKKAVL 440
Cdd:cd07113 426 PRIEAGTVWVN---MHTFLdPAVPFGGMKQSGIGREFGSAFIDDYTELKSVM 474
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
106-440 |
1.46e-48 |
|
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: 173.41 E-value: 1.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 106 IVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQYLDSSAVRVVEGAVTET--TLLL 183
Cdd:cd07117 132 VLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNIVTGKGSKSgeYLLN 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 184 EQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWgCNNGQACISPDYILTTKEF 263
Cdd:cd07117 212 HPGLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGIL-FNQGQVCCAGSRIFVQEGI 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 264 SPKVIDALKQELEAFYGKNPME-SKDMSRIVNSNHFDRLSKMLE-EKEVSDKIVYGGQK----NRDK-LKIAPTILVDVP 336
Cdd:cd07117 291 YDEFVAKLKEKFENVKVGNPLDpDTQMGAQVNKDQLDKILSYVDiAKEEGAKILTGGHRltenGLDKgFFIEPTLIVNVT 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 337 LDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNdiaVHLAVPT-LPFGG 415
Cdd:cd07117 371 NDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVN---TYNQIPAgAPFGG 447
|
330 340
....*....|....*....|....*
gi 1824090424 416 VGESGMGSYHGKFSFDAFSHKKAVL 440
Cdd:cd07117 448 YKKSGIGRETHKSMLDAYTQMKNIY 472
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
107-423 |
4.06e-48 |
|
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: 173.18 E-value: 4.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 107 VYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQY-LDSSAVRVV--EGAVTETTLLL 183
Cdd:cd07124 163 VYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAgLPPGVVNFLpgPGEEVGDYLVE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 184 EQKWDKIFYTGSSRIGRIIMMAAAK------HLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGCnNGQACISPDYI 257
Cdd:cd07124 243 HPDVRFIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGF-QGQKCSACSRV 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 258 LTTKEFSPKVIDALKQELEAFYGKNPMESK-DMSRIVNSNHFDRLSKMLEEKEVSDKIVYGGQKNRDKLK---IAPTILV 333
Cdd:cd07124 322 IVHESVYDEFLERLVERTKALKVGDPEDPEvYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVLELAAEgyfVQPTIFA 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 334 DVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVND------IAVHla 407
Cdd:cd07124 402 DVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRkitgalVGRQ-- 479
|
330
....*....|....*.
gi 1824090424 408 vptlPFGGVGESGMGS 423
Cdd:cd07124 480 ----PFGGFKMSGTGS 491
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
109-439 |
1.13e-47 |
|
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: 170.56 E-value: 1.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 109 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLL-EQYLDSSAVRVVEGAvTETTLLLEQKW 187
Cdd:cd07090 115 EPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILtEAGLPDGVFNVVQGG-GETGQLLCEHP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 188 D--KIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWgCNNGQACISPDYILTTKEFSP 265
Cdd:cd07090 194 DvaKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANF-LSQGQVCSNGTRVFVQRSIKD 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 266 KVIDALKQELEAFYGKNPM-ESKDMSRIVNSNHFDRLSKMLEE-KEVSDKIVYGGQ--KNRDKLK----IAPTILVDVPL 337
Cdd:cd07090 273 EFTERLVERTKKIRIGDPLdEDTQMGALISEEHLEKVLGYIESaKQEGAKVLCGGErvVPEDGLEngfyVSPCVLTDCTD 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 338 DSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDIAVhlaVPT-LPFGGV 416
Cdd:cd07090 353 DMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINTYNI---SPVeVPFGGY 429
|
330 340
....*....|....*....|...
gi 1824090424 417 GESGMGSYHGKFSFDAFSHKKAV 439
Cdd:cd07090 430 KQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
108-442 |
1.64e-47 |
|
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: 170.79 E-value: 1.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 108 YEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLL-EQYLDSSAVRVV--EGAVTETTLLLE 184
Cdd:cd07143 142 HEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIpEAGFPPGVINVVsgYGRTCGNAISSH 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 185 QKWDKIFYTGSSRIGRIIMMAAAK-HLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWgCNNGQACISPDYILTTKEF 263
Cdd:cd07143 222 MDIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIF-FNHGQVCCAGSRIYVQEGI 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 264 SPKVIDALKQELEAFYGKNPM-ESKDMSRIVNSNHFDRLSKMLEE-KEVSDKIVYGGQKNRDK-LKIAPTILVDVPLDSQ 340
Cdd:cd07143 301 YDKFVKRFKEKAKKLKVGDPFaEDTFQGPQVSQIQYERIMSYIESgKAEGATVETGGKRHGNEgYFIEPTIFTDVTEDMK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 341 IMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNdiAVHLAVPTLPFGGVGESG 420
Cdd:cd07143 381 IVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVN--CYNLLHHQVPFGGYKQSG 458
|
330 340
....*....|....*....|..
gi 1824090424 421 MGSYHGKFSFDAFSHKKAVLYK 442
Cdd:cd07143 459 IGRELGEYALENYTQIKAVHIN 480
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
7-440 |
2.71e-47 |
|
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: 169.98 E-value: 2.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 7 AADATDLVTELRRSFDDGV---TRGYEwRVTQLKKLLLICDNHEPEIVSALHDDLGKPelessvYEVALLRNsINLAVKQ 83
Cdd:cd07142 40 AEDVDRAVKAARKAFDEGPwprMTGYE-RSRILLRFADLLEKHADELAALETWDNGKP------YEQARYAE-VPLAARL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 84 LK---DWMAPDKAKTSLTTFPASAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKL- 159
Cdd:cd07142 112 FRyyaGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLa 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 160 LEQYLDSSAVRVVE--GAVTETTLLLEQKWDKIFYTGSSRIGRIIMMAAAK-HLTPVVLELGGKSPVVIDSDTNLKitaK 236
Cdd:cd07142 192 AEAGLPDGVLNIVTgfGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVD---K 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 237 RIIAGKWGC--NNGQACISPDYILTTKEFSPKVIDALKQELEAFYGKNPMESK-DMSRIVNSNHFDRLSKMLEE-KEVSD 312
Cdd:cd07142 269 AVELAHFALffNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGvEQGPQVDKEQFEKILSYIEHgKEEGA 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 313 KIVYGGQKNRDK-LKIAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALT 391
Cdd:cd07142 349 TLITGGDRIGSKgYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRA 428
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1824090424 392 VSAGGIVVNdiAVHLAVPTLPFGGVGESGMGSYHGKFSFDAFSHKKAVL 440
Cdd:cd07142 429 LKAGTVWVN--CYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVV 475
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
6-440 |
8.04e-47 |
|
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: 168.52 E-value: 8.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 6 QAADATDLVTELRRSFDDGvtrgyEW-------RVTQLKKLLLICDNHEPEIVSALHDDLGKPELESSVYE----VALLR 74
Cdd:cd07139 34 TPADVDAAVAAARRAFDNG-----PWprlspaeRAAVLRRLADALEARADELARLWTAENGMPISWSRRAQgpgpAALLR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 75 NSINLAvkqlKDWMAPDKAKTSLTtfpASAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSS 154
Cdd:cd07139 109 YYAALA----RDFPFEERRPGSGG---GHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 155 LLAKLLEQY-LDSSAVRVVEGAVTETTLLLEQK-WDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLK 232
Cdd:cd07139 182 LLAEAAEEAgLPPGVVNVVPADREVGEYLVRHPgVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 233 ITAKRIIAGKWGcNNGQACISPDYILTTKEFSPKVIDALKQELEAFYGKNPME-SKDMSRIVNSNHFDRLSKMLEE-KEV 310
Cdd:cd07139 262 AAVPGLVPASLM-NNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDpATQIGPLASARQRERVEGYIAKgRAE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 311 SDKIVYGGQKNRDKLK---IAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKER 387
Cdd:cd07139 341 GARLVTGGGRPAGLDRgwfVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLA 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1824090424 388 FALTVSAGGIVVNDIAVHlavPTLPFGGVGESGMGSYHGKFSFDAFSHKKAVL 440
Cdd:cd07139 421 VARRIRTGTVGVNGFRLD---FGAPFGGFKQSGIGREGGPEGLDAYLETKSIY 470
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
110-435 |
8.45e-47 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 167.86 E-value: 8.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 110 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSS-LLAKLLEQY-LDSSAVRVVEGAV-TETTLLLEQK 186
Cdd:cd07152 110 PLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGvVIARLFEEAgLPAGVLHVLPGGAdAGEALVEDPN 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 187 WDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGcNNGQACISPDYILTTKEFSPK 266
Cdd:cd07152 190 VAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFL-HQGQICMAAGRHLVHESVADA 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 267 VIDALKQELEAFYGKNPMESK-DMSRIVNSNHFDRLSKMLEEK-EVSDKIVYGGQknRDKLKIAPTILVDVPLDSQIMSE 344
Cdd:cd07152 269 YTAKLAAKAKHLPVGDPATGQvALGPLINARQLDRVHAIVDDSvAAGARLEAGGT--YDGLFYRPTVLSGVKPGMPAFDE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 345 EIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQN----QKLKERfaltVSAGGIVVNDIAVhLAVPTLPFGGVGESG 420
Cdd:cd07152 347 EIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDvgraMALADR----LRTGMLHINDQTV-NDEPHNPFGGMGASG 421
|
330
....*....|....*.
gi 1824090424 421 MGSYH-GKFSFDAFSH 435
Cdd:cd07152 422 NGSRFgGPANWEEFTQ 437
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
102-427 |
8.55e-47 |
|
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: 168.26 E-value: 8.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 102 ASAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQY-LDSSAVRVV--EGAVTE 178
Cdd:cd07101 110 TRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAgLPRDLWQVVtgPGSEVG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 179 TTLLleQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGcNNGQACISPDYIL 258
Cdd:cd07101 190 GAIV--DNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFS-NAGQLCVSIERIY 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 259 TTKEFSPKVIDALKQELEAFYGKNPME-SKDMSRIVNSNHFDRLSKMLEEKEVSDKIVYGGQKNRDKLK---IAPTILVD 334
Cdd:cd07101 267 VHESVYDEFVRRFVARTRALRLGAALDyGPDMGSLISQAQLDRVTAHVDDAVAKGATVLAGGRARPDLGpyfYEPTVLTG 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 335 VPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVND--IAVHLAVPTlP 412
Cdd:cd07101 347 VTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEgyAAAWASIDA-P 425
|
330
....*....|....*
gi 1824090424 413 FGGVGESGMGSYHGK 427
Cdd:cd07101 426 MGGMKDSGLGRRHGA 440
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
106-439 |
1.12e-46 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 169.14 E-value: 1.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 106 IVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLL-EQYLDSSAVRVVEGAVTET--TLL 182
Cdd:PLN02467 147 VLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICrEVGLPPGVLNVVTGLGTEAgaPLA 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 183 LEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKitakriIAGKW---GC--NNGQACISPDYI 257
Cdd:PLN02467 227 SHPGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLD------KAVEWamfGCfwTNGQICSATSRL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 258 LTTKEFSPKVIDALKQELEAFYGKNPMESK-DMSRIVNSNHFDRLSKMLEE-KEVSDKIVYGGQKNRDKLK---IAPTIL 332
Cdd:PLN02467 301 LVHERIASEFLEKLVKWAKNIKISDPLEEGcRLGPVVSEGQYEKVLKFISTaKSEGATILCGGKRPEHLKKgffIEPTII 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 333 VDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNdiavhLAVPT-- 410
Cdd:PLN02467 381 TDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN-----CSQPCfc 455
|
330 340 350
....*....|....*....|....*....|
gi 1824090424 411 -LPFGGVGESGMGSYHGKFSFDAFSHKKAV 439
Cdd:PLN02467 456 qAPWGGIKRSGFGRELGEWGLENYLSVKQV 485
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
103-426 |
1.08e-45 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 166.59 E-value: 1.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 103 SAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQY-LDSSAVRVV--EGAVTET 179
Cdd:PRK09407 147 KTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAgLPRDLWQVVtgPGPVVGT 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 180 TLLleQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAgkwGC--NNGQACISPDYI 257
Cdd:PRK09407 227 ALV--DNADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVR---ACfsNAGQLCISIERI 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 258 LTTK----EFSPKVIDALKQ-ELEAFYGKNPmeskDMSRIVNSNHFDRLSKMLEE-KEVSDKIVYGGQKNRD--KLKIAP 329
Cdd:PRK09407 302 YVHEsiydEFVRAFVAAVRAmRLGAGYDYSA----DMGSLISEAQLETVSAHVDDaVAKGATVLAGGKARPDlgPLFYEP 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 330 TILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDI-AVHLAV 408
Cdd:PRK09407 378 TVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGyAAAWGS 457
|
330
....*....|....*...
gi 1824090424 409 PTLPFGGVGESGMGSYHG 426
Cdd:PRK09407 458 VDAPMGGMKDSGLGRRHG 475
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
7-426 |
5.02e-45 |
|
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: 163.30 E-value: 5.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 7 AADATDLVTELRRSFDDGVTRgYEwRVTQLKKLLLICDNHEPEIVSALHDDLGKPELESsVYEVALLRNSINLAVKQLK- 85
Cdd:cd07146 19 TEEALREALALAASYRSTLTR-YQ-RSAILNKAAALLEARREEFARLITLESGLCLKDT-RYEVGRAADVLRFAAAEALr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 86 --------DWMAPDKAKTSLTTfpasaeivYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLA 157
Cdd:cd07146 96 ddgesfscDLTANGKARKIFTL--------REPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 158 KLL-EQYLDSSAVRVVEGAVTETT--LLLEQKWDKIFYTGSSRIGRIIM-MAAAKHLtpvVLELGGKSPVVIDSDTNLKI 233
Cdd:cd07146 168 DLLyEAGLPPDMLSVVTGEPGEIGdeLITHPDVDLVTFTGGVAVGKAIAaTAGYKRQ---LLELGGNDPLIVMDDADLER 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 234 TAKRIIAGKWGcNNGQACISPDYILTTKEfspkVIDALKQELEAFYGK----NPM-ESKDMSRIVNSNHFDRLSKMLEEK 308
Cdd:cd07146 245 AATLAVAGSYA-NSGQRCTAVKRILVHES----VADEFVDLLVEKSAAlvvgDPMdPATDMGTVIDEEAAIQIENRVEEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 309 -EVSDKIVYGGQknRDKLKIAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKER 387
Cdd:cd07146 320 iAQGARVLLGNQ--RQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKR 397
|
410 420 430
....*....|....*....|....*....|....*....
gi 1824090424 388 FALTVSAGGIVVNDIAvHLAVPTLPFGGVGESGMGSYHG 426
Cdd:cd07146 398 LVERLDVGTVNVNEVP-GFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
8-439 |
7.52e-45 |
|
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: 163.67 E-value: 7.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 8 ADATDLVTELRRSFDDGVTRGYE--------WRVTQ-------LKKLL-LICDNHEpEIVSALHDDLGKPELESsvyeva 71
Cdd:cd07131 22 ADLEEVVGTFPLSTASDVDAAVEaareafpeWRKVPaprraeyLFRAAeLLKKRKE-ELARLVTREMGKPLAEG------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 72 llRNSINLAVkQLKDWMAPDKAKTSLTTFPAS-----AEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPS 146
Cdd:cd07131 95 --RGDVQEAI-DMAQYAAGEGRRLFGETVPSElpnkdAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 147 ELAPASSSLLAKLL-EQYLDSSAVRVVEGAVTETTLLLEQ--KWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPV 223
Cdd:cd07131 172 EDTPACALKLVELFaEAGLPPGVVNVVHGRGEEVGEALVEhpDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 224 VIDSDTNLKITAKRIIAGKWGcNNGQACISPDYILTTKEFSPKVIDALKQELEAFYGKNPMESK-DMSRIVNSNHFDRLS 302
Cdd:cd07131 252 IVMDDADLDLALEGALWSAFG-TTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEEtDMGPLINEAQLEKVL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 303 KMLE-EKEVSDKIVYGG-QKNRDKLK----IAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAY 376
Cdd:cd07131 331 NYNEiGKEEGATLLLGGeRLTGGGYEkgyfVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSA 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 377 LFTQNQKLKERFALTVSAGGIVVNdiavhlaVPT------LPFGGVGESGMGSYH-GKFSFDAFSHKKAV 439
Cdd:cd07131 411 IYTEDVNKAFRARRDLEAGITYVN-------APTigaevhLPFGGVKKSGNGHREaGTTALDAFTEWKAV 473
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
107-439 |
1.15e-43 |
|
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: 160.42 E-value: 1.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 107 VYEPLGVVLVISAWNYPFllsidPVIG-----AISAGNAVVLKPSELAPASSSLLAKLLEQYLDS-----SAVRVVEGAV 176
Cdd:cd07086 130 QWNPLGVVGVITAFNFPV-----AVPGwnaaiALVCGNTVVWKPSETTPLTAIAVTKILAEVLEKnglppGVVNLVTGGG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 177 TETTLLLEQKW-DKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITakrIIAGKWGC--NNGQACIS 253
Cdd:cd07086 205 DGGELLVHDPRvPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLA---VRAVLFAAvgTAGQRCTT 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 254 PDYILTTKefspKVIDALKQELEAFYGK----NPMESK-DMSRIVNSNHFDRLSKMLEE-KEVSDKIVYGGQKNRDKLK- 326
Cdd:cd07086 282 TRRLIVHE----SVYDEFLERLVKAYKQvrigDPLDEGtLVGPLINQAAVEKYLNAIEIaKSQGGTVLTGGKRIDGGEPg 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 327 --IAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERF--ALTVSAGGIVVNdi 402
Cdd:cd07086 358 nyVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVN-- 435
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1824090424 403 avhlaVPT------LPFGGVGESGMGSYHGKFSFDAFSHKKAV 439
Cdd:cd07086 436 -----IPTsgaeigGAFGGEKETGGGRESGSDAWKQYMRRSTC 473
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
110-422 |
1.90e-43 |
|
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: 158.95 E-value: 1.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 110 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLL-EQYLDSSAVRVVEGAVTETTLLLEQKWD 188
Cdd:cd07147 123 PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLaETGLPKGAFSVLPCSRDDADLLVTDERI 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 189 KIF-YTGSSRIGRIIMMAAAKHltPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGcNNGQACISPDYILTTKEfspkV 267
Cdd:cd07147 203 KLLsFTGSPAVGWDLKARAGKK--KVVLELGGNAAVIVDSDADLDFAAQRIIFGAFY-QAGQSCISVQRVLVHRS----V 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 268 IDALKQELEAFYGK----NPMESK-DMSRIVNSNHFDRLSKMLEEK-EVSDKIVYGGQknRDKLKIAPTILVDVPLDSQI 341
Cdd:cd07147 276 YDEFKSRLVARVKAlktgDPKDDAtDVGPMISESEAERVEGWVNEAvDAGAKLLTGGK--RDGALLEPTILEDVPPDMEV 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 342 MSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDiavhlaVPT-----LPFGGV 416
Cdd:cd07147 354 NCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVIND------VPTfrvdhMPYGGV 427
|
....*.
gi 1824090424 417 GESGMG 422
Cdd:cd07147 428 KDSGIG 433
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
101-437 |
1.96e-43 |
|
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: 159.59 E-value: 1.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 101 PASAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQY-LDSSAVRVVEGAVTET 179
Cdd:TIGR01804 124 PSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAgLPKGVFNVVQGDGAEV 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 180 -TLLLEQK-WDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWgCNNGQACISPDYI 257
Cdd:TIGR01804 204 gPLLVNHPdVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNF-FSAGQVCSNGTRV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 258 LTTKEFSPKVIDALKQELEAFYGKNPM-ESKDMSRIVNSNHFDRLSKMLEE-KEVSDKIVYGGQK-NRDKLK----IAPT 330
Cdd:TIGR01804 283 FVHKKIKERFLARLVERTERIKLGDPFdEATEMGPLISAAHRDKVLSYIEKgKAEGATLATGGGRpENVGLQngffVEPT 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 331 ILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDIavHLAVPT 410
Cdd:TIGR01804 363 VFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTY--NLYPAE 440
|
330 340
....*....|....*....|....*..
gi 1824090424 411 LPFGGVGESGMGSYHGKFSFDAFSHKK 437
Cdd:TIGR01804 441 APFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
110-381 |
2.58e-43 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 157.98 E-value: 2.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 110 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQY-LDSSAVRVV--EGAVTETTLLLEQK 186
Cdd:PRK10090 71 ALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVlgRGETVGQELAGNPK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 187 WDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWgCNNGQACISPDYILTTKEFSPK 266
Cdd:PRK10090 151 VAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRV-INSGQVCNCAERVYVQKGIYDQ 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 267 VIDALKQELEAFYGKNPMESK--DMSRIVNSNHFDRLSKMLEE-KEVSDKIVYGGQKNRDK-LKIAPTILVDVPLDSQIM 342
Cdd:PRK10090 230 FVNRLGEAMQAVQFGNPAERNdiAMGPLINAAALERVEQKVARaVEEGARVALGGKAVEGKgYYYPPTLLLDVRQEMSIM 309
|
250 260 270
....*....|....*....|....*....|....*....
gi 1824090424 343 SEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQN 381
Cdd:PRK10090 310 HEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQN 348
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
6-439 |
3.59e-43 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 159.29 E-value: 3.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 6 QAADATDLVTELRRSFDDGvtrgyEW-------RVTQLKKLLLICDNHEPEIVSALHDDLGKPELESsvyevalLRNSIN 78
Cdd:PRK09847 55 KSVDIDRAVSAARGVFERG-----DWslsspakRKAVLNKLADLMEAHAEELALLETLDTGKPIRHS-------LRDDIP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 79 LAVKQLKdWMAP--DK--AKTSLTTFPASAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSS 154
Cdd:PRK09847 123 GAARAIR-WYAEaiDKvyGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 155 LLAKLL-EQYLDSSAVRVVEGAVTET--TLLLEQKWDKIFYTGSSRIGRIIMM-AAAKHLTPVVLELGGKSPVVIDSDT- 229
Cdd:PRK09847 202 RLAGLAkEAGLPDGVLNVVTGFGHEAgqALSRHNDIDAIAFTGSTRTGKQLLKdAGDSNMKRVWLEAGGKSANIVFADCp 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 230 NLKITAKRIIAGKWgCNNGQACISPDYILTTKEFSPKVIDALKQELEAFYGKNPME-SKDMSRIVNSNHFDRLSKMLEEK 308
Cdd:PRK09847 282 DLQQAASATAAGIF-YNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDpATTMGTLIDCAHADSVHSFIREG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 309 EVSDKIVYGGQKNRDKLKIAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERF 388
Cdd:PRK09847 361 ESKGQLLLDGRNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRM 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1824090424 389 ALTVSAGGIVVNDiaVHLAVPTLPFGGVGESGMGSYHGKFSFDAFSHKKAV 439
Cdd:PRK09847 441 SRRLKAGSVFVNN--YNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
104-439 |
6.32e-42 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 155.37 E-value: 6.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 104 AEIVYEPLGVVLVISAWNYPFL--LSIDPVigAISAGNAVVLKPSELAPASSSLLAKLLEQY-LDSSAVRVVEGAVTETT 180
Cdd:cd07085 130 TYSYRQPLGVVAGITPFNFPAMipLWMFPM--AIACGNTFVLKPSERVPGAAMRLAELLQEAgLPDGVLNVVHGGKEAVN 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 181 LLLEQKWDK-IFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGCNnGQACISPDYILT 259
Cdd:cd07085 208 ALLDHPDIKaVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAA-GQRCMALSVAVA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 260 TKEFSPKVIDALKQELEAFYGKNPMESK-DMSRIVNSNHFDRLSKMLE--EKEVSDKIVYGGQKNRDKLK----IAPTIL 332
Cdd:cd07085 287 VGDEADEWIPKLVERAKKLKVGAGDDPGaDMGPVISPAAKERIEGLIEsgVEEGAKLVLDGRGVKVPGYEngnfVGPTIL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 333 VDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNdiaVHLAVPT-- 410
Cdd:cd07085 367 DNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN---VPIPVPLaf 443
|
330 340 350
....*....|....*....|....*....|.
gi 1824090424 411 LPFGGVGESGMGSYH--GKFSFDAFSHKKAV 439
Cdd:cd07085 444 FSFGGWKGSFFGDLHfyGKDGVRFYTQTKTV 474
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
108-427 |
7.90e-42 |
|
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: 155.25 E-value: 7.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 108 YEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQY-LDSSAVRVVEG-AVTETTLLLEQ 185
Cdd:cd07111 145 WKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAgLPPGVLNIVTGnGSFGSALANHP 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 186 KWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWgCNNGQACISPDYILTTKEFSP 265
Cdd:cd07111 225 GVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIW-FNQGQVCCAGSRLLVQESVAE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 266 KVIDALKQELEAFYGKNPME-SKDMSRIVNSNHFDRLSKMLEE--KEVSDKIVYGGQKNRDKLKIAPTILVDVPLDSQIM 342
Cdd:cd07111 304 ELIRKLKERMSHLRVGDPLDkAIDMGAIVDPAQLKRIRELVEEgrAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIA 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 343 SEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNdiAVHLAVPTLPFGGVGESGMG 422
Cdd:cd07111 384 QEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWIN--GHNLFDAAAGFGGYRESGFG 461
|
....*
gi 1824090424 423 SYHGK 427
Cdd:cd07111 462 REGGK 466
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
7-439 |
1.49e-41 |
|
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: 154.04 E-value: 1.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 7 AADATDLVTELRRSFDDGvtrgyEWRVTQLKK---LLLICD----NHEpEIVSALHDDLGKPELESsvyevallRNSINL 79
Cdd:cd07120 18 VAEAEAAIAAARRAFDET-----DWAHDPRLRarvLLELADafeaNAE-RLARLLALENGKILGEA--------RFEISG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 80 AVKQLKDWmapdkAKTSLTTFPASAE--------IVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPA 151
Cdd:cd07120 84 AISELRYY-----AGLARTEAGRMIEpepgsfslVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 152 SSSLLAKLLEQ--YLDSSAVRVV--EGAVTETTLLLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDS 227
Cdd:cd07120 159 INAAIIRILAEipSLPAGVVNLFteSGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 228 DTNLKITAKRIIAGKWgCNNGQACISPDYILTTKEFSPKVIDALKQELEAF-YGKNPMESKDMSRIVNSNHFDRLSKMLE 306
Cdd:cd07120 239 DADLDAALPKLERALT-IFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVkVGPGLDPASDMGPLIDRANVDRVDRMVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 307 EKEVS-DKIVYGGQKNRDKLK----IAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQN 381
Cdd:cd07120 318 RAIAAgAEVVLRGGPVTEGLAkgafLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1824090424 382 QKLKERFALTVSAGGIVVNDiavHLAV-PTLPFGGVGESGMGSYHGKFSFDAFSHKKAV 439
Cdd:cd07120 398 LARAMRVARAIRAGTVWIND---WNKLfAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
6-442 |
1.54e-41 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 154.43 E-value: 1.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 6 QAADATDL---VTELRRSFDdgvtRGYEWRVTQ-------LKKLLLICDNHEPEIVSALHDDLGKPELESSVYEVallrn 75
Cdd:cd07141 39 QEGDKADVdkaVKAARAAFK----LGSPWRTMDasergrlLNKLADLIERDRAYLASLETLDNGKPFSKSYLVDL----- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 76 siNLAVKQLKdWMAPDKAKTSLTTFPASAEIV----YEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPA 151
Cdd:cd07141 110 --PGAIKVLR-YYAGWADKIHGKTIPMDGDFFtytrHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 152 SSSLLAKLL-EQYLDSSAVRVVEG-------AVTEttlllEQKWDKIFYTGSSRIGRIIMMAAAK-HLTPVVLELGGKSP 222
Cdd:cd07141 187 TALYLASLIkEAGFPPGVVNVVPGygptagaAISS-----HPDIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 223 VVIDSDTNLKITAKRIIAGKWgCNNGQACISPDYILTTK----EFSPKVIDALKQELEAfygkNPMESK-DMSRIVNSNH 297
Cdd:cd07141 262 NIVFADADLDYAVEQAHEALF-FNMGQCCCAGSRTFVQEsiydEFVKRSVERAKKRVVG----NPFDPKtEQGPQIDEEQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 298 FDRLSKMLEE-KEVSDKIVYGGQKNRDK-LKIAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAA 375
Cdd:cd07141 337 FKKILELIESgKKEGAKLECGGKRHGDKgYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAA 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1824090424 376 YLFTQNQKLKERFALTVSAGGIVVNdiAVHLAVPTLPFGGVGESGMGSYHGKFSFDAFSHKKAVLYK 442
Cdd:cd07141 417 AVFTKDIDKAITFSNALRAGTVWVN--CYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 481
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
109-423 |
4.39e-40 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 150.44 E-value: 4.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 109 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQYLDSSAVRVV--EGAVTETTLLLEQK 186
Cdd:PRK13473 137 DPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVtgRGATVGDALVGHPK 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 187 WDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWgCNNGQACISPDYILTTKEFSPK 266
Cdd:PRK13473 217 VRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGY-YNAGQDCTAACRIYAQRGIYDD 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 267 VIDALKQELEAF-YGKNPMESKDMSRIVNSNHFDRLSKMLEE--KEVSDKIVYGGQK-NRDKLKIAPTILVDVPLDSQIM 342
Cdd:PRK13473 296 LVAKLAAAVATLkVGDPDDEDTELGPLISAAHRDRVAGFVERakALGHIRVVTGGEApDGKGYYYEPTLLAGARQDDEIV 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 343 SEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDiavHL-AVPTLPFGGVGESGM 421
Cdd:PRK13473 376 QREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNT---HFmLVSEMPHGGQKQSGY 452
|
..
gi 1824090424 422 GS 423
Cdd:PRK13473 453 GK 454
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
9-440 |
3.04e-39 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 149.19 E-value: 3.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 9 DATDL---VTELRRSFDDGV---TRGYEwRVTQLKKLLLICDNHEPEIVSALHDDLGKPELESSVYEVALlrnsinlaVK 82
Cdd:PLN02466 93 DAEDVnraVAAARKAFDEGPwpkMTAYE-RSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPM--------FA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 83 QLKDWMAPDKAKTSLTTFPASA----EIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAK 158
Cdd:PLN02466 164 RLFRYYAGWADKIHGLTVPADGphhvQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 159 LL-EQYLDSSAVRVVE--GAVTETTLLLEQKWDKIFYTGSSRIGRIIMMAAAK-HLTPVVLELGGKSPVVIDSDTNLKiT 234
Cdd:PLN02466 244 LLhEAGLPPGVLNVVSgfGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVD-K 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 235 AKRIIAGKWGCNNGQACISPDYILTTK----EFSPK---------VIDALKQELEafygKNPMeskdmsriVNSNHFDRL 301
Cdd:PLN02466 323 AVELAHFALFFNQGQCCCAGSRTFVHErvydEFVEKakaralkrvVGDPFKKGVE----QGPQ--------IDSEQFEKI 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 302 SKMLEEK-EVSDKIVYGGQKNRDK-LKIAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFT 379
Cdd:PLN02466 391 LRYIKSGvESGATLECGGDRFGSKgYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFT 470
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1824090424 380 QNQKLKERFALTVSAGGIVVNDIAVHLAvpTLPFGGVGESGMGSYHGKFSFDAFSHKKAVL 440
Cdd:PLN02466 471 QNLDTANTLSRALRVGTVWVNCFDVFDA--AIPFGGYKMSGIGREKGIYSLNNYLQVKAVV 529
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
109-440 |
6.62e-39 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 147.66 E-value: 6.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 109 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQY-LDSSAVRVVE--GAVTETTLLLEQ 185
Cdd:PLN02766 157 EPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAgVPDGVINVVTgfGPTAGAAIASHM 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 186 KWDKIFYTGSSRIGRIIMMAAAK-HLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWgCNNGQACISPDYILTTKEFS 264
Cdd:PLN02766 237 DVDKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIF-YNKGEICVASSRVYVQEGIY 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 265 PKVIDALKQELEAFYGKNPMESK-DMSRIVNSNHFDRLSKMLEE-KEVSDKIVYGGQKNRDK-LKIAPTILVDVPLDSQI 341
Cdd:PLN02766 316 DEFVKKLVEKAKDWVVGDPFDPRaRQGPQVDKQQFEKILSYIEHgKREGATLLTGGKPCGDKgYYIEPTIFTDVTEDMKI 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 342 MSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNdiaVHLAV-PTLPFGGVGESG 420
Cdd:PLN02766 396 AQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN---CYFAFdPDCPFGGYKMSG 472
|
330 340
....*....|....*....|
gi 1824090424 421 MGSYHGKFSFDAFSHKKAVL 440
Cdd:PLN02766 473 FGRDQGMDALDKYLQVKSVV 492
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
105-423 |
1.50e-37 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 143.92 E-value: 1.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 105 EIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLE---------QYLDSSAVRVVEGA 175
Cdd:PRK03137 166 RYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEeaglpagvvNFVPGSGSEVGDYL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 176 VT--ETTLlleqkwdkIFYTGSSRIGRIIMMAAAK------HLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGCNn 247
Cdd:PRK03137 246 VDhpKTRF--------ITFTGSREVGLRIYERAAKvqpgqiWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFS- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 248 GQACISPDYILTTKEFSPKVIDALKQELEAFYGKNPMESKDMSRIVNSNHFDRLSKMLEEKEVSDKIVYGGqkNRDKLK- 326
Cdd:PRK03137 317 GQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNAYMGPVINQASFDKIMSYIEIGKEEGRLVLGG--EGDDSKg 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 327 --IAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDIAV 404
Cdd:PRK03137 395 yfIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCT 474
|
330
....*....|....*....
gi 1824090424 405 HLAVPTLPFGGVGESGMGS 423
Cdd:PRK03137 475 GAIVGYHPFGGFNMSGTDS 493
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
32-422 |
4.10e-37 |
|
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: 141.79 E-value: 4.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 32 RVTQLKKLLLICDNHEPEIVSALHDDLGKPELESSVyEVALLRNSINLAVKQLKDwMAPDKAKTSLTtfPASA-EIVY-- 108
Cdd:cd07148 46 RIAILERLADLMEERADELALLIAREGGKPLVDAKV-EVTRAIDGVELAADELGQ-LGGREIPMGLT--PASAgRIAFtt 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 109 -EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLL-EQYLDSSAVRVV--EGAVTETtLLLE 184
Cdd:cd07148 122 rEPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLhEAGLPEGWCQAVpcENAVAEK-LVTD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 185 QKWDKIFYTGSSRIGRIIMMAAAKHlTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWgCNNGQACISPDYILTTKEFS 264
Cdd:cd07148 201 PRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGF-YHAGQVCVSVQRVFVPAEIA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 265 PKVIDALKQELEAFYGKNPMESK-DMSRIVNSNHFDRLSKMLEEKEVSDKIVYGGQKNRDKLKIAPTILVDVPLDSQIMS 343
Cdd:cd07148 279 DDFAQRLAAAAEKLVVGDPTDPDtEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKRLSDTTYAPTVLLDPPRDAKVST 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 344 EEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDiavHLA--VPTLPFGGVGESGM 421
Cdd:cd07148 359 QEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVND---HTAfrVDWMPFAGRRQSGY 435
|
.
gi 1824090424 422 G 422
Cdd:cd07148 436 G 436
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
108-440 |
5.50e-37 |
|
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: 141.82 E-value: 5.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 108 YEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQYLDSSAVRVVEGAVTET--TLLLEQ 185
Cdd:cd07116 134 HEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGFGLEAgkPLASSK 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 186 KWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITA--KRIIAG--KWGCNNGQACISPDYILTTK 261
Cdd:cd07116 214 RIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPNIFFADVMDADDAffDKALEGfvMFALNQGEVCTCPSRALIQE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 262 EFSPKVIDALKQELEAFYGKNPMESKDMSRIVNSNhfDRLSKMLEE----KEVSDKIVYGGQKNR-----DKLKIAPTiL 332
Cdd:cd07116 294 SIYDRFMERALERVKAIKQGNPLDTETMIGAQASL--EQLEKILSYidigKEEGAEVLTGGERNElggllGGGYYVPT-T 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 333 VDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNdiAVHLAVPTLP 412
Cdd:cd07116 371 FKGGNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN--CYHLYPAHAA 448
|
330 340
....*....|....*....|....*...
gi 1824090424 413 FGGVGESGMGSYHGKFSFDAFSHKKAVL 440
Cdd:cd07116 449 FGGYKQSGIGRENHKMMLDHYQQTKNLL 476
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
18-420 |
3.04e-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: 138.94 E-value: 3.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 18 RRSFDDGVTRGYEWRVTQLKKLLLICDNHEPEIVSALHDDLGKPELESSVyEVALLRNSINLAVKQLKDwMAPDKAktsL 97
Cdd:cd07095 10 RAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQT-EVAAMAGKIDISIKAYHE-RTGERA---T 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 98 TTFPASAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQY-LDSSAVRVVEGAV 176
Cdd:cd07095 85 PMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAgLPPGVLNLVQGGR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 177 TETTLLLEQKW-DKIFYTGSSRIGRIIMMAAAKHltPVV---LELGGKSPVVIDSDTNLKITAKRIIAGKWgCNNGQAC- 251
Cdd:cd07095 165 ETGEALAAHEGiDGLLFTGSAATGLLLHRQFAGR--PGKilaLEMGGNNPLVVWDVADIDAAAYLIVQSAF-LTAGQRCt 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 252 -----ISPDyilttKEFSPKVIDALKQELEAFYGKNPMESKD-MSRIVNSNHFDRLskmleEKEVSDKIVYGGQK----- 320
Cdd:cd07095 242 carrlIVPD-----GAVGDAFLERLVEAAKRLRIGAPDAEPPfMGPLIIAAAAARY-----LLAQQDLLALGGEPllame 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 321 --NRDKLKIAPTILvDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGgiV 398
Cdd:cd07095 312 rlVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAG--I 388
|
410 420
....*....|....*....|...
gi 1824090424 399 VN-DIAVHLAVPTLPFGGVGESG 420
Cdd:cd07095 389 VNwNRPTTGASSTAPFGGVGLSG 411
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
30-426 |
1.13e-33 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 133.09 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 30 EWRVTQLKKLLLICDNHEPEIVSALHDDLGKPELESSVyEVALLRNSINLAVKQLKDWMAPDKAKTSLTtfPASAEIVYE 109
Cdd:cd07083 77 EDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAID-DVAEAIDFIRYYARAALRLRYPAVEVVPYP--GEDNESFYV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 110 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQY-LDSSAVRVV--EGAVTETTLLLEQK 186
Cdd:cd07083 154 GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAgFPPGVVQFLpgVGEEVGAYLTEHER 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 187 WDKIFYTGSSRIGRIIMMAAAKHLT------PVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGcNNGQACISPDYILTT 260
Cdd:cd07083 234 IRGINFTGSLETGKKIYEAAARLAPgqtwfkRLYVETGGKNAIIVDETADFELVVEGVVVSAFG-FQGQKCSAASRLILT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 261 KEFSPKVIDALKQELEAFYGKNPMESK-DMSRIVNSNHFDRLSKMLEEKEVSDKIVYGGQK-NRDKLKIAPTILVDVPLD 338
Cdd:cd07083 313 QGAYEPVLERLLKRAERLSVGPPEENGtDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGKRlEGEGYFVAPTVVEEVPPK 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 339 SQIMSEEIFGPLLPVITL--NNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNDIAVHLAVPTLPFGGV 416
Cdd:cd07083 393 ARIAQEEIFGPVLSVIRYkdDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGF 472
|
410
....*....|
gi 1824090424 417 GESGMGSYHG 426
Cdd:cd07083 473 KLSGTNAKTG 482
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
109-440 |
1.65e-31 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 126.53 E-value: 1.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 109 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLL-EQYLDSSAVRVVEGAVTETTLLLEQ-K 186
Cdd:PRK13252 141 EPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYtEAGLPDGVFNVVQGDGRVGAWLTEHpD 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 187 WDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGkwgcN---NGQACISPDYILTTKEF 263
Cdd:PRK13252 221 IAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLA----NfysSGQVCTNGTRVFVQKSI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 264 SPKVIDALKQELEAFYGKNPM-ESKDMSRIVNSNHFDRLSKMLEE-KEVSDKIVYGGQKNRDKLK-----IAPTILVDVP 336
Cdd:PRK13252 297 KAAFEARLLERVERIRIGDPMdPATNFGPLVSFAHRDKVLGYIEKgKAEGARLLCGGERLTEGGFangafVAPTVFTDCT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 337 LDSQIMSEEIFGPLLPVITLNNLEEcfdVIR---SRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNdiAVHLAVPTLPF 413
Cdd:PRK13252 377 DDMTIVREEIFGPVMSVLTFDDEDE---VIAranDTEYGLAAGVFTADLSRAHRVIHQLEAGICWIN--TWGESPAEMPV 451
|
330 340
....*....|....*....|....*..
gi 1824090424 414 GGVGESGMGSYHGKFSFDAFSHKKAVL 440
Cdd:PRK13252 452 GGYKQSGIGRENGIATLEHYTQIKSVQ 478
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
109-439 |
2.33e-31 |
|
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: 126.07 E-value: 2.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 109 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKL-LEQYLDSSAVRVVEGAVTETTLLLEQKW 187
Cdd:cd07140 146 EPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELtVKAGFPKGVINILPGSGSLVGQRLSDHP 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 188 D--KIFYTGSSRIGRIIMMAAAK-HLTPVVLELGGKSPVVIDSDTNLKiTAKRIIAGKWGCNNGQACISPDYILTTKEFS 264
Cdd:cd07140 226 DvrKLGFTGSTPIGKHIMKSCAVsNLKKVSLELGGKSPLIIFADCDMD-KAVRMGMSSVFFNKGENCIAAGRLFVEESIH 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 265 PKVIDALKQELEAFYGKNPME-SKDMSrivNSNHFDRLSKMLE--EKEVSD--KIVYGG-QKNRDKLKIAPTILVDVPLD 338
Cdd:cd07140 305 DEFVRRVVEEVKKMKIGDPLDrSTDHG---PQNHKAHLDKLVEycERGVKEgaTLVYGGkQVDRPGFFFEPTVFTDVEDH 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 339 SQIMSEEIFGPLLPVITLNNlEECFDVIRSRPKP---LAAYLFTQNQKLKERFALTVSAGGIVVN-----DIAVhlavpt 410
Cdd:cd07140 382 MFIAKEESFGPIMIISKFDD-GDVDGVLQRANDTeygLASGVFTKDINKALYVSDKLEAGTVFVNtynktDVAA------ 454
|
330 340
....*....|....*....|....*....
gi 1824090424 411 lPFGGVGESGMGSYHGKFSFDAFSHKKAV 439
Cdd:cd07140 455 -PFGGFKQSGFGKDLGEEALNEYLKTKTV 482
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
2-430 |
5.10e-31 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 124.85 E-value: 5.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 2 VKVFQAADATDLVTELRRS---FDDGVTRGYEWRVTQLKKLLLICDNHEPEIVSALHDDLGKPeLESSVYEVALlrnsin 78
Cdd:PRK09406 14 VKTFTALTDDEVDAAIARAharFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKT-LASAKAEALK------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 79 lAVKQLKdWMApDKAKTSLTTFPASAEIV--------YEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAP 150
Cdd:PRK09406 87 -CAKGFR-YYA-EHAEALLADEPADAAAVgasrayvrYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 151 ASSSLLAKLLEQ-----------YLDSSAVRVV--EGAVTETTLlleqkwdkifyTGSSRIGRIIMMAAAKHLTPVVLEL 217
Cdd:PRK09406 164 QTALYLADLFRRagfpdgcfqtlLVGSGAVEAIlrDPRVAAATL-----------TGSEPAGRAVAAIAGDEIKKTVLEL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 218 GGKSPVVIDSDTNLKITAKRIIAGKwgC-NNGQACISPDYILTTKEFSPKVIDALKQELEAFYGKNPM-ESKDMSRIVNS 295
Cdd:PRK09406 233 GGSDPFIVMPSADLDRAAETAVTAR--VqNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTdPDTDVGPLATE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 296 NHFDRLSKMLEEK-EVSDKIVYGGQK-NRDKLKIAPTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPL 373
Cdd:PRK09406 311 QGRDEVEKQVDDAvAAGATILCGGKRpDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGL 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 374 AAYLFTQNQKLKERFALTVSAGGIVVNDIAVhlAVPTLPFGGVGESGMG---SYHGKFSF 430
Cdd:PRK09406 391 GSNAWTRDEAEQERFIDDLEAGQVFINGMTV--SYPELPFGGVKRSGYGrelSAHGIREF 448
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
106-433 |
1.97e-30 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 123.48 E-value: 1.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 106 IVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQY-LDSSAVRVVEGAVTET--TLL 182
Cdd:PRK11241 142 VIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAgIPAGVFNVVTGSAGAVggELT 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 183 LEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGcNNGQACISPDYILTTKe 262
Cdd:PRK11241 222 SNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFR-NAGQTCVCANRLYVQD- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 263 fspKVIDALKQELEAFYGKNPMESKDMSRIVNSNHFDRLSKMLEEKEVSD------KIVYGGQKN-RDKLKIAPTILVDV 335
Cdd:PRK11241 300 ---GVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADalekgaRVVCGGKAHeLGGNFFQPTILVDV 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 336 PLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAG------GIVVNDIAvhlavp 409
Cdd:PRK11241 377 PANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGivgintGIISNEVA------ 450
|
330 340
....*....|....*....|....
gi 1824090424 410 tlPFGGVGESGMGSYHGKFSFDAF 433
Cdd:PRK11241 451 --PFGGIKASGLGREGSKYGIEDY 472
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
109-425 |
3.00e-28 |
|
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: 116.90 E-value: 3.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 109 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLL-EQYLDSSAVRVVEGAVTETTLLLEQKW 187
Cdd:TIGR01722 135 QPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFsEAGAPDGVLNVVHGDKEAVDRLLEHPD 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 188 DK-IFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGCnNGQACISPDYIL---TTKEF 263
Cdd:TIGR01722 215 VKaVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGA-AGQRCMAISAAVlvgAADEW 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 264 SPKVIDALKQeLEAFYGKNPmeSKDMSRIVNSNHFDRLSKMLEE--KE----VSDKIVYGGQKNRDKLKIAPTILVDVPL 337
Cdd:TIGR01722 294 VPEIRERAEK-IRIGPGDDP--GAEMGPLITPQAKDRVASLIAGgaAEgaevLLDGRGYKVDGYEEGNWVGPTLLERVPP 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 338 DSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNdIAVHLAVPTLPFGGVG 417
Cdd:TIGR01722 371 TMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVN-VPIPVPLPYFSFTGWK 449
|
....*...
gi 1824090424 418 ESGMGSYH 425
Cdd:TIGR01722 450 DSFFGDHH 457
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
107-422 |
1.07e-27 |
|
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: 115.38 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 107 VYEPLGVVLVISAWNYPFllsidPVIG---AISA--GNAVVLKPSELAP----ASSSLLAKLLEQY-LDSSAVRVVEGAV 176
Cdd:cd07130 129 QWNPLGVVGVITAFNFPV-----AVWGwnaAIALvcGNVVVWKPSPTTPltaiAVTKIVARVLEKNgLPGAIASLVCGGA 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 177 TETTLLLE-QKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGcNNGQACISPD 255
Cdd:cd07130 204 DVGEALVKdPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVG-TAGQRCTTTR 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 256 YILTTKefspKVIDALKQELEAFYGK----NPMESKD-MSRIVNSNHFDRLSKMLEE-KEVSDKIVYGGQK-NRDKLKIA 328
Cdd:cd07130 283 RLIVHE----SIYDEVLERLKKAYKQvrigDPLDDGTlVGPLHTKAAVDNYLAAIEEaKSQGGTVLFGGKViDGPGNYVE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 329 PTIlVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERF-ALTVSAGGIV-VNdiavhl 406
Cdd:cd07130 359 PTI-VEGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWlGPKGSDCGIVnVN------ 431
|
330 340
....*....|....*....|..
gi 1824090424 407 aVPTL------PFGGVGESGMG 422
Cdd:cd07130 432 -IGTSgaeiggAFGGEKETGGG 452
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
25-439 |
3.29e-26 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 110.72 E-value: 3.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 25 VTRGY-EWRVT-------QLKKLLLICDNHEPEIVSALHDDLGKPELESSVyEVAllrNSINLAvkqlkDWMApDKAKTS 96
Cdd:PRK13968 38 AAAGFrDWRETnidyraqKLRDIGKALRARSEEMAQMITREMGKPINQARA-EVA---KSANLC-----DWYA-EHGPAM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 97 LTTFPASAE-----IVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEqylDSSAVRV 171
Cdd:PRK13968 108 LKAEPTLVEnqqavIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFK---DAGIPQG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 172 VEGAVTETT-----LLLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGcN 246
Cdd:PRK13968 185 VYGWLNADNdgvsqMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQ-N 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 247 NGQAC-ISPDYIL---TTKEFSPKVIDALKQ-------ELEAFYGknPMESKDMSrivnsnhfDRLSKMLeEKEVSD--K 313
Cdd:PRK13968 264 TGQVCaAAKRFIIeegIASAFTERFVAAAAAlkmgdprDEENALG--PMARFDLR--------DELHHQV-EATLAEgaR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 314 IVYGGQKNRDKLKI-APTILVDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTV 392
Cdd:PRK13968 333 LLLGGEKIAGAGNYyAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARL 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1824090424 393 SAGGIVVNDIAVhlAVPTLPFGGVGESGMGSYHGKFSFDAFSHKKAV 439
Cdd:PRK13968 413 ECGGVFINGYCA--SDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
107-439 |
1.26e-25 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 110.22 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 107 VYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKL-LEQYLDSSAVRVVEGAV-TETTLLLE 184
Cdd:PLN02419 246 IREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELaMEAGLPDGVLNIVHGTNdTVNAICDD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 185 QKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGCNnGQACISPD---YILTTK 261
Cdd:PLN02419 326 EDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAA-GQRCMALStvvFVGDAK 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 262 EFSPKVIDALKQeLEAFYGKNPmeSKDMSRIVNSNHFDRLSKMLEEK---------EVSDKIVYGGQKNRdklKIAPTIL 332
Cdd:PLN02419 405 SWEDKLVERAKA-LKVTCGSEP--DADLGPVISKQAKERICRLIQSGvddgaklllDGRDIVVPGYEKGN---FIGPTIL 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 333 VDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNdIAVHLAVPTLP 412
Cdd:PLN02419 479 SGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN-VPIPVPLPFFS 557
|
330 340
....*....|....*....|....*....
gi 1824090424 413 FGGVGESGMG--SYHGKFSFDAFSHKKAV 439
Cdd:PLN02419 558 FTGNKASFAGdlNFYGKAGVDFFTQIKLV 586
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
6-420 |
6.79e-25 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 107.35 E-value: 6.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 6 QAADATDL---VTELRRSFDDGVTRGYEWRVTQLKKLLLICDNHEPEIVSALHDDLGKPELESSVyEVALLRNSINLAVK 82
Cdd:PRK09457 32 NDATAAQVdaaVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAAT-EVTAMINKIAISIQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 83 QLKDWMAPDKAKTSlttfPASAEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQ 162
Cdd:PRK09457 111 AYHERTGEKRSEMA----DGAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 163 Y-LDSSAVRVVEGAV-TETTLLLEQKWDKIFYTGSSRIGRIIMMAAAKHltP---VVLELGGKSPVVIDSDTNLKITAKR 237
Cdd:PRK09457 187 AgLPAGVLNLVQGGReTGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQ--PekiLALEMGGNNPLVIDEVADIDAAVHL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 238 IIAGKWgCNNGQACISPDYILTTK-----EFSPKVIDALKQ--------ELEAFYGknPMES-KDMSRIVNSNHfdrlsK 303
Cdd:PRK09457 265 IIQSAF-ISAGQRCTCARRLLVPQgaqgdAFLARLVAVAKRltvgrwdaEPQPFMG--AVISeQAAQGLVAAQA-----Q 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 304 MLEEKEVSdkIVYGGQKNRDKLKIAPTILvDVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQK 383
Cdd:PRK09457 337 LLALGGKS--LLEMTQLQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDRE 413
|
410 420 430
....*....|....*....|....*....|....*...
gi 1824090424 384 LKERFALTVSAGgiVVN-DIAVHLAVPTLPFGGVGESG 420
Cdd:PRK09457 414 DYDQFLLEIRAG--IVNwNKPLTGASSAAPFGGVGASG 449
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
105-422 |
7.72e-23 |
|
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: 101.12 E-value: 7.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 105 EIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLL-EQYLDSSAVRVV--EGAVTETTL 181
Cdd:cd07125 162 GLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLhEAGVPRDVLQLVpgDGEEIGEAL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 182 LLEQKWDKIFYTGSSRIGRII--MMAAAKH-LTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGcNNGQACISPDYIL 258
Cdd:cd07125 242 VAHPRIDGVIFTGSTETAKLInrALAERDGpILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFG-SAGQRCSALRLLY 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 259 TTKEFSPKVIDALKQELEAFYGKNPMESK-DMSRIVNSNHFDRLSKMLEEKEVSDKIVYGGQKNRDK--LkIAPTILVDV 335
Cdd:cd07125 321 LQEEIAERFIEMLKGAMASLKVGDPWDLStDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDGNgyF-VAPGIIEIV 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 336 PLDSqiMSEEIFGPLLPVIT--LNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVN-DI--AVhlaVPT 410
Cdd:cd07125 400 GIFD--LTTEVFGPILHVIRfkAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINrNItgAI---VGR 474
|
330
....*....|..
gi 1824090424 411 LPFGGVGESGMG 422
Cdd:cd07125 475 QPFGGWGLSGTG 486
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
4-426 |
6.85e-21 |
|
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: 95.36 E-value: 6.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 4 VFQAADAtdlvtELRRSFDDGVTRGYEW-------RVTQLKKLLLICDNHEPEIVSALHDDLGKpELESSVYEVALLRNS 76
Cdd:TIGR01238 68 VFHANLA-----HVQAAIDSAQQAFPTWnatpakeRAAKLDRLADLLELHMPELMALCVREAGK-TIHNAIAEVREAVDF 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 77 INLAVKQLKDwmapdkaktsltTFPasaEIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAP-ASSSL 155
Cdd:TIGR01238 142 CRYYAKQVRD------------VLG---EFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSlIAYRA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 156 LAKLLEQYLDSSAVRVVEGAVTE--TTLLLEQKWDKIFYTGSSRIGRIIMMAAAKHL---TPVVLELGGKSPVVIDSDTN 230
Cdd:TIGR01238 207 VELMQEAGFPAGTIQLLPGRGADvgAALTSDPRIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTAL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 231 LKITAKRIIAGKWGcNNGQACISPDYILTTKEFSPKVIDALKQELEAFYGKNPME-SKDMSRIVNSNHFDRLSKMLEEKE 309
Cdd:TIGR01238 287 PEQVVRDVLRSAFD-SAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLlTTDVGPVIDAEAKQNLLAHIEHMS 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 310 VSDKIVYggQKNRDKLK-------IAPTILvdvPLDS-QIMSEEIFGPLLPVITL--NNLEECFDVIRSRPKPLAAYLFT 379
Cdd:TIGR01238 366 QTQKKIA--QLTLDDSRacqhgtfVAPTLF---ELDDiAELSEEVFGPVLHVVRYkaRELDQIVDQINQTGYGLTMGVHS 440
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1824090424 380 QNQKLKERFALTVSAGGIVVNDIAVHLAVPTLPFGGVGESGMGSYHG 426
Cdd:TIGR01238 441 RIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFGGQGLSGTGPKAG 487
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
107-436 |
6.67e-19 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 89.12 E-value: 6.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 107 VYEPLGVVLVISAWNYP-FLLSIDPVIgAISAGNAVVLKPSELAP----ASSSLLAKLLEQYLDSSAV--RVVEGAVTET 179
Cdd:PLN02315 151 VWNPLGIVGVITAFNFPcAVLGWNACI-ALVCGNCVVWKGAPTTPlitiAMTKLVAEVLEKNNLPGAIftSFCGGAEIGE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 180 TLLLEQKWDKIFYTGSSRIGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGcNNGQACISPDYILT 259
Cdd:PLN02315 230 AIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVG-TAGQRCTTCRRLLL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 260 TKEFSPKVIDALKQELEAFYGKNPMESKDMSRIVNSNHF-DRLSKMLEE-KEVSDKIVYGGQK-NRDKLKIAPTIlVDVP 336
Cdd:PLN02315 309 HESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESkKNFEKGIEIiKSQGGKILTGGSAiESEGNFVQPTI-VEIS 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 337 LDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERF-ALTVSAGGIVVNDIAVHLAVPTLPFGG 415
Cdd:PLN02315 388 PDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWiGPLGSDCGIVNVNIPTNGAEIGGAFGG 467
|
330 340
....*....|....*....|.
gi 1824090424 416 VGESGMGSYHGKFSFDAFSHK 436
Cdd:PLN02315 468 EKATGGGREAGSDSWKQYMRR 488
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
32-423 |
7.07e-18 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 85.96 E-value: 7.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 32 RVTQLKKLLLICDNHEPEIVSALHDDLGKPeLESSVYEVALLRNSINLAVKQLKDWMAPDKAKTSlTTFPASAEIVY--- 108
Cdd:PLN00412 77 RAELLHKAAAILKEHKAPIAECLVKEIAKP-AKDAVTEVVRSGDLISYTAEEGVRILGEGKFLVS-DSFPGNERNKYclt 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 109 --EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQY-LDSSAVRVVEGAVTETT--LLL 183
Cdd:PLN00412 155 skIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAgFPKGLISCVTGKGSEIGdfLTM 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 184 EQKWDKIFYTGSSrIGriIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKWGcNNGQACISPDYILTTKEF 263
Cdd:PLN00412 235 HPGVNCISFTGGD-TG--IAISKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFS-YSGQRCTAVKVVLVMESV 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 264 SPKVIDALKQELEAFYGKNPMESKDMSRIVNSNHFDRLSKMLEEKEVSDKIVYGGQKNRDKLkIAPTILVDVPLDSQIMS 343
Cdd:PLN00412 311 ADALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKREGNL-IWPLLLDNVRPDMRIAW 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 344 EEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVNdiavhlAVPT-----LPFGGVGE 418
Cdd:PLN00412 390 EEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQIN------SAPArgpdhFPFQGLKD 463
|
....*
gi 1824090424 419 SGMGS 423
Cdd:PLN00412 464 SGIGS 468
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
108-420 |
6.15e-15 |
|
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: 76.86 E-value: 6.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 108 YEPL-GVVLVISAWNYPFL---LSIDPVIgaisAGNAVVLKPSELAPASSSLLAKLLEQY-LDSSAVRVV--EGAVTETT 180
Cdd:cd07123 167 YRPLeGFVYAVSPFNFTAIggnLAGAPAL----MGNVVLWKPSDTAVLSNYLVYKILEEAgLPPGVINFVpgDGPVVGDT 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 181 LLLEQKWDKIFYTGSSRIGRIIMMAAAKHLT-----P-VVLELGGKSPVVIDSDTNLKITAKRIIAGKWGcNNGQAC--I 252
Cdd:cd07123 243 VLASPHLAGLHFTGSTPTFKSLWKQIGENLDryrtyPrIVGETGGKNFHLVHPSADVDSLVTATVRGAFE-YQGQKCsaA 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 253 SPDYIltTKEFSPKVIDALKQELEAFYGKNPME-SKDMSRIVNSNHFDRLSKMLEEKEVSD--KIVYGGqkNRDKLK--- 326
Cdd:cd07123 322 SRAYV--PESLWPEVKERLLEELKEIKMGDPDDfSNFMGAVIDEKAFDRIKGYIDHAKSDPeaEIIAGG--KCDDSVgyf 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 327 IAPTILVDVPLDSQIMSEEIFGPLLPVITL--NNLEECFDVI-RSRPKPLAAYLFTQNQK--LKERFALTVSAGGIVVND 401
Cdd:cd07123 398 VEPTVIETTDPKHKLMTEEIFGPVLTVYVYpdSDFEETLELVdTTSPYALTGAIFAQDRKaiREATDALRNAAGNFYIND 477
|
330
....*....|....*....
gi 1824090424 402 IAVHLAVPTLPFGGVGESG 420
Cdd:cd07123 478 KPTGAVVGQQPFGGARASG 496
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
110-349 |
2.51e-14 |
|
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: 74.97 E-value: 2.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 110 PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQ--YLDSSAVRVVEG-AVTETTLLLEQK 186
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYagLLPPEDVTLINGdGKTMQALLLHPN 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 187 WDKIFYTGSSRIGRiiMMAAAKHLTPVVLELGGKSPVVIDSDTN-LKITAKRIIAGKWGCnNGQACISPDYILTTKEFS- 264
Cdd:cd07084 180 PKMVLFTGSSRVAE--KLALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTAC-SGQKCTAQSMLFVPENWSk 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 265 PKVIDALKQELEafygKNPMESKDMSRIVNSNHFDRLSKMleEKEVSDKIVYGGQ--KNRDKLKI-----APTILVDVPL 337
Cdd:cd07084 257 TPLVEKLKALLA----RRKLEDLLLGPVQTFTTLAMIAHM--ENLLGSVLLFSGKelKNHSIPSIygacvASALFVPIDE 330
|
250
....*....|....*
gi 1824090424 338 D---SQIMSEEIFGP 349
Cdd:cd07084 331 IlktYELVTEEIFGP 345
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
110-410 |
4.27e-12 |
|
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: 67.95 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 110 PLGVVLVISAWNYPFLLSidpVIG-----AISAGNAVVLKPSELAPASSSLLAKLLEQYLDSSA-----VRVVEGAVTET 179
Cdd:cd07129 105 PLGPVAVFGASNFPLAFS---VAGgdtasALAAGCPVVVKAHPAHPGTSELVARAIRAALRATGlpagvFSLLQGGGREV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 180 TLLLEQkwDK----IFYTGSSRIGRIIMMAAAKHLT--PVVLELGGKSPVVI-------DSDTnlkitakriIAGKW--- 243
Cdd:cd07129 182 GVALVK--HPaikaVGFTGSRRGGRALFDAAAARPEpiPFYAELGSVNPVFIlpgalaeRGEA---------IAQGFvgs 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 244 ---GCnnGQACISPDYILTTK-EFSPKVIDALKQELEAFyGKNPMESkdmSRIVNSnhFDR-LSKMLEEKEVSdkIVYGG 318
Cdd:cd07129 251 ltlGA--GQFCTNPGLVLVPAgPAGDAFIAALAEALAAA-PAQTMLT---PGIAEA--YRQgVEALAAAPGVR--VLAGG 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 319 QKNRDKLKIAPTILV---DVPLDSQIMSEEIFGPLLPVITLNNLEECFDVIRSRPKPLAAYLFTQNQKLKE----RFALT 391
Cdd:cd07129 321 AAAEGGNQAAPTLFKvdaAAFLADPALQEEVFGPASLVVRYDDAAELLAVAEALEGQLTATIHGEEDDLALarelLPVLE 400
|
330
....*....|....*....
gi 1824090424 392 VSAGGIVVNdiavhlAVPT 410
Cdd:cd07129 401 RKAGRLLFN------GWPT 413
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
109-422 |
8.37e-11 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 64.50 E-value: 8.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 109 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSElapaSSSLLA----KLLEQY-LDSSAVRVV--EGAVTETTL 181
Cdd:PRK11905 675 KPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAE----QTPLIAaravRLLHEAgVPKDALQLLpgDGRTVGAAL 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 182 LLEQKWDKIFYTGSSRIGRIIMMAAAKHL---TPVVLELGGKSPVVIDSdtnlkiTA------KRIIAGKWGcNNGQACi 252
Cdd:PRK11905 751 VADPRIAGVMFTGSTEVARLIQRTLAKRSgppVPLIAETGGQNAMIVDS------SAlpeqvvADVIASAFD-SAGQRC- 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 253 SPDYILTTKE-FSPKVIDALKQELEAFYGKNPME-SKDMSRIVNSNHFDRLSKMLEEKEVSDKIVYGGQKNRDKLK---I 327
Cdd:PRK11905 823 SALRVLCLQEdVADRVLTMLKGAMDELRIGDPWRlSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHQLPLPAETEKgtfV 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 328 APTILvdvPLDS-QIMSEEIFGPLLPVITL--NNLEECFDVIRSRPKPLAAYLFTqnqKLKERFALTVS---AGGIVVND 401
Cdd:PRK11905 903 APTLI---EIDSiSDLEREVFGPVLHVVRFkaDELDRVIDDINATGYGLTFGLHS---RIDETIAHVTSrirAGNIYVNR 976
|
330 340
....*....|....*....|.
gi 1824090424 402 IAVHLAVPTLPFGGVGESGMG 422
Cdd:PRK11905 977 NIIGAVVGVQPFGGEGLSGTG 997
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
106-361 |
1.97e-10 |
|
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: 62.67 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 106 IVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQ-YLDSSAVRVVEGAVTETTLLLE 184
Cdd:cd07081 91 IIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQaAVAAGAPENLIGWIDNPSIELA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 185 QK------WDKIFYTGssriGRIIMMAAAKHLTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKwGCNNGQACISPDYIL 258
Cdd:cd07081 171 QRlmkfpgIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSK-TFDNGVICASEQSVI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 259 TTKEfspkVIDALKQELEAFYGknpmeskdmsRIVNSNHFDRLSK-MLEEKEVSDKIVyggqkNRDKLKIAPTILVDVPL 337
Cdd:cd07081 246 VVDS----VYDEVMRLFEGQGA----------YKLTAEELQQVQPvILKNGDVNRDIV-----GQDAYKIAAAAGLKVPQ 306
|
250 260 270
....*....|....*....|....*....|....*..
gi 1824090424 338 DSQIM-------------SEEIFGPLLPVITLNNLEE 361
Cdd:cd07081 307 ETRILigevtslaehepfAHEKLSPVLAMYRAANFAD 343
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
105-276 |
3.95e-09 |
|
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: 58.39 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 105 EIVYEPLGVVLVISAWNYPfLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQYLDSSAVRVVEGAVTETTLLLE 184
Cdd:cd07077 95 YVRAFPIGVTMHILPSTNP-LSGITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAADAAHGPKILVLYVPHPSDELA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 185 Q------KWDKIFYTGssriGRIIMMAAAKH--LTPVVLELGGKSPVVIDSDTNLKITAKRIIAGKwgCNNGQACISPDY 256
Cdd:cd07077 174 EellshpKIDLIVATG----GRDAVDAAVKHspHIPVIGFGAGNSPVVVDETADEERASGSVHDSK--FFDQNACASEQN 247
|
170 180
....*....|....*....|
gi 1824090424 257 ILttkeFSPKVIDALKQELE 276
Cdd:cd07077 248 LY----VVDDVLDPLYEEFK 263
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
108-227 |
3.97e-09 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 59.22 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 108 YEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAP-ASSSLLAKLLEQYLDSSAVRVVEGAvTETT---LLL 183
Cdd:PRK11809 766 HRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPlIAAQAVRILLEAGVPAGVVQLLPGR-GETVgaaLVA 844
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1824090424 184 EQKWDKIFYTGSSRIGRIIMMAAAKHL------TPVVLELGGKSPVVIDS 227
Cdd:PRK11809 845 DARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDS 894
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
105-422 |
9.36e-09 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 57.90 E-value: 9.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 105 EIVYEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLL-EQYLDSSAVRVV--EGAVTETTL 181
Cdd:PRK11904 679 ELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLhEAGIPKDVLQLLpgDGATVGAAL 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 182 LLEQKWDKIFYTGSSRIGRIIMMA-AAKHLTPVVL--ELGGKSPVVIDSdtnlkiTA------KRIIAGKWGcNNGQACI 252
Cdd:PRK11904 759 TADPRIAGVAFTGSTETARIINRTlAARDGPIVPLiaETGGQNAMIVDS------TAlpeqvvDDVVTSAFR-SAGQRCS 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 253 SPDYILTTKEFSPKVIDALK---QELEAfyGkNPME-SKDMSRIVNSNHFDRLSKMLEEKEVSDKIVYGGQKNRDKLK-- 326
Cdd:PRK11904 832 ALRVLFVQEDIADRVIEMLKgamAELKV--G-DPRLlSTDVGPVIDAEAKANLDAHIERMKREARLLAQLPLPAGTENgh 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 327 -IAPTIlvdVPLDS-QIMSEEIFGPLLPVITLN--NLEECFDVIRSRPKPLAAYLFTQNQKLKERFALTVSAGGIVVN-D 401
Cdd:PRK11904 909 fVAPTA---FEIDSiSQLEREVFGPILHVIRYKasDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNrN 985
|
330 340
....*....|....*....|...
gi 1824090424 402 I--AVhlaVPTLPFGGVGESGMG 422
Cdd:PRK11904 986 QigAV---VGVQPFGGQGLSGTG 1005
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
109-417 |
7.68e-07 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 51.34 E-value: 7.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 109 EPLGVVL-VISAWNyPFLLSIDPVIGAISAGNAVVLKPSELAPASSSLLAKLLEQYLDSS-----AVRVVEGAVTETTLL 182
Cdd:cd07122 94 EPVGVIAaLIPSTN-PTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAAVAAgapegLIQWIEEPSIELTQE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 183 L--EQKWDKIFYTGSSrigriIMMAAA-KHLTPVvleLG---GKSPVVIDSDTNLKITAKRIIAGKwGCNNGQACISPDY 256
Cdd:cd07122 173 LmkHPDVDLILATGGP-----GMVKAAySSGKPA---IGvgpGNVPAYIDETADIKRAVKDIILSK-TFDNGTICASEQS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 257 ILTTKEFSPKVIDALKQELEAFYgkNPMESKDMSRIVnsnhFDrlskmlEEKEVSDKIVygGQKNRdklKIAPTILVDVP 336
Cdd:cd07122 244 VIVDDEIYDEVRAELKRRGAYFL--NEEEKEKLEKAL----FD------DGGTLNPDIV--GKSAQ---KIAELAGIEVP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824090424 337 LDSQI-------------MSEEIFGPLLPVITLNNLEECFDVIRSrpkpLAAY--------LFTQNQKLKERFALTVSAG 395
Cdd:cd07122 307 EDTKVlvaeetgvgpeepLSREKLSPVLAFYRAEDFEEALEKARE----LLEYggaghtavIHSNDEEVIEEFALRMPVS 382
|
330 340
....*....|....*....|..
gi 1824090424 396 GIVVNDIAvhlavptlPFGGVG 417
Cdd:cd07122 383 RILVNTPS--------SLGGIG 396
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
103-150 |
1.76e-06 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 50.71 E-value: 1.76e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1824090424 103 SAEIVYEPLGVVLVISAWNYPflLSIdpVIG----AISAGNAVVLKPSELAP 150
Cdd:COG4230 673 AAPTVLRGRGVFVCISPWNFP--LAI--FTGqvaaALAAGNTVLAKPAEQTP 720
|
|
| |
