|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
20-447 |
0e+00 |
|
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: 678.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 20 AQRSHAKAAGIENYQQRREHLLALKAMITENQARIIEAINQDYGNRSRHETLLAEIINACADINSTLKHLKKWMKVQKRH 99
Cdd:cd07133 6 RQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFGHRSRHETLLAEILPSIAGIKHARKHLKKWMKPSRRH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 100 VDhRMYLGAKSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNYFKPEKLQFYC 179
Cdd:cd07133 86 VG-LLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEVAVVT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 180 ETGEVGIAFSKLPFDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNV 259
Cdd:cd07133 165 GGADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 260 DYVFVHQSQLALFIDTATRWAKKHVPDI-HSQDYTAIIDDRAFKRLTNCIEEAKQLGADVITLSDQVAD-ANTRKLPLTL 337
Cdd:cd07133 245 DYVLVPEDKLEEFVAAAKAAVAKMYPTLaDNPDYTSIINERHYARLQGLLEDARAKGARVIELNPAGEDfAATRKLPPTL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 338 ILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDALFHVGQHDL 417
Cdd:cd07133 325 VLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHVAQDDL 404
|
410 420 430
....*....|....*....|....*....|
gi 1859350786 418 PFGGVGASGMGHYHGYEGFLTFSKLRPVFY 447
Cdd:cd07133 405 PFGGVGASGMGAYHGKEGFLTFSHAKPVFK 434
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
16-447 |
9.01e-161 |
|
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: 461.61 E-value: 9.01e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 16 ADLVA-QRSHAKAAGIENYQQRREHLLALKAMITENQARIIEAINQDYGnRSRHETLLAEIINACADINSTLKHLKKWMK 94
Cdd:cd07087 1 AELVArLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLG-KPPAEAYLTEIAVVLGEIDHALKHLKKWMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 95 vqKRHVD-HRMYLGAKSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNYFKPE 173
Cdd:cd07087 80 --PRRVSvPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 174 KLQFYCETGEVGIAFSKLPFDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAG 253
Cdd:cd07087 158 AVAVVEGGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 254 QICTNVDYVFVHQSQLALFIDTATRWAKKHVPD--IHSQDYTAIIDDRAFKRLTNCIEEAKQL-GADVitlsdqvaDANT 330
Cdd:cd07087 238 QTCIAPDYVLVHESIKDELIEELKKAIKEFYGEdpKESPDYGRIINERHFDRLASLLDDGKVViGGQV--------DKEE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 331 RKLPLTLILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDALF 410
Cdd:cd07087 310 RYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLL 389
|
410 420 430
....*....|....*....|....*....|....*..
gi 1859350786 411 HVGQHDLPFGGVGASGMGHYHGYEGFLTFSKLRPVFY 447
Cdd:cd07087 390 HAAIPNLPFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
20-446 |
2.13e-140 |
|
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: 410.08 E-value: 2.13e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 20 AQRSHAKAAGIENYQQRREHLLALKAMITENQARIIEAINQDYGnRSRHETLLAEIINACADINSTLKHLKKWMKVQKRH 99
Cdd:cd07134 6 AQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFR-KPAAEVDLTEILPVLSEINHAIKHLKKWMKPKRVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 100 vDHRMYLGAKSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNYFkPEKLQFYC 179
Cdd:cd07134 85 -TPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAF-DEDEVAVF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 180 ETG-EVGIAFSKLPFDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTN 258
Cdd:cd07134 163 EGDaEVAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 259 VDYVFVHQSQLALFIDTATRWAKKH----VPDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADVITLSDqvADANTRKLP 334
Cdd:cd07134 243 PDYVFVHESVKDAFVEHLKAEIEKFygkdAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQ--FDAAQRYIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 335 LTLILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDALFHVGQ 414
Cdd:cd07134 321 PTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLN 400
|
410 420 430
....*....|....*....|....*....|..
gi 1859350786 415 HDLPFGGVGASGMGHYHGYEGFLTFSKLRPVF 446
Cdd:cd07134 401 PNLPFGGVNNSGIGSYHGVYGFKAFSHERAVL 432
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
34-446 |
5.95e-134 |
|
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: 393.89 E-value: 5.95e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 34 QQRREHLLALKAMITENQARIIEAINQDYGnRSRHETLLAEIINACADINSTLKHLKKWMKVQKRHVDHRMYLGAKSRVI 113
Cdd:cd07135 27 EYRLWQLKQLYWAVKDNEEAIVEALKKDLG-RPPFETLLTEVSGVKNDILHMLKNLKKWAKDEKVKDGPLAFMFGKPRIR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 114 PQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNYFKPEklQFYCETGEVG--IAFSKL 191
Cdd:cd07135 106 KEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLDPD--AFQVVQGGVPetTALLEQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 192 PFDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQSQLAL 271
Cdd:cd07135 184 KFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 272 FIDTATRWAKKHVP--DIHSQDYTAIIDDRAFKRLTNCIEEAKQlgaDVITlsDQVADANTRKLPLTLILNSNDSMSIDT 349
Cdd:cd07135 264 FVEELKKVLDEFYPggANASPDYTRIVNPRHFNRLKSLLDTTKG---KVVI--GGEMDEATRFIPPTIVSDVSWDDSLMS 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 350 RETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDALFHVGQHDLPFGGVGASGMGH 429
Cdd:cd07135 339 EELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAPFGGVGDSGYGA 418
|
410
....*....|....*..
gi 1859350786 430 YHGYEGFLTFSKLRPVF 446
Cdd:cd07135 419 YHGKYGFDTFTHERTVV 435
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
33-461 |
1.45e-133 |
|
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: 393.02 E-value: 1.45e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 33 YQQRREHLLALKAMITENQARIIEAINQDYgNRSRHETLLAEIINACADINSTLKHLKKWMKVQKrhVDHRMY-LGAKSR 111
Cdd:cd07136 19 VEFRIEQLKKLKQAIKKYENEILEALKKDL-GKSEFEAYMTEIGFVLSEINYAIKHLKKWMKPKR--VKTPLLnFPSKSY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 112 VIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNYFKPEKLqfYCETG--EVGIAFS 189
Cdd:cd07136 96 IYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYV--AVVEGgvEENQELL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 190 KLPFDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQSQL 269
Cdd:cd07136 174 DQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 270 ALFIDTATRWAKKHVPD--IHSQDYTAIIDDRAFKRLTNCIEEAKQL-GADvitlsdqvADANTRKLPLTLILNSNDSMS 346
Cdd:cd07136 254 EKFIKELKEEIKKFYGEdpLESPDYGRIINEKHFDRLAGLLDNGKIVfGGN--------TDRETLYIEPTILDNVTWDDP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 347 IDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDALFHVGQHDLPFGGVGASG 426
Cdd:cd07136 326 VMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYLPFGGVGNSG 405
|
410 420 430
....*....|....*....|....*....|....*
gi 1859350786 427 MGHYHGYEGFLTFSKLRPVFYQAKFSSVKFLMPPY 461
Cdd:cd07136 406 MGSYHGKYSFDTFSHKKSILKKSTWFDLPLRYPPY 440
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
35-476 |
1.33e-128 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 382.07 E-value: 1.33e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 35 QRREHLLALKAMITENQARIIEAINQDYGnRSRHETLLAEIINACADINSTLKHLKKWMKvqKRHVD-HRMYLGAKSRVI 113
Cdd:PTZ00381 30 FRKQQLRNLLRMLEENKQEFSEAVHKDLG-RHPFETKMTEVLLTVAEIEHLLKHLDEYLK--PEKVDtVGVFGPGKSYII 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 114 PQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNYFKPEKLQFyCETG-EVGIAFSKLP 192
Cdd:PTZ00381 107 PEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPSYVRV-IEGGvEVTTELLKEP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 193 FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQSQLALF 272
Cdd:PTZ00381 186 FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 273 IDTATRWAKKHV-PDI-HSQDYTAIIDDRAFKRLTNCIeeaKQLGADVITLSDqvADANTRKLPLTLILNSNDSMSIDTR 350
Cdd:PTZ00381 266 IEALKEAIKEFFgEDPkKSEDYSRIVNEFHTKRLAELI---KDHGGKVVYGGE--VDIENKYVAPTIIVNPDLDSPLMQE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 351 ETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDALFHVGQHDLPFGGVGASGMGHY 430
Cdd:PTZ00381 341 EIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGGVGNSGMGAY 420
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1859350786 431 HGYEGFLTFSKLRPVFYQAKFSSVKF--LMPPYGRFADKLLAFLSKLN 476
Cdd:PTZ00381 421 HGKYGFDTFSHPKPVLNKSTGNSFDLslRYPPYTSFKSWVLSFLLKLS 468
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
16-461 |
1.52e-110 |
|
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: 334.19 E-value: 1.52e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 16 ADLVAQRSHAKAAGI-ENYQQRREHLLALKAMITENQARIIEAINQDYgNRSRHETLLAEIINACADINSTLKHLKKWMK 94
Cdd:cd07132 1 AEAVRRAREAFSSGKtRPLEFRIQQLEALLRMLEENEDEIVEALAKDL-RKPKFEAVLSEILLVKNEIKYAISNLPEWMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 95 ---VQKRHVDhrmyLGAKSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNYFK 171
Cdd:cd07132 80 pepVKKNLAT----LLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 172 PEKLQFYC----ETGEVgiafSKLPFDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYV 247
Cdd:cd07132 156 KECYPVVLggveETTEL----LKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 248 KQMNAGQICTNVDYVFVHQSQLALFIDTAtrwaKKHVPDI------HSQDYTAIIDDRAFKRLTNCIEEAK-QLGADVit 320
Cdd:cd07132 232 KFINAGQTCIAPDYVLCTPEVQEKFVEAL----KKTLKEFygedpkESPDYGRIINDRHFQRLKKLLSGGKvAIGGQT-- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 321 lsdqvaDANTRKLPLTLILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMS 400
Cdd:cd07132 306 ------DEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSS 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1859350786 401 GGVSVNDALFHVGQHDLPFGGVGASGMGHYHGYEGFLTFSKLRPVFYQA----KFSSVKFlmPPY 461
Cdd:cd07132 380 GGVCVNDTIMHYTLDSLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVKSlnmeKLNSLRY--PPY 442
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
20-445 |
8.87e-98 |
|
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: 301.05 E-value: 8.87e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 20 AQRSHAKAAGIeNYQQRREHLLALKAMITENQARIIEAINQDYGNRsrHETLLAEIINACADINSTLKHLKKWMKVQKRh 99
Cdd:cd07078 7 ARAAFKAWAAL-PPAERAAILRKLADLLEERREELAALETLETGKP--IEEALGEVARAADTFRYYAGLARRLHGEVIP- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 100 vdhRMYLGAKSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNYFKPEK-LQFY 178
Cdd:cd07078 83 ---SPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGvLNVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 179 CETG-EVGIAFSKLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQIC 256
Cdd:cd07078 160 TGDGdEVGAALASHPrVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 257 TNVDYVFVHQSQLALFIDTATRWAKKHV---PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADVITLSDQVADANTRKL 333
Cdd:cd07078 240 TAASRLLVHESIYDEFVERLVERVKALKvgnPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGKGYFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 334 PLTLILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDALFHVG 413
Cdd:cd07078 320 PPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAE 399
|
410 420 430
....*....|....*....|....*....|..
gi 1859350786 414 QHdLPFGGVGASGMGHYHGYEGFLTFSKLRPV 445
Cdd:cd07078 400 PS-APFGGVKQSGIGREGGPYGLEEYTEPKTV 430
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
33-447 |
6.11e-94 |
|
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: 291.24 E-value: 6.11e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 33 YQQRREHLLALKAMITENQARIIEAINQDYGnRSRHETLLAEIINACADINSTLKHLKKWMKVQKRHVDHRMYlGAKSRV 112
Cdd:cd07137 20 AEWRKSQLKGLLRLVDENEDDIFAALRQDLG-KPSAESFRDEVSVLVSSCKLAIKELKKWMAPEKVKTPLTTF-PAKAEI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 113 IPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNYFKPEKLQFYCETGEVGIAFSKLP 192
Cdd:cd07137 98 VSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIKVIEGGVPETTALLEQK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 193 FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVK-QMNAGQICTNVDYVFVHQSQLAL 271
Cdd:cd07137 178 WDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKwGCNNGQACIAPDYVLVEESFAPT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 272 FIDTATRWAKKHVPD--IHSQDYTAIIDDRAFKRLTNCIEEAKQlgADVITLSDQVaDANTRKLPLTLILNSNDSMSIDT 349
Cdd:cd07137 258 LIDALKNTLEKFFGEnpKESKDLSRIVNSHHFQRLSRLLDDPSV--ADKIVHGGER-DEKNLYIEPTILLDPPLDSSIMT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 350 RETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDALFHVGQHDLPFGGVGASGMGH 429
Cdd:cd07137 335 EEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTLPFGGVGESGFGA 414
|
410
....*....|....*...
gi 1859350786 430 YHGYEGFLTFSKLRPVFY 447
Cdd:cd07137 415 YHGKFSFDAFSHKKAVLY 432
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
36-469 |
1.24e-77 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 250.41 E-value: 1.24e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 36 RREHLLALKAMITENQARIIEAINQDYGnRSRHETLLAEIINACADINSTLKHLKKWMKVQKRHVDhRMYLGAKSRVIPQ 115
Cdd:PLN02203 30 RKSQLKGLLRLLKDNEEAIFKALHQDLG-KHRVEAYRDEVGVLTKSANLALSNLKKWMAPKKAKLP-LVAFPATAEVVPE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 116 PLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNYFKPEKLQFYCETGEVGIAFSKLPFDH 195
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAVKVIEGGPAVGEQLLQHKWDK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 196 LMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAV---IATDYPMQKAVERIMYVKQMN-AGQICTNVDYVFVHQSQLAL 271
Cdd:PLN02203 188 IFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIvdsLSSSRDTKVAVNRIVGGKWGScAGQACIAIDYVLVEERFAPI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 272 FIDTATRWAKKHVPD--IHSQDYTAIIDDRAFKRLTNCIEEaKQLGADVItlSDQVADANTRKLPLTLILNSNDSMSIDT 349
Cdd:PLN02203 268 LIELLKSTIKKFFGEnpRESKSMARILNKKHFQRLSNLLKD-PRVAASIV--HGGSIDEKKLFIEPTILLNPPLDSDIMT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 350 RETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDALFHVGQHDLPFGGVGASGMGH 429
Cdd:PLN02203 345 EEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYACDSLPFGGVGESGFGR 424
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1859350786 430 YHGYEGFLTFSKLRPVFYQAKFSSVKFLMPPYGRFADKLL 469
Cdd:PLN02203 425 YHGKYSFDTFSHEKAVLRRSLLTEFEFRYPPWNDFKLGFL 464
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
34-448 |
1.65e-76 |
|
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: 247.35 E-value: 1.65e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 34 QQRREHLLALKAMITENQARIIEAINQDYGnRSRHETLlaeiinacADINSTLKHLK---KWMKVQKRHVDHRMYLGAKS 110
Cdd:COG1012 65 AERAAILLRAADLLEERREELAALLTLETG-KPLAEAR--------GEVDRAADFLRyyaGEARRLYGETIPSDAPGTRA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 111 RVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSEL---VGnyFKPEKLQF-YCETGEVGI 186
Cdd:COG1012 136 YVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELleeAG--LPAGVLNVvTGDGSEVGA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 187 AFSKLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVH 265
Cdd:COG1012 214 ALVAHPdVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVH 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 266 QSQLALFIDTATRWAKKHV---PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADVITLSDQVADANTRKLPLTLILNSN 342
Cdd:COG1012 294 ESIYDEFVERLVAAAKALKvgdPLDPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGEGGYFVEPTVLADVT 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 343 DSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDALFHVGQHdLPFGGV 422
Cdd:COG1012 374 PDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQ-APFGGV 452
|
410 420
....*....|....*....|....*.
gi 1859350786 423 GASGMGHYHGYEGFLTFSKLRPVFYQ 448
Cdd:COG1012 453 KQSGIGREGGREGLEEYTETKTVTIR 478
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
25-445 |
1.95e-76 |
|
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: 243.68 E-value: 1.95e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 25 AKAAGIE----NYQQRREHLLALKAMITENQARIIEAINQDygNRSRHETLLAEIINACADINSTLKHLKKWMKVQKRhv 100
Cdd:cd06534 3 ARAAFKAwaalPPAERAAILRKIADLLEERREELAALETLE--TGKPIEEALGEVARAIDTFRYAAGLADKLGGPELP-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 101 dhRMYLGAKSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNYFKPEK-LQFYC 179
Cdd:cd06534 79 --SPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGvVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 180 ETG-EVGIAFSKLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICT 257
Cdd:cd06534 157 GGGdEVGAALLSHPrVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 258 NVDYVFVHQSQLALFIDtatrwakkhvpdihsqdytaiiddrafkRLtncieeakqlgadvitlsdqvadantrklpLTL 337
Cdd:cd06534 237 AASRLLVHESIYDEFVE----------------------------KL------------------------------VTV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 338 ILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDALFHVGQHdL 417
Cdd:cd06534 259 LVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPE-A 337
|
410 420
....*....|....*....|....*...
gi 1859350786 418 PFGGVGASGMGHYHGYEGFLTFSKLRPV 445
Cdd:cd06534 338 PFGGVKNSGIGREGGPYGLEEYTRTKTV 365
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
16-443 |
9.14e-73 |
|
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: 236.73 E-value: 9.14e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 16 ADLVAQ-RSHAKAAGIENYQQRREHLLALKAMITENQARIIEAINQDYGnRSRHEtLLAEIInacadinSTLKHLKKWMK 94
Cdd:cd07099 21 AAAVARaRAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETG-KPRAD-AGLEVL-------LALEAIDWAAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 95 -----VQKRHVDHR-MYLGAKSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELV-G 167
Cdd:cd07099 92 naprvLAPRKVPTGlLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWaA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 168 NYFKPEKLQFYCETGEVGIAFSKLPFDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYV 247
Cdd:cd07099 172 AGPPQGVLQVVTGDGATGAALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 248 KQMNAGQICTNVDYVFVHQSQLALFIDTATRWAKK---HVPDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADVITlsdQ 324
Cdd:cd07099 252 AMVNAGQTCISVERVYVHESVYDEFVARLVAKARAlrpGADDIGDADIGPMTTARQLDIVRRHVDDAVAKGAKALT---G 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 325 VADANTRKL--PLTLILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGG 402
Cdd:cd07099 329 GARSNGGGPfyEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGA 408
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1859350786 403 VSVNDALFHVGQHDLPFGGVGASGMGHYHGYEGFLTFSKLR 443
Cdd:cd07099 409 VSINDVLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPK 449
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
4-445 |
1.16e-72 |
|
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: 236.81 E-value: 1.16e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 4 ATKPVSIDSILMADLVAQRSHAKAagieNYQQRREHLLALKAMITENQARIIEAINQDYGnRSRHETLLAEIINACADIN 83
Cdd:cd07098 14 ADTPEDVDEAIAAARAAQREWAKT----SFAERRKVLRSLLKYILENQEEICRVACRDTG-KTMVDASLGEILVTCEKIR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 84 STLKHLKKWMKVQKRHVDHRMYLgAKSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLS 163
Cdd:cd07098 89 WTLKHGEKALRPESRPGGLLMFY-KRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 164 ELVGNYFK-----PEKLQFYCETGEVGIAFSKLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPM 237
Cdd:cd07098 168 SIIRECLAacghdPDLVQLVTCLPETAEALTSHPvIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 238 QKAVERIMYVKQMNAGQICTNVDYVFVHQSQLALFIDTATRWAKKHVPDIHSQ---DYTAIIDDRAFKRLTNCIEEAKQL 314
Cdd:cd07098 248 DQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDgdvDVGAMISPARFDRLEELVADAVEK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 315 GADVITLSDQVADANTRK---LPLTLILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLI 391
Cdd:cd07098 328 GARLLAGGKRYPHPEYPQghyFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRA 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1859350786 392 NFYIEQVMSGGVSVND-ALFHVGQhDLPFGGVGASGMGHYHGYEGFLTFSKLRPV 445
Cdd:cd07098 408 RRIASQLETGMVAINDfGVNYYVQ-QLPFGGVKGSGFGRFAGEEGLRGLCNPKSV 461
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
34-445 |
7.21e-69 |
|
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: 227.03 E-value: 7.21e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 34 QQRREHLLALKAMITENQARIIEAINQDYGnRSRHETLlaeiinacADINSTLKHLK----KWMKVQKRHVDhrMYLGAK 109
Cdd:pfam00171 51 AERAAILRKAADLLEERKDELAELETLENG-KPLAEAR--------GEVDRAIDVLRyyagLARRLDGETLP--SDPGRL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 110 SRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELV---GnyFKPEKLQFYCETG-EVG 185
Cdd:pfam00171 120 AYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFeeaG--LPAGVLNVVTGSGaEVG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 186 IAFSKLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFV 264
Cdd:pfam00171 198 EALVEHPdVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 265 HQSQLALFIDTATRWAKKHV---PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADVITLSDQVaDANTRKLPLTLILNS 341
Cdd:pfam00171 278 HESIYDEFVEKLVEAAKKLKvgdPLDPDTDMGPLISKAQLERVLKYVEDAKEEGAKLLTGGEAG-LDNGYFVEPTVLANV 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 342 NDSMSIDTRETFGPILMVKTYQDSQQVVDyIA-----GrdrpLAFYPFSYNKQLINFYIEQVMSGGVSVNDalFHVGQHD 416
Cdd:pfam00171 357 TPDMRIAQEEIFGPVLSVIRFKDEEEAIE-IAndteyG----LAAGVFTSDLERALRVARRLEAGMVWIND--YTTGDAD 429
|
410 420 430
....*....|....*....|....*....|
gi 1859350786 417 -LPFGGVGASGMGHYHGYEGFLTFSKLRPV 445
Cdd:pfam00171 430 gLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
82-476 |
5.61e-67 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 222.61 E-value: 5.61e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 82 INSTLKHLKKWMKVQKRHVDHRMYlGAKSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSAL 161
Cdd:PLN02174 79 IKLALKQLKNWMAPEKAKTSLTTF-PASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSAL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 162 LSELVGNYFKPEKLQFYCETGEVGIAFSKLPFDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAV 241
Cdd:PLN02174 158 LAKLLEQYLDSSAVRVVEGAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTV 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 242 ERIMYVK-QMNAGQICTNVDYVFVHQSQLALFIDTATRWAKKHVPD--IHSQDYTAIIDDRAFKRLTNCIEEAKQlgADV 318
Cdd:PLN02174 238 RRIIAGKwGCNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKnpMESKDMSRIVNSTHFDRLSKLLDEKEV--SDK 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 319 ITLSDQVADANTRKLPLTLILNSNDSMsIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQV 398
Cdd:PLN02174 316 IVYGGEKDRENLKIAPTILLDVPLDSL-IMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATV 394
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1859350786 399 MSGGVSVNDALFHVGQHDLPFGGVGASGMGHYHGYEGFLTFSKLRPVFYQAKFSSVKFLMPPYGRFADKLLAFLSKLN 476
Cdd:PLN02174 395 SAGGIVVNDIAVHLALHTLPFGGVGESGMGAYHGKFSFDAFSHKKAVLYRSLFGDSAVRYPPYSRGKLRLLKALVDSN 472
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
115-446 |
3.46e-53 |
|
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: 185.04 E-value: 3.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 115 QPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRhLSAL-LSELVGNYFKPEKLQFYCETGEVGIAFSKLP- 192
Cdd:cd07106 113 KPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTP-LCTLkLGELAQEVLPPGVLNVVSGGDELGPALTSHPd 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 193 FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQSQLALF 272
Cdd:cd07106 192 IRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEF 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 273 IDTATRWAKKHVPDIHSQDYTAI--IDDRA-FKRLTNCIEEAKQLGADVITLSdQVADANTRKLPLTLILNSNDSMSIDT 349
Cdd:cd07106 272 CEALVALAKAAVVGDGLDPGTTLgpVQNKMqYDKVKELVEDAKAKGAKVLAGG-EPLDGPGYFIPPTIVDDPPEGSRIVD 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 350 RETFGPILMVKTYQDSQQVV------DY-----IAGRDRPLAFYpfsynkqlinfYIEQVMSGGVSVNdALFHVGqHDLP 418
Cdd:cd07106 351 EEQFGPVLPVLKYSDEDEVIarandsEYglgasVWSSDLERAEA-----------VARRLEAGTVWIN-THGALD-PDAP 417
|
330 340
....*....|....*....|....*...
gi 1859350786 419 FGGVGASGMGHYHGYEGFLTFSKLRPVF 446
Cdd:cd07106 418 FGGHKQSGIGVEFGIEGLKEYTQTQVIN 445
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
116-445 |
1.51e-48 |
|
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: 172.80 E-value: 1.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 116 PLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSrHLSAL-LSEL---VGnyFKPEKLQFYCETG-EVGIAFSK 190
Cdd:cd07109 117 PHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDA-PLTALrLAELaeeAG--LPAGALNVVTGLGaEAGAALVA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 191 LP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQSQL 269
Cdd:cd07109 194 HPgVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIY 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 270 ALFIDTATRWAKKHV--PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADVITLSDQVADANTRK--LPLTLILNSNDSM 345
Cdd:cd07109 274 DEVLERLVERFRALRvgPGLEDPDLGPLISAKQLDRVEGFVARARARGARIVAGGRIAEGAPAGGyfVAPTLLDDVPPDS 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 346 SIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDaLFHVGQHDLPFGGVGAS 425
Cdd:cd07109 354 RLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNN-YGAGGGIELPFGGVKKS 432
|
330 340
....*....|....*....|
gi 1859350786 426 GMGHYHGYEGFLTFSKLRPV 445
Cdd:cd07109 433 GHGREKGLEALYNYTQTKTV 452
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
98-437 |
3.22e-48 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 171.85 E-value: 3.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 98 RHVDHRMylgaksRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRhLSAL-LSEL---VGnyFKPE 173
Cdd:cd07103 105 PAPGKRI------LVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETP-LSALaLAELaeeAG--LPAG 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 174 KLQF-YCETGEVGIAFSKLPFDHLM-FTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMN 251
Cdd:cd07103 176 VLNVvTGSPAEIGEALCASPRVRKIsFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRN 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 252 AGQICTNVDYVFVHQSQLALFIDT-ATRWAKKHV-----PDIhsqDYTAIIDDRAFKRLTNCIEEAKQLGADVITLSDQV 325
Cdd:cd07103 256 AGQTCVCANRIYVHESIYDEFVEKlVERVKKLKVgngldEGT---DMGPLINERAVEKVEALVEDAVAKGAKVLTGGKRL 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 326 ADANTRKLPlTLILNSNDSMSIDTRETFGPILMVKTYQDSQQVV----DYIAGrdrpLAFYPFSYNKQLINFYIEQVMSG 401
Cdd:cd07103 333 GLGGYFYEP-TVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIaranDTPYG----LAAYVFTRDLARAWRVAEALEAG 407
|
330 340 350
....*....|....*....|....*....|....*....
gi 1859350786 402 GVSVNDALfhVGQHDLPFGGVGASGMGH---YHGYEGFL 437
Cdd:cd07103 408 MVGINTGL--ISDAEAPFGGVKESGLGReggKEGLEEYL 444
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
115-437 |
4.52e-48 |
|
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: 172.06 E-value: 4.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 115 QPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNYFKPEK-LQFYCETGE-VGIAFSKLP 192
Cdd:cd07088 132 VPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGvLNIVTGRGSvVGDALVAHP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 193 FDHLM-FTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQSQLAL 271
Cdd:cd07088 212 KVGMIsLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDE 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 272 FIDTATRwAKKHV----PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADVITLSDQVADANTRKLPLTLILNSNDSMSI 347
Cdd:cd07088 292 FMEKLVE-KMKAVkvgdPFDAATDMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEGEKGYFYEPTVLTNVRQDMEI 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 348 DTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVN----DAL--FHVGqhdlpFGG 421
Cdd:cd07088 371 VQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINrenfEAMqgFHAG-----WKK 445
|
330
....*....|....*.
gi 1859350786 422 VGASGMGHYHGYEGFL 437
Cdd:cd07088 446 SGLGGADGKHGLEEYL 461
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
115-445 |
5.81e-48 |
|
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: 171.91 E-value: 5.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 115 QPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRhLSALLselVGNYFKPEKL--------QFYCETGEVGI 186
Cdd:cd07142 140 EPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTP-LSALL---AAKLAAEAGLpdgvlnivTGFGPTAGAAI 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 187 AfSKLPFDHLMFTGSGETGKKVMAAAAQ-NLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVH 265
Cdd:cd07142 216 A-SHMDVDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVH 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 266 QSQLALFIDTATRWAKKHV---PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADVITLSDQVADANTRKLPlTLILNSN 342
Cdd:cd07142 295 ESIYDEFVEKAKARALKRVvgdPFRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQP-TIFSDVK 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 343 DSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNdaLFHVGQHDLPFGGV 422
Cdd:cd07142 374 DDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVN--CYDVFDASIPFGGY 451
|
330 340
....*....|....*....|...
gi 1859350786 423 GASGMGHYHGYEGFLTFSKLRPV 445
Cdd:cd07142 452 KMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
112-446 |
7.65e-47 |
|
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: 168.28 E-value: 7.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 112 VIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNYFKPEKLqFYCETG---EVGIAF 188
Cdd:cd07118 115 VLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGV-VNIVTGygaTVGQAM 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 189 SKLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQS 267
Cdd:cd07118 194 TEHPdVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHES 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 268 QLALFID-TATRWAKKHVPDI--HSQDYTAIIDDRAFKRLTNCIEEAKQLGADVITLSDQVADANTRKLPLTLILNSNDS 344
Cdd:cd07118 274 IADAFVAaVVARSRKVRVGDPldPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLASAAGLFYQPTIFTDVTPD 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 345 MSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDALfhVGQHDLPFGGVGA 424
Cdd:cd07118 354 MAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFL--DGSPELPFGGFKQ 431
|
330 340
....*....|....*....|..
gi 1859350786 425 SGMGHYHGYEGFLTFSKLRPVF 446
Cdd:cd07118 432 SGIGRELGRYGVEEYTELKTVH 453
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
115-436 |
1.54e-46 |
|
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: 167.77 E-value: 1.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 115 QPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEdSRHLSAL-LSELV---GnyFKPEKLQFYCETGEV-GIAFS 189
Cdd:cd07091 140 EPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAE-QTPLSALyLAELIkeaG--FPPGVVNIVPGFGPTaGAAIS 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 190 KLP-FDHLMFTGSGETGKKVMAAAAQ-NLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQS 267
Cdd:cd07091 217 SHMdVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQES 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 268 QLALFIDTATRWAKKHV---PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADVITLSDQVADANTRKLPlTLILNSNDS 344
Cdd:cd07091 297 IYDEFVEKFKARAEKRVvgdPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQP-TVFTDVKDD 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 345 MSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDalFHVGQHDLPFGGVGA 424
Cdd:cd07091 376 MKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNT--YNVFDAAVPFGGFKQ 453
|
330
....*....|..
gi 1859350786 425 SGMGHYHGYEGF 436
Cdd:cd07091 454 SGFGRELGEEGL 465
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
20-445 |
3.49e-46 |
|
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: 166.33 E-value: 3.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 20 AQRSHAKAAGIEnyqqRREHLLALKAMITENQARIIEAINQDYGNRSRHEtlLAEIINACADINSTLKHLKKWMKVQKRH 99
Cdd:cd07101 30 AQRAWAARPFAE----RAAVFLRFHDLVLERRDELLDLIQLETGKARRHA--FEEVLDVAIVARYYARRAERLLKPRRRR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 100 vdHRMYLGAKSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKmsEDSRH-LSALLS-ELVGNYFKPEKL-Q 176
Cdd:cd07101 104 --GAIPVLTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLK--PDSQTaLTALWAvELLIEAGLPRDLwQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 177 FYCETG-EVGIAFSKlPFDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQI 255
Cdd:cd07101 180 VVTGPGsEVGGAIVD-NADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 256 CTNVDYVFVHQSQLALFID---TATRwAKKHVPDIH-SQDYTAIIDDRAFKRLTNCIEEAKQLGADVITLSDQVADANtr 331
Cdd:cd07101 259 CVSIERIYVHESVYDEFVRrfvARTR-ALRLGAALDyGPDMGSLISQAQLDRVTAHVDDAVAKGATVLAGGRARPDLG-- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 332 klPL----TLILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVND 407
Cdd:cd07101 336 --PYfyepTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNE 413
|
410 420 430
....*....|....*....|....*....|....*....
gi 1859350786 408 AL-FHVGQHDLPFGGVGASGMGHYHGYEGFLTFSKLRPV 445
Cdd:cd07101 414 GYaAAWASIDAPMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
112-445 |
3.94e-46 |
|
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: 167.20 E-value: 3.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 112 VIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRhLSALLselVGNYFKpeklqfycETG--------- 182
Cdd:cd07144 140 TLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTP-LSLLY---FANLVK--------EAGfppgvvnii 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 183 -----EVGIAFSKLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVE----RIMYvkqmNA 252
Cdd:cd07144 208 pgygaVAGSALAEHPdVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKwaaaGIMY----NS 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 253 GQICTNVDYVFVHQSQLALFIDTATRWAKKH--VPDIHSQDYTA--IIDDRAFKRLTNCIEEAKQLGADVItLSDQVADA 328
Cdd:cd07144 284 GQNCTATSRIYVQESIYDKFVEKFVEHVKQNykVGSPFDDDTVVgpQVSKTQYDRVLSYIEKGKKEGAKLV-YGGEKAPE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 329 NTRK---LPLTLILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGV-- 403
Cdd:cd07144 363 GLGKgyfIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVwi 442
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1859350786 404 -SVNDALFHVgqhdlPFGGVGASGMGHYHGYEGFLTFSKLRPV 445
Cdd:cd07144 443 nSSNDSDVGV-----PFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
107-443 |
1.03e-43 |
|
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: 159.80 E-value: 1.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 107 GAKSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNYFKPEKL--QFYCETGEV 184
Cdd:cd07150 110 GTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVfnVVTGGGAEV 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 185 GIAFSKLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVF 263
Cdd:cd07150 190 GDELVDDPrVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRII 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 264 VHQSQLALFIDT-ATRWAKKHVPDIHSQDyTAI---IDDRAFKRLTNCIEEAKQLGADVITlsdqvadANTRKLPL---T 336
Cdd:cd07150 270 VEEPVYDEFVKKfVARASKLKVGDPRDPD-TVIgplISPRQVERIKRQVEDAVAKGAKLLT-------GGKYDGNFyqpT 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 337 LILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDALFHVGQHd 416
Cdd:cd07150 342 VLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHINDPTILDEAH- 420
|
330 340
....*....|....*....|....*..
gi 1859350786 417 LPFGGVGASGMGHYHGYEGFLTFSKLR 443
Cdd:cd07150 421 VPFGGVKASGFGREGGEWSMEEFTELK 447
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
103-437 |
5.30e-43 |
|
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: 157.91 E-value: 5.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 103 RMYLG----AKSRVIP-----------QPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVG 167
Cdd:cd07108 89 RYFGGlageLKGETLPfgpdvltytvrEPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 168 NYFKPEKLQFYCETG-EVGIAFSKLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIM 245
Cdd:cd07108 169 QVLPAGVLNVITGYGeECGAALVDHPdVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGAI 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 246 ----YVKQmnaGQICTNVDYVFVHQSQLALFID---TATRWAKKHVPDIHSQDYTAIIDDRAFKRLTNCIEEAKQL-GAD 317
Cdd:cd07108 249 agmrFTRQ---GQSCTAGSRLFVHEDIYDAFLEklvAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLGLSTsGAT 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 318 VITLSDQVADANTRK----LPlTLILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINF 393
Cdd:cd07108 326 VLRGGPLPGEGPLADgffvQP-TIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALR 404
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1859350786 394 YIEQVMSGGVSVNDAlfHVGQHDLPFGGVGASGMGHYHGYEGFL 437
Cdd:cd07108 405 AAHALEAGWVQVNQG--GGQQPGQSYGGFKQSGLGREASLEGML 446
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
107-443 |
5.86e-43 |
|
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: 157.35 E-value: 5.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 107 GAKSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSEL---------VGN--YFKPEkl 175
Cdd:cd07105 89 GTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVfheaglpkgVLNvvTHSPE-- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 176 qfycETGEVGIAFSKLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQ 254
Cdd:cd07105 167 ----DAPEVVEALIAHPaVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQ 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 255 ICTNVDYVFVHQSQLALFIDTATRWAKKHVPD---IHSqdytaIIDDRAFKRLTNCIEEAKQLGADVITLSDQVADANTR 331
Cdd:cd07105 243 ICMSTERIIVHESIADEFVEKLKAAAEKLFAGpvvLGS-----LVSAAAADRVKELVDDALSKGAKLVVGGLADESPSGT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 332 KLPLTLILNSNDSMSIDTRETFGPILMVKTYQDSQQVV------DY-----IAGRDRPLAFYpfsynkqlinfYIEQVMS 400
Cdd:cd07105 318 SMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVriandsEYglsaaVFTRDLARALA-----------VAKRIES 386
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1859350786 401 GGVSVNDALFHVgQHDLPFGGVGASGMGHYHGYEGFLTFSKLR 443
Cdd:cd07105 387 GAVHINGMTVHD-EPTLPHGGVKSSGYGRFNGKWGIDEFTETK 428
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
112-428 |
4.08e-42 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 156.39 E-value: 4.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 112 VIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRhLSAL----LSELVGnyFKPEKLQFYC-ETGEVGI 186
Cdd:PLN02278 156 VLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTP-LTALaaaeLALQAG--IPPGVLNVVMgDAPEIGD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 187 AFSKLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVH 265
Cdd:PLN02278 233 ALLASPkVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 266 QSQLALFIDTATRWAKK-HVPDIHSQDYT--AIIDDRAFKRLTNCIEEAKQLGADVITLSDQVADANTRKLPlTLILNSN 342
Cdd:PLN02278 313 EGIYDKFAEAFSKAVQKlVVGDGFEEGVTqgPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEP-TVLGDVT 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 343 DSMSIDTRETFGPILMVKTYQDSQQVV----DYIAGrdrpLAFYPFSYNKQLINFYIEQVMSGGVSVNDALfhVGQHDLP 418
Cdd:PLN02278 392 EDMLIFREEVFGPVAPLTRFKTEEEAIaianDTEAG----LAAYIFTRDLQRAWRVSEALEYGIVGVNEGL--ISTEVAP 465
|
330
....*....|
gi 1859350786 419 FGGVGASGMG 428
Cdd:PLN02278 466 FGGVKQSGLG 475
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
15-445 |
8.01e-42 |
|
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: 154.81 E-value: 8.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 15 MADLVAQRSHAKAAGIENYQQRREHLLALKAMITENQARIIEAINQDYGNrsrhetLLAEIINACADINSTLKHLKKWMk 94
Cdd:cd07120 23 AAIAAARRAFDETDWAHDPRLRARVLLELADAFEANAERLARLLALENGK------ILGEARFEISGAISELRYYAGLA- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 95 vqkRHVDHRMYL---GAKSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGN--Y 169
Cdd:cd07120 96 ---RTEAGRMIEpepGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEipS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 170 FKPEKLQFYCETGEVG---IAFSKLpFDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMY 246
Cdd:cd07120 173 LPAGVVNLFTESGSEGaahLVASPD-VDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLER 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 247 VKQMNAGQICTNVDYVFVHQSQLALFIDT-ATRWAKKHV-PDIH-SQDYTAIIDDRAFKRLTNCIEEAKQLGADVITLSD 323
Cdd:cd07120 252 ALTIFAGQFCMAGSRVLVQRSIADEVRDRlAARLAAVKVgPGLDpASDMGPLIDRANVDRVDRMVERAIAAGAEVVLRGG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 324 QVAD--ANTRKLPLTLILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSG 401
Cdd:cd07120 332 PVTEglAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAG 411
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1859350786 402 GVSVNDalfHVGQHD-LPFGGVGASGMGHYHGYEGFLTFSKLRPV 445
Cdd:cd07120 412 TVWIND---WNKLFAeAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
34-428 |
1.19e-41 |
|
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: 154.26 E-value: 1.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 34 QQRREHLLALKAMITENQARIIEAINQDYGnRSRHETLLAEIINAC------ADinstlkhlkkwMKVQKRHVDHRMYLG 107
Cdd:cd07093 41 AERARILHKVADLIEARADELALLESLDTG-KPITLARTRDIPRAAanfrffAD-----------YILQLDGESYPQDGG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 108 AKSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSEL------------VGNYFKPEkl 175
Cdd:cd07093 109 ALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELaneaglppgvvnVVHGFGPE-- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 176 qfycetgeVGIAFSKLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQ 254
Cdd:cd07093 187 --------AGAALVAHPdVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 255 ICTNVDYVFVHQSQLALFIDTATRWAKKHVPDIHSQDYT---AIIDDRAFKRLTNCIEEAKQLGADVIT---LSDQVADA 328
Cdd:cd07093 259 VCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTevgPLISKEHLEKVLGYVELARAEGATILTgggRPELPDLE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 329 NTRKLPLTLILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYN-KQLINFyIEQVMSGGVSVND 407
Cdd:cd07093 339 GGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDlGRAHRV-ARRLEAGTVWVNC 417
|
410 420
....*....|....*....|...
gi 1859350786 408 alFHVgqHDL--PFGGVGASGMG 428
Cdd:cd07093 418 --WLV--RDLrtPFGGVKASGIG 436
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
109-370 |
1.22e-41 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 155.28 E-value: 1.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 109 KSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEdsrhLSAL----LSEL---VGnyFKPEKLQFYCET 181
Cdd:PLN02467 144 KGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSE----LASVtcleLADIcreVG--LPPGVLNVVTGL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 182 G-EVGIAFSKLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNV 259
Cdd:PLN02467 218 GtEAGAPLASHPgVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSAT 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 260 DYVFVHQSQLALFIDTATRWAKK-HVPDIHSQD--YTAIIDDRAFKRLTNCIEEAKQLGADVitLSDQVADANTRK---L 333
Cdd:PLN02467 298 SRLLVHERIASEFLEKLVKWAKNiKISDPLEEGcrLGPVVSEGQYEKVLKFISTAKSEGATI--LCGGKRPEHLKKgffI 375
|
250 260 270
....*....|....*....|....*....|....*..
gi 1859350786 334 PLTLILNSNDSMSIDTRETFGPILMVKTYQDSQQVVD 370
Cdd:PLN02467 376 EPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIE 412
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
109-472 |
3.30e-41 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 154.27 E-value: 3.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 109 KSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKmsEDSRH-LSAL-LSELVGNYFKPEKL-QFYCETG-EV 184
Cdd:PRK09407 147 KTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLK--PDSQTpLTALaAVELLYEAGLPRDLwQVVTGPGpVV 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 185 GIAFSKLPfDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFV 264
Cdd:PRK09407 225 GTALVDNA-DYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYV 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 265 HQSQLALFID---TATR---------WAkkhvPDIHSqdytaIIDDRAFKRLTNCIEEAKQLGADVITLSDQVADANtrk 332
Cdd:PRK09407 304 HESIYDEFVRafvAAVRamrlgagydYS----ADMGS-----LISEAQLETVSAHVDDAVAKGATVLAGGKARPDLG--- 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 333 lPL----TLILNSNDSMSIDTRETFGPILMVKTYQDSQQVV------DY-----IAGRD----RPLAfypfsynkqlinf 393
Cdd:PRK09407 372 -PLfyepTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVerandtPYglnasVWTGDtargRAIA------------- 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 394 yiEQVMSGGVSVNDAL-FHVGQHDLPFGGVGASGMGHYHGYEGFLTFSKLRPVFYQAKFSsvkfLMPPYG----RFADKL 468
Cdd:PRK09407 438 --ARIRAGTVNVNEGYaAAWGSVDAPMGGMKDSGLGRRHGAEGLLKYTESQTIATQRVLP----LAPPPGmpyeKYAKLM 511
|
....
gi 1859350786 469 LAFL 472
Cdd:PRK09407 512 LTGL 515
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
110-428 |
4.10e-41 |
|
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: 153.27 E-value: 4.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 110 SRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEdSRHLSAL-LSELVGNYFKPEKLQFYCETG-EVGIA 187
Cdd:cd07559 130 SYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPAS-QTPLSILvLMELIGDLLPKGVVNVVTGFGsEAGKP 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 188 FSKLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVI-----ATDYPMQKAVERIMYVKQMNAGQICTNVDY 261
Cdd:cd07559 209 LASHPrIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFfddamDADDDFDDKAEEGQLGFAFNQGEVCTCPSR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 262 VFVHQSQLALFIDTATRwAKKHVPDIHSQDYT----AIIDDRAFKRLTNCIEEAKQLGADVITLSDQVADANTRK----L 333
Cdd:cd07559 289 ALVQESIYDEFIERAVE-RFEAIKVGNPLDPEtmmgAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKgyfyE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 334 PlTLILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNdaLFHVG 413
Cdd:cd07559 368 P-TLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVN--CYHQY 444
|
330
....*....|....*
gi 1859350786 414 QHDLPFGGVGASGMG 428
Cdd:cd07559 445 PAHAPFGGYKKSGIG 459
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
109-370 |
4.48e-41 |
|
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: 152.51 E-value: 4.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 109 KSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDS----RHLSALLSElVGnyFKPEKLQFYCETG-E 183
Cdd:cd07110 113 KARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTslteLELAEIAAE-AG--LPPGVLNVVTGTGdE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 184 VGIAFSKLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYV 262
Cdd:cd07110 190 AGAPLAAHPgIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 263 FVHQSQLALFIDTATRWAKKHV---PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADVITlSDQVADANTRK--LPLTL 337
Cdd:cd07110 270 LVHESIADAFLERLATAAEAIRvgdPLEEGVRLGPLVSQAQYEKVLSFIARGKEEGARLLC-GGRRPAHLEKGyfIAPTV 348
|
250 260 270
....*....|....*....|....*....|...
gi 1859350786 338 ILNSNDSMSIDTRETFGPILMVKTYQDSQQVVD 370
Cdd:cd07110 349 FADVPTDSRIWREEIFGPVLCVRSFATEDEAIA 381
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
116-446 |
9.85e-41 |
|
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: 151.69 E-value: 9.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 116 PLGVVGLIVPWNFPINLAFSQLAAAFSAGNkAMV-KMSEDSRHLSALLSELVGNYFKPEKL----QFYcetGEVGIAFSK 190
Cdd:cd07090 116 PLGVCAGIGAWNYPIQIASWKSAPALACGN-AMVyKPSPFTPLTALLLAEILTEAGLPDGVfnvvQGG---GETGQLLCE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 191 LP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQSQL 269
Cdd:cd07090 192 HPdVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIK 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 270 ALFID-TATRWAKKHVPDIHSQD--YTAIIDDRAFKRLTNCIEEAKQLGADVITLSDQVAD----ANTRKLPLTLILNSN 342
Cdd:cd07090 272 DEFTErLVERTKKIRIGDPLDEDtqMGALISEEHLEKVLGYIESAKQEGAKVLCGGERVVPedglENGFYVSPCVLTDCT 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 343 DSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDalFHVGQHDLPFGGV 422
Cdd:cd07090 352 DDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINT--YNISPVEVPFGGY 429
|
330 340
....*....|....*....|....
gi 1859350786 423 GASGMGHYHGYEGFLTFSKLRPVF 446
Cdd:cd07090 430 KQSGFGRENGTAALEHYTQLKTVY 453
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
19-447 |
2.97e-40 |
|
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: 150.47 E-value: 2.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 19 VAQRSHAKAAGIENYQQRREHLLALkaMITEN-QARIIEAINQDYGnrsrhetlLAEIINACADinstlkHLKKWMKVQK 97
Cdd:cd07089 41 AEERARCLRQLHEALEARKEELRAL--LVAEVgAPVMTARAMQVDG--------PIGHLRYFAD------LADSFPWEFD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 98 RHVDHRMYLGAKSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGnyfkpeklqf 177
Cdd:cd07089 105 LPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIA---------- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 178 ycETG--------------EVGIAFSKLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVE 242
Cdd:cd07089 175 --ETDlpagvvnvvtgsdnAVGEALTTDPrVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 243 RIMYVKQMNAGQICTNVDYVFVHQSQLALFIDTATRwAKKHVPDIHSQDYTAI----IDDRAFKRLTNCIEEAKQLGADV 318
Cdd:cd07089 253 AAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAA-AFEALPVGDPADPGTVmgplISAAQRDRVEGYIARGRDEGARL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 319 ITlsdqvadANTRKLPL--------TLILNSNDSMSIDTRETFGPILMVKTYQDSQQVV-----------DYIAGRDRPL 379
Cdd:cd07089 332 VT-------GGGRPAGLdkgfyvepTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVriandsdyglsGGVWSADVDR 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1859350786 380 AFYpfsynkqlinfYIEQVMSGGVSVNDALFhvGQHDLPFGGVGASGMGHYHGYEGFLTFSKLRPVFY 447
Cdd:cd07089 405 AYR-----------VARRIRTGSVGINGGGG--YGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
20-432 |
6.50e-40 |
|
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: 148.83 E-value: 6.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 20 AQRSHAKAagieNYQQRREHLLALKAMITENQARIIEAINQDYGnrsrhetllAEIINACADINSTLKHLKkwmkvQKRH 99
Cdd:cd07104 12 AQKAWAAT----PPQERAAILRKAAEILEERRDEIADWLIRESG---------STRPKAAFEVGAAIAILR-----EAAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 100 VDHRM--------YLGAKSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDS---------RHLSA-- 160
Cdd:cd07104 74 LPRRPegeilpsdVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTpvtgglliaEIFEEag 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 161 ----LLSELVGNYfkpeklqfycetGEVGIAFSKLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDY 235
Cdd:cd07104 154 lpkgVLNVVPGGG------------SEIGDALVEHPrVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 236 PMQKAVERIMYVKQMNAGQICTNVDYVFVHQSQLALFIDTATRWAKK-HVPDIHSQDyTAI---IDDRAFKRLTNCIEEA 311
Cdd:cd07104 222 DLDLAVSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKAlPVGDPRDPD-TVIgplINERQVDRVHAIVEDA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 312 KQLGADVITLsdqvADANTRKLPLTLILNSNDSMSIDTRETFGPILMVKTYQDSQQVV------DY-----IAGRD--RP 378
Cdd:cd07104 301 VAAGARLLTG----GTYEGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVelandtEYglsaaVFTRDleRA 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1859350786 379 LAFypfsynkqlinfyIEQVMSGGVSVNDALFHVGQHdLPFGGVGASGMGHYHG 432
Cdd:cd07104 377 MAF-------------AERLETGMVHINDQTVNDEPH-VPFGGVKASGGGRFGG 416
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
35-445 |
1.45e-39 |
|
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: 148.24 E-value: 1.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 35 QRREHLLALKAMITENQARIIEAINQDYGnRSRHETLLAEIINAcadinstlkhlkkwmkvqkrhVDH-RMYLGAkSRVI 113
Cdd:cd07092 42 ERSKALLKLADAIEENAEELAALESRNTG-KPLHLVRDDELPGA---------------------VDNfRFFAGA-ARTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 114 P-----------------QPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNYFKPEKLQ 176
Cdd:cd07092 99 EgpaageylpghtsmirrEPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGVVN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 177 FYCETGE-VGIAFSKLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQ 254
Cdd:cd07092 179 VVCGGGAsAGDALVAHPrVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 255 ICTNVDYVFVHQSQLALFIDTATRWAKKHV---PDIHSQDYTAIIDDRAFKRLTNCIEEAKQlGADVITlSDQVADANTR 331
Cdd:cd07092 259 DCTAACRVYVHESVYDEFVAALVEAVSAIRvgdPDDEDTEMGPLNSAAQRERVAGFVERAPA-HARVLT-GGRRAEGPGY 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 332 KLPLTLILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDalFH 411
Cdd:cd07092 337 FYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNT--HI 414
|
410 420 430
....*....|....*....|....*....|....
gi 1859350786 412 VGQHDLPFGGVGASGMGHYHGYEGFLTFSKLRPV 445
Cdd:cd07092 415 PLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
112-445 |
1.69e-39 |
|
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: 148.36 E-value: 1.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 112 VIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRhLSAL-LSEL---VGnyFKPEKLQFYCETGEV-GI 186
Cdd:cd07115 113 TVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP-LSALrIAELmaeAG--FPAGVLNVVTGFGEVaGA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 187 AFSKLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVH 265
Cdd:cd07115 190 ALVEHPdVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVH 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 266 QSQLALFIDTATRWAKKHVP----DIHSQdYTAIIDDRAFKRLTNCIEEAKQLGADVITlSDQVADANTRKLPLTLILNS 341
Cdd:cd07115 270 ESIYDEFLERFTSLARSLRPgdplDPKTQ-MGPLVSQAQFDRVLDYVDVGREEGARLLT-GGKRPGARGFFVEPTIFAAV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 342 NDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVND-ALFHVGqhdLPFG 420
Cdd:cd07115 348 PPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWINTyNRFDPG---SPFG 424
|
330 340
....*....|....*....|....*
gi 1859350786 421 GVGASGMGHYHGYEGFLTFSKLRPV 445
Cdd:cd07115 425 GYKQSGFGREMGREALDEYTEVKSV 449
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
116-446 |
4.28e-39 |
|
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: 147.31 E-value: 4.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 116 PLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRhLSAL-LSELV---GnyFKPEKLQFYCETG-EVGIAFSK 190
Cdd:cd07114 119 PLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTP-ASTLeLAKLAeeaG--FPPGVVNVVTGFGpETGEALVE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 191 LP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQSQL 269
Cdd:cd07114 196 HPlVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIY 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 270 ALFID---TATRWAKKHVPDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADVITLSDQVADANTRK----LPlTLILNSN 342
Cdd:cd07114 276 DEFVErlvARARAIRVGDPLDPETQMGPLATERQLEKVERYVARAREEGARVLTGGERPSGADLGAgyffEP-TILADVT 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 343 DSMSIDTRETFGPILMVKTYQDSQQVV------DY--IAG---RDRPLAFYpfsynkqlinfYIEQVMSGGVSVNDalFH 411
Cdd:cd07114 355 NDMRIAQEEVFGPVLSVIPFDDEEEAIalandsEYglAAGiwtRDLARAHR-----------VARAIEAGTVWVNT--YR 421
|
330 340 350
....*....|....*....|....*....|....*
gi 1859350786 412 VGQHDLPFGGVGASGMGHYHGYEGFLTFSKLRPVF 446
Cdd:cd07114 422 ALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVW 456
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
109-439 |
7.20e-39 |
|
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: 146.88 E-value: 7.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 109 KSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRhLSA-LLSELVGnyfkpeklqfycETG----- 182
Cdd:cd07138 123 NSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAP-LSAiILAEILD------------EAGlpagv 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 183 ---------EVGIAFSKLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNA 252
Cdd:cd07138 190 fnlvngdgpVVGEALSAHPdVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANS 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 253 GQICTNVDYVFVHQSQLALFIDTATRWAKKHVPDIHSQDYTAI---IDDRAFKRLTNCIEEAKQLGADVIT-LSDQVADA 328
Cdd:cd07138 270 GQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLgplASAAQFDRVQGYIQKGIEEGARLVAgGPGRPEGL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 329 NT----RklPlTLILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDyIAGrDRP--LAFYPFSYNKQLINFYIEQVMSGG 402
Cdd:cd07138 350 ERgyfvK--P-TVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIA-IAN-DTPygLAGYVWSADPERARAVARRLRAGQ 424
|
330 340 350
....*....|....*....|....*....|....*..
gi 1859350786 403 VSVNDALFHVGqhdLPFGGVGASGMGHYHGYEGFLTF 439
Cdd:cd07138 425 VHINGAAFNPG---APFGGYKQSGNGREWGRYGLEEF 458
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
25-432 |
1.43e-38 |
|
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: 145.91 E-value: 1.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 25 AKAAGIE----NYQQRREHLLALKAMITENQARIIEAINQDYGnrsrhetllAEIINACADINSTLKHLKKWMKVQKR-H 99
Cdd:cd07151 41 AAAAQKEwaatLPQERAEILEKAAQILEERRDEIVEWLIRESG---------STRIKANIEWGAAMAITREAATFPLRmE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 100 VDHRMYL--GAKSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLselVGNYFK----PE 173
Cdd:cd07151 112 GRILPSDvpGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGLL---LAKIFEeaglPK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 174 KLqFYCETG---EVGIAFSKLPFDHLM-FTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQ 249
Cdd:cd07151 189 GV-LNVVVGagsEIGDAFVEHPVPRLIsFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKF 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 250 MNAGQICTNVDYVFVHQSQLALFIDTATRWAKK------HVPDIHsqdYTAIIDDRAFKRLTNCIEEAKQLGADVITLSd 323
Cdd:cd07151 268 LHQGQICMAINRIIVHEDVYDEFVEKFVERVKAlpygdpSDPDTV---VGPLINESQVDGLLDKIEQAVEEGATLLVGG- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 324 qvaDANTRKLPLTLILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQL-INFyIEQVMSGG 402
Cdd:cd07151 344 ---EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERgVQF-ARRIDAGM 419
|
410 420 430
....*....|....*....|....*....|
gi 1859350786 403 VSVNDALFHVGQHdLPFGGVGASGMGHYHG 432
Cdd:cd07151 420 THINDQPVNDEPH-VPFGGEKNSGLGRFNG 448
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
107-439 |
1.52e-38 |
|
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: 145.80 E-value: 1.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 107 GAKSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVgnyfkpeklqfycetGEVGI 186
Cdd:cd07139 128 GGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAA---------------EEAGL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 187 ---AFSKLPFD-----HLM---------FTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQ 249
Cdd:cd07139 193 ppgVVNVVPADrevgeYLVrhpgvdkvsFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASL 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 250 MNAGQICTNVDYVFVHQSQLALFIDTATRWAKK-HVPDIHSQDyTAI---IDDRAFKRLTNCIEEAKQLGADVITLSDQV 325
Cdd:cd07139 273 MNNGQVCVALTRILVPRSRYDEVVEALAAAVAAlKVGDPLDPA-TQIgplASARQRERVEGYIAKGRAEGARLVTGGGRP 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 326 ADantrkLPL------TLILNSNDSMSIDTRETFGPILMVKTYQDSQQVV------DY-IAG------RDRPLAFYPfsy 386
Cdd:cd07139 352 AG-----LDRgwfvepTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVriandsDYgLSGsvwtadVERGLAVAR--- 423
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1859350786 387 nkqlinfyieQVMSGGVSVNDALFHVGqhdLPFGGVGASGMGHYHGYEGFLTF 439
Cdd:cd07139 424 ----------RIRTGTVGVNGFRLDFG---APFGGFKQSGIGREGGPEGLDAY 463
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
53-445 |
1.62e-38 |
|
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: 145.92 E-value: 1.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 53 RIIEAINQDYGNRSRHETL-----LAEIINACADINSTLKH---LKKWMKVQKRHVDHRMylgaKSRVIPQPLGVVGLIV 124
Cdd:cd07119 67 RIADKIREDAEELARLETLntgktLRESEIDIDDVANCFRYyagLATKETGEVYDVPPHV----ISRTVREPVGVCGLIT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 125 PWNFPINLAFSQLAAAFSAGNKAMVKMSE----DSRHLSALLSElVGnyFKPEKLQFYCETG-EVGIAFSKLP-FDHLMF 198
Cdd:cd07119 143 PWNYPLLQAAWKLAPALAAGNTVVIKPSEvtplTTIALFELIEE-AG--LPAGVVNLVTGSGaTVGAELAESPdVDLVSF 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 199 TGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQSQLALFIDTATR 278
Cdd:cd07119 220 TGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 279 WAKKHV---PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADVITLSDQVADANTRK----LPlTLILNSNDSMSIDTRE 351
Cdd:cd07119 300 RAKKIKlgnGLDADTEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKgyfvEP-TIFDDVDRTMRIVQEE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 352 TFGPILMVKTYQDSQQVV----DYIAGrdrpLAFYPFSYNKQLINFYIEQVMSGGVSVNDalFHVGQHDLPFGGVGASGM 427
Cdd:cd07119 379 IFGPVLTVERFDTEEEAIrlanDTPYG----LAGAVWTKDIARANRVARRLRAGTVWIND--YHPYFAEAPWGGYKQSGI 452
|
410
....*....|....*...
gi 1859350786 428 GHYHGYEGFLTFSKLRPV 445
Cdd:cd07119 453 GRELGPTGLEEYQETKHI 470
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
115-439 |
4.05e-38 |
|
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: 144.44 E-value: 4.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 115 QPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRhLSAL-LSELVGNYFKPEKLQFYCETGE-VGIAFSKLP 192
Cdd:cd07107 115 EPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP-LSALrLAELAREVLPPGVFNILPGDGAtAGAALVRHP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 193 -FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERImyVKQMN---AGQICTNVDYVFVHQSQ 268
Cdd:cd07107 194 dVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAA--VAGMNftwCGQSCGSTSRLFVHESI 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 269 LALFIDTATRWAKKHVPDIHSQDYT---AIIDDRAFKRLTNCIEEAKQLGADVITLSDQVADANTRK---LPLTLILNSN 342
Cdd:cd07107 272 YDEVLARVVERVAAIKVGDPTDPATtmgPLVSRQQYDRVMHYIDSAKREGARLVTGGGRPEGPALEGgfyVEPTVFADVT 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 343 DSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDalfhVGQHDL--PFG 420
Cdd:cd07107 352 PGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVWING----SSRHFLgaPFG 427
|
330
....*....|....*....
gi 1859350786 421 GVGASGMGHYHGYEGFLTF 439
Cdd:cd07107 428 GVKNSGIGREECLEELLSY 446
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
112-370 |
6.20e-38 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 142.95 E-value: 6.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 112 VIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNYFKPeKLQFYCETG---EVGIAF 188
Cdd:PRK10090 67 LFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLP-KGVFNLVLGrgeTVGQEL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 189 SKLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQS 267
Cdd:PRK10090 146 AGNPkVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 268 QLALFIDTATRwAKKHV----PDIHSQ-DYTAIIDDRAFKRLTNCIEEAKQLGAdVITLSDQVADANTRKLPLTLILNSN 342
Cdd:PRK10090 226 IYDQFVNRLGE-AMQAVqfgnPAERNDiAMGPLINAAALERVEQKVARAVEEGA-RVALGGKAVEGKGYYYPPTLLLDVR 303
|
250 260
....*....|....*....|....*...
gi 1859350786 343 DSMSIDTRETFGPILMVKTYQDSQQVVD 370
Cdd:PRK10090 304 QEMSIMHEETFGPVLPVVAFDTLEEAIA 331
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
115-445 |
1.77e-37 |
|
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: 143.26 E-value: 1.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 115 QPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRhLSAL-LSELVGNY-FKP---EKLQFYCETGEVGIAfS 189
Cdd:cd07141 144 EPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTP-LTALyLASLIKEAgFPPgvvNVVPGYGPTAGAAIS-S 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 190 KLPFDHLMFTGSGETGKKVM-AAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQSQ 268
Cdd:cd07141 222 HPDIDKVAFTGSTEVGKLIQqAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESI 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 269 LALFIDTATRWAKKHV---PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADVITLSDQVADANTRKLPlTLILNSNDSM 345
Cdd:cd07141 302 YDEFVKRSVERAKKRVvgnPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQP-TVFSDVTDDM 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 346 SIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNdaLFHVGQHDLPFGGVGAS 425
Cdd:cd07141 381 RIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVN--CYNVVSPQAPFGGYKMS 458
|
330 340
....*....|....*....|
gi 1859350786 426 GMGHYHGYEGFLTFSKLRPV 445
Cdd:cd07141 459 GNGRELGEYGLQEYTEVKTV 478
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
107-428 |
2.70e-37 |
|
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: 141.96 E-value: 2.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 107 GAKSRV---IPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRhLSAL-LSE-LVGNYFKPEKLQFYCET 181
Cdd:cd07149 111 GGEGRIgftIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTP-LSALkLAElLLEAGLPKGALNVVTGS 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 182 GE-VGIAFSKLPfDHLM--FTGSGETGKKVMAAAAqnLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTN 258
Cdd:cd07149 190 GEtVGDALVTDP-RVRMisFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCIS 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 259 VDYVFVHQSQLALFIDTATRWAKKHV---PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADVITlsdqvadANTRK--- 332
Cdd:cd07149 267 VQRIFVHEDIYDEFLERFVAATKKLVvgdPLDEDTDVGPMISEAEAERIEEWVEEAVEGGARLLT-------GGKRDgai 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 333 LPLTLILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDA-LFH 411
Cdd:cd07149 340 LEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINDSsTFR 419
|
330
....*....|....*..
gi 1859350786 412 VGQhdLPFGGVGASGMG 428
Cdd:cd07149 420 VDH--MPYGGVKESGTG 434
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
115-429 |
3.09e-37 |
|
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: 141.97 E-value: 3.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 115 QPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRhLSAL-LSELVGNYFKPEK-LQFYCETG-EVGIAFSKL 191
Cdd:cd07112 123 EPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSP-LTALrLAELALEAGLPAGvLNVVPGFGhTAGEALGLH 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 192 P-FDHLMFTGSGETGKKVMAAAAQ-NLTPVTLELGGKSPAVIATDYP-MQKAVERIMYVKQMNAGQICTNVDYVFVHQSQ 268
Cdd:cd07112 202 MdVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADAPdLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESI 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 269 LALFIDTATRWAKKHVP----DIHSQdYTAIIDDRAFKRLTNCIEEAKQLGADVITLSDQV-ADANTRKLPLTLILNSND 343
Cdd:cd07112 282 KDEFLEKVVAAAREWKPgdplDPATR-MGALVSEAHFDKVLGYIESGKAEGARLVAGGKRVlTETGGFFVEPTVFDGVTP 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 344 SMSIDTRETFGPILMVKTYQDSQQVV----DYIAGrdrpLAFYPFSYNKQLINFYIEQVMSGGVSVNDalFHVGQHDLPF 419
Cdd:cd07112 361 DMRIAREEIFGPVLSVITFDSEEEAValanDSVYG----LAASVWTSDLSRAHRVARRLRAGTVWVNC--FDEGDITTPF 434
|
330
....*....|
gi 1859350786 420 GGVGASGMGH 429
Cdd:cd07112 435 GGFKQSGNGR 444
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
110-428 |
3.12e-37 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 142.59 E-value: 3.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 110 SRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEdSRHLSAL-LSELVGNYFKPEKLQFYCETG-EVGIA 187
Cdd:cd07117 130 SIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSS-TTSLSLLeLAKIIQDVLPKGVVNIVTGKGsKSGEY 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 188 FSKLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQ 266
Cdd:cd07117 209 LLNHPgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQE 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 267 SQLALFIDTAT-RWAKKHVPDIHSQDYT--AIIDDRAFKRLTNCIEEAKQLGADVITLSDQVADANTRK---LPLTLILN 340
Cdd:cd07117 289 GIYDEFVAKLKeKFENVKVGNPLDPDTQmgAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKgffIEPTLIVN 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 341 SNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNkqlINFYI---EQVMSGGVSVNdaLFHVGQHDL 417
Cdd:cd07117 369 VTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKD---INRALrvaRAVETGRVWVN--TYNQIPAGA 443
|
330
....*....|.
gi 1859350786 418 PFGGVGASGMG 428
Cdd:cd07117 444 PFGGYKKSGIG 454
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
113-445 |
8.01e-37 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 141.88 E-value: 8.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 113 IPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRhLSAL----LSELVGnyfKPEK----LQFYCETGEV 184
Cdd:PLN02766 155 LKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTP-LSALfyahLAKLAG---VPDGvinvVTGFGPTAGA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 185 GIAfSKLPFDHLMFTGSGETGKKVM-AAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVF 263
Cdd:PLN02766 231 AIA-SHMDVDKVSFTGSTEVGRKIMqAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVY 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 264 VHQSQLALFIDTATRWAKKHV---PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADVITLSDQVADANTRKLPlTLILN 340
Cdd:PLN02766 310 VQEGIYDEFVKKLVEKAKDWVvgdPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEP-TIFTD 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 341 SNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNdaLFHVGQHDLPFG 420
Cdd:PLN02766 389 VTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN--CYFAFDPDCPFG 466
|
330 340
....*....|....*....|....*
gi 1859350786 421 GVGASGMGHYHGYEGFLTFSKLRPV 445
Cdd:PLN02766 467 GYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
115-432 |
8.80e-36 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 138.34 E-value: 8.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 115 QPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRhLSAL-LSELVGNY-FKPEKLQFYCETGEVGIAFSKLP 192
Cdd:cd07113 141 EPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTP-LTLLrVAELAKEAgIPDGVLNVVNGKGAVGAQLISHP 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 193 -FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQSQLal 271
Cdd:cd07113 220 dVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKF-- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 272 fiDTATRWAKKHVPDIH---SQDYTAIIDDRA----FKRLTNCIEEAKQLGADVITLSDQVADANTRKLPlTLILNSNDS 344
Cdd:cd07113 298 --DELVTKLKQALSSFQvgsPMDESVMFGPLAnqphFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQP-TLVLARSAD 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 345 MSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDALFHvgQHDLPFGGVGA 424
Cdd:cd07113 375 SRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFL--DPAVPFGGMKQ 452
|
....*...
gi 1859350786 425 SGMGHYHG 432
Cdd:cd07113 453 SGIGREFG 460
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
111-432 |
1.11e-35 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 139.17 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 111 RVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRhLSALLselVGNYFKPEKL--------QFYCETG 182
Cdd:PLN02466 190 QTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTP-LSALY---AAKLLHEAGLppgvlnvvSGFGPTA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 183 EVGIAfSKLPFDHLMFTGSGETGKKVMAAAAQ-NLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDY 261
Cdd:PLN02466 266 GAALA-SHMDVDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSR 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 262 VFVHQSQLALFIDTATRWAKKHV---PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADVITLSDQVADANTRKLPlTLI 338
Cdd:PLN02466 345 TFVHERVYDEFVEKAKARALKRVvgdPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQP-TVF 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 339 LNSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNdaLFHVGQHDLP 418
Cdd:PLN02466 424 SNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVN--CFDVFDAAIP 501
|
330
....*....|....
gi 1859350786 419 FGGVGASGMGHYHG 432
Cdd:PLN02466 502 FGGYKMSGIGREKG 515
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
115-429 |
1.85e-35 |
|
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: 137.48 E-value: 1.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 115 QPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNYFKPEK----LQFYCEtgEVGIAFSK 190
Cdd:cd07131 134 QPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGvvnvVHGRGE--EVGEALVE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 191 LP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQSQL 269
Cdd:cd07131 212 HPdVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 270 ALFIDTATRWAKKHV---PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADVITLSDQVADANTRK---LPLTLILNSND 343
Cdd:cd07131 292 DEFLKRFVERAKRLRvgdGLDEETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKgyfVEPTVFTDVTP 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 344 SMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPL--AFYPFSYNKqlINFYIEQVMSGGVSVNDALFHVGQHdLPFGG 421
Cdd:cd07131 372 DMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLssAIYTEDVNK--AFRARRDLEAGITYVNAPTIGAEVH-LPFGG 448
|
....*...
gi 1859350786 422 VGASGMGH 429
Cdd:cd07131 449 VKKSGNGH 456
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
115-428 |
5.41e-35 |
|
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: 135.94 E-value: 5.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 115 QPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNY-FKPEKLQFYceTG---EVGIAFSK 190
Cdd:cd07145 122 EPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPGVINVV--TGygsEVGDEIVT 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 191 LP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQSQL 269
Cdd:cd07145 200 NPkVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVY 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 270 ALFIDTATRWAKKHV---PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADVITLSDQVADAntrKLPLTLILNSNDSMS 346
Cdd:cd07145 280 DKFLKLLVEKVKKLKvgdPLDESTDLGPLISPEAVERMENLVNDAVEKGGKILYGGKRDEGS---FFPPTVLENDTPDMI 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 347 IDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFS--YNKQLinFYIEQVMSGGVSVNDA-LFHVGqhDLPFGGVG 423
Cdd:cd07145 357 VMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTndINRAL--KVARELEAGGVVINDStRFRWD--NLPFGGFK 432
|
....*
gi 1859350786 424 ASGMG 428
Cdd:cd07145 433 KSGIG 437
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
4-428 |
6.32e-34 |
|
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: 132.94 E-value: 6.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 4 ATKPVSIDSiLMADLVAQRSHAKAAGIenyQQRREHLLALKAMITENQARIIEAINQDYGNrsrhetllaEIINACADIN 83
Cdd:cd07094 17 ADDRADAEE-ALATARAGAENRRALPP---HERMAILERAADLLKKRAEEFAKIIACEGGK---------PIKDARVEVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 84 STLKHLKKWMKVQKRHVDHRMYLGAKSR-------VIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSR 156
Cdd:cd07094 84 RAIDTLRLAAEEAERIRGEEIPLDATQGsdnrlawTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 157 hLSAL-LSELVGNYFKPEK-LQ-FYCETGEVGIAFSKLP-FDHLMFTGSGETGKKVMAAAAqnLTPVTLELGGKSPAVIA 232
Cdd:cd07094 164 -LSALeLAKILVEAGVPEGvLQvVTGEREVLGDAFAADErVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 233 TDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQSQLALFIDT-ATRWAKKHV--PDIHSQDYTAIIDDRAFKRLTNCIE 309
Cdd:cd07094 241 RDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAfVAAVKKLKVgdPLDEDTDVGPLISEEAAERVERWVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 310 EAKQLGADVITlsdqvadANTRK----LPLTLILNSNDSMsIDTRETFGPILMVKTYQDSQQVVDyiAGRDRPLAFYPFS 385
Cdd:cd07094 321 EAVEAGARLLC-------GGERDgalfKPTVLEDVPRDTK-LSTEETFGPVVPIIRYDDFEEAIR--IANSTDYGLQAGI 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1859350786 386 YNKQL-INFYI-EQVMSGGVSVNDALfHVGQHDLPFGGVGASGMG 428
Cdd:cd07094 391 FTRDLnVAFKAaEKLEVGGVMVNDSS-AFRTDWMPFGGVKESGVG 434
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
115-447 |
7.48e-34 |
|
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: 133.04 E-value: 7.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 115 QPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRhLSAL-LSELVGNY-FKPEKLQFYCETGE-VGIAFSKL 191
Cdd:cd07143 143 EPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTP-LSALyMTKLIPEAgFPPGVINVVSGYGRtCGNAISSH 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 192 P-FDHLMFTGSGETGKKVMAAAAQ-NLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQSQL 269
Cdd:cd07143 222 MdIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIY 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 270 ALFIDTATRWAKK-HVPDIHSQD--YTAIIDDRAFKRLTNCIEEAKQLGADVITLSDQVADANTRKLPlTLILNSNDSMS 346
Cdd:cd07143 302 DKFVKRFKEKAKKlKVGDPFAEDtfQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEP-TIFTDVTEDMK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 347 IDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNkqlINFYIE---QVMSGGVSVNDA-LFHvgqHDLPFGGV 422
Cdd:cd07143 381 IVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNN---INNAIRvanALKAGTVWVNCYnLLH---HQVPFGGY 454
|
330 340
....*....|....*....|....*
gi 1859350786 423 GASGMGHYHGYEGFLTFSKLRPVFY 447
Cdd:cd07143 455 KQSGIGRELGEYALENYTQIKAVHI 479
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
116-369 |
1.05e-33 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 132.70 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 116 PLGVVGLIVPWNFPINLAFSQLAAAFSAGNkAMV-KMSEDSRhLSAL-LSELvgnyfkpeklqfYCE------------- 180
Cdd:PRK13252 142 PLGVCAGIGAWNYPIQIACWKSAPALAAGN-AMIfKPSEVTP-LTALkLAEI------------YTEaglpdgvfnvvqg 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 181 TGEVGIAFSKLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNV 259
Cdd:PRK13252 208 DGRVGAWLTEHPdIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNG 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 260 DYVFVHQSQLALFIDT-ATRWAKKHVPDIHSQD--YTAIIDDRAFKRLTNCIEEAKQLGADVIT----LSDQVADANTRK 332
Cdd:PRK13252 288 TRVFVQKSIKAAFEARlLERVERIRIGDPMDPAtnFGPLVSFAHRDKVLGYIEKGKAEGARLLCggerLTEGGFANGAFV 367
|
250 260 270
....*....|....*....|....*....|....*..
gi 1859350786 333 LPlTLILNSNDSMSIDTRETFGPILMVKTYQDSQQVV 369
Cdd:PRK13252 368 AP-TVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVI 403
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
107-443 |
1.69e-33 |
|
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: 131.60 E-value: 1.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 107 GAKSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSrhlsALLSELVGNYFK----PEKL-QFYCET 181
Cdd:cd07102 107 GFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQT----PLCGERFAAAFAeaglPEGVfQVLHLS 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 182 GEVGIAFSKLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVD 260
Cdd:cd07102 183 HETSAALIADPrIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIE 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 261 YVFVHQSQLALFIDTATRWAKKHV---PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGAdvITLSD----QVADANTRKL 333
Cdd:cd07102 263 RIYVHESIYDAFVEAFVAVVKGYKlgdPLDPSTTLGPVVSARAADFVRAQIADAIAKGA--RALIDgalfPEDKAGGAYL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 334 PLTLILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVN--DALfh 411
Cdd:cd07102 341 APTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNrcDYL-- 418
|
330 340 350
....*....|....*....|....*....|..
gi 1859350786 412 vgQHDLPFGGVGASGMGHYHGYEGFLTFSKLR 443
Cdd:cd07102 419 --DPALAWTGVKDSGRGVTLSRLGYDQLTRPK 448
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
112-437 |
4.57e-32 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 128.10 E-value: 4.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 112 VIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNYFKPEKLqFYCETGEVGIAFSKL 191
Cdd:PRK11241 142 VIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGV-FNVVTGSAGAVGGEL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 192 PFD----HLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQS 267
Cdd:PRK11241 221 TSNplvrKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 268 QLALFIDT-ATRWAKKHVPDIHSQDYTA--IIDDRAFKRLTNCIEEAKQLGADVITLSDQVADANTRKLPlTLILNSNDS 344
Cdd:PRK11241 301 VYDRFAEKlQQAVSKLHIGDGLEKGVTIgpLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQP-TILVDVPAN 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 345 MSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDALfhVGQHDLPFGGVGA 424
Cdd:PRK11241 380 AKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGI--ISNEVAPFGGIKA 457
|
330
....*....|....*.
gi 1859350786 425 SGMGH---YHGYEGFL 437
Cdd:PRK11241 458 SGLGRegsKYGIEDYL 473
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
113-428 |
1.21e-31 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 126.80 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 113 IPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNYFKPEKLQFYCETG-EVGIAFSKL 191
Cdd:cd07116 133 FHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGFGlEAGKPLASS 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 192 P-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVI------ATDYPMQKAVER-IMYVkqMNAGQICTNVDYVF 263
Cdd:cd07116 213 KrIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPNIFfadvmdADDAFFDKALEGfVMFA--LNQGEVCTCPSRAL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 264 VHQSQLALFIDTATRWAKKhVPDIHSQDYTAIIDDRA----FKRLTNCIEEAKQLGADVIT------LSDQVADANTRKl 333
Cdd:cd07116 291 IQESIYDRFMERALERVKA-IKQGNPLDTETMIGAQAsleqLEKILSYIDIGKEEGAEVLTggerneLGGLLGGGYYVP- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 334 plTLILNSNDsMSIDTRETFGPILMVKTYQDSQQVV----DYIAG-------RDRPLAfYPFSYNKQlinfyieqvmSGG 402
Cdd:cd07116 369 --TTFKGGNK-MRIFQEEIFGPVLAVTTFKDEEEALeianDTLYGlgagvwtRDGNTA-YRMGRGIQ----------AGR 434
|
330 340
....*....|....*....|....*.
gi 1859350786 403 VSVNdaLFHVGQHDLPFGGVGASGMG 428
Cdd:cd07116 435 VWTN--CYHLYPAHAAFGGYKQSGIG 458
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
20-428 |
2.35e-31 |
|
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: 125.76 E-value: 2.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 20 AQRSHAKAAGIEnyqQRREHLLALKAMITENQARIIEAINQDYGnRSRHETLlAEIINACADINSTLKHLKKWMKVQKRH 99
Cdd:cd07082 50 AGRGWWPTMPLE---ERIDCLHKFADLLKENKEEVANLLMWEIG-KTLKDAL-KEVDRTIDYIRDTIEELKRLDGDSLPG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 100 VDHRMYLGAKSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEdsrhLSALLSELVGNYFK----PEKL 175
Cdd:cd07082 125 DWFPGTKGKIAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPAT----QGVLLGIPLAEAFHdagfPKGV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 176 qFYCETG---EVGiafsklpfDHLM---------FTGSGETGKKVMAAAAqnLTPVTLELGGKSPAVIATDYPMQKAVER 243
Cdd:cd07082 201 -VNVVTGrgrEIG--------DPLVthgridvisFTGSTEVGNRLKKQHP--MKRLVLELGGKDPAIVLPDADLELAAKE 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 244 IM-----YvkqmnAGQICTNVDYVFVHQSQLALFIDT-ATRWAKKHV--PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLG 315
Cdd:cd07082 270 IVkgalsY-----SGQRCTAIKRVLVHESVADELVELlKEEVAKLKVgmPWDNGVDITPLIDPKSADFVEGLIDDAVAKG 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 316 ADVITlsdqvadANTRKLPL----TLILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLI 391
Cdd:cd07082 345 ATVLN-------GGGREGGNliypTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKA 417
|
410 420 430
....*....|....*....|....*....|....*..
gi 1859350786 392 NFYIEQVMSGGVSVNDALFHvGQHDLPFGGVGASGMG 428
Cdd:cd07082 418 RKLADALEVGTVNINSKCQR-GPDHFPFLGRKDSGIG 453
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
116-428 |
2.80e-30 |
|
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: 122.35 E-value: 2.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 116 PLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSeDSRHLSAL-LSELVGnyfkpeklqfycETGEVGIAFSKLPFD 194
Cdd:cd07147 123 PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPA-SRTPLSALiLGEVLA------------ETGLPKGAFSVLPCS 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 195 H--------------LMFTGSGETGKKVMAAAAQNltPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVD 260
Cdd:cd07147 190 RddadllvtderiklLSFTGSPAVGWDLKARAGKK--KVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQ 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 261 YVFVHQSQLALFIDTATRWAKKHV---PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADVITlsdqvadANTRKLPL-- 335
Cdd:cd07147 268 RVLVHRSVYDEFKSRLVARVKALKtgdPKDDATDVGPMISESEAERVEGWVNEAVDAGAKLLT-------GGKRDGALle 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 336 -TLILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDYI--------AG---RDRPLAFYPFsynkqlinfyiEQVMSGGV 403
Cdd:cd07147 341 pTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVndskfglqAGvftRDLEKALRAW-----------DELEVGGV 409
|
330 340
....*....|....*....|....*.
gi 1859350786 404 SVNDA-LFHVGQhdLPFGGVGASGMG 428
Cdd:cd07147 410 VINDVpTFRVDH--MPYGGVKDSGIG 433
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
101-429 |
3.32e-30 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 122.67 E-value: 3.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 101 DHRMYlgaksrVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNYFKPEKL----- 175
Cdd:cd07086 124 GHRLM------EQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLEKNGLppgvv 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 176 QFYCETGEVGIAFSKLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQ 254
Cdd:cd07086 198 NLVTGGGDGGELLVHDPrVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQ 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 255 ICTNVDYVFVHQSQLALFIDTATRWAKKHV---PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADVITlSDQVADANTR 331
Cdd:cd07086 278 RCTTTRRLIVHESVYDEFLERLVKAYKQVRigdPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLT-GGKRIDGGEP 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 332 K---LPlTLILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMS--GGVSVN 406
Cdd:cd07086 357 GnyvEP-TIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKGSdcGIVNVN 435
|
330 340
....*....|....*....|....*..
gi 1859350786 407 ----DALFHvgqhdLPFGGVGASGMGH 429
Cdd:cd07086 436 iptsGAEIG-----GAFGGEKETGGGR 457
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
105-435 |
6.49e-30 |
|
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: 121.31 E-value: 6.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 105 YLGAKSR---VIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRhLSA--LLSELVGNYFKPEKLQFYC 179
Cdd:cd07146 106 TANGKARkifTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTP-LSAiyLADLLYEAGLPPDMLSVVT 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 180 -ETGEVGIAFSKLP-FDHLMFTGSGETGKKVMAAAAQNLTpvTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICT 257
Cdd:cd07146 185 gEPGEIGDELITHPdVDLVTFTGGVAVGKAIAATAGYKRQ--LLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 258 NVDYVFVHQSQLALFIDTATRWAKKHV---PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADVITlsdqvadANTRK-- 332
Cdd:cd07146 263 AVKRILVHESVADEFVDLLVEKSAALVvgdPMDPATDMGTVIDEEAAIQIENRVEEAIAQGARVLL-------GNQRQga 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 333 -LPLTLILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDalfh 411
Cdd:cd07146 336 lYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNE---- 411
|
330 340
....*....|....*....|....*..
gi 1859350786 412 VGQHDL---PFGGVGASGMGhyhGYEG 435
Cdd:cd07146 412 VPGFRSelsPFGGVKDSGLG---GKEG 435
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
112-428 |
4.48e-29 |
|
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: 119.28 E-value: 4.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 112 VIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNYFKPEK-LQFYCETG-EVGIAFS 189
Cdd:cd07097 131 TTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGvFNLVMGSGsEVGQALV 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 190 KLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQSQ 268
Cdd:cd07097 211 EHPdVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGI 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 269 LALFIDTATRWAKKHVPDiHSQDYTA----IIDDRAFKRLTNCIEEAKQLGADVITLSDQVadanTRK-----LPLTLIL 339
Cdd:cd07097 291 HDRFVEALVERTKALKVG-DALDEGVdigpVVSERQLEKDLRYIEIARSEGAKLVYGGERL----KRPdegyyLAPALFA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 340 NSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDALFHVGQHdLPF 419
Cdd:cd07097 366 GVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYH-VPF 444
|
....*....
gi 1859350786 420 GGVGASGMG 428
Cdd:cd07097 445 GGRKGSSYG 453
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
114-444 |
4.07e-28 |
|
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: 116.73 E-value: 4.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 114 PQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRhLSALL-SELVGNY-FKPEKLQFYCETGEVGIAFSKL 191
Cdd:cd07111 145 WKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTP-LTALLfAEICAEAgLPPGVLNIVTGNGSFGSALANH 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 192 P-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQSQLA 270
Cdd:cd07111 224 PgVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 271 LFIDT-ATRWAKKHVPDI--HSQDYTAIIDDRAFKRLTNCIEEAKQLGADVItlsdQVADANTRK---LPLTLILNSNDS 344
Cdd:cd07111 304 ELIRKlKERMSHLRVGDPldKAIDMGAIVDPAQLKRIRELVEEGRAEGADVF----QPGADLPSKgpfYPPTLFTNVPPA 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 345 MSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNdalfhvgQHDL-----PF 419
Cdd:cd07111 380 SRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWIN-------GHNLfdaaaGF 452
|
330 340
....*....|....*....|....*
gi 1859350786 420 GGVGASGMGHYHGYEGFLTFskLRP 444
Cdd:cd07111 453 GGYRESGFGREGGKEGLYEY--LRP 475
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
116-432 |
2.25e-27 |
|
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: 113.93 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 116 PLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKmsEDSR------HLSALLSELVGnyFKPEKLQFYCETGEVGIAFS 189
Cdd:cd07152 110 PLGVVGVISPFNFPLILAMRSVAPALALGNAVVLK--PDPRtpvsggVVIARLFEEAG--LPAGVLHVLPGGADAGEALV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 190 KLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQSQ 268
Cdd:cd07152 186 EDPnVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 269 LALFIDTATRWAKK-HVPDIHSQDYT--AIIDDRAFKRLTNCIEEAKQLGADVITlsdqVADANTRKLPLTLILNSNDSM 345
Cdd:cd07152 266 ADAYTAKLAAKAKHlPVGDPATGQVAlgPLINARQLDRVHAIVDDSVAAGARLEA----GGTYDGLFYRPTVLSGVKPGM 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 346 SIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDALFHVGQHDlPFGGVGAS 425
Cdd:cd07152 342 PAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQTVNDEPHN-PFGGMGAS 420
|
....*..
gi 1859350786 426 GMGHYHG 432
Cdd:cd07152 421 GNGSRFG 427
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
112-446 |
2.71e-26 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 111.53 E-value: 2.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 112 VIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRhLSAL-LSELVGNYFKPEK-LQFYCETG-EVGIAF 188
Cdd:PRK09847 153 IVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSP-LSAIrLAGLAKEAGLPDGvLNVVTGFGhEAGQAL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 189 SKLP-FDHLMFTGSGETGKKVMAAAAQ-NLTPVTLELGGKSPAVIATDYP-MQKAVER----IMYvkqmNAGQICTNVDY 261
Cdd:PRK09847 232 SRHNdIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIVFADCPdLQQAASAtaagIFY----NQGQVCIAGTR 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 262 VFVHQSQ----LALFIDTATRWAKKHVPDIHSQDYTAIIDDRAFKrLTNCIEEAKQLGAdviTLSDQVADANTRKLPLTL 337
Cdd:PRK09847 308 LLLEESIadefLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADS-VHSFIREGESKGQ---LLLDGRNAGLAAAIGPTI 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 338 ILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDalFHVGQHDL 417
Cdd:PRK09847 384 FVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNN--YNDGDMTV 461
|
330 340
....*....|....*....|....*....
gi 1859350786 418 PFGGVGASGMGHYHGYEGFLTFSKLRPVF 446
Cdd:PRK09847 462 PFGGYKQSGNGRDKSLHALEKFTELKTIW 490
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
115-445 |
2.79e-26 |
|
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: 111.43 E-value: 2.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 115 QPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRhLSAL----LSELVGnyFKPEKLQFYCETGE-VGIAFS 189
Cdd:cd07140 146 EPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTP-LTALkfaeLTVKAG--FPKGVINILPGSGSlVGQRLS 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 190 KLP-FDHLMFTGSGETGKKVM-AAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQS 267
Cdd:cd07140 223 DHPdVRKLGFTGSTPIGKHIMkSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEES 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 268 QLALFIDTATRWAKK------------HVPdihsQDYTAIIDdrafkRLTNCIEEAKQLGADVITLSDQVaDANTRKLPL 335
Cdd:cd07140 303 IHDEFVRRVVEEVKKmkigdpldrstdHGP----QNHKAHLD-----KLVEYCERGVKEGATLVYGGKQV-DRPGFFFEP 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 336 TLILNSNDSMSIDTRETFGPILMVKTYQDS--QQVVDYIAGRDRPLAFYPFS--YNKQLinFYIEQVMSGGVSVNdaLFH 411
Cdd:cd07140 373 TVFTDVEDHMFIAKEESFGPIMIISKFDDGdvDGVLQRANDTEYGLASGVFTkdINKAL--YVSDKLEAGTVFVN--TYN 448
|
330 340 350
....*....|....*....|....*....|....
gi 1859350786 412 VGQHDLPFGGVGASGMGHYHGYEGFLTFSKLRPV 445
Cdd:cd07140 449 KTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
116-371 |
9.87e-26 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 109.61 E-value: 9.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 116 PLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRhLSAL-LSELVGNYFKPEKLQFYCETGE-VGIAFSKLP- 192
Cdd:PRK13473 138 PVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITP-LTALkLAELAADILPPGVLNVVTGRGAtVGDALVGHPk 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 193 FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQSQLALF 272
Cdd:PRK13473 217 VRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDL 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 273 I-DTATRWAKKHV--PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLG-ADVITLSDQVADANTRKLPlTLILNSNDSMSID 348
Cdd:PRK13473 297 VaKLAAAVATLKVgdPDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEP-TLLAGARQDDEIV 375
|
250 260
....*....|....*....|...
gi 1859350786 349 TRETFGPILMVKTYQDSQQVVDY 371
Cdd:PRK13473 376 QREVFGPVVSVTPFDDEDQAVRW 398
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
102-428 |
7.51e-25 |
|
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: 107.31 E-value: 7.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 102 HRMYLGAKSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSEL---VGnyFKPEKLQFY 178
Cdd:cd07124 152 VEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEIleeAG--LPPGVVNFL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 179 ceTG---EVGIAFSKLPFDHLM-FTGSGETGKKVMAAAAQ------NLTPVTLELGGKSPAVIATDYPMQKAVERIMYVK 248
Cdd:cd07124 230 --PGpgeEVGDYLVEHPDVRFIaFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSA 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 249 QMNAGQICTNVDYVFVHQSQLALFID---TATRWAKKHVPDIHSQDYTAIIDDRAFKRLTNCIEEAKQ-----LGADVIT 320
Cdd:cd07124 308 FGFQGQKCSACSRVIVHESVYDEFLErlvERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSegrllLGGEVLE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 321 LSDQ--------VADAntrklpltlilnsnDSMS-IDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLI 391
Cdd:cd07124 388 LAAEgyfvqptiFADV--------------PPDHrLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHL 453
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1859350786 392 NFYIEQVMSGGVSVN----DALfhVGQHdlPFGGVGASGMG 428
Cdd:cd07124 454 ERARREFEVGNLYANrkitGAL--VGRQ--PFGGFKMSGTG 490
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
19-438 |
3.83e-24 |
|
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: 104.97 E-value: 3.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 19 VAQRSHA--KAAGIenYQQRREHLLALKAMitENQARIIEAINQdygnrsrhetlLAEIINACAdinstlKHLKKWMKVQ 96
Cdd:cd07083 76 QEDRARLllKAADL--LRRRRRELIATLTY--EVGKNWVEAIDD-----------VAEAIDFIR------YYARAALRLR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 97 KRHVDHRMYLGAKSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNY-FKPEKL 175
Cdd:cd07083 135 YPAVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAgFPPGVV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 176 QFYCETGE-VGIAFSKLP-FDHLMFTGSGETGKKVMAAAAQNLT------PVTLELGGKSPAVIATDYPMQKAVERIMYV 247
Cdd:cd07083 215 QFLPGVGEeVGAYLTEHErIRGINFTGSLETGKKIYEAAARLAPgqtwfkRLYVETGGKNAIIVDETADFELVVEGVVVS 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 248 KQMNAGQICTNVDYVFVHQSQLALFIDTATRWAKKHV---PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGAdvITLSDQ 324
Cdd:cd07083 295 AFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSvgpPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQ--LVLGGK 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 325 VADANTRKLPLTLILNSNDSMSIDTRETFGPILMVKTYQDSQ--QVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGG 402
Cdd:cd07083 373 RLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGN 452
|
410 420 430
....*....|....*....|....*....|....*...
gi 1859350786 403 VSVNDALFH--VGQHdlPFGGVGASGMGHYHGYEGFLT 438
Cdd:cd07083 453 LYINRKITGalVGVQ--PFGGFKLSGTNAKTGGPHYLR 488
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
33-439 |
1.02e-23 |
|
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: 102.92 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 33 YQQRREHLLALKAMITENQARIIEAINQDYGNRSRHEtlLAEIiNACADI-NSTLKHLKKWMKVQKRHVDhrmylGAKSR 111
Cdd:cd07100 20 FAERAALLRKLADLLRERKDELARLITLEMGKPIAEA--RAEV-EKCAWIcRYYAENAEAFLADEPIETD-----AGKAY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 112 VIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKmsedsrH-----LSALLSELVgnyFKpeklqfycetgEVGI 186
Cdd:cd07100 92 VRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLK------HasnvpGCALAIEEL---FR-----------EAGF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 187 ---AFSKLPFDH-----LM---------FTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQ 249
Cdd:cd07100 152 pegVFQNLLIDSdqveaIIadprvrgvtLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 250 MNAGQICTNVDYVFVHQSQLALFIDTATRWAKKHV---PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADViTLSDQVA 326
Cdd:cd07100 232 QNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKvgdPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATL-LLGGKRP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 327 DANTRKLPLTLILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDyIAGrDRP--LAFYPFSYNKQLINFYIEQVMSGGVS 404
Cdd:cd07100 311 DGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIA-LAN-DSPfgLGGSVFTTDLERAERVARRLEAGMVF 388
|
410 420 430
....*....|....*....|....*....|....*.
gi 1859350786 405 VNDalfHVGQH-DLPFGGVGASGMGHYHGYEGFLTF 439
Cdd:cd07100 389 ING---MVKSDpRLPFGGVKRSGYGRELGRFGIREF 421
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
115-428 |
1.34e-22 |
|
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: 100.19 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 115 QPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRhLSAL-LSELVGNYFKPEK-LQFY-CE--TGEVGIAFS 189
Cdd:cd07148 123 EPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATP-LSCLaFVDLLHEAGLPEGwCQAVpCEnaVAEKLVTDP 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 190 KLPFdhLMFTGSGETGKKVMAAAAQNlTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQSQL 269
Cdd:cd07148 202 RVAF--FSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIA 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 270 ALFIDTATRWAKKHV---PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADVITLSDQVADanTRKLPlTLILNSNDSMS 346
Cdd:cd07148 279 DDFAQRLAAAAEKLVvgdPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKRLSD--TTYAP-TVLLDPPRDAK 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 347 IDTRETFGPILMVKTYQDSQQVVDyiAGRDRPLAFYP--FSYNKQLINFYIEQVMSGGVSVND-ALFHVgqhD-LPFGGV 422
Cdd:cd07148 356 VSTQEIFGPVVCVYSYDDLDEAIA--QANSLPVAFQAavFTKDLDVALKAVRRLDATAVMVNDhTAFRV---DwMPFAGR 430
|
....*.
gi 1859350786 423 GASGMG 428
Cdd:cd07148 431 RQSGYG 436
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
103-428 |
1.59e-22 |
|
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: 100.37 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 103 RMYLGAKSRVIPQ----PLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNY-FKPEKLQF 177
Cdd:TIGR01238 143 RYYAKQVRDVLGEfsveSRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAgFPAGTIQL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 178 YCETGE-VGIAFSKLP-FDHLMFTGSGETGKKVMAAAAQNL---TPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNA 252
Cdd:TIGR01238 223 LPGRGAdVGAALTSDPrIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 253 GQICTNVDYVFVHQS---QLALFIDTATRWAKKHVPDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADV--ITLSDQVAD 327
Cdd:TIGR01238 303 GQRCSALRVLCVQEDvadRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIaqLTLDDSRAC 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 328 ANTRKLPLTLI-LNSNDSMSidtRETFGPILMVKTYQDSQ--QVVDYIAGRDRPLAFYPFSYNKQLI----------NFY 394
Cdd:TIGR01238 383 QHGTFVAPTLFeLDDIAELS---EEVFGPVLHVVRYKAREldQIVDQINQTGYGLTMGVHSRIETTYrwiekharvgNCY 459
|
330 340 350
....*....|....*....|....*....|....
gi 1859350786 395 IEQVMSGGVsvndalfhVGQHdlPFGGVGASGMG 428
Cdd:TIGR01238 460 VNRNQVGAV--------VGVQ--PFGGQGLSGTG 483
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
33-426 |
1.08e-20 |
|
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: 94.26 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 33 YQQRREHLLALKAMITENQARIIEAINQDYGnRSRHETLlAEIINACADINSTLKHLkkwmkvQKRHVDHRMYLG-AKSR 111
Cdd:cd07095 21 LEERAAILRRFAELLKANKEELARLISRETG-KPLWEAQ-TEVAAMAGKIDISIKAY------HERTGERATPMAqGRAV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 112 VIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEdsrhLSALLSELVGNY-----FKPEKLQFYCETGEVGI 186
Cdd:cd07095 93 LRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSE----LTPAVAELMVELweeagLPPGVLNLVQGGRETGE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 187 AFSKLP-FDHLMFTGSGETGKKVMAAAAQNltP---VTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYV 262
Cdd:cd07095 169 ALAAHEgIDGLLFTGSAATGLLLHRQFAGR--PgkiLALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 263 FVHQSQLA-LFIDTATRWAKKHVPDIHSQDYT----AIIDDRAFKRLTNCiEEAKQLGADVItLSDQVADANTRKLPLTL 337
Cdd:cd07095 247 IVPDGAVGdAFLERLVEAAKRLRIGAPDAEPPfmgpLIIAAAAARYLLAQ-QDLLALGGEPL-LAMERLVAGTAFLSPGI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 338 ILNSNDSMSIDtRETFGPILMVKTYQDSQQVVDyIAGRDR-PLAFYPFSYNKQLINFYIEQVMSGGVSVNDAL-FHVGqh 415
Cdd:cd07095 325 IDVTDAADVPD-EEIFGPLLQVYRYDDFDEAIA-LANATRfGLSAGLLSDDEALFERFLARIRAGIVNWNRPTtGASS-- 400
|
410
....*....|.
gi 1859350786 416 DLPFGGVGASG 426
Cdd:cd07095 401 TAPFGGVGLSG 411
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
115-428 |
5.44e-20 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 92.64 E-value: 5.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 115 QPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELvgnYFK----PEKLQF-YCETGEVGIAFS 189
Cdd:cd07125 166 HGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVEL---LHEagvpRDVLQLvPGDGEEIGEALV 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 190 KLP-FDHLMFTGSGETGK---KVMAAAAQNLTPVTLELGGKSpAVIATdyPM---QKAVERIMYVKQMNAGQICTNVDYV 262
Cdd:cd07125 243 AHPrIDGVIFTGSTETAKlinRALAERDGPILPLIAETGGKN-AMIVD--STalpEQAVKDVVQSAFGSAGQRCSALRLL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 263 FVHQS----QLALFIDTAtrwAKKHV--PDIHSQDYTAIIDDRAFKRLTNCIEEAKqlGADVITLSDQVADANTRKLPLT 336
Cdd:cd07125 320 YLQEEiaerFIEMLKGAM---ASLKVgdPWDLSTDVGPLIDKPAGKLLRAHTELMR--GEAWLIAPAPLDDGNGYFVAPG 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 337 LILNSNDSMSidTRETFGPILMVKTYQDSQ--QVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVN----DALf 410
Cdd:cd07125 395 IIEIVGIFDL--TTEVFGPILHVIRFKAEDldEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINrnitGAI- 471
|
330
....*....|....*....
gi 1859350786 411 hVG-QhdlPFGGVGASGMG 428
Cdd:cd07125 472 -VGrQ---PFGGWGLSGTG 486
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
71-368 |
5.92e-19 |
|
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: 88.83 E-value: 5.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 71 LLAEIINACADINSTLKHLKKWMKVQKRHVdhrmylgaksRVipqPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVK 150
Cdd:cd07084 68 ARAFVIYSYRIPHEPGNHLGQGLKQQSHGY----------RW---PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 151 MSEDSRHLSALLSELVGNYFK--PEKLQFYCETGEVGIAFSKLP-FDHLMFTGSGETGKKVMAAAAQnlTPVTLELGGKS 227
Cdd:cd07084 135 PHTAVSIVMQIMVRLLHYAGLlpPEDVTLINGDGKTMQALLLHPnPKMVLFTGSSRVAEKLALDAKQ--ARIYLELAGFN 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 228 PAVIATDYP----MQKAVERIMYVKqmnAGQICTNVDYVFVHQS-QLALFIDTATRWAKKHVPD------IHSQDYTAII 296
Cdd:cd07084 213 WKVLGPDAQavdyVAWQCVQDMTAC---SGQKCTAQSMLFVPENwSKTPLVEKLKALLARRKLEdlllgpVQTFTTLAMI 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 297 -----DDRAFKRLTNCIEEAKQL----GADVITLSDQVADANTRKLPLTlilnsndsmsidTRETFGPILMVKTYQDSQQ 367
Cdd:cd07084 290 ahmenLLGSVLLFSGKELKNHSIpsiyGACVASALFVPIDEILKTYELV------------TEEIFGPFAIVVEYKKDQL 357
|
.
gi 1859350786 368 V 368
Cdd:cd07084 358 A 358
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
101-371 |
7.57e-18 |
|
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: 85.72 E-value: 7.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 101 DHRMYlgaksrVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEdSRHLSAL------LSELVGNYFKPEK 174
Cdd:cd07130 123 GHRMM------EQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSP-TTPLTAIavtkivARVLEKNGLPGAI 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 175 LQFYCETGEVGIAFSKLP-FDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAG 253
Cdd:cd07130 196 ASLVCGGADVGEALVKDPrVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAG 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 254 QICTNVDYVFVHQSQLALFIDTATRwAKKHV-------PDIHsqdYTAIIDDRAFKRLTNCIEEAKQLGADVITLSDQVA 326
Cdd:cd07130 276 QRCTTTRRLIVHESIYDEVLERLKK-AYKQVrigdpldDGTL---VGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVID 351
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1859350786 327 DANTRKLPlTLILNSNDsMSIDTRETFGPILMVKTYQDSQQVVDY 371
Cdd:cd07130 352 GPGNYVEP-TIVEGLSD-APIVKEETFAPILYVLKFDTLEEAIAW 394
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
115-315 |
7.46e-15 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 76.51 E-value: 7.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 115 QPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELV---GnyFKPEKLQFYCETG-EVGIAFSK 190
Cdd:PRK03137 170 IPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLeeaG--LPAGVVNFVPGSGsEVGDYLVD 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 191 LPFDHLM-FTGSGETGKKVMAAAA-----QN-LTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVF 263
Cdd:PRK03137 248 HPKTRFItFTGSREVGLRIYERAAkvqpgQIwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAI 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1859350786 264 VHQSQLALFIDTATRWAKK-HVPDIHSQDY-TAIIDDRAFKRLTNCIEEAKQLG 315
Cdd:PRK03137 328 VHEDVYDEVLEKVVELTKElTVGNPEDNAYmGPVINQASFDKIMSYIEIGKEEG 381
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
116-426 |
4.62e-14 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 74.22 E-value: 4.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 116 PLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEdsrhLSALLSELVgnyfkpekLQFYCETG------------- 182
Cdd:PRK09457 134 PHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSE----LTPWVAELT--------VKLWQQAGlpagvlnlvqggr 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 183 EVGIAFSKLP-FDHLMFTGSGETG-----------KKVMAaaaqnltpvtLELGGKSPAVIATDYPMQKAVERIMYVKQM 250
Cdd:PRK09457 202 ETGKALAAHPdIDGLLFTGSANTGyllhrqfagqpEKILA----------LEMGGNNPLVIDEVADIDAAVHLIIQSAFI 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 251 NAGQICTNVDYVFVHQSQ-----LALFIDTATRwAKKHVPDIHSQDYT-AIIDDRAFKRLTNCIEEAKQLGADVItLSDQ 324
Cdd:PRK09457 272 SAGQRCTCARRLLVPQGAqgdafLARLVAVAKR-LTVGRWDAEPQPFMgAVISEQAAQGLVAAQAQLLALGGKSL-LEMT 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 325 VADANTRKLPLTLIlnsnDSMSIDTR---ETFGPILMVKTYQDSQQVVDyIAGRDR-PLAFYPFSYNKQLINFYIEQVMS 400
Cdd:PRK09457 350 QLQAGTGLLTPGII----DVTGVAELpdeEYFGPLLQVVRYDDFDEAIR-LANNTRfGLSAGLLSDDREDYDQFLLEIRA 424
|
330 340
....*....|....*....|....*..
gi 1859350786 401 GGVSVNDALfhVG-QHDLPFGGVGASG 426
Cdd:PRK09457 425 GIVNWNKPL--TGaSSAAPFGGVGASG 449
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
116-428 |
1.92e-13 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 72.10 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 116 PLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVK----------MSEDSRHLSALLSELVGnyfkpeklqfyCETG--- 182
Cdd:PLN00412 158 PLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKpptqgavaalHMVHCFHLAGFPKGLIS-----------CVTGkgs 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 183 EVGIAFSKLP-FDHLMFTGsGETGKKVMAAAAqnLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDY 261
Cdd:PLN00412 227 EIGDFLTMHPgVNCISFTG-GDTGIAISKKAG--MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKV 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 262 VFVHQSQL-ALFIDTATRWAKKHV-PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGAdviTLSDQVADANTRKLPLtLIL 339
Cdd:PLN00412 304 VLVMESVAdALVEKVNAKVAKLTVgPPEDDCDITPVVSESSANFIEGLVMDAKEKGA---TFCQEWKREGNLIWPL-LLD 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 340 NSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFS--YNKQLInfyIEQVM-SGGVSVNDALFHVGQHd 416
Cdd:PLN00412 380 NVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTrdINKAIL---ISDAMeTGTVQINSAPARGPDH- 455
|
330
....*....|..
gi 1859350786 417 LPFGGVGASGMG 428
Cdd:PLN00412 456 FPFQGLKDSGIG 467
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
36-445 |
8.80e-13 |
|
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: 70.24 E-value: 8.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 36 RREHLLALKAMITENQARIIEAINQDYG---NRSRHETLLA-EIINACADINSTLKhlKKWMKVQKRHVDHRMYlgaksR 111
Cdd:cd07085 62 RQQVMFKFRQLLEENLDELARLITLEHGktlADARGDVLRGlEVVEFACSIPHLLK--GEYLENVARGIDTYSY-----R 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 112 vipQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSEL---------VGN--YFKPEKLQFYCE 180
Cdd:cd07085 135 ---QPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELlqeaglpdgVLNvvHGGKEAVNALLD 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 181 TGEVGiAFSklpfdhlmFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVd 260
Cdd:cd07085 212 HPDIK-AVS--------FVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMAL- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 261 yvfvhqsQLALFI-DTATRWAKKHVPDIHS----------QDYTAIIDDRAFKRLTNCIEEAKQLGADVitlsdqVADAN 329
Cdd:cd07085 282 -------SVAVAVgDEADEWIPKLVERAKKlkvgagddpgADMGPVISPAAKERIEGLIESGVEEGAKL------VLDGR 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 330 TRKLPL---------TLILNSNDSMSIDTRETFGP---ILMVKTYQDSQQVVD---Y-----IAGRDRPLAFYpfsynkq 389
Cdd:cd07085 349 GVKVPGyengnfvgpTILDNVTPDMKIYKEEIFGPvlsIVRVDTLDEAIAIINanpYgngaaIFTRSGAAARK------- 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1859350786 390 linfYIEQVMSGGVSVN------DALFhvgqhdlPFGGVGAS--GMGHYHGYEGFLTFSKLRPV 445
Cdd:cd07085 422 ----FQREVDAGMVGINvpipvpLAFF-------SFGGWKGSffGDLHFYGKDGVRFYTQTKTV 474
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
115-428 |
1.17e-12 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 69.77 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 115 QPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNYFKPEKlqfyC-ETGEVGI-AFSKLP 192
Cdd:PRK09406 122 QPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAGFPDG----CfQTLLVGSgAVEAIL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 193 FDHLM----FTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQSQ 268
Cdd:PRK09406 198 RDPRVaaatLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADV 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 269 LALFIDT-ATRWAKKHV--PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADVITLSDQVaDANTRKLPLTLILNSNDSM 345
Cdd:PRK09406 278 YDAFAEKfVARMAALRVgdPTDPDTDVGPLATEQGRDEVEKQVDDAVAAGATILCGGKRP-DGPGWFYPPTVITDITPDM 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 346 SIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDalFHVGQHDLPFGGVGAS 425
Cdd:PRK09406 357 RLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFING--MTVSYPELPFGGVKRS 434
|
...
gi 1859350786 426 GMG 428
Cdd:PRK09406 435 GYG 437
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
115-428 |
1.20e-12 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 70.28 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 115 QPLGVVGLIVPWNFPinLA-FS-QLAAAFSAGNKAMVKMSEDSRHLSALLSEL---VGnyfKPEK-LQFYCETGE-VGIA 187
Cdd:PRK11905 675 KPLGPVVCISPWNFP--LAiFTgQIAAALVAGNTVLAKPAEQTPLIAARAVRLlheAG---VPKDaLQLLPGDGRtVGAA 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 188 FSKLP-FDHLMFTGSGETGK---KVMAAAAQNLTPVTLELGGKSpAVI--ATDYPMQkAVERIMYVKQMNAGQICT--NV 259
Cdd:PRK11905 750 LVADPrIAGVMFTGSTEVARliqRTLAKRSGPPVPLIAETGGQN-AMIvdSSALPEQ-VVADVIASAFDSAGQRCSalRV 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 260 DYVfvhQSQLALFIDTATRWAKK--HV--PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADVITLSDQVADANTRKLPL 335
Cdd:PRK11905 828 LCL---QEDVADRVLTMLKGAMDelRIgdPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHQLPLPAETEKGTFVAP 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 336 TLIlnSNDSMSIDTRETFGPILMVKTYQDSQ--QVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVN----DAL 409
Cdd:PRK11905 905 TLI--EIDSISDLEREVFGPVLHVVRFKADEldRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNrniiGAV 982
|
330 340
....*....|....*....|
gi 1859350786 410 fhVG-QhdlPFGGVGASGMG 428
Cdd:PRK11905 983 --VGvQ---PFGGEGLSGTG 997
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
115-446 |
2.06e-12 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 68.73 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 115 QPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNYFKPEKLQFYCETGEVGIafSKLPFD 194
Cdd:PRK13968 125 RPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGV--SQMIND 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 195 H----LMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQSQLA 270
Cdd:PRK13968 203 SriaaVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIAS 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 271 LFID---TATRWAKKHVPDIHSQDYTAI----IDDRAFKRLTNCIEEakqlGADVITLSDQVADANTRKLPlTLILNSND 343
Cdd:PRK13968 283 AFTErfvAAAAALKMGDPRDEENALGPMarfdLRDELHHQVEATLAE----GARLLLGGEKIAGAGNYYAP-TVLANVTP 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 344 SMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDalFHVGQHDLPFGGVG 423
Cdd:PRK13968 358 EMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFING--YCASDARVAFGGVK 435
|
330 340
....*....|....*....|...
gi 1859350786 424 ASGMGHYHGYEGFLTFSKLRPVF 446
Cdd:PRK13968 436 KSGFGRELSHFGLHEFCNIQTVW 458
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
116-428 |
8.45e-11 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 64.61 E-value: 8.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 116 PLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSA----LLSElVGnyFKPEKLQFYCETGE-VGIAFSK 190
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAqavrILLE-AG--VPAGVVQLLPGRGEtVGAALVA 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 191 lpfDH----LMFTGSGETGKKVMAAAAQNL------TPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVD 260
Cdd:PRK11809 845 ---DArvrgVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALR 921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 261 yVFVHQSQLALFIDTATRWAKKHV----PDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADVitlsDQVADANTRK---- 332
Cdd:PRK11809 922 -VLCLQDDVADRTLKMLRGAMAECrmgnPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPV----FQAARENSEDwqsg 996
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 333 --LPLTLI-LNSNDSMsidTRETFGPILMVKTYQDSQ--QVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVND 407
Cdd:PRK11809 997 tfVPPTLIeLDSFDEL---KREVFGPVLHVVRYNRNQldELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNR 1073
|
330 340
....*....|....*....|....*.
gi 1859350786 408 ALfhVG-----QhdlPFGGVGASGMG 428
Cdd:PRK11809 1074 NM--VGavvgvQ---PFGGEGLSGTG 1094
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
116-370 |
2.78e-10 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 62.54 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 116 PLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNYFKPEKL-----QFYCETGEVGIAFSK 190
Cdd:PLN02315 154 PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLpgaifTSFCGGAEIGEAIAK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 191 ---LPFdhLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVFVHQS 267
Cdd:PLN02315 234 dtrIPL--VSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHES 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 268 QLALFID---TATRWAKKHVPDIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADVITLSDQVADANTRKLPlTLILNSNDS 344
Cdd:PLN02315 312 IYDDVLEqllTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQP-TIVEISPDA 390
|
250 260
....*....|....*....|....*.
gi 1859350786 345 mSIDTRETFGPILMVKTYQDSQQVVD 370
Cdd:PLN02315 391 -DVVKEELFGPVLYVMKFKTLEEAIE 415
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
107-426 |
1.13e-09 |
|
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: 60.29 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 107 GAKSRVIPQPL-GVVGLIVPWNF-PI--NLAfsqLAAAFsAGNKAMVKMSEdsrhlSALLSelvgNYF----------KP 172
Cdd:cd07123 160 GVWNRLEYRPLeGFVYAVSPFNFtAIggNLA---GAPAL-MGNVVLWKPSD-----TAVLS----NYLvykileeaglPP 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 173 EKLQF-YCETGEVG-IAFSKLPFDHLMFTGSGETGKKVMAAAAQNLT-----P-VTLELGGKSPAVIATDYPMQKAVE-- 242
Cdd:cd07123 227 GVINFvPGDGPVVGdTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDryrtyPrIVGETGGKNFHLVHPSADVDSLVTat 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 243 -RIMYVKQmnaGQICTNVDYVFVHQSqlalfidtatRW--AKKHVPDIHSQ-------DYT----AIIDDRAFKRLTNCI 308
Cdd:cd07123 307 vRGAFEYQ---GQKCSAASRAYVPES----------LWpeVKERLLEELKEikmgdpdDFSnfmgAVIDEKAFDRIKGYI 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 309 EEAKQlgADVITLsdqVADANTRK-----LPLTLILNSNDSMSIDTRETFGPILMVKTYQDSQ-----QVVD----Y--- 371
Cdd:cd07123 374 DHAKS--DPEAEI---IAGGKCDDsvgyfVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSDfeetlELVDttspYalt 448
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1859350786 372 --IAGRDRplafypfsynkQLI------------NFYIEQVMSGGVsvndalfhVGQHdlPFGGVGASG 426
Cdd:cd07123 449 gaIFAQDR-----------KAIreatdalrnaagNFYINDKPTGAV--------VGQQ--PFGGARASG 496
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
35-445 |
2.68e-09 |
|
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: 59.12 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 35 QRREHLLALKAMITENQARIIEAINQDYGNRsrHETLLA------EIINACADINSTLKhlKKWMKVQKRHVDhrmylga 108
Cdd:TIGR01722 61 QRTSVLLRYQALLKEHRDEIAELITAEHGKT--HSDALGdvarglEVVEHACGVNSLLK--GETSTQVATRVD------- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 109 kSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNYFKPEKLQFYCETGEVGIAF 188
Cdd:TIGR01722 130 -VYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 189 SklpFDH-----LMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVdyvf 263
Cdd:TIGR01722 209 L---LEHpdvkaVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAI---- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 264 vhqsQLALFIDTATRW-------AKKHVP---DIHSQDYTAIIDDRAFKRLTNCIEEAKQLGADVitlsdqVADANTRKL 333
Cdd:TIGR01722 282 ----SAAVLVGAADEWvpeirerAEKIRIgpgDDPGAEMGPLITPQAKDRVASLIAGGAAEGAEV------LLDGRGYKV 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 334 P---------LTLILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVS 404
Cdd:TIGR01722 352 DgyeegnwvgPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVG 431
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1859350786 405 VNDAL-FHVGQHDlpFGGVGASGMG--HYHGYEGFLTFSKLRPV 445
Cdd:TIGR01722 432 VNVPIpVPLPYFS--FTGWKDSFFGdhHIYGKQGTHFYTRGKTV 473
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
107-459 |
5.27e-09 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 58.60 E-value: 5.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 107 GAKSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLSALLSELVGNYFKPEKLQ--FYCETGEV 184
Cdd:PLN02419 240 GVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLniVHGTNDTV 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 185 GIAFSKLPFDHLMFTGSGETGKKVMAAAAQNLTPVTLELGGKSPAVIATDYPMQKAVERIMYVKQMNAGQICTNVDYVfv 264
Cdd:PLN02419 320 NAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTV-- 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 265 hqsqlaLFIDTATRWAKKHV-------------PDihsQDYTAIIDDRAFKRLTNCIEEAKQLGADVITLSDQVADANTR 331
Cdd:PLN02419 398 ------VFVGDAKSWEDKLVerakalkvtcgsePD---ADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 332 K---LPLTLILNSNDSMSIDTRETFGPILMVKTYQDSQQVVDYIAGRDRPLAFYPFSYNKQLINFYIEQVMSGGVSVNDA 408
Cdd:PLN02419 469 KgnfIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVP 548
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1859350786 409 LfHVGQHDLPFGGVGASGMG--HYHGYEGFLTFSKLRPVFYQAKF--SSVKFLMP 459
Cdd:PLN02419 549 I-PVPLPFFSFTGNKASFAGdlNFYGKAGVDFFTQIKLVTQKQKDihSPFSLAIP 602
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
115-430 |
2.92e-08 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 56.36 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 115 QPLGVVGLIVPWNFPinLA-F-SQLAAAFSAGNKAMVKMSEDSRHLSALLSELvgnYFK----PEKLQFYCETGE-VGIA 187
Cdd:PRK11904 683 HGRGVFVCISPWNFP--LAiFlGQVAAALAAGNTVIAKPAEQTPLIAAEAVKL---LHEagipKDVLQLLPGDGAtVGAA 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 188 FSKLP-FDHLMFTGSGETGKKV-MAAAAQNLTPVTL--ELGGKSpAVI--ATDYPMQKAVERIMYVKQmNAGQICTNVDY 261
Cdd:PRK11904 758 LTADPrIAGVAFTGSTETARIInRTLAARDGPIVPLiaETGGQN-AMIvdSTALPEQVVDDVVTSAFR-SAGQRCSALRV 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 262 VFVHQsqlalfiDTATR--------WAKKHV--PDIHSQDYTAIIDDRAFKRLTNCIE----EAKQLGAdvITLSDQVAD 327
Cdd:PRK11904 836 LFVQE-------DIADRviemlkgaMAELKVgdPRLLSTDVGPVIDAEAKANLDAHIErmkrEARLLAQ--LPLPAGTEN 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 328 ANTrkLPLTLI-LnsnDSMSIDTRETFGPILMVKTYQDSQ--QVVDYIAGRDRPLAFYPFSYNKQLI----------NFY 394
Cdd:PRK11904 907 GHF--VAPTAFeI---DSISQLEREVFGPILHVIRYKASDldKVIDAINATGYGLTLGIHSRIEETAdriadrvrvgNVY 981
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1859350786 395 IEQVMSGGVsvndalfhVG-QhdlPFGGVGASGMG------HY 430
Cdd:PRK11904 982 VNRNQIGAV--------VGvQ---PFGGQGLSGTGpkaggpHY 1013
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
99-373 |
4.92e-08 |
|
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: 55.24 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 99 HVDHRMYLGaksrvipqPLGVVGLIVPWNFPinLAFSQL----AAAFSAGNKAMVKMSEDSRHLSALLSELVGNYFK--- 171
Cdd:cd07129 96 RPDLRRMLV--------PLGPVAVFGASNFP--LAFSVAggdtASALAAGCPVVVKAHPAHPGTSELVARAIRAALRatg 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 172 -PEKL--QFYCETGEVGIAFSKLPfdhLM----FTGSGETGKKVMAAAAQNLT--PVTLELGGKSPAV------------ 230
Cdd:cd07129 166 lPAGVfsLLQGGGREVGVALVKHP---AIkavgFTGSRRGGRALFDAAAARPEpiPFYAELGSVNPVFilpgalaergea 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 231 IATDYpmqkaVERIMyvkqMNAGQICTNVDYVFVHQSQ-LALFIDTATRWAKKHV------PDIHsqdytaiiddRAFKR 303
Cdd:cd07129 243 IAQGF-----VGSLT----LGAGQFCTNPGLVLVPAGPaGDAFIAALAEALAAAPaqtmltPGIA----------EAYRQ 303
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1859350786 304 LTNCIEEAKqlGADVITLSDQVADANTRKLPLTLI----LNSNDSMSidtRETFGPILMVKTYQDSQQVVDYIA 373
Cdd:cd07129 304 GVEALAAAP--GVRVLAGGAAAEGGNQAAPTLFKVdaaaFLADPALQ---EEVFGPASLVVRYDDAAELLAVAE 372
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
118-408 |
5.99e-08 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 54.97 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 118 GVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMSEDSRHLS-ALLSELVGNYFKPE-KLQFYCetGEVGIAFSKL-PFD 194
Cdd:cd07128 146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTeAVVKDIVESGLLPEgALQLIC--GSVGDLLDHLgEQD 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 195 HLMFTGSGETGKK--VMAAAAQNLTPVTLELGGKSPAVIATDY-PMQ-------KAVERIMYVKqmnAGQICTNVDYVFV 264
Cdd:cd07128 224 VVAFTGSAATAAKlrAHPNIVARSIRFNAEADSLNAAILGPDAtPGTpefdlfvKEVAREMTVK---AGQKCTAIRRAFV 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 265 HQSQL-ALFIDTATRWAKKHVPDIHSQDYT----AIIDDRA--FKRLTNCIEEAKQLGADVITLSDQVADANTRK-LPLT 336
Cdd:cd07128 301 PEARVdAVIEALKARLAKVVVGDPRLEGVRmgplVSREQREdvRAAVATLLAEAEVVFGGPDRFEVVGADAEKGAfFPPT 380
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1859350786 337 LILNSN--DSMSIDTRETFGPILMVKTYQDSQQVVDyIAGRDR-PLAFYPFSYNKQLINFYIEQVMS--GGVSVNDA 408
Cdd:cd07128 381 LLLCDDpdAATAVHDVEAFGPVATLMPYDSLAEAIE-LAARGRgSLVASVVTNDPAFARELVLGAAPyhGRLLVLNR 456
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
115-430 |
5.89e-07 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 52.25 E-value: 5.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 115 QPLGVVGLIVPWNFPinLA-FS-QLAAAFSAGNKAMVKMSEDSRHLSALLSEL---VGnyFKPEKLQFYCETGE-VGIAF 188
Cdd:COG4230 679 RGRGVFVCISPWNFP--LAiFTgQVAAALAAGNTVLAKPAEQTPLIAARAVRLlheAG--VPADVLQLLPGDGEtVGAAL 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 189 SKLP-FDHLMFTGSGETGKKV-MAAAAQNLTPVTL--ELGGkspaviatdypmQKAveriMYV------KQM-------- 250
Cdd:COG4230 755 VADPrIAGVAFTGSTETARLInRTLAARDGPIVPLiaETGG------------QNA----MIVdssalpEQVvddvlasa 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 251 --NAGQICtnvdyvfvhqSQL-ALFI--DTAtrwakKHV---------------PDIHSQDYTAIIDDRAFKRLTNCIEE 310
Cdd:COG4230 819 fdSAGQRC----------SALrVLCVqeDIA-----DRVlemlkgamaelrvgdPADLSTDVGPVIDAEARANLEAHIER 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 311 AKQLGADVITLSDQVADANTRKLPLTLI-LNSNDSMsidTRETFGPILMVKTYQDSQ--QVVDYIAGRDRPLAFYPFSYN 387
Cdd:COG4230 884 MRAEGRLVHQLPLPEECANGTFVAPTLIeIDSISDL---EREVFGPVLHVVRYKADEldKVIDAINATGYGLTLGVHSRI 960
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1859350786 388 KQLINFYIEQVMSGGVSVN----DALfhVG-QhdlPFGGVGASGMG------HY 430
Cdd:COG4230 961 DETIDRVAARARVGNVYVNrniiGAV--VGvQ---PFGGEGLSGTGpkaggpHY 1009
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
105-266 |
1.23e-04 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 44.41 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 105 YLGAKSRVIPQPLGVVGLIVPWNFPINLAFSQLAAAFSAGNKAMVKMseDSRhLSALLSELVGNYFK----PEKLQF-YC 179
Cdd:cd07126 131 HQGQQSSGYRWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKV--DSK-VSVVMEQFLRLLHLcgmpATDVDLiHS 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859350786 180 ETGEVGIAFSKLPFDHLMFTGSGETGKKVmaaAAQNLTPVTLELGG-----KSPAVIATDYpmqkaverIMYVKQMNA-- 252
Cdd:cd07126 208 DGPTMNKILLEANPRMTLFTGSSKVAERL---ALELHGKVKLEDAGfdwkiLGPDVSDVDY--------VAWQCDQDAya 276
|
170
....*....|....*.
gi 1859350786 253 --GQICTNVDYVFVHQ 266
Cdd:cd07126 277 csGQKCSAQSILFAHE 292
|
|
| |
