|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
5-394 |
0e+00 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 699.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 5 EQKFYDSKAFFNTQQTKDISFRKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAYATEIGITLKSIKNARKELKNWTKT 84
Cdd:cd07136 1 ESLVEKQRAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 85 KNVDTPLYLFPTKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINETFDANYIE 164
Cdd:cd07136 81 KRVKTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 165 VIEGGIEETQTLIHLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTC 244
Cdd:cd07136 161 VVEGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 245 VAPDYILVHESVKDDLITALSKTLREFYGQNIQQSPDYGRIVNLKHYHRLTSLLNSAqmNIVFGGHSDEDERYIEPTLLD 324
Cdd:cd07136 241 VAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNG--KIVFGGNTDRETLYIEPTILD 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 325 HVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAINDTL 394
Cdd:cd07136 319 NVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTI 388
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
8-394 |
0e+00 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 616.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 8 FYDSKAFFNTQQTKDISFRKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAYATEIGITLKSIKNARKELKNWTKTKNV 87
Cdd:cd07087 4 VARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKPRRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 88 DTPLYLFPTKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINETFDANYIEVIE 167
Cdd:cd07087 84 SVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVAVVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 168 GGIEETQTLIHLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAP 247
Cdd:cd07087 164 GGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 248 DYILVHESVKDDLITALSKTLREFYGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQmnIVFGGHSDEDERYIEPTLLDHVT 327
Cdd:cd07087 244 DYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGK--VVIGGQVDKEERYIAPTILDDVS 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616915334 328 NDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAINDTL 394
Cdd:cd07087 322 PDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVL 388
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
15-394 |
0e+00 |
|
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: 516.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 15 FNTQQ-------TKDISFRKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAYATEIGITLKSIKNARKELKNWTKTKNV 87
Cdd:cd07134 4 FAAQQahalalrASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKPKRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 88 DTPLYLFPTKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINETFDANYIEVIE 167
Cdd:cd07134 84 RTPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 168 GGIEETQTLIHLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAP 247
Cdd:cd07134 164 GDAEVAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 248 DYILVHESVKDDLITALSKTLREFYGQN--IQQSPDYGRIVNLKHYHRLTSLLNSAQ---MNIVFGGHSDEDERYIEPTL 322
Cdd:cd07134 244 DYVFVHESVKDAFVEHLKAEIEKFYGKDaaRKASPDLARIVNDRHFDRLKGLLDDAVakgAKVEFGGQFDAAQRYIAPTV 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616915334 323 LDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAINDTL 394
Cdd:cd07134 324 LTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVV 395
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
3-394 |
2.81e-178 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 505.33 E-value: 2.81e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 3 IIEQKFYDSKAFFNTQQTKDISFRKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAYATEIGITLKSIKNARKELKNWT 82
Cdd:PTZ00381 8 IIPPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 83 KTKNVDTPLYLFPTKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINETFDANY 162
Cdd:PTZ00381 88 KPEKVDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPSY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 163 IEVIEGGIEETQTLIHLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQ 242
Cdd:PTZ00381 168 VRVIEGGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 243 TCVAPDYILVHESVKDDLITALSKTLREFYGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQMNIVFGGHSDEDERYIEPTL 322
Cdd:PTZ00381 248 TCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKDHGGKVVYGGEVDIENKYVAPTI 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616915334 323 LDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAINDTL 394
Cdd:PTZ00381 328 IVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCV 399
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
15-394 |
5.46e-178 |
|
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: 502.52 E-value: 5.46e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 15 FNTQQTKDISFRKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAYATEIGITLKSIKNARKELKNWTKTKNVDTPlylF 94
Cdd:cd07132 11 FSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKPEPVKKN---L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 95 PTKS---YIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINETFDANYIEVIEGGIE 171
Cdd:cd07132 88 ATLLddvYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYPVVLGGVE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 172 ETQTLIHLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYIL 251
Cdd:cd07132 168 ETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 252 VHESVKDDLITALSKTLREFYGQNIQQSPDYGRIVNLKHYHRLTSLLNSaqMNIVFGGHSDEDERYIEPTLLDHVTNDSA 331
Cdd:cd07132 248 CTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSG--GKVAIGGQTDEKERYIAPTVLTDVKPSDP 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616915334 332 IMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAINDTL 394
Cdd:cd07132 326 VMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTI 388
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
4-394 |
7.15e-178 |
|
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: 502.14 E-value: 7.15e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 4 IEQKFYDSKAFFNTQQTKDISFRKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAYATEIGITLKSIKNARKELKNWTK 83
Cdd:cd07135 7 IDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKKWAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 84 TKNV-DTPLYLFPTKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINETFDANY 162
Cdd:cd07135 87 DEKVkDGPLAFMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLDPDA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 163 IEVIEGGIEETQTLIHLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQ 242
Cdd:cd07135 167 FQVVQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQ 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 243 TCVAPDYILVHESVKDDLITALSKTLREFYGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQMNIVFGGHSDEDERYIEPTL 322
Cdd:cd07135 247 ICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDTTKGKVVIGGEMDEATRFIPPTI 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616915334 323 LDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAINDTL 394
Cdd:cd07135 327 VSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTL 398
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
26-394 |
1.22e-160 |
|
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: 458.10 E-value: 1.22e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 26 RKEQLKKLSKAIKSYESDILEALYTDLG-KNKVEAYATEIGITLKSIKNARKELKNWTKTKNVDTPLYLFPTKSYIKKEP 104
Cdd:cd07133 22 RRDRLDRLKALLLDNQDALAEAISADFGhRSRHETLLAEILPSIAGIKHARKHLKKWMKPSRRHVGLLFLPAKAEVEYQP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 105 YGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINETFDANYIEVIEGGIEETQTLIHLPFDYV 184
Cdd:cd07133 102 LGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEVAVVTGGADVAAAFSSLPFDHL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 185 FFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHESVKDDLITAL 264
Cdd:cd07133 182 LFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 265 SKTLREFYGQnIQQSPDYGRIVNLKHYHRLTSLLNSAQM------NIVFGGHSDEDERYIEPTLLDHVTNDSAIMQEEIF 338
Cdd:cd07133 262 KAAVAKMYPT-LADNPDYTSIINERHYARLQGLLEDARAkgarviELNPAGEDFAATRKLPPTLVLNVTDDMRVMQEEIF 340
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 616915334 339 GPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAINDTL 394
Cdd:cd07133 341 GPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTL 396
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
12-393 |
1.31e-152 |
|
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: 438.00 E-value: 1.31e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 12 KAFFNTQQTKDISFRKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAYATEIGITLKSIKNARKELKNWTKTKNVDTPL 91
Cdd:cd07137 9 RETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMAPEKVKTPL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 92 YLFPTKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINETFDANYIEVIEGGIE 171
Cdd:cd07137 89 TTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIKVIEGGVP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 172 ETQTLIHLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKF-TNAGQTCVAPDYI 250
Cdd:cd07137 169 ETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 251 LVHESVKDDLITALSKTLREFYGQNIQQSPDYGRIVNLKHYHRLTSLL--NSAQMNIVFGGHSDEDERYIEPTLLDHVTN 328
Cdd:cd07137 249 LVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLddPSVADKIVHGGERDEKNLYIEPTILLDPPL 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616915334 329 DSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAINDT 393
Cdd:cd07137 329 DSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDT 393
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
12-394 |
1.60e-131 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 386.00 E-value: 1.60e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 12 KAFFNTQQTKDISFRKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAYATEIGITLKSIKNARKELKNWTKTKNVDTPL 91
Cdd:PLN02203 16 RETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSNLKKWMAPKKAKLPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 92 YLFPTKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINETFDANYIEVIEGGIE 171
Cdd:PLN02203 96 VAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAVKVIEGGPA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 172 ETQTLIHLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVD---ETANIKVASERICFGKF-TNAGQTCVAP 247
Cdd:PLN02203 176 VGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWgSCAGQACIAI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 248 DYILVHESVKDDLITALSKTLREFYGQNIQQSPDYGRIVNLKHYHRLTSLL--NSAQMNIVFGGHSDEDERYIEPTLLDH 325
Cdd:PLN02203 256 DYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLkdPRVAASIVHGGSIDEKKLFIEPTILLN 335
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616915334 326 VTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAINDTL 394
Cdd:PLN02203 336 PPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAI 404
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
11-392 |
3.84e-118 |
|
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: 349.97 E-value: 3.84e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 11 SKAFFNTQQTKDISFRKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAyATEIGITLKSIKNARKELKNWTKTKNVDTP 90
Cdd:cd07078 7 ARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEA-LGEVARAADTFRYYAGLARRLHGEVIPSPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 91 LylfPTKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGG 169
Cdd:cd07078 86 P---GELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLPPGVLNVVTGD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 170 IEET-QTLIHLP-FDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAP 247
Cdd:cd07078 163 GDEVgAALASHPrVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 248 DYILVHESVKDDLITALSKTLREFYGQN-IQQSPDYGRIVNLKHYHRLTSLLNSAQMN---IVFGGHSDEDE--RYIEPT 321
Cdd:cd07078 243 SRLLVHESIYDEFVERLVERVKALKVGNpLDPDTDMGPLISAAQLDRVLAYIEDAKAEgakLLCGGKRLEGGkgYFVPPT 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616915334 322 LLDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIND 392
Cdd:cd07078 323 VLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIND 393
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
15-392 |
7.24e-101 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 307.74 E-value: 7.24e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 15 FNTQQTKDISFRKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAYATEIGITLKSIKNARKELKNWTKTKNVDTPLYLF 94
Cdd:PLN02174 23 FDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEKAKTSLTTF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 95 PTKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINETFDANYIEVIEGGIEETQ 174
Cdd:PLN02174 103 PASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVEGAVTETT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 175 TLIHLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKF-TNAGQTCVAPDYILVH 253
Cdd:PLN02174 183 ALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 254 ESVKDDLITALSKTLREFYGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQMN--IVFGGHSDEDERYIEPTLLDHVTNDSA 331
Cdd:PLN02174 263 KEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDEKEVSdkIVYGGEKDRENLKIAPTILLDVPLDSL 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616915334 332 IMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIND 392
Cdd:PLN02174 343 IMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVND 403
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
26-392 |
3.42e-100 |
|
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: 305.51 E-value: 3.42e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 26 RKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAYAtEIGITLKSIKNARKELKnwtKTKNVDTPLYLFPTKSYIKKEPY 105
Cdd:COG1012 67 RAAILLRAADLLEERREELAALLTLETGKPLAEARG-EVDRAADFLRYYAGEAR---RLYGETIPSDAPGTRAYVRREPL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 106 GTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEET-QTLIHLP-FD 182
Cdd:COG1012 143 GVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAgLPAGVLNVVTGDGSEVgAALVAHPdVD 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 183 YVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHESVKDDLIT 262
Cdd:COG1012 223 KISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 263 ALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQM---NIVFGGHSDEDER--YIEPTLLDHVTNDSAIMQEE 336
Cdd:COG1012 303 RLVAAAKALkVGDPLDPGTDMGPLISEAQLERVLAYIEDAVAegaELLTGGRRPDGEGgyFVEPTVLADVTPDMRIAREE 382
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 616915334 337 IFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIND 392
Cdd:COG1012 383 IFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWIND 438
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
11-392 |
1.01e-96 |
|
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: 292.98 E-value: 1.01e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 11 SKAFFNTQQTKDISFRKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAYAtEIGITLKSIKNARKELKNWTKTKNVDTP 90
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALG-EVARAIDTFRYAAGLADKLGGPELPSPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 91 LylfPTKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGG 169
Cdd:cd06534 82 P---GGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVVNVVPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 170 IEET-QTLIHLP-FDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAP 247
Cdd:cd06534 159 GDEVgAALLSHPrVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 248 DYILVHESVKDDLITALSktlrefygqniqqspdygrivnlkhyhrltsllnsaqmnivfgghsdederyiepTLLDHVT 327
Cdd:cd06534 239 SRLLVHESIYDEFVEKLV-------------------------------------------------------TVLVDVD 263
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616915334 328 NDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIND 392
Cdd:cd06534 264 PDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYIND 328
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
26-392 |
7.92e-90 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 278.26 E-value: 7.92e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 26 RKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAyATEIGITLKSIKNARKELKNWT-KTKNVDTPlylfpTKSYIKKEP 104
Cdd:pfam00171 53 RAAILRKAADLLEERKDELAELETLENGKPLAEA-RGEVDRAIDVLRYYAGLARRLDgETLPSDPG-----RLAYTRREP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 105 YGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEET-QTLIHLP-F 181
Cdd:pfam00171 127 LGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAgLPAGVLNVVTGSGAEVgEALVEHPdV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 182 DYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHESVKDDLI 261
Cdd:pfam00171 207 RKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFV 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 262 ---TALSKTLRefYGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQ---MNIVFGGHSDEDE-RYIEPTLLDHVTNDSAIMQ 334
Cdd:pfam00171 287 eklVEAAKKLK--VGDPLDPDTDMGPLISKAQLERVLKYVEDAKeegAKLLTGGEAGLDNgYFVEPTVLANVTPDMRIAQ 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 616915334 335 EEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIND 392
Cdd:pfam00171 365 EEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWIND 422
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
26-394 |
6.41e-77 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 244.82 E-value: 6.41e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 26 RKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAYAtEIGITLKSI----KNARKELKnwtkTKNVDTPLYLFPTKSYIK 101
Cdd:cd07099 42 RAQRLLRWKRALADHADELAELLHAETGKPRADAGL-EVLLALEAIdwaaRNAPRVLA----PRKVPTGLLMPNKKATVE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 102 KEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEETQTLIHLP 180
Cdd:cd07099 117 YRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAgPPQGVLQVVTGDGATGAALIDAG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 181 FDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHESVKD-- 258
Cdd:cd07099 197 VDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDef 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 259 -DLITALSKTLREfyGQNIQQSPDYGrivnlkhyhrltSLLNSAQMNIVF----------------GGHSDEDERYIEPT 321
Cdd:cd07099 277 vARLVAKARALRP--GADDIGDADIG------------PMTTARQLDIVRrhvddavakgakaltgGARSNGGGPFYEPT 342
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616915334 322 LLDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAINDTL 394
Cdd:cd07099 343 VLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVL 415
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
26-391 |
1.26e-69 |
|
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: 226.38 E-value: 1.26e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 26 RKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAYaTEIGITLKSIK----NARKELKNWTKTKNVDTPLYLFptksyik 101
Cdd:cd07088 59 RAAYLRKLADLIRENADELAKLIVEEQGKTLSLAR-VEVEFTADYIDymaeWARRIEGEIIPSDRPNENIFIF------- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 102 KEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINE-TFDANYIEVIEGGIEETQTLI--H 178
Cdd:cd07088 131 KVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEaGLPAGVLNIVTGRGSVVGDALvaH 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 179 LPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHESVKD 258
Cdd:cd07088 211 PKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYD 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 259 ---DLITALSKTLRefYGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQMN---IVFGGHSDEDER--YIEPTLLDHVTNDS 330
Cdd:cd07088 291 efmEKLVEKMKAVK--VGDPFDAATDMGPLVNEAALDKVEEMVERAVEAgatLLTGGKRPEGEKgyFYEPTVLTNVRQDM 368
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616915334 331 AIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIN 391
Cdd:cd07088 369 EIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYIN 429
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
12-392 |
3.79e-68 |
|
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: 222.56 E-value: 3.79e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 12 KAFFNTQQTkDISFRKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAYATEIGITLKSIKNARKELKNWTKTKNVDTPL 91
Cdd:cd07098 29 AAQREWAKT-SFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEILVTCEKIRWTLKHGEKALRPESRPGGL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 92 YLFPTKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELT-----PNVARVIKRLINETFDANYIEVI 166
Cdd:cd07098 108 LMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVawssgFFLSIIRECLAACGHDPDLVQLV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 167 EGGIEETQTLI-HLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCV 245
Cdd:cd07098 188 TCLPETAEALTsHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 246 APDYILVHESVKDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSA---QMNIVFGGH-----SDEDER 316
Cdd:cd07098 268 GIERVIVHEKIYDKLLEILTDRVQALrQGPPLDGDVDVGAMISPARFDRLEELVADAvekGARLLAGGKryphpEYPQGH 347
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616915334 317 YIEPTLLDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIND 392
Cdd:cd07098 348 YFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAIND 423
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
102-394 |
1.29e-63 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 210.37 E-value: 1.29e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 102 KEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEE-TQTLIHL 179
Cdd:cd07103 115 KQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEAgLPAGVLNVVTGSPAEiGEALCAS 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 180 P-FDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHESVKD 258
Cdd:cd07103 195 PrVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYD 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 259 DLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQMN---IVFGGHSDEDE-RYIEPTLLDHVTNDSAIM 333
Cdd:cd07103 275 EFVEKLVERVKKLkVGNGLDEGTDMGPLINERAVEKVEALVEDAVAKgakVLTGGKRLGLGgYFYEPTVLTDVTDDMLIM 354
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616915334 334 QEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAINDTL 394
Cdd:cd07103 355 NEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGL 415
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
100-391 |
2.73e-63 |
|
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: 208.97 E-value: 2.73e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 100 IKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVI----EGGIEETQ 174
Cdd:cd07105 94 VVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAgLPKGVLNVVthspEDAPEVVE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 175 TLI-HLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVH 253
Cdd:cd07105 174 ALIaHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIVH 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 254 ESVKDDLITALSKTLREfygqnIQQSPDY-GRIVNLKHYHRLTSLLNSAQMN---IVFGGHSDEDER--YIEPTLLDHVT 327
Cdd:cd07105 254 ESIADEFVEKLKAAAEK-----LFAGPVVlGSLVSAAAADRVKELVDDALSKgakLVVGGLADESPSgtSMPPTILDNVT 328
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616915334 328 NDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIN 391
Cdd:cd07105 329 PDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHIN 392
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
13-391 |
3.18e-63 |
|
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: 209.41 E-value: 3.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 13 AFFNTQQTKDISFRKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAYATEIGITLKSIKN-ARKELKNWTKTKNVDTPL 91
Cdd:cd07089 31 AFDTGDWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQVDGPIGHLRYfADLADSFPWEFDLPVPAL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 92 YLFPTKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGI 170
Cdd:cd07089 111 RGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAETdLPAGVVNVVTGSD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 171 EETQTLI--HLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPD 248
Cdd:cd07089 191 NAVGEALttDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 249 YILVHESVKDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQMN----IVFGGHSDEDER--YIEPT 321
Cdd:cd07089 271 RLLVPRSRYDEVVEALAAAFEALpVGDPADPGTVMGPLISAAQRDRVEGYIARGRDEgarlVTGGGRPAGLDKgfYVEPT 350
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 322 LLDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIN 391
Cdd:cd07089 351 LFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGIN 420
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
102-387 |
1.31e-60 |
|
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: 202.57 E-value: 1.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 102 KEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEG-GIEETQTLI-H 178
Cdd:cd07118 117 REPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAgLPAGVVNIVTGyGATVGQAMTeH 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 179 LPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHESVKD 258
Cdd:cd07118 197 PDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIAD 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 259 DLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQ---MNIVFGGHSDEDE--RYIEPTLLDHVTNDSAI 332
Cdd:cd07118 277 AFVAAVVARSRKVrVGDPLDPETKVGAIINEAQLAKITDYVDAGRaegATLLLGGERLASAagLFYQPTIFTDVTPDMAI 356
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616915334 333 MQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDEN----ATQRV------IN-------ELSFGG 387
Cdd:cd07118 357 AREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDtaltVARRIragtvwVNtfldgspELPFGG 428
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
12-391 |
3.17e-60 |
|
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: 201.22 E-value: 3.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 12 KAFFNTQQTKDISFRKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAYAtEIGITLKSIKnARKELKNWTKTKNvDTPl 91
Cdd:cd07106 29 KAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF-EVGGAVAWLR-YTASLDLPDEVIE-DDD- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 92 ylfPTKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINETFDANYIEVIEGGIE 171
Cdd:cd07106 105 ---TRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEVLPPGVLNVVSGGDE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 172 ETQTL-IHLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYI 250
Cdd:cd07106 182 LGPALtSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 251 LVHESVKDDLITALSKTLREFY-GQNIQQSPDYGRIVNLKHYHRLTSLLNSAQMN---IVFGGHSDEDERY-IEPTLLDH 325
Cdd:cd07106 262 YVHESIYDEFCEALVALAKAAVvGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKgakVLAGGEPLDGPGYfIPPTIVDD 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616915334 326 VTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIN 391
Cdd:cd07106 342 PPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWIN 407
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
4-391 |
5.36e-60 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 200.94 E-value: 5.36e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 4 IEQKFYDSKAFFNTQQTKDISFRKEQLKKLSKAIKSYESDILEALYTDLGKnKVEAYATEIGITLKS----IKNARKELK 79
Cdd:cd07102 20 VRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGR-PIAQAGGEIRGMLERarymISIAEEALA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 80 nwtktknvDTPLYLFPT-KSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET- 157
Cdd:cd07102 99 --------DIRVPEKDGfERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAg 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 158 FDANYIEVIEGGIEETQTLIHLP-FDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGK 236
Cdd:cd07102 171 LPEGVFQVLHLSHETSAALIADPrIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 237 FTNAGQTCVAPDYILVHESVKDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNS-----AQMNIvfGGH 310
Cdd:cd07102 251 FFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYkLGDPLDPSTTLGPVVSARAADFVRAQIADaiakgARALI--DGA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 311 ----SDEDERYIEPTLLDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFG 386
Cdd:cd07102 329 lfpeDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETG 408
|
....*
gi 616915334 387 GGAIN 391
Cdd:cd07102 409 TVFMN 413
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
92-392 |
1.29e-59 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 199.86 E-value: 1.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 92 YLFPTKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINETFDANYIEVIEGGIE 171
Cdd:cd07092 106 YLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGVVNVVCGGGA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 172 ET-QTLI-HLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDY 249
Cdd:cd07092 186 SAgDALVaHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACR 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 250 ILVHESVKDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQMN--IVFGGHS-DEDERYIEPTLLDH 325
Cdd:cd07092 266 VYVHESVYDEFVAALVEAVSAIrVGDPDDEDTEMGPLNSAAQRERVAGFVERAPAHarVLTGGRRaEGPGYFYEPTVVAG 345
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616915334 326 VTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIND 392
Cdd:cd07092 346 VAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNT 412
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
32-393 |
2.66e-59 |
|
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: 198.97 E-value: 2.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 32 KLSKAIKSYE-SDILEALYTDLGKNKVEA---YATEIGitlKSIKNARKELknwtkTKNVDT----------------PL 91
Cdd:cd07149 35 KEMKSLPAYErAEILERAAQLLEERREEFartIALEAG---KPIKDARKEV-----DRAIETlrlsaeeakrlagetiPF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 92 YLFP----TKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVI 166
Cdd:cd07149 107 DASPggegRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEAgLPKGALNVV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 167 EGGIEET-QTLIHLP-FDYVFFTGSENVGKIVYQAASenLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTC 244
Cdd:cd07149 187 TGSGETVgDALVTDPrVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVC 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 245 VAPDYILVHESVKDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQ---MNIVFGGHsdEDERYIEP 320
Cdd:cd07149 265 ISVQRIFVHEDIYDEFLERFVAATKKLvVGDPLDEDTDVGPMISEAEAERIEEWVEEAVeggARLLTGGK--RDGAILEP 342
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616915334 321 TLLDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAINDT 393
Cdd:cd07149 343 TVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINDS 415
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
87-355 |
9.19e-59 |
|
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: 197.77 E-value: 9.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 87 VDTPLYLfptkSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEV 165
Cdd:cd07114 106 VDKGDYL----NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAgFPPGVVNV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 166 IEGGIEET-QTLI-HLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQT 243
Cdd:cd07114 182 VTGFGPETgEALVeHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 244 CVAPDYILVHESVKD---DLITALSKTLRefYGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQMN---IVFGGH-SDEDER 316
Cdd:cd07114 262 CVAGSRLLVQRSIYDefvERLVARARAIR--VGDPLDPETQMGPLATERQLEKVERYVARAREEgarVLTGGErPSGADL 339
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 616915334 317 ----YIEPTLLDHVTNDSAIMQEEIFGPILPILTYQSLDEAIA 355
Cdd:cd07114 340 gagyFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIA 382
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
26-393 |
3.73e-58 |
|
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: 196.86 E-value: 3.73e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 26 RKEQLKKLSKAIKSyESDILEALYT-DLGKNKVEAYATEIGITLKSIKnarkELKNWTKTKNVDTpLYLFPTK-SYIKKE 103
Cdd:cd07144 70 RGELLDKLADLVEK-NRDLLAAIEAlDSGKPYHSNALGDLDEIIAVIR----YYAGWADKIQGKT-IPTSPNKlAYTLHE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 104 PYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEG-GIEETQTLI-HLP 180
Cdd:cd07144 144 PYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVNIIPGyGAVAGSALAeHPD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 181 FDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHESVKDDL 260
Cdd:cd07144 224 VDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKF 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 261 ITALSKTLREFY--GQNIQQSPDYGRIVNLKHYHRLTSLLNSAQMNI---VFGG--HSDEDER--YIEPTLLDHVTNDSA 331
Cdd:cd07144 304 VEKFVEHVKQNYkvGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGaklVYGGekAPEGLGKgyFIPPTIFTDVPQDMR 383
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616915334 332 IMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAINDT 393
Cdd:cd07144 384 IVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSS 445
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
99-355 |
4.11e-58 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 195.92 E-value: 4.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 99 YIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEG-GIEETQTL 176
Cdd:cd07109 112 YTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAgLPAGALNVVTGlGAEAGAAL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 177 I-HLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHES 255
Cdd:cd07109 192 VaHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRS 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 256 VKDDLITALSKTLREFYGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQ---MNIVFGGHSDEDER----YIEPTLLDHVTN 328
Cdd:cd07109 272 IYDEVLERLVERFRALRVGPGLEDPDLGPLISAKQLDRVEGFVARARargARIVAGGRIAEGAPaggyFVAPTLLDDVPP 351
|
250 260
....*....|....*....|....*..
gi 616915334 329 DSAIMQEEIFGPILPILTYQSLDEAIA 355
Cdd:cd07109 352 DSRLAQEEIFGPVLAVMPFDDEAEAIA 378
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
95-391 |
4.67e-55 |
|
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: 188.33 E-value: 4.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 95 PTK-SYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEE 172
Cdd:cd07131 125 PNKdAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAgLPPGVVNVVHGRGEE 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 173 T-QTLI-HLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYI 250
Cdd:cd07131 205 VgEALVeHPDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 251 LVHESVKDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQ---MNIVFGG-----HSDEDERYIEPT 321
Cdd:cd07131 285 IVHESVYDEFLKRFVERAKRLrVGDGLDEETDMGPLINEAQLEKVLNYNEIGKeegATLLLGGerltgGGYEKGYFVEPT 364
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 322 LLDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIN 391
Cdd:cd07131 365 VFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVN 434
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
12-386 |
4.88e-55 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 188.19 E-value: 4.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 12 KAFFNTQQTK-DISFRKEQLKKLSKAIksyESDI-----LEALytDLGKNKVEAYATEIGItlkSIKNARKEL----KNW 81
Cdd:cd07091 52 AAFETGWWRKmDPRERGRLLNKLADLI---ERDRdelaaLESL--DNGKPLEESAKGDVAL---SIKCLRYYAgwadKIQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 82 TKTKNVDTPlYLFptksYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDA 160
Cdd:cd07091 124 GKTIPIDGN-FLA----YTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAgFPP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 161 NYIEVIEG-GIEETQTLI-HLPFDYVFFTGSENVGKIVYQAASE-NLVPVTLEMGGKSPVIVDETANIKVASERICFGKF 237
Cdd:cd07091 199 GVVNIVPGfGPTAGAAISsHMDVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 238 TNAGQTCVAPDYILVHESVKDDLITALSKTLREFY-GQNIQQSPDYGRIVNLKHYHRLTSLLNSAQ---MNIVFGGHSDE 313
Cdd:cd07091 279 FNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVvGDPFDPDTFQGPQVSKAQFDKILSYIESGKkegATLLTGGERHG 358
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616915334 314 DERY-IEPTLLDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFG 386
Cdd:cd07091 359 SKGYfIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAG 432
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
26-386 |
4.85e-54 |
|
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: 185.50 E-value: 4.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 26 RKEQLKKLSKAIKSY--ESDILEALytDLGKNKVEAYATEIGITLKSIKnarkelknWTkTKNVDTpLY--LFPTK---- 97
Cdd:cd07112 50 RKAVLLRLADLIEAHrdELALLETL--DMGKPISDALAVDVPSAANTFR--------WY-AEAIDK-VYgeVAPTGpdal 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 98 SYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEETQTL 176
Cdd:cd07112 118 ALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAgLPAGVLNVVPGFGHTAGEA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 177 I--HLPFDYVFFTGSENVGKIVYQAASE-NLVPVTLEMGGKSPVIV-DETANIKVASERICFGKFTNAGQTCVAPDYILV 252
Cdd:cd07112 198 LglHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVfADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 253 HESVKDDLITALSKTLREFY-GQNIQQSPDYGRIVNLKHYHRLTSLLNSAQ---MNIVFGGHSDEDER---YIEPTLLDH 325
Cdd:cd07112 278 HESIKDEFLEKVVAAAREWKpGDPLDPATRMGALVSEAHFDKVLGYIESGKaegARLVAGGKRVLTETggfFVEPTVFDG 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616915334 326 VTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFG 386
Cdd:cd07112 358 VTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAG 418
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
104-372 |
1.25e-53 |
|
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: 184.69 E-value: 1.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 104 PYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINETFDAN-----YIEVIEGGIEETQTLIH 178
Cdd:cd07086 133 PLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLEKNglppgVVNLVTGGGDGGELLVH 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 179 LP-FDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHESVK 257
Cdd:cd07086 213 DPrVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVY 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 258 DDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQM---NIVFGGHS---DEDERYIEPTLLDHVTNDS 330
Cdd:cd07086 293 DEFLERLVKAYKQVrIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSqggTVLTGGKRidgGEPGNYVEPTIVTGVTDDA 372
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 616915334 331 AIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSED 372
Cdd:cd07086 373 RIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTED 414
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
26-393 |
1.41e-53 |
|
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: 184.24 E-value: 1.41e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 26 RKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAYATEIGITLKSIKNARKELKN--WTKTKNvdtplylfptKSYIKKE 103
Cdd:cd07138 60 RAALLERIAEAYEARADELAQAITLEMGAPITLARAAQVGLGIGHLRAAADALKDfeFEERRG----------NSLVVRE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 104 PYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEETQTLI--HLP 180
Cdd:cd07138 130 PIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAgLPAGVFNLVNGDGPVVGEALsaHPD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 181 FDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHESVKDDL 260
Cdd:cd07138 210 VDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 261 ITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQ---MNIVFGG--HSDEDER--YIEPTLLDHVTNDSAI 332
Cdd:cd07138 290 EEIAAAAAEAYvVGDPRDPATTLGPLASAAQFDRVQGYIQKGIeegARLVAGGpgRPEGLERgyFVKPTVFADVTPDMTI 369
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616915334 333 MQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAINDT 393
Cdd:cd07138 370 AREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGA 430
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
95-392 |
1.49e-53 |
|
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: 184.44 E-value: 1.49e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 95 PTKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEET 173
Cdd:cd07119 125 HVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAgLPAGVVNLVTGSGATV 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 174 QTLI--HLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYIL 251
Cdd:cd07119 205 GAELaeSPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 252 VHESVKDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQMN---IVFGGHSDEDER-----YIEPTL 322
Cdd:cd07119 285 VEESIHDKFVAALAERAKKIkLGNGLDADTEMGPLVSAEHREKVLSYIQLGKEEgarLVCGGKRPTGDElakgyFVEPTI 364
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 323 LDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIND 392
Cdd:cd07119 365 FDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIND 434
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
30-391 |
3.21e-53 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 181.86 E-value: 3.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 30 LKKLSKAIKSYESDILEALYTDLGKNKVEAyATEIGITLKSIKN----ARKELKNWTKTKNVDTPLYLFptksyikKEPY 105
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLA-EVEVAFTADYIDYmaewARRYEGEIIQSDRPGENILLF-------KRAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 106 GTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEETQTLI--HLPFD 182
Cdd:PRK10090 73 GVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQELagNPKVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 183 YVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHESVKDDLIT 262
Cdd:PRK10090 153 MVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 263 ALSKTLREF-YGQNIQQS-PDYGRIVNLKHYHRLTSLLNSAQMN---IVFGGHSDEDERYI-EPTLLDHVTNDSAIMQEE 336
Cdd:PRK10090 233 RLGEAMQAVqFGNPAERNdIAMGPLINAAALERVEQKVARAVEEgarVALGGKAVEGKGYYyPPTLLLDVRQEMSIMHEE 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 616915334 337 IFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIN 391
Cdd:PRK10090 313 TFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN 367
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
26-393 |
3.24e-53 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 182.93 E-value: 3.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 26 RKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAYAtEIGITLKSIKNARKELKNWT-KTKNVDTPLYLFPTKSYIKKEP 104
Cdd:cd07145 45 RYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV-EVERTIRLFKLAAEEAKVLRgETIPVDAYEYNERRIAFTVREP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 105 YGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEET--QTLIHLPF 181
Cdd:cd07145 124 IGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPGVINVVTGYGSEVgdEIVTNPKV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 182 DYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHESVKDDLI 261
Cdd:cd07145 204 NMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 262 TAL---SKTLRefYGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQM---NIVFGGHSDEDErYIEPTLLDHVTNDSAIMQE 335
Cdd:cd07145 284 KLLvekVKKLK--VGDPLDESTDLGPLISPEAVERMENLVNDAVEkggKILYGGKRDEGS-FFPPTVLENDTPDMIVMKE 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 616915334 336 EIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAINDT 393
Cdd:cd07145 361 EVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDS 418
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
98-392 |
3.89e-53 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 183.19 E-value: 3.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 98 SYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINETFDANYIEVIEGGIEET-QTL 176
Cdd:PRK13473 132 SMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVgDAL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 177 I-HLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHES 255
Cdd:PRK13473 212 VgHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRG 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 256 VKDDLITALS---KTLRefYGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQ----MNIVFGGH-SDEDERYIEPTLLDHVT 327
Cdd:PRK13473 292 IYDDLVAKLAaavATLK--VGDPDDEDTELGPLISAAHRDRVAGFVERAKalghIRVVTGGEaPDGKGYYYEPTLLAGAR 369
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616915334 328 NDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIND 392
Cdd:PRK13473 370 QDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNT 434
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
98-386 |
3.14e-52 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 180.63 E-value: 3.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 98 SYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINETFDANYIEVIEG-GIEETQTL 176
Cdd:cd07108 111 TYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQVLPAGVLNVITGyGEECGAAL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 177 I-HLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFG-KFTNAGQTCVAPDYILVHE 254
Cdd:cd07108 191 VdHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 255 SVKDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQ----MNIVFGGHSDEDER-----YIEPTLLD 324
Cdd:cd07108 271 DIYDAFLEKLVAKLSKLkIGDPLDEATDIGAIISEKQFAKVCGYIDLGLstsgATVLRGGPLPGEGPladgfFVQPTIFS 350
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616915334 325 HVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFG 386
Cdd:cd07108 351 GVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAG 412
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
98-391 |
3.86e-52 |
|
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: 180.80 E-value: 3.86e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 98 SYIKKEPYGTVLIIAPFNYPFqLVFEPLIG-AIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEETQT 175
Cdd:cd07143 138 TYTRHEPIGVCGQIIPWNFPL-LMCAWKIApALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGYGRTCGN 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 176 LI--HLPFDYVFFTGSENVGKIVYQAASE-NLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILV 252
Cdd:cd07143 217 AIssHMDIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYV 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 253 HESVKDDLITALSKTLREF-----YGQNIQQSPDYGRIvnlkHYHRLTSLLNSAQM---NIVFGGHSDEDERY-IEPTLL 323
Cdd:cd07143 297 QEGIYDKFVKRFKEKAKKLkvgdpFAEDTFQGPQVSQI----QYERIMSYIESGKAegaTVETGGKRHGNEGYfIEPTIF 372
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616915334 324 DHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIN 391
Cdd:cd07143 373 TDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVN 440
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
97-391 |
1.04e-51 |
|
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: 179.08 E-value: 1.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 97 KSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEETQT 175
Cdd:cd07110 113 KARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIAAEAgLPPGVLNVVTGTGDEAGA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 176 LI--HLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVH 253
Cdd:cd07110 193 PLaaHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVH 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 254 ESVKDDLITALSKTLRefygqNIQQSP------DYGRIVNLKHYHRLTSLLNSAQ---MNIVFGGHSDEDER---YIEPT 321
Cdd:cd07110 273 ESIADAFLERLATAAE-----AIRVGDpleegvRLGPLVSQAQYEKVLSFIARGKeegARLLCGGRRPAHLEkgyFIAPT 347
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 322 LLDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIN 391
Cdd:cd07110 348 VFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVWIN 417
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
98-386 |
1.57e-51 |
|
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: 178.53 E-value: 1.57e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 98 SYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEETQTL 176
Cdd:cd07093 111 NYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAgLPPGVVNVVHGFGPEAGAA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 177 I--HLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHE 254
Cdd:cd07093 191 LvaHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQR 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 255 SVKDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQM---NIVFGGHSDEDER-----YIEPTLLDH 325
Cdd:cd07093 271 SIYDEFLERFVERAKALkVGDPLDPDTEVGPLISKEHLEKVLGYVELARAegaTILTGGGRPELPDleggyFVEPTVITG 350
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616915334 326 VTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFG 386
Cdd:cd07093 351 LDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAG 411
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
98-355 |
4.56e-51 |
|
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: 176.57 E-value: 4.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 98 SYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVikrLINETFD-----ANYIEVIEGGIEE 172
Cdd:cd07104 92 SMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGL---LIAEIFEeaglpKGVLNVVPGGGSE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 173 T-QTLIHLP-FDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYI 250
Cdd:cd07104 169 IgDALVEHPrVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRI 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 251 LVHESVKDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQ---MNIVFGGHsdEDERYIEPTLLDHV 326
Cdd:cd07104 249 LVHESVYDEFVEKLVAKAKALpVGDPRDPDTVIGPLINERQVDRVHAIVEDAVaagARLLTGGT--YEGLFYQPTVLSDV 326
|
250 260
....*....|....*....|....*....
gi 616915334 327 TNDSAIMQEEIFGPILPILTYQSLDEAIA 355
Cdd:cd07104 327 TPDMPIFREEIFGPVAPVIPFDDDEEAVE 355
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
102-394 |
4.04e-50 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 175.65 E-value: 4.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 102 KEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEET-QTLIHL 179
Cdd:PLN02278 158 KQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAgIPPGVLNVVMGDAPEIgDALLAS 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 180 P-FDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHESVKD 258
Cdd:PLN02278 238 PkVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYD 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 259 DLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSA---QMNIVFGGHSDEDER-YIEPTLLDHVTNDSAIM 333
Cdd:PLN02278 318 KFAEAFSKAVQKLvVGDGFEEGVTQGPLINEAAVQKVESHVQDAvskGAKVLLGGKRHSLGGtFYEPTVLGDVTEDMLIF 397
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616915334 334 QEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAINDTL 394
Cdd:PLN02278 398 REEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGL 458
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
96-379 |
1.37e-49 |
|
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: 174.07 E-value: 1.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 96 TKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINETFDANYIEVIEG-GIEETQ 174
Cdd:cd07559 128 TLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVNVVTGfGSEAGK 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 175 TLIHLP-FDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIV-----DETANIKVASERICFGKFTNAGQTCVAPD 248
Cdd:cd07559 208 PLASHPrIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFfddamDADDDFDDKAEEGQLGFAFNQGEVCTCPS 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 249 YILVHESVKDDLITALsktLREFygQNIQQ----SPD--YGRIVNLKHYHRLTSLLNSAQ---MNIVFGGH-----SDED 314
Cdd:cd07559 288 RALVQESIYDEFIERA---VERF--EAIKVgnplDPEtmMGAQVSKDQLEKILSYVDIGKeegAEVLTGGErltlgGLDK 362
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616915334 315 ERYIEPTLLDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRV 379
Cdd:cd07559 363 GYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRV 427
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
98-393 |
9.10e-49 |
|
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: 171.40 E-value: 9.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 98 SYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINETFDANYIEVIEGGIEET-QTL 176
Cdd:cd07107 110 HYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREVLPPGVFNILPGDGATAgAAL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 177 I-HLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFG-KFTNAGQTCVAPDYILVHE 254
Cdd:cd07107 190 VrHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAAVAGmNFTWCGQSCGSTSRLFVHE 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 255 SVKDDLITALSKTLREFY-GQNIQQSPDYGRIVNLKHYHRLTSLLNSAQ---MNIVFGGHSDEDER-----YIEPTLLDH 325
Cdd:cd07107 270 SIYDEVLARVVERVAAIKvGDPTDPATTMGPLVSRQQYDRVMHYIDSAKregARLVTGGGRPEGPAleggfYVEPTVFAD 349
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616915334 326 VTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAINDT 393
Cdd:cd07107 350 VTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVWINGS 417
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
99-391 |
1.45e-48 |
|
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: 170.70 E-value: 1.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 99 YIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEET-QTL 176
Cdd:cd07115 112 YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAgFPAGVLNVVTGFGEVAgAAL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 177 I-HLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHES 255
Cdd:cd07115 192 VeHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHES 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 256 VKDDLI---TALSKTLRefYGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQMN---IVFGGHSDeDER--YIEPTLLDHVT 327
Cdd:cd07115 272 IYDEFLerfTSLARSLR--PGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREEgarLLTGGKRP-GARgfFVEPTIFAAVP 348
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616915334 328 NDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIN 391
Cdd:cd07115 349 PEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWIN 412
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
99-355 |
2.03e-48 |
|
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: 170.89 E-value: 2.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 99 YIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEG-GIEETQTL 176
Cdd:cd07097 130 ETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAgLPAGVFNLVMGsGSEVGQAL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 177 I-HLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHES 255
Cdd:cd07097 210 VeHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEG 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 256 VKDDLITAL---SKTLRefYGQNIQQSPDYGRIVN---LKHYHRLTSLLNSAQMNIVFGGH---SDEDERYIEPTLLDHV 326
Cdd:cd07097 290 IHDRFVEALverTKALK--VGDALDEGVDIGPVVSerqLEKDLRYIEIARSEGAKLVYGGErlkRPDEGYYLAPALFAGV 367
|
250 260
....*....|....*....|....*....
gi 616915334 327 TNDSAIMQEEIFGPILPILTYQSLDEAIA 355
Cdd:cd07097 368 TNDMRIAREEIFGPVAAVIRVRDYDEALA 396
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
95-386 |
3.52e-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: 170.37 E-value: 3.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 95 PTKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEET 173
Cdd:cd07142 132 PHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAgLPDGVLNIVTGFGPTA 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 174 QTLI--HLPFDYVFFTGSENVGKIVYQAASE-NLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYI 250
Cdd:cd07142 212 GAAIasHMDVDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRT 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 251 LVHESVKDDLI-----TALSKTLREFYGQNIQQSPDygriVNLKHYHRLTSLLNSAQ---MNIVFGGHSDEDE-RYIEPT 321
Cdd:cd07142 292 FVHESIYDEFVekakaRALKRVVGDPFRKGVEQGPQ----VDKEQFEKILSYIEHGKeegATLITGGDRIGSKgYYIQPT 367
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616915334 322 LLDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFG 386
Cdd:cd07142 368 IFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAG 432
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
20-392 |
3.91e-48 |
|
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: 170.06 E-value: 3.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 20 TKDISFRKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAyATEIGITLKSIKNARKELKN----------WTKTKNvdt 89
Cdd:cd07082 57 TMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDA-LKEVDRTIDYIRDTIEELKRldgdslpgdwFPGTKG--- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 90 plylfpTKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEG 168
Cdd:cd07082 133 ------KIAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAgFPKGVVNVVTG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 169 GIEETQTLI--HLPFDYVFFTGSENVGKIVYQAASenLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVA 246
Cdd:cd07082 207 RGREIGDPLvtHGRIDVISFTGSTEVGNRLKKQHP--MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 247 PDYILVHESVKDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQMN---IVFGGHSdEDERYIEPTL 322
Cdd:cd07082 285 IKRVLVHESVADELVELLKEEVAKLkVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKgatVLNGGGR-EGGNLIYPTL 363
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 323 LDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIND 392
Cdd:cd07082 364 LDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINS 433
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
99-392 |
5.42e-48 |
|
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: 169.41 E-value: 5.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 99 YIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEETQTLI 177
Cdd:cd07090 111 YTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAgLPDGVFNVVQGGGETGQLLC 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 178 HLP-FDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHESV 256
Cdd:cd07090 191 EHPdVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSI 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 257 KDDLITAL-SKTLREFYGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQMN---IVFGG---HSDEDER---YIEPTLLDHV 326
Cdd:cd07090 271 KDEFTERLvERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQEgakVLCGGervVPEDGLEngfYVSPCVLTDC 350
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616915334 327 TNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIND 392
Cdd:cd07090 351 TDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINT 416
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
95-392 |
5.85e-48 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 169.22 E-value: 5.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 95 PTKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVA-RVIKRLINETFDANYIEVIEGGIEET 173
Cdd:TIGR01804 124 PSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTAlKVAEIMEEAGLPKGVFNVVQGDGAEV 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 174 QTLI--HLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYIL 251
Cdd:TIGR01804 204 GPLLvnHPDVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVF 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 252 VHESVKDDLITAL-SKTLREFYGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQ---MNIVFGGHSDEDER-----YIEPTL 322
Cdd:TIGR01804 284 VHKKIKERFLARLvERTERIKLGDPFDEATEMGPLISAAHRDKVLSYIEKGKaegATLATGGGRPENVGlqngfFVEPTV 363
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 323 LDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIND 392
Cdd:TIGR01804 364 FADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINT 433
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
20-391 |
6.34e-48 |
|
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: 169.45 E-value: 6.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 20 TKDISFRKEQLKKLSKAIksyESDI-----LEALytDLGKNKVEAYATEIGITLKSIKN-ARKELKNWTKTKNVDTPLYl 93
Cdd:cd07141 65 TMDASERGRLLNKLADLI---ERDRaylasLETL--DNGKPFSKSYLVDLPGAIKVLRYyAGWADKIHGKTIPMDGDFF- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 94 fptkSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEE 172
Cdd:cd07141 139 ----TYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAgFPPGVVNVVPGYGPT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 173 TQTLI--HLPFDYVFFTGSENVGKIVYQAASE-NLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDY 249
Cdd:cd07141 215 AGAAIssHPDIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSR 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 250 ILVHESVKDDLIT-----ALSKTLREFYGQNIQQSPDygriVNLKHYHRLTSLLNSAQ---MNIVFGGHSDEDERY-IEP 320
Cdd:cd07141 295 TFVQESIYDEFVKrsverAKKRVVGNPFDPKTEQGPQ----IDEEQFKKILELIESGKkegAKLECGGKRHGDKGYfIQP 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616915334 321 TLLDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIN 391
Cdd:cd07141 371 TVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVN 441
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
4-392 |
1.05e-47 |
|
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: 167.64 E-value: 1.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 4 IEQKFYDSKAFFNTQQTKDISFRKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAYAtEIGitlKSI-------KNARK 76
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARA-EVE---KCAwicryyaENAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 77 ELKnwtktknvDTPLYLFPTKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINE 156
Cdd:cd07100 77 FLA--------DEPIETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFRE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 157 -TFDANYIEVIEGGIEETQTLIHLPF-DYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICF 234
Cdd:cd07100 149 aGFPEGVFQNLLIDSDQVEAIIADPRvRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 235 GKFTNAGQTCVAPDYILVHESVKDDLITALSKTLREF-YGQNIQQSPDYG---RIVNLKHYHRL--TSLLNSAQmnIVFG 308
Cdd:cd07100 229 GRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALkVGDPMDEDTDLGplaRKDLRDELHEQveEAVAAGAT--LLLG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 309 GH-SDEDERYIEPTLLDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGG 387
Cdd:cd07100 307 GKrPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGM 386
|
....*
gi 616915334 388 GAIND 392
Cdd:cd07100 387 VFING 391
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
26-392 |
1.79e-47 |
|
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: 167.61 E-value: 1.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 26 RKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAYAtEIGITLKSIKNARKELKnwtKTKNVDTPLYLFPTKS----YIK 101
Cdd:cd07094 45 RMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV-EVDRAIDTLRLAAEEAE---RIRGEEIPLDATQGSDnrlaWTI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 102 KEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVA-RVIKRLINETFDANYIEVIEGGIEETQTLI--H 178
Cdd:cd07094 121 REPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSAlELAKILVEAGVPEGVLQVVTGEREVLGDAFaaD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 179 LPFDYVFFTGSENVGKIVYQAASenLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHESVKD 258
Cdd:cd07094 201 ERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYD 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 259 DLITAL---SKTLRefYGQNIQQSPDYGRIVNLKHYHRLTSLLNSA---QMNIVFGGHsdEDERYIEPTLLDHVTNDSAI 332
Cdd:cd07094 279 EFIEAFvaaVKKLK--VGDPLDEDTDVGPLISEEAAERVERWVEEAveaGARLLCGGE--RDGALFKPTVLEDVPRDTKL 354
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 333 MQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIND 392
Cdd:cd07094 355 STEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVND 414
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
97-392 |
1.81e-47 |
|
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: 167.54 E-value: 1.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 97 KSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEE-TQ 174
Cdd:cd07146 113 KIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAgLPPDMLSVVTGEPGEiGD 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 175 TLIHLP-FDYVFFTGSENVGKIVyqAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVH 253
Cdd:cd07146 193 ELITHPdVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVH 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 254 ESVKD---DLITALSKTLRefYGQNIQQSPDYGRIVNLKHYHRLTSLLNSA--QMNIVFGGHSDEDERYiEPTLLDHVTN 328
Cdd:cd07146 271 ESVADefvDLLVEKSAALV--VGDPMDPATDMGTVIDEEAAIQIENRVEEAiaQGARVLLGNQRQGALY-APTVLDHVPP 347
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616915334 329 DSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIND 392
Cdd:cd07146 348 DAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNE 411
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
12-392 |
2.26e-46 |
|
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: 164.82 E-value: 2.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 12 KAFFNTQQTKDISFRKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAyATEIGITLKSIKN----ARkelknwTKTKNV 87
Cdd:cd07120 30 RAFDETDWAHDPRLRARVLLELADAFEANAERLARLLALENGKILGEA-RFEISGAISELRYyaglAR------TEAGRM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 88 DTPLylfPTK-SYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINE--TFDANYIE 164
Cdd:cd07120 103 IEPE---PGSfSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEipSLPAGVVN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 165 VI-EGGIEETQTLIHLP-FDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQ 242
Cdd:cd07120 180 LFtESGSEGAAHLVASPdVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 243 TCVAPDYILVHESVKDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQMN----IVFGGHSDEDER- 316
Cdd:cd07120 260 FCMAGSRVLVQRSIADEVRDRLAARLAAVkVGPGLDPASDMGPLIDRANVDRVDRMVERAIAAgaevVLRGGPVTEGLAk 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616915334 317 --YIEPTLLDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIND 392
Cdd:cd07120 340 gaFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWIND 417
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
26-374 |
2.77e-46 |
|
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: 164.43 E-value: 2.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 26 RKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAYAtEIGITLKSIKNARKELKNWT-KTKNVDTPlylfPTKSYIKKEP 104
Cdd:cd07150 45 RERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWF-ETTFTPELLRAAAGECRRVRgETLPSDSP----GTVSMSVRRP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 105 YGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEETQTLI--HLPF 181
Cdd:cd07150 120 LGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAgLPKGVFNVVTGGGAEVGDELvdDPRV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 182 DYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHESVKDDLI 261
Cdd:cd07150 200 RMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 262 TALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQ---MNIVFGGHsdEDERYIEPTLLDHVTNDSAIMQEEI 337
Cdd:cd07150 280 KKFVARASKLkVGDPRDPDTVIGPLISPRQVERIKRQVEDAVakgAKLLTGGK--YDGNFYQPTVLTDVTPDMRIFREET 357
|
330 340 350
....*....|....*....|....*....|....*..
gi 616915334 338 FGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDEN 374
Cdd:cd07150 358 FGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQ 394
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
98-386 |
4.90e-46 |
|
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: 164.54 E-value: 4.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 98 SYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTP-NVARVIKRLINETFDANYIEVIEGGIEETQTL 176
Cdd:cd07113 136 AFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPlTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 177 IHLP-FDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHES 255
Cdd:cd07113 216 ISHPdVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRS 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 256 VKDDLITALSKTLREFY-GQNIQQSPDYGRIVNLKHYHRLTSLLNSAQM---NIVFGGHS-DEDERYIEPTLLDHVTNDS 330
Cdd:cd07113 296 KFDELVTKLKQALSSFQvGSPMDESVMFGPLANQPHFDKVCSYLDDARAegdEIVRGGEAlAGEGYFVQPTLVLARSADS 375
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 616915334 331 AIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFG 386
Cdd:cd07113 376 RLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAG 431
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
98-391 |
6.71e-46 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 163.90 E-value: 6.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 98 SYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEETQTL 176
Cdd:cd07139 131 VLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAgLPPGVVNVVPADREVGEYL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 177 I-HLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHES 255
Cdd:cd07139 211 VrHPGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRS 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 256 VKDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQMN----IVFGGHSDEDER--YIEPTLLDHVTN 328
Cdd:cd07139 291 RYDEVVEALAAAVAALkVGDPLDPATQIGPLASARQRERVEGYIAKGRAEgarlVTGGGRPAGLDRgwFVEPTLFADVDN 370
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616915334 329 DSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIN 391
Cdd:cd07139 371 DMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN 433
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
96-391 |
6.86e-46 |
|
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: 164.16 E-value: 6.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 96 TKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINETFDANYIEVIEG-GIEETQ 174
Cdd:cd07117 128 TLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNIVTGkGSKSGE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 175 TLIHLP-FDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVH 253
Cdd:cd07117 208 YLLNHPgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQ 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 254 ESVKDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQ---MNIVFGGH----SDED-ERYIEPTLLD 324
Cdd:cd07117 288 EGIYDEFVAKLKEKFENVkVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKeegAKILTGGHrlteNGLDkGFFIEPTLIV 367
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616915334 325 HVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIN 391
Cdd:cd07117 368 NVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVN 434
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
26-393 |
2.51e-45 |
|
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: 162.09 E-value: 2.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 26 RKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAyATEIGITLKSIKNA-----RKELKnwtktknvDTPlYLFPTK-SY 99
Cdd:cd07151 56 RAEILEKAAQILEERRDEIVEWLIRESGSTRIKA-NIEWGAAMAITREAatfplRMEGR--------ILP-SDVPGKeNR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 100 IKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVikrLINETFD-----ANYIEVIEGGIEET- 173
Cdd:cd07151 126 VYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGL---LLAKIFEeaglpKGVLNVVVGAGSEIg 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 174 -QTLIHLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILV 252
Cdd:cd07151 203 dAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 253 HESVKDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQ---MNIVFGGHSdeDERYIEPTLLDHVTN 328
Cdd:cd07151 283 HEDVYDEFVEKFVERVKALpYGDPSDPDTVVGPLINESQVDGLLDKIEQAVeegATLLVGGEA--EGNVLEPTVLSDVTN 360
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616915334 329 DSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAINDT 393
Cdd:cd07151 361 DMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQ 425
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
103-386 |
8.04e-45 |
|
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: 162.01 E-value: 8.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 103 EPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDA---NYI----EVIEGGIEEtq 174
Cdd:cd07124 165 RPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAgLPPgvvNFLpgpgEEVGDYLVE-- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 175 tliHLPFDYVFFTGSENVGKIVYQAAS------ENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPD 248
Cdd:cd07124 243 ---HPDVRFIAFTGSREVGLRIYERAAkvqpgqKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACS 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 249 YILVHESVKDDLIT---ALSKTLRefYGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQMN--IVFGGHSDEDER---YIEP 320
Cdd:cd07124 320 RVIVHESVYDEFLErlvERTKALK--VGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEgrLLLGGEVLELAAegyFVQP 397
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616915334 321 TLLDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFG 386
Cdd:cd07124 398 TIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVG 463
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
98-392 |
1.05e-44 |
|
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: 160.15 E-value: 1.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 98 SYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPnVAR--VIKRLINET-FDANYIEVIEGGIEETQ 174
Cdd:cd07152 104 SLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTP-VSGgvVIARLFEEAgLPAGVLHVLPGGADAGE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 175 TLIHLP-FDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVH 253
Cdd:cd07152 183 ALVEDPnVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVH 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 254 ESVKDDLITALSKTLREF-YGQNIQQSPDYGRIVN---LKHYHRLTSLLNSAQMNIVFGGHSdeDERYIEPTLLDHVTND 329
Cdd:cd07152 263 ESVADAYTAKLAAKAKHLpVGDPATGQVALGPLINarqLDRVHAIVDDSVAAGARLEAGGTY--DGLFYRPTVLSGVKPG 340
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616915334 330 SAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIND 392
Cdd:cd07152 341 MPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHIND 403
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
99-392 |
4.70e-44 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 158.56 E-value: 4.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 99 YIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEETQTLI 177
Cdd:cd07147 118 LVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETgLPKGAFSVLPCSRDDADLLV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 178 HLP-FDYVFFTGSENVG-KIVYQAASEnlvPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHES 255
Cdd:cd07147 198 TDErIKLLSFTGSPAVGwDLKARAGKK---KVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRS 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 256 VKDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSA---QMNIVFGGHSDEDerYIEPTLLDHVTNDSA 331
Cdd:cd07147 275 VYDEFKSRLVARVKALkTGDPKDDATDVGPMISESEAERVEGWVNEAvdaGAKLLTGGKRDGA--LLEPTILEDVPPDME 352
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616915334 332 IMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIND 392
Cdd:cd07147 353 VNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVIND 413
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
96-392 |
1.14e-43 |
|
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: 157.47 E-value: 1.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 96 TKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEETQ 174
Cdd:cd07101 110 TRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAgLPRDLWQVVTGPGSEVG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 175 TLIHLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHE 254
Cdd:cd07101 190 GAIVDNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHE 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 255 SVKDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQ---MNIVFGGHSDED--ERYIEPTLLDHVTN 328
Cdd:cd07101 270 SVYDEFVRRFVARTRALrLGAALDYGPDMGSLISQAQLDRVTAHVDDAVakgATVLAGGRARPDlgPYFYEPTVLTGVTE 349
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616915334 329 DSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIND 392
Cdd:cd07101 350 DMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNE 413
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
87-386 |
2.72e-43 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 157.59 E-value: 2.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 87 VDTPLYLFptKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTP-------NVARVIKrlinetFD 159
Cdd:PLN02467 136 VSLPMETF--KGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASvtclelaDICREVG------LP 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 160 ANYIEVIEG-GIEETQTL-IHLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKF 237
Cdd:PLN02467 208 PGVLNVVTGlGTEAGAPLaSHPGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCF 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 238 TNAGQTCVAPDYILVHESVKDDLITALSKtlrefYGQNIQQSPDY------GRIVNLKHYHRLTSLLNSAQMN---IVFG 308
Cdd:PLN02467 288 WTNGQICSATSRLLVHERIASEFLEKLVK-----WAKNIKISDPLeegcrlGPVVSEGQYEKVLKFISTAKSEgatILCG 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 309 GHSDEDER---YIEPTLLDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSF 385
Cdd:PLN02467 363 GKRPEHLKkgfFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQA 442
|
.
gi 616915334 386 G 386
Cdd:PLN02467 443 G 443
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
103-391 |
2.48e-41 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 152.65 E-value: 2.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 103 EPYGTVLIIAPFNYPFqLVFEPLIG-AIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEG-GIEETQTLI-H 178
Cdd:PLN02466 194 EPIGVAGQIIPWNFPL-LMFAWKVGpALACGNTIVLKTAEQTPLSALYAAKLLHEAgLPPGVLNVVSGfGPTAGAALAsH 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 179 LPFDYVFFTGSENVGKIVYQ-AASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHESVK 257
Cdd:PLN02466 273 MDVDKLAFTGSTDTGKIVLElAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVY 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 258 DDLIT-----ALSKTLREFYGQNIQQSPDygriVNLKHYHRLTSLLNS---AQMNIVFGGHSDEDERY-IEPTLLDHVTN 328
Cdd:PLN02466 353 DEFVEkakarALKRVVGDPFKKGVEQGPQ----IDSEQFEKILRYIKSgveSGATLECGGDRFGSKGYyIQPTVFSNVQD 428
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616915334 329 DSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIN 391
Cdd:PLN02466 429 DMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVN 491
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
84-357 |
6.97e-41 |
|
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: 150.36 E-value: 6.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 84 TKNVDTplylfptksYIKKEPYGTVLIIAPFNYPFQ--LVFEPLigAIAAGNTAIIKPSELTPNVARVIKRLINET-FDA 160
Cdd:cd07085 125 ARGIDT---------YSYRQPLGVVAGITPFNFPAMipLWMFPM--AIACGNTFVLKPSERVPGAAMRLAELLQEAgLPD 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 161 NYIEVIEGGIEETQTLIHLP-FDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTN 239
Cdd:cd07085 194 GVLNVVHGGKEAVNALLDHPdIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 240 AGQTCVAPDYILVHESVKDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNS-----AQM-----NIVFG 308
Cdd:cd07085 274 AGQRCMALSVAVAVGDEADEWIPKLVERAKKLkVGAGDDPGADMGPVISPAAKERIEGLIESgveegAKLvldgrGVKVP 353
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 616915334 309 GHsdEDERYIEPTLLDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFI 357
Cdd:cd07085 354 GY--ENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAII 400
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
99-354 |
1.61e-40 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 149.97 E-value: 1.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 99 YIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEETQTLI 177
Cdd:PLN02766 153 YTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAgVPDGVINVVTGFGPTAGAAI 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 178 --HLPFDYVFFTGSENVGKIVYQAASE-NLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHE 254
Cdd:PLN02766 233 asHMDVDKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 255 SVKDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQ---MNIVFGGHSDEDERY-IEPTLLDHVTND 329
Cdd:PLN02766 313 GIYDEFVKKLVEKAKDWvVGDPFDPRARQGPQVDKQQFEKILSYIEHGKregATLLTGGKPCGDKGYyIEPTIFTDVTED 392
|
250 260
....*....|....*....|....*
gi 616915334 330 SAIMQEEIFGPILPILTYQSLDEAI 354
Cdd:PLN02766 393 MKIAQDEIFGPVMSLMKFKTVEEAI 417
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
4-386 |
1.83e-40 |
|
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: 148.57 E-value: 1.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 4 IEQKFYDSKAFFNTQQTKDISFRKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAyATEIGITLKSIKNARKELKNWTK 83
Cdd:cd07095 2 VDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEA-QTEVAAMAGKIDISIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 84 TKNVDTPlylfPTKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANY 162
Cdd:cd07095 81 ERATPMA----QGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAgLPPGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 163 IEVIEGGIEETQTLI-HLPFDYVFFTGSENVGKIVYQAASENL-VPVTLEMGGKSPVIVDETANIKVASERICFGKFTNA 240
Cdd:cd07095 157 LNLVQGGRETGEALAaHEGIDGLLFTGSAATGLLLHRQFAGRPgKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 241 GQTCVAPDYILVHESVK-DDLITAL---SKTLRefYGQNIQQSPDYGRIVNlkhYHRLTSLLNSAQMNIVFGGHS----- 311
Cdd:cd07095 237 GQRCTCARRLIVPDGAVgDAFLERLveaAKRLR--IGAPDAEPPFMGPLII---AAAAARYLLAQQDLLALGGEPllame 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616915334 312 --DEDERYIEPTLLDhVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFG 386
Cdd:cd07095 312 rlVAGTAFLSPGIID-VTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAG 387
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
96-392 |
9.99e-40 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 148.10 E-value: 9.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 96 TKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVA-RVIKRLINETFDANYIEVIEG-GIEET 173
Cdd:PRK09407 146 TKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTAlAAVELLYEAGLPRDLWQVVTGpGPVVG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 174 QTLIHLPfDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVH 253
Cdd:PRK09407 226 TALVDNA-DYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVH 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 254 ESVKDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQ---MNIVFGGHSDED--ERYIEPTLLDHVT 327
Cdd:PRK09407 305 ESIYDEFVRAFVAAVRAMrLGAGYDYSADMGSLISEAQLETVSAHVDDAVakgATVLAGGKARPDlgPLFYEPTVLTGVT 384
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616915334 328 NDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIND 392
Cdd:PRK09407 385 PDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNE 449
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
104-372 |
2.40e-38 |
|
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: 143.50 E-value: 2.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 104 PYGTVLIIAPFNYPFQlVFepliG---AIAA--GNTAIIKPSELTPNVARVIKRLINETFDANYI-----EVIEGGIEET 173
Cdd:cd07130 132 PLGVVGVITAFNFPVA-VW----GwnaAIALvcGNVVVWKPSPTTPLTAIAVTKIVARVLEKNGLpgaiaSLVCGGADVG 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 174 QTLIHLP-FDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILV 252
Cdd:cd07130 207 EALVKDPrVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIV 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 253 HESVKDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQM---NIVFGGHS-DEDERYIEPTLLDhVT 327
Cdd:cd07130 287 HESIYDEVLERLKKAYKQVrIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSqggTVLFGGKViDGPGNYVEPTIVE-GL 365
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 616915334 328 NDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSED 372
Cdd:cd07130 366 SDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTD 410
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
103-354 |
1.90e-37 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 141.61 E-value: 1.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 103 EPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVArvikrlinetfdANYIEVIE--------------G 168
Cdd:PRK03137 170 IPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIA------------AKFVEVLEeaglpagvvnfvpgS 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 169 GIEETQTLI-HLPFDYVFFTGSENVGKIVYQAASEN------LVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAG 241
Cdd:PRK03137 238 GSEVGDYLVdHPKTRFITFTGSREVGLRIYERAAKVqpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSG 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 242 QTCVAPDYILVHESVKDDLITALSKTLREFYGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQMN--IVFGGHSDEDERY-I 318
Cdd:PRK03137 318 QKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNAYMGPVINQASFDKIMSYIEIGKEEgrLVLGGEGDDSKGYfI 397
|
250 260 270
....*....|....*....|....*....|....*.
gi 616915334 319 EPTLLDHVTNDSAIMQEEIFGPILPILTYQSLDEAI 354
Cdd:PRK03137 398 QPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHAL 433
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
103-372 |
8.53e-37 |
|
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: 139.45 E-value: 8.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 103 EPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEETQTLIHLP- 180
Cdd:cd07111 146 KPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAgLPPGVLNIVTGNGSFGSALANHPg 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 181 FDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHESVKDDL 260
Cdd:cd07111 226 VDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEEL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 261 ITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNS--AQMNIVFGGHSD--EDERYIEPTLLDHVTNDSAIMQE 335
Cdd:cd07111 306 IRKLKERMSHLrVGDPLDKAIDMGAIVDPAQLKRIRELVEEgrAEGADVFQPGADlpSKGPFYPPTLFTNVPPASRIAQE 385
|
250 260 270
....*....|....*....|....*....|....*..
gi 616915334 336 EIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSED 372
Cdd:cd07111 386 EIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSEN 422
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
99-391 |
1.10e-35 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 136.55 E-value: 1.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 99 YIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLinetfdanYIE---------VIEGG 169
Cdd:PRK13252 137 YTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEI--------YTEaglpdgvfnVVQGD 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 170 IEETQTLIHLP-FDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPD 248
Cdd:PRK13252 209 GRVGAWLTEHPdIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGT 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 249 YILVHESVKDDLITAL-SKTLREFYGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQMN---IVFGGHSDEDER-----YIE 319
Cdd:PRK13252 289 RVFVQKSIKAAFEARLlERVERIRIGDPMDPATNFGPLVSFAHRDKVLGYIEKGKAEgarLLCGGERLTEGGfangaFVA 368
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616915334 320 PTLLDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIN 391
Cdd:PRK13252 369 PTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWIN 440
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
97-378 |
3.02e-34 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 132.39 E-value: 3.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 97 KSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEETQT 175
Cdd:PRK09457 127 AAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAgLPAGVLNLVQGGRETGKA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 176 LIHLP-FDYVFFTGSENVGKIVYQAASENlvP---VTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYIL 251
Cdd:PRK09457 207 LAAHPdIDGLLFTGSANTGYLLHRQFAGQ--PekiLALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 252 VHESVKDDLI----TALSKTLRefYGQ-NIQQSPDYGRIVNLKHYHRLTsllnSAQMNIV-FGGHS-------DEDERYI 318
Cdd:PRK09457 285 VPQGAQGDAFlarlVAVAKRLT--VGRwDAEPQPFMGAVISEQAAQGLV----AAQAQLLaLGGKSllemtqlQAGTGLL 358
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 319 EPTLLDhVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQR 378
Cdd:PRK09457 359 TPGIID-VTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQ 417
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
4-392 |
4.94e-34 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 131.93 E-value: 4.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 4 IEQKFYDSKAFFNTQQTKDISFRKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAYAtEIGITLKSIK-NARKELKnwT 82
Cdd:cd07083 57 AEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAID-DVAEAIDFIRyYARAALR--L 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 83 KTKNVDTPLYLFPTKSYIKKePYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDAN 161
Cdd:cd07083 134 RYPAVEVVPYPGEDNESFYV-GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAgFPPG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 162 YIEVIEG-GIEETQTLIHLP-FDYVFFTGSENVGKIVYQAASENL------VPVTLEMGGKSPVIVDETANIKVASERIC 233
Cdd:cd07083 213 VVQFLPGvGEEVGAYLTEHErIRGINFTGSLETGKKIYEAAARLApgqtwfKRLYVETGGKNAIIVDETADFELVVEGVV 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 234 FGKFTNAGQTCVAPDYILVHESVKDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQ--MNIVFGGH 310
Cdd:cd07083 293 VSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLsVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKneGQLVLGGK 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 311 SDEDERY-IEPTLLDHVTNDSAIMQEEIFGPILPILTYQSLD--EAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGG 387
Cdd:cd07083 373 RLEGEGYfVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGN 452
|
....*
gi 616915334 388 GAIND 392
Cdd:cd07083 453 LYINR 457
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
96-379 |
8.21e-34 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 131.04 E-value: 8.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 96 TKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINETFDANYIEVIEG-GIEETQ 174
Cdd:cd07116 128 TVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGfGLEAGK 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 175 TLIHLP-FDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSP------VIVDETANIKVASERICFGKFtNAGQTCVAP 247
Cdd:cd07116 208 PLASSKrIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPniffadVMDADDAFFDKALEGFVMFAL-NQGEVCTCP 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 248 DYILVHESVKDDLIT-ALSKTLREFYGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQ---MNIVFGGH-----SDEDERYI 318
Cdd:cd07116 287 SRALIQESIYDRFMErALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKeegAEVLTGGErnelgGLLGGGYY 366
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616915334 319 EPTLLdHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRV 379
Cdd:cd07116 367 VPTTF-KGGNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRM 426
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
98-391 |
6.91e-32 |
|
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: 125.69 E-value: 6.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 98 SYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRL-INETFDANYIEVIEG-GIEETQT 175
Cdd:cd07140 141 TLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELtVKAGFPKGVINILPGsGSLVGQR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 176 LI-HLPFDYVFFTGSENVGK-IVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVH 253
Cdd:cd07140 221 LSdHPDVRKLGFTGSTPIGKhIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 254 ESVKDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSA---QMNIVFGG-HSDEDERYIEPTLLDHVTN 328
Cdd:cd07140 301 ESIHDEFVRRVVEEVKKMkIGDPLDRSTDHGPQNHKAHLDKLVEYCERGvkeGATLVYGGkQVDRPGFFFEPTVFTDVED 380
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616915334 329 DSAIMQEEIFGPILPILTYQslDEAIAFIHQRPKP----LSLYLFSEDENATQRVINELSFGGGAIN 391
Cdd:cd07140 381 HMFIAKEESFGPIMIISKFD--DGDVDGVLQRANDteygLASGVFTKDINKALYVSDKLEAGTVFVN 445
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
100-392 |
1.71e-31 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 125.01 E-value: 1.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 100 IKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEG-GIEETQTL- 176
Cdd:PRK09847 153 IVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGfGHEAGQALs 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 177 IHLPFDYVFFTGSENVGK-IVYQAASENLVPVTLEMGGKSPVIV-DETANIKVASERICFGKFTNAGQTCVAPDYILVHE 254
Cdd:PRK09847 233 RHNDIDAIAFTGSTRTGKqLLKDAGDSNMKRVWLEAGGKSANIVfADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 255 SVKDDLITALSKTLREFY-GQNIQQSPDYGRIVNLKHYHRLTSLLN--SAQMNIVFGGHSDEDERYIEPTLLDHVTNDSA 331
Cdd:PRK09847 313 SIADEFLALLKQQAQNWQpGHPLDPATTMGTLIDCAHADSVHSFIRegESKGQLLLDGRNAGLAAAIGPTIFVDVDPNAS 392
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616915334 332 IMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIND 392
Cdd:PRK09847 393 LSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNN 453
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
102-394 |
2.65e-30 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 121.55 E-value: 2.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 102 KEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEG-----GIEETQT 175
Cdd:PRK11241 144 KQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAgIPAGVFNVVTGsagavGGELTSN 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 176 LIhlpFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHES 255
Cdd:PRK11241 224 PL---VRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 256 VKDDLITALSKTLREFY-GQNIQQSPDYGRIVNLKHYHRLTSLLNSA---QMNIVFGGHSDEDE-RYIEPTLLDHVTNDS 330
Cdd:PRK11241 301 VYDRFAEKLQQAVSKLHiGDGLEKGVTIGPLIDEKAVAKVEEHIADAlekGARVVCGGKAHELGgNFFQPTILVDVPANA 380
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616915334 331 AIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAINDTL 394
Cdd:PRK11241 381 KVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGI 444
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
53-392 |
8.49e-30 |
|
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: 119.45 E-value: 8.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 53 GKNKVEAyATEIGITLKSIKNARKELKNWTKTknvDTPLYLFPTKS----YIKKEPYGTVLIIAPFNYPFQLVFEPLIGA 128
Cdd:cd07148 73 GKPLVDA-KVEVTRAIDGVELAADELGQLGGR---EIPMGLTPASAgriaFTTREPIGVVVAISAFNHPLNLIVHQVAPA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 129 IAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEETQTLIHLP-FDYVFFTGSENVGKIVyqaaSENLVP 206
Cdd:cd07148 149 IAAGCPVIVKPALATPLSCLAFVDLLHEAgLPEGWCQAVPCENAVAEKLVTDPrVAFFSFIGSARVGWML----RSKLAP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 207 VT---LEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHESVKDDLITALS-KTLREFYGQNIQQSPDY 282
Cdd:cd07148 225 GTrcaLEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAaAAEKLVVGDPTDPDTEV 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 283 GRIVNLKHYHRLTSLLNSAQM---NIVFGGHSDEDERYiEPTLLDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQ 359
Cdd:cd07148 305 GPLIRPREVDRVEEWVNEAVAagaRLLCGGKRLSDTTY-APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANS 383
|
330 340 350
....*....|....*....|....*....|...
gi 616915334 360 RPKPLSLYLFSEDENATQRVINELSFGGGAIND 392
Cdd:cd07148 384 LPVAFQAAVFTKDLDVALKAVRRLDATAVMVND 416
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
4-391 |
9.25e-30 |
|
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: 119.60 E-value: 9.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 4 IEQKFYDSKAFFNTQQTKDISFRKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAYAtEIGITLKSIKNA---RKELKN 80
Cdd:TIGR01722 40 VDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDALG-DVARGLEVVEHAcgvNSLLKG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 81 WTK---TKNVDTplylfptksYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET 157
Cdd:TIGR01722 119 ETStqvATRVDV---------YSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 158 -FDANYIEVIEGGIEET-QTLIHLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFG 235
Cdd:TIGR01722 190 gAPDGVLNVVHGDKEAVdRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 236 KFTNAGQTCVA-PDYILVHESvkDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQ---MNIVFGGH 310
Cdd:TIGR01722 270 AYGAAGQRCMAiSAAVLVGAA--DEWVPEIRERAEKIrIGPGDDPGAEMGPLITPQAKDRVASLIAGGAaegAEVLLDGR 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 311 S-----DEDERYIEPTLLDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSF 385
Cdd:TIGR01722 348 GykvdgYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEV 427
|
....*.
gi 616915334 386 GGGAIN 391
Cdd:TIGR01722 428 GQVGVN 433
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
102-391 |
1.74e-26 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 110.62 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 102 KEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPseltPNVARVIKRLINETFD-----ANYIEVIEGGIEETQTL 176
Cdd:PLN00412 156 KIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKP----PTQGAVAALHMVHCFHlagfpKGLISCVTGKGSEIGDF 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 177 I--HLPFDYVFFTGSENVGKIVYQAAsenLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHE 254
Cdd:PLN00412 232 LtmHPGVNCISFTGGDTGIAISKKAG---MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVME 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 255 SVKDDLITALSKTLREFYGQNIQQSPDYGRIVNLKHYHRLTSLLNSA-QMNIVFGGHSDEDERYIEPTLLDHVTNDSAIM 333
Cdd:PLN00412 309 SVADALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVMDAkEKGATFCQEWKREGNLIWPLLLDNVRPDMRIA 388
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 616915334 334 QEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIN 391
Cdd:PLN00412 389 WEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQIN 446
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
104-370 |
3.77e-26 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 109.54 E-value: 3.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 104 PYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINETFDANYI-----EVIEGGIEETQTL-- 176
Cdd:PLN02315 154 PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLpgaifTSFCGGAEIGEAIak 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 177 -IHLPFdyVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHES 255
Cdd:PLN02315 234 dTRIPL--VSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHES 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 256 VKDDLITALSKTlrefYGQ-NIQQSPDYGRIVNLKH-------YHRLTSLLNSAQMNIVFGGHS-DEDERYIEPTLLDhV 326
Cdd:PLN02315 312 IYDDVLEQLLTV----YKQvKIGDPLEKGTLLGPLHtpeskknFEKGIEIIKSQGGKILTGGSAiESEGNFVQPTIVE-I 386
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 616915334 327 TNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFS 370
Cdd:PLN02315 387 SPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFT 430
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
96-391 |
1.22e-25 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 107.90 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 96 TKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINEtfdanyievieGGIEET-- 173
Cdd:PRK09406 115 SRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRR-----------AGFPDGcf 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 174 QTLIhLPFDYV------------FFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAG 241
Cdd:PRK09406 184 QTLL-VGSGAVeailrdprvaaaTLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNG 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 242 QTCVAPDYILVHESVKDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQMN---IVFGGHS-DEDER 316
Cdd:PRK09406 263 QSCIAAKRFIVHADVYDAFAEKFVARMAALrVGDPTDPDTDVGPLATEQGRDEVEKQVDDAVAAgatILCGGKRpDGPGW 342
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616915334 317 YIEPTLLDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIN 391
Cdd:PRK09406 343 FYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFIN 417
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
100-391 |
2.23e-24 |
|
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: 104.58 E-value: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 100 IKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLInetFDA-------NYieVIEGGIEE 172
Cdd:cd07125 163 LELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELL---HEAgvprdvlQL--VPGDGEEI 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 173 TQTLIHLP-FDYVFFTGSENVGKIVYQAASEN---LVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPD 248
Cdd:cd07125 238 GEALVAHPrIDGVIFTGSTETAKLINRALAERdgpILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALR 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 249 YILVHESVKDDLITALS---KTLREFYGQNIqqSPDYGRIV---NLKHYHRLTSLLnSAQMNIVFGGHSDE-DERYIEPT 321
Cdd:cd07125 318 LLYLQEEIAERFIEMLKgamASLKVGDPWDL--STDVGPLIdkpAGKLLRAHTELM-RGEAWLIAPAPLDDgNGYFVAPG 394
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616915334 322 LLDHVTNDSaiMQEEIFGPILPILTYQS--LDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIN 391
Cdd:cd07125 395 IIEIVGIFD--LTTEVFGPILHVIRFKAedLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYIN 464
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
4-391 |
4.64e-24 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 103.40 E-value: 4.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 4 IEQKFYDSKAFFNTQQTKDISFRKEQLKKLSKAIKSYESDILEALYTDLGKnkveayateigitlkSIKNARKELknwTK 83
Cdd:PRK13968 31 IENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGK---------------PINQARAEV---AK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 84 TKNV------DTPLYLFP-------TKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSeltPNVARVi 150
Cdd:PRK13968 93 SANLcdwyaeHGPAMLKAeptlvenQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHA---PNVMGC- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 151 KRLINETF-DANYIEVIEGGIEET-----QTLIHLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETAN 224
Cdd:PRK13968 169 AQLIAQVFkDAGIPQGVYGWLNADndgvsQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDAD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 225 IKVASERICFGKFTNAGQTCVAPDYILVHESVKDDL---ITALSKTLRefYGQNIQQSPDYGRIVNLK-----HYHRLTS 296
Cdd:PRK13968 249 LELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFterFVAAAAALK--MGDPRDEENALGPMARFDlrdelHHQVEAT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 297 LLNSAQMniVFGGHSDEDE-RYIEPTLLDHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENA 375
Cdd:PRK13968 327 LAEGARL--LLGGEKIAGAgNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQ 404
|
410
....*....|....*.
gi 616915334 376 TQRVINELSFGGGAIN 391
Cdd:PRK13968 405 ARQMAARLECGGVFIN 420
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
103-391 |
5.70e-24 |
|
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: 103.45 E-value: 5.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 103 EPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVA-RVIKRLINETFDANYIEVIEGGIEETQTLI--HL 179
Cdd:TIGR01238 159 ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAyRAVELMQEAGFPAGTIQLLPGRGADVGAALtsDP 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 180 PFDYVFFTGSENVGKIVYQAASENL---VPVTLEMGGKSPVIVDETAnikvASERICF----GKFTNAGQTCVAPDYILV 252
Cdd:TIGR01238 239 RIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTA----LPEQVVRdvlrSAFDSAGQRCSALRVLCV 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 253 HESVKDDLITALSKTLREF-YGQNIQQSPDYGRIVN-------LKHYHRLTSLLNSAQMNIVFGGHSDEDERYIEPTLLD 324
Cdd:TIGR01238 315 QEDVADRVLTMIQGAMQELkVGVPHLLTTDVGPVIDaeakqnlLAHIEHMSQTQKKIAQLTLDDSRACQHGTFVAPTLFE 394
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616915334 325 hvTNDSAIMQEEIFGPILPILTYQS--LDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIN 391
Cdd:TIGR01238 395 --LDDIAELSEEVFGPVLHVVRYKAreLDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVN 461
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
98-391 |
5.57e-23 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 100.98 E-value: 5.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 98 SYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINETFDANYIEVIEGGIEETQTLI 177
Cdd:PLN02419 243 TYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 178 HLPFDY--VFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHES 255
Cdd:PLN02419 323 CDDEDIraVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGD 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 256 VK--DDLITALSKTLREFYGQniQQSPDYGRIVNLKHYHRLTSLLNS-----AQM-----NIVFGGHsdEDERYIEPTLL 323
Cdd:PLN02419 403 AKswEDKLVERAKALKVTCGS--EPDADLGPVISKQAKERICRLIQSgvddgAKLlldgrDIVVPGY--EKGNFIGPTIL 478
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616915334 324 DHVTNDSAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINELSFGGGAIN 391
Cdd:PLN02419 479 SGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
104-387 |
2.22e-21 |
|
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: 95.38 E-value: 2.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 104 PYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET--FDANYIEVIEGGIEETQTLI-HLP 180
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAglLPPEDVTLINGDGKTMQALLlHPN 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 181 FDYVFFTGSENVGKIVYQAASEnlVPVTLEMGGKSPVIVDETANIKVASERIC-FGKFTNAGQTCVAPDYILVHEsvkDD 259
Cdd:cd07084 180 PKMVLFTGSSRVAEKLALDAKQ--ARIYLELAGFNWKVLGPDAQAVDYVAWQCvQDMTACSGQKCTAQSMLFVPE---NW 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 260 LITALSKTLREFYGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQMNIVFGG----HSDEDERY--IEPTLLdHVTNDSA-- 331
Cdd:cd07084 255 SKTPLVEKLKALLARRKLEDLLLGPVQTFTTLAMIAHMENLLGSVLLFSGkelkNHSIPSIYgaCVASAL-FVPIDEIlk 333
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616915334 332 ---IMQEEIFGPILPILTYQSLDEA--IAFIHQRPKPLSLYLFSEDENATQRVINELSFGG 387
Cdd:cd07084 334 tyeLVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQELIGNLWVAG 394
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
104-390 |
1.73e-17 |
|
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: 83.74 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 104 PYGTVLIIAPFNYPFqlVFEPLIG----AIAAGNTAIIKP-------SELtpnVARVIKRLINET-FDANYIEVIEG-GI 170
Cdd:cd07129 105 PLGPVAVFGASNFPL--AFSVAGGdtasALAAGCPVVVKAhpahpgtSEL---VARAIRAALRATgLPAGVFSLLQGgGR 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 171 EETQTLI-HLPFDYVFFTGSENVGKIVYQAASENL--VPVTLEMGGKSPVIV---------DETANIKVASerICFGkft 238
Cdd:cd07129 180 EVGVALVkHPAIKAVGFTGSRRGGRALFDAAAARPepIPFYAELGSVNPVFIlpgalaergEAIAQGFVGS--LTLG--- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 239 nAGQTCVAPDYILVHESVK-DDLITALSKTLREFYGQ-----NIQQSpdygrivnlkHYHRLTSLLNSAQMNIVFGGHSD 312
Cdd:cd07129 255 -AGQFCTNPGLVLVPAGPAgDAFIAALAEALAAAPAQtmltpGIAEA----------YRQGVEALAAAPGVRVLAGGAAA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 313 EDERYIEPTLL----DHVTNDSAiMQEEIFGPILPILTYQSLDEAIAFIHQRPKPL--SLYLFSEDENATQRVINELSFG 386
Cdd:cd07129 324 EGGNQAAPTLFkvdaAAFLADPA-LQEEVFGPASLVVRYDDAAELLAVAEALEGQLtaTIHGEEDDLALARELLPVLERK 402
|
....
gi 616915334 387 GGAI 390
Cdd:cd07129 403 AGRL 406
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
106-392 |
2.55e-17 |
|
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: 83.40 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 106 GTVLIIAPFNYPfqlvfepligAIAA---------GNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEG-GIEETQ 174
Cdd:cd07123 172 GFVYAVSPFNFT----------AIGGnlagapalmGNVVLWKPSDTAVLSNYLVYKILEEAgLPPGVINFVPGdGPVVGD 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 175 TLIHLP-FDYVFFTGSENVGKIVYQAASENLV-----P-VTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAP 247
Cdd:cd07123 242 TVLASPhLAGLHFTGSTPTFKSLWKQIGENLDryrtyPrIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAA 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 248 DYILVHESVKDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLL----NSAQMNIVFGGHSDEDERY-IEPT 321
Cdd:cd07123 322 SRAYVPESLWPEVKERLLEELKEIkMGDPDDFSNFMGAVIDEKAFDRIKGYIdhakSDPEAEIIAGGKCDDSVGYfVEPT 401
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616915334 322 LLdhVTND--SAIMQEEIFGPILPILTY--QSLDEAIAFIHQ-RPKPLSLYLFSEDENATQRVINELSFGGGA--IND 392
Cdd:cd07123 402 VI--ETTDpkHKLMTEEIFGPVLTVYVYpdSDFEETLELVDTtSPYALTGAIFAQDRKAIREATDALRNAAGNfyIND 477
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
111-355 |
4.98e-14 |
|
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: 73.46 E-value: 4.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 111 IAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET--FDANYIEVIEGGIeeTQTLIHL-PFDYVFFT 187
Cdd:cd07128 151 INAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESglLPEGALQLICGSV--GDLLDHLgEQDVVAFT 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 188 GSENVGKI--VYQAASENLVPVTLEMGGKSPVIVDETAN---------IK-VASERIcfgkfTNAGQTCVAPDYILVHES 255
Cdd:cd07128 229 GSAATAAKlrAHPNIVARSIRFNAEADSLNAAILGPDATpgtpefdlfVKeVAREMT-----VKAGQKCTAIRRAFVPEA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 256 VKDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYH----RLTSLLNSAqmNIVFGGHSDEDER--------YIEPTL 322
Cdd:cd07128 304 RVDAVIEALKARLAKVvVGDPRLEGVRMGPLVSREQREdvraAVATLLAEA--EVVFGGPDRFEVVgadaekgaFFPPTL 381
|
250 260 270
....*....|....*....|....*....|....*
gi 616915334 323 L--DHVTNDSAIMQEEIFGPILPILTYQSLDEAIA 355
Cdd:cd07128 382 LlcDDPDAATAVHDVEAFGPVATLMPYDSLAEAIE 416
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
17-280 |
8.52e-14 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 72.26 E-value: 8.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 17 TQQTKDISFRKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAYATEIGITLKS----IKNARKELKNWTKTKNVDTPLY 92
Cdd:cd07077 9 TLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSesklYKNIDTERGITASVGHIQDVLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 93 LFPTKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGaIAAGNTAIIKPSELTPNVARVIKrLINETFDANY------IEVI 166
Cdd:cd07077 89 PDNGETYVRAFPIGVTMHILPSTNPLSGITSALRG-IATRNQCIFRPHPSAPFTNRALA-LLFQAADAAHgpkilvLYVP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 167 EGGIEETQTLIHLP-FDYVFFTGSENVGKIVYQAAseNLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNaGQTCV 245
Cdd:cd07077 167 HPSDELAEELLSHPkIDLIVATGGRDAVDAAVKHS--PHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFD-QNACA 243
|
250 260 270
....*....|....*....|....*....|....*
gi 616915334 246 APDYILVHESVKDDLITALSKTLREfYGQNIQQSP 280
Cdd:cd07077 244 SEQNLYVVDDVLDPLYEEFKLKLVV-EGLKVPQET 277
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
103-357 |
5.90e-13 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 70.66 E-value: 5.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 103 EPYGTVLIIAPFNYP---F--QLVfepliGAIAAGNTAIIKPSELTPNVARVIKRLINetfdanyieviEGGIEETqTLI 177
Cdd:PRK11905 675 KPLGPVVCISPWNFPlaiFtgQIA-----AALVAGNTVLAKPAEQTPLIAARAVRLLH-----------EAGVPKD-ALQ 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 178 HLPFD---------------YVFFTGSENVGKIVYQAASENL---VPVTLEMGGKSPVIVDETANIK------VASeric 233
Cdd:PRK11905 738 LLPGDgrtvgaalvadpriaGVMFTGSTEVARLIQRTLAKRSgppVPLIAETGGQNAMIVDSSALPEqvvadvIAS---- 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 234 fgKFTNAGQTCVAPDYILVHESVKDDLITALSKTLREFY-GQNIQQSPDYGRIVN-------LKHYHRLTS---LLNSAQ 302
Cdd:PRK11905 814 --AFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRiGDPWRLSTDVGPVIDaeaqaniEAHIEAMRAagrLVHQLP 891
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 616915334 303 MNIVFGGHSdederYIEPTLLDhvTNDSAIMQEEIFGPILPILTYQS--LDEAIAFI 357
Cdd:PRK11905 892 LPAETEKGT-----FVAPTLIE--IDSISDLEREVFGPVLHVVRFKAdeLDRVIDDI 941
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
99-357 |
2.11e-12 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 68.69 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 99 YIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVA-RVIKRLINETFDANYIEVIEG-GIEETQTL 176
Cdd:PRK11904 679 ELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAaEAVKLLHEAGIPKDVLQLLPGdGATVGAAL 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 177 IHLP-FDYVFFTGSENVGKIVYQ--AASEN-LVPVTLEMGGKSPVIVDETANIK------VASericfgKFTNAGQTCVA 246
Cdd:PRK11904 759 TADPrIAGVAFTGSTETARIINRtlAARDGpIVPLIAETGGQNAMIVDSTALPEqvvddvVTS------AFRSAGQRCSA 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 247 PDYILVHESVKDDLITALSKTLREF-YGQNIQQSPDYGRIVN-------LKHYHRLTsllnsAQMNIVFGGHSDEDER-- 316
Cdd:PRK11904 833 LRVLFVQEDIADRVIEMLKGAMAELkVGDPRLLSTDVGPVIDaeakanlDAHIERMK-----REARLLAQLPLPAGTEng 907
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 616915334 317 -YIEPTL--LDHVtndsAIMQEEIFGPILPILTYQS--LDEAIAFI 357
Cdd:PRK11904 908 hFVAPTAfeIDSI----SQLEREVFGPILHVIRYKAsdLDKVIDAI 949
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
104-357 |
6.41e-12 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 67.31 E-value: 6.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 104 PYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINETfdanyiEVIEG------GIEET---Q 174
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEA------GVPAGvvqllpGRGETvgaA 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 175 TLIHLPFDYVFFTGSENVGKIVYQAASENL------VPVTLEMGGKSPVIVDETA------NIKVASericfgKFTNAGQ 242
Cdd:PRK11809 842 LVADARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSAlteqvvADVLAS------AFDSAGQ 915
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 243 TCVAPDYILVHESVKDDLITALSKTLREFYGQNIQQ-SPDYGRIVNlkhyhrltsllNSAQMNIV-------FGGHS--- 311
Cdd:PRK11809 916 RCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRlSTDIGPVID-----------AEAKANIErhiqamrAKGRPvfq 984
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 616915334 312 -----DEDER---YIEPTL--LDHVTNdsaiMQEEIFGPILPILTYQS--LDEAIAFI 357
Cdd:PRK11809 985 aarenSEDWQsgtFVPPTLieLDSFDE----LKREVFGPVLHVVRYNRnqLDELIEQI 1038
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
6-274 |
4.92e-11 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 63.82 E-value: 4.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 6 QKFYDSKaffnTQQTKDISFRKEQLKKLSKAIksyesDILEALYTDLGKNKVEAyateigitlKSIKNARKELKNWTKTK 85
Cdd:cd07081 12 QQGLSCK----SQEMVDLIFRAAAEAAEDARI-----DLAKLAVSETGMGRVED---------KVIKNHFAAEYIYNVYK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 86 NVDTPLYLFPTKSY---IKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINETFDA-- 160
Cdd:cd07081 74 DEKTCGVLTGDENGgtlIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAag 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 161 ---NYIEVI-EGGIEETQTLIHLP-FDYVFFTGSENVGKIVYQAASenlvPVTLEMGGKSPVIVDETANIKVASERICFG 235
Cdd:cd07081 154 apeNLIGWIdNPSIELAQRLMKFPgIGLLLATGGPAVVKAAYSSGK----PAIGVGAGNTPVVIDETADIKRAVQSIVKS 229
|
250 260 270
....*....|....*....|....*....|....*....
gi 616915334 236 KFTNAGQTCVAPDYILVHESVKDDLitalsktLREFYGQ 274
Cdd:cd07081 230 KTFDNGVICASEQSVIVVDSVYDEV-------MRLFEGQ 261
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
104-355 |
1.20e-10 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 62.64 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 104 PYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIE-----VIEGGIEETQTLI 177
Cdd:cd07121 97 PFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAiAEAGGPDnlvvtVEEPTIETTNELM 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 178 HLP-FDYVFFTGSENVGKIVYQAASENLVPvtlemG-GKSPVIVDETANIKVASERICFG-KFTNaGQTCVAPDYILVHE 254
Cdd:cd07121 177 AHPdINLLVVTGGPAVVKAALSSGKKAIGA-----GaGNPPVVVDETADIEKAARDIVQGaSFDN-NLPCIAEKEVIAVD 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 255 SVKDDLITALSKT-LREFYGQNIQQ------SPDYGRIVNLKHYHRLTSLLNSAqmnivFGGHSDEDERYIeptlLDHVT 327
Cdd:cd07121 251 SVADYLIAAMQRNgAYVLNDEQAEQllevvlLTNKGATPNKKWVGKDASKILKA-----AGIEVPADIRLI----IVETD 321
|
250 260
....*....|....*....|....*...
gi 616915334 328 NDSAIMQEEIFGPILPILTYQSLDEAIA 355
Cdd:cd07121 322 KDHPFVVEEQMMPILPVVRVKNFDEAIE 349
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
81-379 |
4.45e-10 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 61.34 E-value: 4.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 81 WTKTKNVDTPLYLFPTKSYIkkePYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSE-------LTPNVARVIkrL 153
Cdd:cd07127 173 WEKPQGKHDPLAMEKTFTVV---PRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPaailplaITVQVAREV--L 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 154 INETFDANYIEVIEGGIEE--TQTLIHLP-FDYVFFTGSENVGKIVYQAASENLVpvTLEMGGKSPVIVDETANIKVASE 230
Cdd:cd07127 248 AEAGFDPNLVTLAADTPEEpiAQTLATRPeVRIIDFTGSNAFGDWLEANARQAQV--YTEKAGVNTVVVDSTDDLKAMLR 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 231 RICFGKFTNAGQTCVAPDYILV-------------HESVKDDLITALSKTLrefyGQNIQQSPDYGRIVNLKHYHRLTSl 297
Cdd:cd07127 326 NLAFSLSLYSGQMCTTPQNIYVprdgiqtddgrksFDEVAADLAAAIDGLL----ADPARAAALLGAIQSPDTLARIAE- 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 298 lnSAQMNIVFG-----GHSD-EDERYIEPTLLDHVTNDSAIMQEEIFGPILPIL----TYQSLDEAIAFIHQRpKPLSLY 367
Cdd:cd07127 401 --ARQLGEVLLaseavAHPEfPDARVRTPLLLKLDASDEAAYAEERFGPIAFVVatdsTDHSIELARESVREH-GAMTVG 477
|
330
....*....|..
gi 616915334 368 LFSEDENATQRV 379
Cdd:cd07127 478 VYSTDPEVVERV 489
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
104-266 |
1.06e-07 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 53.75 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 104 PYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIE-----VIEGGIEETQTLI 177
Cdd:PRK15398 129 PFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLNEAiVAAGGPEnlvvtVAEPTIETAQRLM 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 178 -HLPFDYVFFTGSENV-------GKIVYQAASenlvpvtlemgGKSPVIVDETANIKVASERICFG-KFTNaGQTCVAPD 248
Cdd:PRK15398 209 kHPGIALLVVTGGPAVvkaamksGKKAIGAGA-----------GNPPVVVDETADIEKAARDIVKGaSFDN-NLPCIAEK 276
|
170
....*....|....*...
gi 616915334 249 YILVHESVKDDLITALSK 266
Cdd:PRK15398 277 EVIVVDSVADELMRLMEK 294
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
103-357 |
1.98e-07 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 53.40 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 103 EPYGTVLIIAPFNYP---FqlvfeplIG----AIAAGNTAIIKPSELTPNVARVIKRLINET-FDANYIEVIEGGIEET- 173
Cdd:COG4230 679 RGRGVFVCISPWNFPlaiF-------TGqvaaALAAGNTVLAKPAEQTPLIAARAVRLLHEAgVPADVLQLLPGDGETVg 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 174 QTLIHLP-FDYVFFTGSENVGKIVYQA-ASENLVPVTL--EMGGKSPVIVDETA-------NIkVASericfgKFTNAGQ 242
Cdd:COG4230 752 AALVADPrIAGVAFTGSTETARLINRTlAARDGPIVPLiaETGGQNAMIVDSSAlpeqvvdDV-LAS------AFDSAGQ 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 243 TCVAPDYILVHESVKDDLITALSKTLREF-YGQNIQQSPDYGRIVNLKHYHRLTSLLNS--AQMNIVF-GGHSDEDER-- 316
Cdd:COG4230 825 RCSALRVLCVQEDIADRVLEMLKGAMAELrVGDPADLSTDVGPVIDAEARANLEAHIERmrAEGRLVHqLPLPEECANgt 904
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 616915334 317 YIEPTL--LDHVtndsAIMQEEIFGPILPILTYQS--LDEAIAFI 357
Cdd:COG4230 905 FVAPTLieIDSI----SDLEREVFGPVLHVVRYKAdeLDKVIDAI 945
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
103-266 |
4.67e-07 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 51.34 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 103 EPYGTVLIIAPFNYPFQ-LVFEPLIgAIAAGNTAIIKPSeltPNVARVIK---RLINETFDA-----NYIEVIEG-GIEE 172
Cdd:cd07122 94 EPVGVIAALIPSTNPTStAIFKALI-ALKTRNAIIFSPH---PRAKKCSIeaaKIMREAAVAagapeGLIQWIEEpSIEL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 173 TQTLIHLP-FDYVFFTGSENVGKIVYQAASENLvpvtlemG---GKSPVIVDETANIKVASERICFGK-FTNaGQTCVAP 247
Cdd:cd07122 170 TQELMKHPdVDLILATGGPGMVKAAYSSGKPAI-------GvgpGNVPAYIDETADIKRAVKDIILSKtFDN-GTICASE 241
|
170
....*....|....*....
gi 616915334 248 DYILVHESVKDDLITALSK 266
Cdd:cd07122 242 QSVIVDDEIYDEVRAELKR 260
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
106-384 |
1.63e-06 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 50.09 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 106 GTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTpnvARVIKRLINETFDANY-----IEVIEGGieETQTLIHL- 179
Cdd:PRK11903 150 GVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATAT---AWLTQRMVKDVVAAGIlpagaLSVVCGS--SAGLLDHLq 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 180 PFDYVFFTGSENVGKIV--YQAASENLVPVTLEMGGKSPVIV--DETAN-------IKVASERICfgkfTNAGQTCVAPD 248
Cdd:PRK11903 225 PFDVVSFTGSAETAAVLrsHPAVVQRSVRVNVEADSLNSALLgpDAAPGseafdlfVKEVVREMT----VKSGQKCTAIR 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 249 YILVHESVKDDLITALSKTLREFygqniqqspdygRIVNLKHYH-RLTSLLNSAQMN--------------IVFGGHS-- 311
Cdd:PRK11903 301 RIFVPEALYDAVAEALAARLAKT------------TVGNPRNDGvRMGPLVSRAQLAavraglaalraqaeVLFDGGGfa 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 312 --DEDER---YIEPTLLdhVTND----SAIMQEEIFGPILPILTYQSLDEAIAFIHQRPKPLSLYLFSEDENATQRVINE 382
Cdd:PRK11903 369 lvDADPAvaaCVGPTLL--GASDpdaaTAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALE 446
|
..
gi 616915334 383 LS 384
Cdd:PRK11903 447 LA 448
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
104-380 |
2.00e-06 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 49.80 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 104 PYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINE----TFDANYIEviEGGIEETQTLIHL 179
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLcgmpATDVDLIH--SDGPTMNKILLEA 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 180 PFDYVFFTGSEnvgKIVYQAASENLVPVTLEMGGKSPVIVD-ETANIKVASERICFGKFTNAGQTCVAPDYILVHES-VK 257
Cdd:cd07126 220 NPRMTLFTGSS---KVAERLALELHGKVKLEDAGFDWKILGpDVSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENwVQ 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616915334 258 DDLITALSKTLREFYGQNIQQSP----DYGRIvnLKHYHRLTSLLNSaqmNIVFGGHSDED----ERY--IEPTL----L 323
Cdd:cd07126 297 AGILDKLKALAEQRKLEDLTIGPvltwTTERI--LDHVDKLLAIPGA---KVLFGGKPLTNhsipSIYgaYEPTAvfvpL 371
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616915334 324 DHVTNDS--AIMQEEIFGPILPILTYQ--SLDEAIAFIHQRPKPLSLYLFSEDENATQRVI 380
Cdd:cd07126 372 EEIAIEEnfELVTTEVFGPFQVVTEYKdeQLPLVLEALERMHAHLTAAVVSNDIRFLQEVL 432
|
|
| |
