|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
9-456 |
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: 753.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 9 RLVKLQKAFFNEHITREIPFRLCALDRLAEALVSREKQLGEALHADLGKSAFESYATEIGFLLHEIRTIKNHLQSWARDR 88
Cdd:cd07136 2 SLVEKQRAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKPK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 89 RRPTPLFLFGSKSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECFEEEYIAV 168
Cdd:cd07136 82 RVKTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 169 TDADRETTELLLQERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCV 248
Cdd:cd07136 162 VEGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 249 APDYLMVHHKVQDKLTEYICDEITRQYGENPQQSPDYPRIVNARHFDRLSALLSHGTILCGGTSDPADRYIAPTLLTDIP 328
Cdd:cd07136 242 APDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGKIVFGGNTDRETLYIEPTILDNVT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 329 LQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTANGNLPFGGI 408
Cdd:cd07136 322 WDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYLPFGGV 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2552840633 409 GNSGMGAYHGRESFETFSYCRSIVDSSLHLYPNFKFPPYADKLKWLKR 456
Cdd:cd07136 402 GNSGMGSYHGKYSFDTFSHKKSILKKSTWFDLPLRYPPYKGKKKKLKK 449
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
10-433 |
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: 693.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 10 LVKLQKAFFNEHITREIPFRLCALDRLAEALVSREKQLGEALHADLGKSAFESYATEIGFLLHEIRTIKNHLQSWARDRR 89
Cdd:cd07087 3 LVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKPRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 90 RPTPLFLFGSKSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECFEEEYIAVT 169
Cdd:cd07087 83 VSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVAVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 170 DADRETTELLLQERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVA 249
Cdd:cd07087 163 EGGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 250 PDYLMVHHKVQDKLTEYICDEITRQYGENPQQSPDYPRIVNARHFDRLSALLSHGTILCGGTSDPADRYIAPTLLTDIPL 329
Cdd:cd07087 243 PDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGKVVIGGQVDKEERYIAPTILDDVSP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 330 QSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTANGNLPFGGIG 409
Cdd:cd07087 323 DSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGGVG 402
|
410 420
....*....|....*....|....
gi 2552840633 410 NSGMGAYHGRESFETFSYCRSIVD 433
Cdd:cd07087 403 NSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
9-431 |
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: 588.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 9 RLVKLQKAFFNEHITREIPFRLCALDRLAEALVSREKQLGEALHADLGKSAFESYATEIGFLLHEIRTIKNHLQSWARDR 88
Cdd:cd07134 2 RVFAAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKPK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 89 RRPTPLFLFGSKSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECFEEEYIAV 168
Cdd:cd07134 82 RVRTPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 169 TDADRETTELLLQERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCV 248
Cdd:cd07134 162 FEGDAEVAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 249 APDYLMVHHKVQDKLTEYICDEITRQYGENP--QQSPDYPRIVNARHFDRLSALL----SHG-TILCGGTSDPADRYIAP 321
Cdd:cd07134 242 APDYVFVHESVKDAFVEHLKAEIEKFYGKDAarKASPDLARIVNDRHFDRLKGLLddavAKGaKVEFGGQFDAAQRYIAP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 322 TLLTDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTANG 401
Cdd:cd07134 322 TVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNP 401
|
410 420 430
....*....|....*....|....*....|
gi 2552840633 402 NLPFGGIGNSGMGAYHGRESFETFSYCRSI 431
Cdd:cd07134 402 NLPFGGVNNSGIGSYHGVYGFKAFSHERAV 431
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
11-459 |
0e+00 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 575.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 11 VKLQKAFFNEHITREIPFRLCALDRLAEALVSREKQLGEALHADLGKSAFESYATEIGFLLHEIRTIKNHLQSWARDRRR 90
Cdd:PTZ00381 13 VKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEYLKPEKV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 91 PTPLFLFGSKSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECFEEEYIAVTD 170
Cdd:PTZ00381 93 DTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPSYVRVIE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 171 ADRETTELLLQERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAP 250
Cdd:PTZ00381 173 GGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 251 DYLMVHHKVQDKLTEYICDEITRQYGENPQQSPDYPRIVNARHFDRLSALL--SHGTILCGGTSDPADRYIAPTLLTDIP 328
Cdd:PTZ00381 253 DYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIkdHGGKVVYGGEVDIENKYVAPTIIVNPD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 329 LQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTANGNLPFGGI 408
Cdd:PTZ00381 333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGGV 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2552840633 409 GNSGMGAYHGRESFETFSYCRSIVDSS--LHLYPNFKFPPYAD-KLKWLKRLMK 459
Cdd:PTZ00381 413 GNSGMGAYHGKYGFDTFSHPKPVLNKStgNSFDLSLRYPPYTSfKSWVLSFLLK 466
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
10-448 |
0e+00 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 564.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 10 LVKLQKAFfNEHITREIPFRLCALDRLAEALVSREKQLGEALHADLGKSAFESYATEIGFLLHEIRTIKNHLQSWARDRR 89
Cdd:cd07132 4 VRRAREAF-SSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKPEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 90 RPTPLFLFGSKSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELI-----DECfeee 164
Cdd:cd07132 83 VKKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIpkyldKEC---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 165 YIAVTDADRETTELLlQERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCG 244
Cdd:cd07132 159 YPVVLGGVEETTELL-KQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 245 QTCVAPDYLMVHHKVQDKLTEYICDEITRQYGENPQQSPDYPRIVNARHFDRLSALLSHGTILCGGTSDPADRYIAPTLL 324
Cdd:cd07132 238 QTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 325 TDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTANGNLP 404
Cdd:cd07132 318 TDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLP 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2552840633 405 FGGIGNSGMGAYHGRESFETFSYCRSIvdsslhLYPNF--------KFPPYA 448
Cdd:cd07132 398 FGGVGNSGMGAYHGKYSFDTFSHKRSC------LVKSLnmeklnslRYPPYS 443
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
10-433 |
0e+00 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 517.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 10 LVKLQKAFFNEHITREIPFRLCALDRLAEALVSREKQLGEALHADLGKSAFESYATEIGFLLHEIRTIKNHLQSWARDRR 89
Cdd:cd07135 10 IHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKKWAKDEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 90 RPT--PLFLFGsKSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECFEEEYIA 167
Cdd:cd07135 90 VKDgpLAFMFG-KPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLDPDAFQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 168 VTDADRETTELLLQERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTC 247
Cdd:cd07135 169 VVQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQIC 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 248 VAPDYLMVHHKVQDKLTE---YICDEItrqYGENPQQSPDYPRIVNARHFDRLSALLSH--GTILCGGTSDPADRYIAPT 322
Cdd:cd07135 249 VAPDYVLVDPSVYDEFVEelkKVLDEF---YPGGANASPDYTRIVNPRHFNRLKSLLDTtkGKVVIGGEMDEATRFIPPT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 323 LLTDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTANGN 402
Cdd:cd07135 326 IVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDN 405
|
410 420 430
....*....|....*....|....*....|.
gi 2552840633 403 LPFGGIGNSGMGAYHGRESFETFSYCRSIVD 433
Cdd:cd07135 406 APFGGVGDSGYGAYHGKYGFDTFTHERTVVK 436
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
8-431 |
0e+00 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 516.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 8 TRLVKLQKAFFNE-HITREIpfRLCALDRLAEALVSREKQLGEALHADLG-KSAFESYATEIGFLLHEIRTIKNHLQSWA 85
Cdd:cd07133 2 ALLERQKAAFLANpPPSLEE--RRDRLDRLKALLLDNQDALAEAISADFGhRSRHETLLAEILPSIAGIKHARKHLKKWM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 86 RDRRRPTPLFLFGSKSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECFEEEY 165
Cdd:cd07133 80 KPSRRHVGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 166 IAVTDADRET----TELllqeRFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFL 241
Cdd:cd07133 160 VAVVTGGADVaaafSSL----PFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 242 NCGQTCVAPDYLMVHHKVQDKLTEYICDEITRQYGeNPQQSPDYPRIVNARHFDRLSALLSHG--------TILCGGTSD 313
Cdd:cd07133 236 NAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYP-TLADNPDYTSIINERHYARLQGLLEDArakgarviELNPAGEDF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 314 PADRYIAPTLLTDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACIND 393
Cdd:cd07133 315 AATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTIND 394
|
410 420 430
....*....|....*....|....*....|....*...
gi 2552840633 394 TIVQTANGNLPFGGIGNSGMGAYHGRESFETFSYCRSI 431
Cdd:cd07133 395 TLLHVAQDDLPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
9-431 |
6.66e-153 |
|
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: 441.08 E-value: 6.66e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 9 RLVKLQKAFFNEHITREIPFRLCALDRLAEALVSREKQLGEALHADLGKSAFESYATEIGFLLHEIRTIKNHLQSWARDR 88
Cdd:cd07137 3 RLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMAPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 89 RRPTPLFLFGSKSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECFEEEYIAV 168
Cdd:cd07137 83 KVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 169 TDADRETTELLLQERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNC-GQTC 247
Cdd:cd07137 163 IEGGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCNnGQAC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 248 VAPDYLMVHHKVQDKLTEYICDEITRQYGENPQQSPDYPRIVNARHFDRLSALLS----HGTILCGGTSDPADRYIAPTL 323
Cdd:cd07137 243 IAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDdpsvADKIVHGGERDEKNLYIEPTI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 324 LTDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTANGNL 403
Cdd:cd07137 323 LLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTL 402
|
410 420
....*....|....*....|....*...
gi 2552840633 404 PFGGIGNSGMGAYHGRESFETFSYCRSI 431
Cdd:cd07137 403 PFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
23-457 |
1.65e-137 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 403.72 E-value: 1.65e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 23 TREIPFRLCALDRLAEALVSREKQLGEALHADLGKSAFESYATEIGFLLHEIRTIKNHLQSWARDRRRPTPLFLFGSKSR 102
Cdd:PLN02203 24 TRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSNLKKWMAPKKAKLPLVAFPATAE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 103 IHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECFEEEYIAVTDADRETTELLLQE 182
Cdd:PLN02203 104 VVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAVKVIEGGPAVGEQLLQH 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 183 RFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVD---DDADLKATARRIVWGKFLNC-GQTCVAPDYLMVHHK 258
Cdd:PLN02203 184 KWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGSCaGQACIAIDYVLVEER 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 259 VQDKLTEYICDEITRQYGENPQQSPDYPRIVNARHFDRLSALLS----HGTILCGGTSDPADRYIAPTLLTDIPLQSPLL 334
Cdd:PLN02203 264 FAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKdprvAASIVHGGSIDEKKLFIEPTILLNPPLDSDIM 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 335 TDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTANGNLPFGGIGNSGMG 414
Cdd:PLN02203 344 TEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYACDSLPFGGVGESGFG 423
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2552840633 415 AYHGRESFETFSYCRSIVDSSLHLYPNFKFPPYAD-KLKWLKRL 457
Cdd:PLN02203 424 RYHGKYSFDTFSHEKAVLRRSLLTEFEFRYPPWNDfKLGFLRLV 467
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
9-432 |
6.65e-135 |
|
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: 395.42 E-value: 6.65e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 9 RLVKLQKAFFNEHITREIPFRLCALDRLAEALVSREKQLGEALHADLGKSAfESYATEIGFLLHEIRtiknHLQSWARDR 88
Cdd:cd07078 2 AAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPI-EEALGEVARAADTFR----YYAGLARRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 89 RRPTPLFLF-GSKSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECFE-EEYI 166
Cdd:cd07078 77 HGEVIPSPDpGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLpPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 167 AVT--DADRETTELLLQERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCG 244
Cdd:cd07078 157 NVVtgDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 245 QTCVAPDYLMVHHKVQDKLTEYICDEITRQYGENP-QQSPDYPRIVNARHFDRLSALLSH-----GTILCGGTSDPAD-- 316
Cdd:cd07078 237 QVCTAASRLLVHESIYDEFVERLVERVKALKVGNPlDPDTDMGPLISAAQLDRVLAYIEDakaegAKLLCGGKRLEGGkg 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 317 RYIAPTLLTDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIV 396
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSV 396
|
410 420 430
....*....|....*....|....*....|....*.
gi 2552840633 397 QtANGNLPFGGIGNSGMGAYHGRESFETFSYCRSIV 432
Cdd:cd07078 397 G-AEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVT 431
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
18-458 |
1.15e-115 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 348.19 E-value: 1.15e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 18 FNEHITREIPFRLCALDRLAEALVSREKQLGEALHADLGKSAFESYATEIGFLLHEIRTIKNHLQSWARDRRRPTPLFLF 97
Cdd:PLN02174 23 FDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEKAKTSLTTF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 98 GSKSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECFEEEYIAVTDADRETTE 177
Cdd:PLN02174 103 PASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVEGAVTETT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 178 LLLQERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKF-LNCGQTCVAPDYLMVH 256
Cdd:PLN02174 183 ALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 257 HKVQDKLTEYICDEITRQYGENPQQSPDYPRIVNARHFDRLSALLSH----GTILCGGTSDPADRYIAPTLLTDIPLQSP 332
Cdd:PLN02174 263 KEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDEkevsDKIVYGGEKDRENLKIAPTILLDVPLDSL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 333 LLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTANGNLPFGGIGNSG 412
Cdd:PLN02174 343 IMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVGESG 422
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2552840633 413 MGAYHGRESFETFSYCRSIVDSSLHLYPNFKFPPYA-DKLKWLKRLM 458
Cdd:PLN02174 423 MGAYHGKFSFDAFSHKKAVLYRSLFGDSAVRYPPYSrGKLRLLKALV 469
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
33-432 |
2.04e-111 |
|
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: 336.71 E-value: 2.04e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 33 LDRLAEALVSREKQLGEALHADLGKSAFESYAtEIGFLLHEIRtiknHLQSWARDRRRPT-PLFLFGSKSRIHYEPYGCA 111
Cdd:COG1012 71 LLRAADLLEERREELAALLTLETGKPLAEARG-EVDRAADFLR----YYAGEARRLYGETiPSDAPGTRAYVRREPLGVV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 112 LIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEcfeeeyiA---------VTDADRETTELLLQ- 181
Cdd:COG1012 146 GAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEE-------AglpagvlnvVTGDGSEVGAALVAh 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 182 ERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQD 261
Cdd:COG1012 219 PDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYD 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 262 KLTEYICDEITR-QYGeNP-QQSPDYPRIVNARHFDRLSALLSHG-----TILCGGTSDPADR--YIAPTLLTDIPLQSP 332
Cdd:COG1012 299 EFVERLVAAAKAlKVG-DPlDPGTDMGPLISEAQLERVLAYIEDAvaegaELLTGGRRPDGEGgyFVEPTVLADVTPDMR 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 333 LLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVqTANGNLPFGGIGNSG 412
Cdd:COG1012 378 IAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTT-GAVPQAPFGGVKQSG 456
|
410 420
....*....|....*....|
gi 2552840633 413 MGAYHGRESFETFSYCRSIV 432
Cdd:COG1012 457 IGREGGREGLEEYTETKTVT 476
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
14-432 |
2.12e-108 |
|
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: 325.34 E-value: 2.12e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 14 QKAFFNEHiTREIPFRLCALDRLAEALVSREKQLGEALHADLGKSAfESYATEIGFLLHEIRTIKNHLQSWARDRRRPTP 93
Cdd:cd06534 4 RAAFKAWA-ALPPAERAAILRKIADLLEERREELAALETLETGKPI-EEALGEVARAIDTFRYAAGLADKLGGPELPSPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 94 LflfGSKSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECFE-EEYIAV--TD 170
Cdd:cd06534 82 P---GGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLpPGVVNVvpGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 171 ADRETTELLLQERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAP 250
Cdd:cd06534 159 GDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 251 DYLMVHHKVQDKLTEyicdeitrqygenpqqspdypRIVnarhfdrlsallshgtilcggtsdpadryiapTLLTDIPLQ 330
Cdd:cd06534 239 SRLLVHESIYDEFVE---------------------KLV--------------------------------TVLVDVDPD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 331 SPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQtANGNLPFGGIGN 410
Cdd:cd06534 266 MPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIG-VGPEAPFGGVKN 344
|
410 420
....*....|....*....|..
gi 2552840633 411 SGMGAYHGRESFETFSYCRSIV 432
Cdd:cd06534 345 SGIGREGGPYGLEEYTRTKTVV 366
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
29-433 |
6.02e-108 |
|
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: 327.26 E-value: 6.02e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 29 RLCALDRLAEALVSREKQLGEALHADLGKSAFEsyateigfLLHEIRTIKNHLQSWAR-------DRRRPTPLFLFGSKS 101
Cdd:cd07099 42 RAQRLLRWKRALADHADELAELLHAETGKPRAD--------AGLEVLLALEAIDWAARnaprvlaPRKVPTGLLMPNKKA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 102 RIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVTDADRETTELLL 180
Cdd:cd07099 114 TVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAgPPQGVLQVVTGDGATGAALI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 181 QERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQ 260
Cdd:cd07099 194 DAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVY 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 261 DKLTEYICdEITRQ--YGENPQQSPDYPRIVNARHFDRLS-----ALLSHGTILCGGTSDPAD-RYIAPTLLTDIPLQSP 332
Cdd:cd07099 274 DEFVARLV-AKARAlrPGADDIGDADIGPMTTARQLDIVRrhvddAVAKGAKALTGGARSNGGgPFYEPTVLTDVPHDMD 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 333 LLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTANGNLPFGGIGNSG 412
Cdd:cd07099 353 VMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSG 432
|
410 420
....*....|....*....|.
gi 2552840633 413 MGAYHGRESFETFSYCRSIVD 433
Cdd:cd07099 433 GGRRHGAEGLREFCRPKAIAR 453
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
33-431 |
8.45e-97 |
|
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: 298.68 E-value: 8.45e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 33 LDRLAEALVSREKQLGEALHADLGKSAFESyateigflLHEIRTIKNHLQSWARDRRRPTPLFLF---GSKSRIHYEPYG 109
Cdd:pfam00171 57 LRKAADLLEERKDELAELETLENGKPLAEA--------RGEVDRAIDVLRYYAGLARRLDGETLPsdpGRLAYTRREPLG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 110 CALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYI-AVTDADRETTELLLQ-ERFDY 186
Cdd:pfam00171 129 VVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAgLPAGVLnVVTGSGAEVGEALVEhPDVRK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 187 IFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQDKLTEY 266
Cdd:pfam00171 209 VSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEK 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 267 ICDEITR-QYG----ENPQQSPdyprIVNARHFDRLSALLSHG-----TILCGGTSDPAD-RYIAPTLLTDIPLQSPLLT 335
Cdd:pfam00171 289 LVEAAKKlKVGdpldPDTDMGP----LISKAQLERVLKYVEDAkeegaKLLTGGEAGLDNgYFVEPTVLANVTPDMRIAQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 336 DEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTANgNLPFGGIGNSGMGA 415
Cdd:pfam00171 365 EEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDAD-GLPFGGFKQSGFGR 443
|
410
....*....|....*.
gi 2552840633 416 YHGRESFETFSYCRSI 431
Cdd:pfam00171 444 EGGPYGLEEYTEVKTV 459
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
54-432 |
7.68e-79 |
|
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: 252.61 E-value: 7.68e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 54 DLGKSAFESYATEIGFLLHEIRTIKNHLQSWARDRRRPTPLFLFGSKSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIA 133
Cdd:cd07098 67 DTGKTMVDASLGEILVTCEKIRWTLKHGEKALRPESRPGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALF 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 134 AGNCAIVKPSGEAPRTAAALQELIDECfeeeyIAVTDADR----------ETTELLLQE-RFDYIFYTGGVEYGRHVMQA 202
Cdd:cd07098 147 AGNAIVVKVSEQVAWSSGFFLSIIREC-----LAACGHDPdlvqlvtclpETAEALTSHpVIDHITFIGSPPVGKKVMAA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 203 ASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQDKLTEYICDEITRQYGENPQQS 282
Cdd:cd07098 222 AAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 283 P-DYPRIVNARHFDRLSALL-----SHGTILCGG-----TSDPADRYIAPTLLTDIPLQSPLLTDEIFGPILPVLPFDDI 351
Cdd:cd07098 302 DvDVGAMISPARFDRLEELVadaveKGARLLAGGkryphPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDD 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 352 DDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTANGNLPFGGIGNSGMGAYHGRESFETFSYCRSI 431
Cdd:cd07098 382 EEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSV 461
|
.
gi 2552840633 432 V 432
Cdd:cd07098 462 T 462
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
32-431 |
2.33e-73 |
|
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: 237.81 E-value: 2.33e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 32 ALDRLAEALVSREKQLGEALHADLGKSAFESYAtEIGFLLHEIR-----TIKNHLQSWARDRRrptplflfgskSRIHYE 106
Cdd:cd07106 46 ALLAIADAIEANAEELARLLTLEQGKPLAEAQF-EVGGAVAWLRytaslDLPDEVIEDDDTRR-----------VELRRK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 107 PYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECFEEEYI-AVTDADRETTELLLQERFD 185
Cdd:cd07106 114 PLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEVLPPGVLnVVSGGDELGPALTSHPDIR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 186 YIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQDKLTE 265
Cdd:cd07106 194 KISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 266 YICDEITRQY-GENPQQSPDYPRIVNARHFDRLSALL-----SHGTILCGGTSDPADRY-IAPTLLTDIPLQSPLLTDEI 338
Cdd:cd07106 274 ALVALAKAAVvGDGLDPGTTLGPVQNKMQYDKVKELVedakaKGAKVLAGGEPLDGPGYfIPPTIVDDPPEGSRIVDEEQ 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 339 FGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDtiVQTANGNLPFGGIGNSGMGAYHG 418
Cdd:cd07106 354 FGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWINT--HGALDPDAPFGGHKQSGIGVEFG 431
|
410
....*....|...
gi 2552840633 419 RESFETFSYCRSI 431
Cdd:cd07106 432 IEGLKEYTQTQVI 444
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
28-432 |
6.52e-73 |
|
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: 236.76 E-value: 6.52e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 28 FRLCALDRLAEALVSREKQLGEALHADLGKSAFESYATEIGFLLHEIRTIKNHLQSWARDRRRP-TPLFLFGSKSRIHYE 106
Cdd:cd07089 43 ERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQVDGPIGHLRYFADLADSFPWEFDLPvPALRGGPGRRVVRRE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 107 PYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEcfeeeyiA---------VTDADRETTE 177
Cdd:cd07089 123 PVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAE-------TdlpagvvnvVTGSDNAVGE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 178 LLLQE-RFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVH 256
Cdd:cd07089 196 ALTTDpRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVP 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 257 HKVQDKLTEyicdEITRQYGENPQQSPDYPR-----IVNARHFDRLSALLSHG-----TILCGG-TSDPADR--YIAPTL 323
Cdd:cd07089 276 RSRYDEVVE----ALAAAFEALPVGDPADPGtvmgpLISAAQRDRVEGYIARGrdegaRLVTGGgRPAGLDKgfYVEPTL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 324 LTDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTANGnl 403
Cdd:cd07089 352 FADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINGGGGYGPDA-- 429
|
410 420
....*....|....*....|....*....
gi 2552840633 404 PFGGIGNSGMGAYHGRESFETFSYCRSIV 432
Cdd:cd07089 430 PFGGYKQSGLGRENGIEGLEEFLETKSIA 458
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
29-431 |
3.96e-71 |
|
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: 231.83 E-value: 3.96e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 29 RLCALDRLAEALVSREKQLGEALHADLGKSAFESYATEIGFLLHEIRtiknHLQSWARDRrrPTPL---FLFGSKSRIHY 105
Cdd:cd07092 43 RSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDELPGAVDNFR----FFAGAARTL--EGPAageYLPGHTSMIRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 106 EPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECFEEEYIAVTDADRETT--ELLLQER 183
Cdd:cd07092 117 EPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGVVNVVCGGGASAgdALVAHPR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 184 FDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQDKL 263
Cdd:cd07092 197 VRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 264 TEYICDEI-TRQYGENPQQSPDYPRIVNARHFDRLSALLS----HGTILCGGTSDPADRY-IAPTLLTDIPLQSPLLTDE 337
Cdd:cd07092 277 VAALVEAVsAIRVGDPDDEDTEMGPLNSAAQRERVAGFVErapaHARVLTGGRRAEGPGYfYEPTVVAGVAQDDEIVQEE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 338 IFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTAngNLPFGGIGNSGMGAYH 417
Cdd:cd07092 357 IFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNTHIPLAA--EMPHGGFKQSGYGKDL 434
|
410
....*....|....
gi 2552840633 418 GRESFETFSYCRSI 431
Cdd:cd07092 435 SIYALEDYTRIKHV 448
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
104-429 |
2.97e-70 |
|
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: 229.81 E-value: 2.97e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 104 HYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDE------CFEeeyiAVTDADRETTE 177
Cdd:cd07109 114 VREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEaglpagALN----VVTGLGAEAGA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 178 LLLQER-FDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVH 256
Cdd:cd07109 190 ALVAHPgVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVH 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 257 HKVQDKLTEYIcDEITRQYGENP-QQSPDYPRIVNARHFDRLSALLSHGT-----ILCGGT--SDPADR--YIAPTLLTD 326
Cdd:cd07109 270 RSIYDEVLERL-VERFRALRVGPgLEDPDLGPLISAKQLDRVEGFVARARargarIVAGGRiaEGAPAGgyFVAPTLLDD 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 327 IPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDtiVQTANG-NLPF 405
Cdd:cd07109 349 VPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNN--YGAGGGiELPF 426
|
330 340
....*....|....*....|....*.
gi 2552840633 406 GGIGNSGmgayHGRE-SFETF-SYCR 429
Cdd:cd07109 427 GGVKKSG----HGREkGLEALyNYTQ 448
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
33-425 |
4.13e-69 |
|
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: 226.54 E-value: 4.13e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 33 LDRLAEALVSREKQLGEALHADLGKSAFESYAteigfllhEIRTIKNHLQSWARDRRR--------PTPlflfGSKSRIH 104
Cdd:cd07103 47 LRRWADLIRERAEDLARLLTLEQGKPLAEARG--------EVDYAASFLEWFAEEARRiygrtipsPAP----GKRILVI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 105 YEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAV--TDADRETTELLLQ 181
Cdd:cd07103 115 KQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEAgLPAGVLNVvtGSPAEIGEALCAS 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 182 ERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQD 261
Cdd:cd07103 195 PRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYD 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 262 KLTEYICDEITR-QYG----ENPQQSPdyprIVNARHFDRLSAL----LSHG-TILCGGTSDPAD-RYIAPTLLTDIPLQ 330
Cdd:cd07103 275 EFVEKLVERVKKlKVGngldEGTDMGP----LINERAVEKVEALvedaVAKGaKVLTGGKRLGLGgYFYEPTVLTDVTDD 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 331 SPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTAngNLPFGGIGN 410
Cdd:cd07103 351 MLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLISDA--EAPFGGVKE 428
|
410
....*....|....*
gi 2552840633 411 SGMGAYHGRESFETF 425
Cdd:cd07103 429 SGLGREGGKEGLEEY 443
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
29-432 |
7.84e-68 |
|
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: 223.99 E-value: 7.84e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 29 RLCALDRLAEALVSREKQLGEALHADLGKSAFESYATEIGFLLHEIRTIKNHLQSWARDRRRPTPlflFGSKSRIHYEPY 108
Cdd:cd07139 62 RAAVLRRLADALEARADELARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEERRPGS---GGGHVLVRREPV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 109 GCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVTDADRETTELL-LQERFDY 186
Cdd:cd07139 139 GVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAgLPPGVVNVVPADREVGEYLvRHPGVDK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 187 IFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQDKLTEY 266
Cdd:cd07139 219 VSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 267 ICDEITRQYGENP-----QQSPdyprIVNARHFDRLSALLSHG-----TILCGGtSDPA--DR--YIAPTLLTDIPLQSP 332
Cdd:cd07139 299 LAAAVAALKVGDPldpatQIGP----LASARQRERVEGYIAKGraegaRLVTGG-GRPAglDRgwFVEPTLFADVDNDMR 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 333 LLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTivqTANGNLPFGGIGNSG 412
Cdd:cd07139 374 IAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF---RLDFGAPFGGFKQSG 450
|
410 420
....*....|....*....|
gi 2552840633 413 MGAYHGRESFETFSYCRSIV 432
Cdd:cd07139 451 IGREGGPEGLDAYLETKSIY 470
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
98-427 |
5.77e-66 |
|
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: 217.78 E-value: 5.77e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 98 GSKSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSgeaPRTAAALQELIDECFEEE-------YIAVTD 170
Cdd:cd07104 89 GKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPD---SRTPVTGGLLIAEIFEEAglpkgvlNVVPGG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 171 ADRETTELLLQERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAP 250
Cdd:cd07104 166 GSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAA 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 251 DYLMVHHKVQDKLTEYICDEITR-QYGeNP-----QQSPdyprIVNARHFDRLSALLSH-----GTILCGGTSDpaDRYI 319
Cdd:cd07104 246 GRILVHESVYDEFVEKLVAKAKAlPVG-DPrdpdtVIGP----LINERQVDRVHAIVEDavaagARLLTGGTYE--GLFY 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 320 APTLLTDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDtivQTA 399
Cdd:cd07104 319 QPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIND---QTV 395
|
330 340 350
....*....|....*....|....*....|
gi 2552840633 400 NG--NLPFGGIGNSGMGAYHGRESFETFSY 427
Cdd:cd07104 396 NDepHVPFGGVKASGGGRFGGPASLEEFTE 425
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
29-425 |
1.95e-65 |
|
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: 217.37 E-value: 1.95e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 29 RLCALDRLAEALVSREKQLGEALHADLGksAFESYATE------IGFLLHEIRTIKNHlqSWARDRrrptplflfgSKSR 102
Cdd:cd07138 60 RAALLERIAEAYEARADELAQAITLEMG--APITLARAaqvglgIGHLRAAADALKDF--EFEERR----------GNSL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 103 IHYEPYG-CALIiAPWNYPL-QLALSpLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC------FEeeyiAVTDADRE 174
Cdd:cd07138 126 VVREPIGvCGLI-TPWNWPLnQIVLK-VAPALAAGCTVVLKPSEVAPLSAIILAEILDEAglpagvFN----LVNGDGPV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 175 TTELLL-QERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYL 253
Cdd:cd07138 200 VGEALSaHPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRM 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 254 MVHHKVQDKLTEYICDEITrqygenpQQSPDYPR--------IVNARHFDRLSALLSHG-----TILCGGTSDPA--DR- 317
Cdd:cd07138 280 LVPRSRYAEAEEIAAAAAE-------AYVVGDPRdpattlgpLASAAQFDRVQGYIQKGieegaRLVAGGPGRPEglERg 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 318 -YIAPTLLTDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTiv 396
Cdd:cd07138 353 yFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGA-- 430
|
410 420
....*....|....*....|....*....
gi 2552840633 397 qTANGNLPFGGIGNSGMGAYHGRESFETF 425
Cdd:cd07138 431 -AFNPGAPFGGYKQSGNGREWGRYGLEEF 458
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
101-426 |
1.71e-64 |
|
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: 214.74 E-value: 1.71e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 101 SRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEcfeeeyiA---------VTDA 171
Cdd:cd07093 111 NYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANE-------AglppgvvnvVHGF 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 172 DRETTELLLQE-RFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAP 250
Cdd:cd07093 184 GPEAGAALVAHpDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 251 DYLMVHHKVQDKLTEYICDEITR-QYGENPQQSPDYPRIVNARHFDRL-----SALLSHGTILCGGTSDPADR-----YI 319
Cdd:cd07093 264 SRILVQRSIYDEFLERFVERAKAlKVGDPLDPDTEVGPLISKEHLEKVlgyveLARAEGATILTGGGRPELPDleggyFV 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 320 APTLLTDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQta 399
Cdd:cd07093 344 EPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNCWLVR-- 421
|
330 340
....*....|....*....|....*..
gi 2552840633 400 NGNLPFGGIGNSGMGAYHGRESFETFS 426
Cdd:cd07093 422 DLRTPFGGVKASGIGREGGDYSLEFYT 448
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
33-425 |
1.77e-64 |
|
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: 215.21 E-value: 1.77e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 33 LDRLAEALVSREKQLGEALHADLGKSAFESYaTEIGFLLHEIRtiknHLQSWAR---------DRRRPTPLflfgsksrI 103
Cdd:cd07088 63 LRKLADLIRENADELAKLIVEEQGKTLSLAR-VEVEFTADYID----YMAEWARriegeiipsDRPNENIF--------I 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 104 HYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVTDADRETT--ELLL 180
Cdd:cd07088 130 FKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAgLPAGVLNIVTGRGSVVgdALVA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 181 QERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQ 260
Cdd:cd07088 210 HPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIY 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 261 DKLTEYICDEI-TRQYGENPQQSPDYPRIVNARHFDRLSALL-----SHGTILCGGTSDPADR--YIAPTLLTDIPLQSP 332
Cdd:cd07088 290 DEFMEKLVEKMkAVKVGDPFDAATDMGPLVNEAALDKVEEMVeraveAGATLLTGGKRPEGEKgyFYEPTVLTNVRQDME 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 333 LLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTANGnlpF-GGIGNS 411
Cdd:cd07088 370 IVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQG---FhAGWKKS 446
|
410
....*....|....
gi 2552840633 412 GMGAYHGRESFETF 425
Cdd:cd07088 447 GLGGADGKHGLEEY 460
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
29-420 |
5.03e-64 |
|
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: 213.32 E-value: 5.03e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 29 RLCALDRLAEALVSREKQLGEALHADLGK---SAFESYATEIGFLLHEIRTIKNHLqswaRDRRRPTPLFLFgSKSRIHY 105
Cdd:cd07101 42 RAAVFLRFHDLVLERRDELLDLIQLETGKarrHAFEEVLDVAIVARYYARRAERLL----KPRRRRGAIPVL-TRTTVNR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 106 EPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECF--EEEYIAVTDADRETTELLLqER 183
Cdd:cd07101 117 RPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGlpRDLWQVVTGPGSEVGGAIV-DN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 184 FDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHhkvqdkl 263
Cdd:cd07101 196 ADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVH------- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 264 tEYICDEITRQYGENPQQ---------SPDYPRIVNARHFDRLS-----ALLSHGTILCGGTSDP--ADRYIAPTLLTDI 327
Cdd:cd07101 269 -ESVYDEFVRRFVARTRAlrlgaaldyGPDMGSLISQAQLDRVTahvddAVAKGATVLAGGRARPdlGPYFYEPTVLTGV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 328 PLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQT-ANGNLPFG 406
Cdd:cd07101 348 TEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEGYAAAwASIDAPMG 427
|
410
....*....|....
gi 2552840633 407 GIGNSGMGAYHGRE 420
Cdd:cd07101 428 GMKDSGLGRRHGAE 441
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
106-432 |
5.79e-62 |
|
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: 208.17 E-value: 5.79e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 106 EPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVTDADRETTELLLQE-- 182
Cdd:cd07114 118 EPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAgFPPGVVNVVTGFGPETGEALVEhp 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 183 RFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQDK 262
Cdd:cd07114 198 LVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 263 LTEYICdEITRQ--YGenpqqSPDYPR-----IVNARHFDRLSALLSH-----GTILCGG-----TSDPADRYIAPTLLT 325
Cdd:cd07114 278 FVERLV-ARARAirVG-----DPLDPEtqmgpLATERQLEKVERYVARareegARVLTGGerpsgADLGAGYFFEPTILA 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 326 DIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDtiVQTANGNLPF 405
Cdd:cd07114 352 DVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNT--YRALSPSSPF 429
|
330 340
....*....|....*....|....*..
gi 2552840633 406 GGIGNSGMGAYHGRESFETFSYCRSIV 432
Cdd:cd07114 430 GGFKDSGIGRENGIEAIREYTQTKSVW 456
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
98-431 |
6.69e-62 |
|
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: 207.43 E-value: 6.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 98 GSKSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTaaalQELIDECFEEE----------YIA 167
Cdd:cd07105 89 GTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRT----HWLIGRVFHEAglpkgvlnvvTHS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 168 VTDAdRETTELLLQE---RFdyIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCG 244
Cdd:cd07105 165 PEDA-PEVVEALIAHpavRK--VNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSG 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 245 QTCVAPDYLMVHHKVQDKLTEYICDEItrqygENPQQSPDY-PRIVNARHFDRLSALLSH-----GTILCGGTSD--PAD 316
Cdd:cd07105 242 QICMSTERIIVHESIADEFVEKLKAAA-----EKLFAGPVVlGSLVSAAAADRVKELVDDalskgAKLVVGGLADesPSG 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 317 RYIAPTLLTDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIV 396
Cdd:cd07105 317 TSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTV 396
|
330 340 350
....*....|....*....|....*....|....*
gi 2552840633 397 QTANGnLPFGGIGNSGMGAYHGRESFETFSYCRSI 431
Cdd:cd07105 397 HDEPT-LPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
29-459 |
6.51e-61 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 207.04 E-value: 6.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 29 RLCALDRLAEALVSREKQLGEALHADLGKS---AFESYATEIGFLLHEIRTIKNHLqswaRDRRRPTPLFLFgSKSRIHY 105
Cdd:PRK09407 78 RAAVLLRFHDLVLENREELLDLVQLETGKArrhAFEEVLDVALTARYYARRAPKLL----APRRRAGALPVL-TKTTELR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 106 EPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVTDADRETTELLLQERF 184
Cdd:PRK09407 153 QPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAgLPRDLWQVVTGPGPVVGTALVDNA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 185 DYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHhkvqdklt 264
Cdd:PRK09407 233 DYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVH-------- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 265 EYICDEITRQYGENPQQ---------SPDYPRIVNARHFDRLSA----LLSHG-TILCGGTSDP--ADRYIAPTLLTDIP 328
Cdd:PRK09407 305 ESIYDEFVRAFVAAVRAmrlgagydySADMGSLISEAQLETVSAhvddAVAKGaTVLAGGKARPdlGPLFYEPTVLTGVT 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 329 LQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQT-ANGNLPFGG 407
Cdd:PRK09407 385 PDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAwGSVDAPMGG 464
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2552840633 408 IGNSGMGAYHGRESFETFSYCRSIVDSSLHlypNFKFPPYADKLKWLK------RLMK 459
Cdd:PRK09407 465 MKDSGLGRRHGAEGLLKYTESQTIATQRVL---PLAPPPGMPYEKYAKlmltglRLMK 519
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
35-431 |
1.30e-60 |
|
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: 204.49 E-value: 1.30e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 35 RLAEALVSREKQLGEALhADLGKSAFESYATEIGFLLHEIRTIknhlqswARDRRRPT----PLFLFGSKSRIHYEPYGC 110
Cdd:cd07150 51 KAAEIMERRADDLIDLL-IDEGGSTYGKAWFETTFTPELLRAA-------AGECRRVRgetlPSDSPGTVSMSVRRPLGV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 111 ALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVTDADRETT--ELLLQERFDYI 187
Cdd:cd07150 123 VAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAgLPKGVFNVVTGGGAEVgdELVDDPRVRMV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 188 FYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQDKLTEYI 267
Cdd:cd07150 203 TFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKF 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 268 CDEITRQYGENPQQsPDY---PRIvNARHFDRL-----SALLSHGTILCGGTSDpaDRYIAPTLLTDIPLQSPLLTDEIF 339
Cdd:cd07150 283 VARASKLKVGDPRD-PDTvigPLI-SPRQVERIkrqveDAVAKGAKLLTGGKYD--GNFYQPTVLTDVTPDMRIFREETF 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 340 GPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTaNGNLPFGGIGNSGMGAYHGR 419
Cdd:cd07150 359 GPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHINDPTILD-EAHVPFGGVKASGFGREGGE 437
|
410
....*....|..
gi 2552840633 420 ESFETFSYCRSI 431
Cdd:cd07150 438 WSMEEFTELKWI 449
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
34-420 |
1.02e-59 |
|
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: 201.53 E-value: 1.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 34 DRLAEaLVSRE--KQLGEALhADLGKSA--FESYAteigfllheirtikNHLQSWARDRRRPTPlflfGSKSRIHYEPYG 109
Cdd:cd07100 39 DELAR-LITLEmgKPIAEAR-AEVEKCAwiCRYYA--------------ENAEAFLADEPIETD----AGKAYVRYEPLG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 110 CALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVTDADRETTELLLQ-ERFDYI 187
Cdd:cd07100 99 VVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAgFPEGVFQNLLIDSDQVEAIIAdPRVRGV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 188 FYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQD----KL 263
Cdd:cd07100 179 TLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDefleKF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 264 TEYIC--------DEITrQYGenPQQSPDyprivnARhfDRLSAL----LSHG-TILCGGtsDPADR---YIAPTLLTDI 327
Cdd:cd07100 259 VEAMAalkvgdpmDEDT-DLG--PLARKD------LR--DELHEQveeaVAAGaTLLLGG--KRPDGpgaFYPPTVLTDV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 328 PLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDtiVQTANGNLPFGG 407
Cdd:cd07100 326 TPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFING--MVKSDPRLPFGG 403
|
410
....*....|...
gi 2552840633 408 IGNSGmgayHGRE 420
Cdd:cd07100 404 VKRSG----YGRE 412
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
106-431 |
3.67e-59 |
|
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: 200.74 E-value: 3.67e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 106 EPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELideCFEEEYIA-----VTDADRETTE-LL 179
Cdd:cd07115 116 EPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAEL---MAEAGFPAgvlnvVTGFGEVAGAaLV 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 180 LQERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKV 259
Cdd:cd07115 193 EHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESI 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 260 QDKLTEYICDEITRQYGENP-----QQSPdyprIVNARHFDRLSALLSHG-----TILCGGTSDPADR-YIAPTLLTDIP 328
Cdd:cd07115 273 YDEFLERFTSLARSLRPGDPldpktQMGP----LVSQAQFDRVLDYVDVGreegaRLLTGGKRPGARGfFVEPTIFAAVP 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 329 LQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINdTIVQTANGnLPFGGI 408
Cdd:cd07115 349 PEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWIN-TYNRFDPG-SPFGGY 426
|
330 340
....*....|....*....|...
gi 2552840633 409 GNSGMGAYHGRESFETFSYCRSI 431
Cdd:cd07115 427 KQSGFGREMGREALDEYTEVKSV 449
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
98-414 |
3.66e-58 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 198.59 E-value: 3.66e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 98 GSKSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECFEEEYI-AVTDADRETT 176
Cdd:PRK13473 129 GHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLnVVTGRGATVG 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 177 ELLL-QERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMV 255
Cdd:PRK13473 209 DALVgHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYA 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 256 HHKVQDKLTEYICDEI-TRQYGENPQQSPDYPRIVNARHFDRLSAL------LSHGTILCGGtSDPADR--YIAPTLLTD 326
Cdd:PRK13473 289 QRGIYDDLVAKLAAAVaTLKVGDPDDEDTELGPLISAAHRDRVAGFverakaLGHIRVVTGG-EAPDGKgyYYEPTLLAG 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 327 IPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTAngNLPFG 406
Cdd:PRK13473 368 ARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVS--EMPHG 445
|
....*...
gi 2552840633 407 GIGNSGMG 414
Cdd:PRK13473 446 GQKQSGYG 453
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
35-431 |
2.55e-57 |
|
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: 195.93 E-value: 2.55e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 35 RLAEALVSREKQLGEALHADLGKSAFEsYATEIGFLLHEIR-TIKNHLQSWARDRRRPTPLFlfgsKSRIHYEPYGCALI 113
Cdd:cd07102 48 RAVELLAANTDEIAEELTWQMGRPIAQ-AGGEIRGMLERARyMISIAEEALADIRVPEKDGF----ERYIRREPLGVVLI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 114 IAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVTDADRETTELLLQE-RFDYIFYTG 191
Cdd:cd07102 123 IAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAgLPEGVFQVLHLSHETSAALIADpRIDHVSFTG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 192 GVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQDKLTEYiCDEI 271
Cdd:cd07102 203 SVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEA-FVAV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 272 TRQY--GENPQQSPDYPRIVNARHFDRL-----SALLSHGTILCGGTSDPADR----YIAPTLLTDIPLQSPLLTDEIFG 340
Cdd:cd07102 282 VKGYklGDPLDPSTTLGPVVSARAADFVraqiaDAIAKGARALIDGALFPEDKaggaYLAPTVLTNVDHSMRVMREETFG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 341 PILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACIN--DTIvqtaNGNLPFGGIGNSGMGAYHG 418
Cdd:cd07102 362 PVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNrcDYL----DPALAWTGVKDSGRGVTLS 437
|
410
....*....|...
gi 2552840633 419 RESFETFSYCRSI 431
Cdd:cd07102 438 RLGYDQLTRPKSY 450
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
107-418 |
4.36e-57 |
|
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: 194.82 E-value: 4.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 107 PYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPsgeAPRTAAALQELIDECFEEE-----YIAVTDADRETTELLLQ 181
Cdd:cd07152 110 PLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKP---DPRTPVSGGVVIARLFEEAglpagVLHVLPGGADAGEALVE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 182 E-RFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQ 260
Cdd:cd07152 187 DpNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 261 DKLTEYICDEITRQYGENPQQSP-DYPRIVNARHFDRLSALLSH-----GTILCGGTSDpaDRYIAPTLLTDIPLQSPLL 334
Cdd:cd07152 267 DAYTAKLAAKAKHLPVGDPATGQvALGPLINARQLDRVHAIVDDsvaagARLEAGGTYD--GLFYRPTVLSGVKPGMPAF 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 335 TDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDtivQTANG--NLPFGGIGNSG 412
Cdd:cd07152 345 DEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHIND---QTVNDepHNPFGGMGASG 421
|
....*.
gi 2552840633 413 MGAYHG 418
Cdd:cd07152 422 NGSRFG 427
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
98-426 |
2.16e-56 |
|
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: 193.67 E-value: 2.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 98 GSKSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALqelIDECFEEEYI------AVTDA 171
Cdd:cd07151 121 GKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGLL---LAKIFEEAGLpkgvlnVVVGA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 172 DRETTELLLQERF-DYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAP 250
Cdd:cd07151 198 GSEIGDAFVEHPVpRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAI 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 251 DYLMVHHKVQDKLTEYICDEITR-QYGEnpQQSPDY---PrIVNARHFDRLSALLSH-----GTILCGGtsDPADRYIAP 321
Cdd:cd07151 278 NRIIVHEDVYDEFVEKFVERVKAlPYGD--PSDPDTvvgP-LINESQVDGLLDKIEQaveegATLLVGG--EAEGNVLEP 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 322 TLLTDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDtivQTANG 401
Cdd:cd07151 353 TVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHIND---QPVND 429
|
330 340
....*....|....*....|....*..
gi 2552840633 402 --NLPFGGIGNSGMGAYHGRESFETFS 426
Cdd:cd07151 430 epHVPFGGEKNSGLGRFNGEWALEEFT 456
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
106-423 |
6.83e-56 |
|
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: 192.19 E-value: 6.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 106 EPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECFEEEYIAV-TDADRETTELLLQER- 183
Cdd:cd07108 116 EPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQVLPAGVLNViTGYGEECGAALVDHPd 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 184 FDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWG-KFLNCGQTCVAPDYLMVHHKVQDK 262
Cdd:cd07108 196 VDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDA 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 263 LTEYICDEITRQYGENP-QQSPDYPRIVNARHFDRLSALLSHG------TILCGGTSDPADR-----YIAPTLLTDIPLQ 330
Cdd:cd07108 276 FLEKLVAKLSKLKIGDPlDEATDIGAIISEKQFAKVCGYIDLGlstsgaTVLRGGPLPGEGPladgfFVQPTIFSGVDNE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 331 SPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTAngNLPFGGIGN 410
Cdd:cd07108 356 WRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQP--GQSYGGFKQ 433
|
330
....*....|....
gi 2552840633 411 SGMgayhGRE-SFE 423
Cdd:cd07108 434 SGL----GREaSLE 443
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
98-420 |
1.47e-55 |
|
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: 191.27 E-value: 1.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 98 GSKSRIHY---EPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVTDADR 173
Cdd:cd07149 111 GGEGRIGFtirEPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEAgLPKGALNVVTGSG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 174 ET--TELLLQERFDYIFYTGGVEYGRHVMQAASrhLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPD 251
Cdd:cd07149 191 ETvgDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQ 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 252 YLMVHHKVQDKLTEYICDEITRQYGENPQQ-----SPdyprIVNARHFDRL-----SALLSHGTILCGGTSDpaDRYIAP 321
Cdd:cd07149 269 RIFVHEDIYDEFLERFVAATKKLVVGDPLDedtdvGP----MISEAEAERIeewveEAVEGGARLLTGGKRD--GAILEP 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 322 TLLTDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTANG 401
Cdd:cd07149 343 TVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINDSSTFRVDH 422
|
330
....*....|....*....
gi 2552840633 402 nLPFGGIGNSGMgayhGRE 420
Cdd:cd07149 423 -MPYGGVKESGT----GRE 436
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
90-420 |
2.26e-55 |
|
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: 190.64 E-value: 2.26e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 90 RPTPLFLFGSKSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDE-CFEEEYIAV 168
Cdd:cd07110 103 RAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIAAEaGLPPGVLNV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 169 T--DADRETTELLLQERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQT 246
Cdd:cd07110 183 VtgTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQI 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 247 CVAPDYLMVHHKVQDKLTEYICDEITR-----QYGENPQQSPdyprIVNARHFDRLSALLSHG-----TILCGGtSDPAD 316
Cdd:cd07110 263 CSATSRLLVHESIADAFLERLATAAEAirvgdPLEEGVRLGP----LVSQAQYEKVLSFIARGkeegaRLLCGG-RRPAH 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 317 R----YIAPTLLTDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACIN 392
Cdd:cd07110 338 LekgyFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVWIN 417
|
330 340
....*....|....*....|....*...
gi 2552840633 393 dtIVQTANGNLPFGGIGNSGmgayHGRE 420
Cdd:cd07110 418 --CSQPCFPQAPWGGYKRSG----IGRE 439
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
8-426 |
3.94e-55 |
|
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: 190.60 E-value: 3.94e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 8 TRLVKLQKAFFNEHITREIPF--RLCALDRLAEALVSREKQLGEALHADLGK-------------SAFESYATEIGFLLH 72
Cdd:cd07119 38 KRAIAAARRAFDSGEWPHLPAqeRAALLFRIADKIREDAEELARLETLNTGKtlreseididdvaNCFRYYAGLATKETG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 73 EIRTIKNHlqswardrrrptplflfgSKSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAA 152
Cdd:cd07119 118 EVYDVPPH------------------VISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 153 LQELIDECFEEEYIA--VT-DADRETTELLLQERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLK 229
Cdd:cd07119 180 LFELIEEAGLPAGVVnlVTgSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 230 ATARRIVWGKFLNCGQTCVAPDYLMVHHKVQDKLTEYICDEITR-QYGENPQQSPDYPRIVNARHFDRLSALLSHG---- 304
Cdd:cd07119 260 TAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKiKLGNGLDADTEMGPLVSAEHREKVLSYIQLGkeeg 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 305 -TILCGGTSdPADR------YIAPTLLTDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRA 377
Cdd:cd07119 340 aRLVCGGKR-PTGDelakgyFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARA 418
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2552840633 378 RYMIQHTTSGGACINDTIVQTANGnlPFGGIGNSGMGAYHGRESFETFS 426
Cdd:cd07119 419 NRVARRLRAGTVWINDYHPYFAEA--PWGGYKQSGIGRELGPTGLEEYQ 465
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
106-423 |
4.73e-55 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 190.50 E-value: 4.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 106 EPYG-CALIIaPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAV-----TDADRETTEl 178
Cdd:cd07091 140 EPIGvCGQII-PWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAgFPPGVVNIvpgfgPTAGAAISS- 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 179 llQERFDYIFYTGGVEYGRHVMQAASR-HLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHH 257
Cdd:cd07091 218 --HMDVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 258 KVQDKLTEYICDEITRQYGENP-----QQSPdyprIVNARHFDRLSALLSHG-----TILCGGtSDPADR--YIAPTLLT 325
Cdd:cd07091 296 SIYDEFVEKFKARAEKRVVGDPfdpdtFQGP----QVSKAQFDKILSYIESGkkegaTLLTGG-ERHGSKgyFIQPTVFT 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 326 DIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTAngNLPF 405
Cdd:cd07091 371 DVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDA--AVPF 448
|
330
....*....|....*...
gi 2552840633 406 GGIGNSGMGAYHGRESFE 423
Cdd:cd07091 449 GGFKQSGFGRELGEEGLE 466
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
29-414 |
1.46e-54 |
|
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: 188.41 E-value: 1.46e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 29 RLCALDRLAEALVSREKQLGEALHADLGKSAFESyateigflLHEI-RTIKNHLQSWARDRRR-----PTPLFLfGSKSR 102
Cdd:cd07094 45 RMAILERAADLLKKRAEEFAKIIACEGGKPIKDA--------RVEVdRAIDTLRLAAEEAERIrgeeiPLDATQ-GSDNR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 103 IHY---EPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVTDADRE--TT 176
Cdd:cd07094 116 LAWtirEPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILVEAgVPEGVLQVVTGEREvlGD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 177 ELLLQERFDYIFYTGGVEYGRHVMQAASrhLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVH 256
Cdd:cd07094 196 AFAADERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVH 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 257 HKVQDKLTEYICDEITRQYGENP-QQSPDYPRIVNARHFDRLS-----ALLSHGTILCGGTSDpaDRYIAPTLLTDIPLQ 330
Cdd:cd07094 274 EELYDEFIEAFVAAVKKLKVGDPlDEDTDVGPLISEEAAERVErwveeAVEAGARLLCGGERD--GALFKPTVLEDVPRD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 331 SPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTANgNLPFGGIGN 410
Cdd:cd07094 352 TKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDSSAFRTD-WMPFGGVKE 430
|
....
gi 2552840633 411 SGMG 414
Cdd:cd07094 431 SGVG 434
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
106-431 |
3.42e-54 |
|
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: 187.54 E-value: 3.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 106 EPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVTDADRET--TELLLQE 182
Cdd:cd07118 118 EPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAgLPAGVVNIVTGYGATvgQAMTEHP 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 183 RFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQDK 262
Cdd:cd07118 198 DVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 263 LTEYICdEITRQ--YGENPQQSPDYPRIVNARHFDRLSALLSHG-----TILCGGTSDP--ADRYIAPTLLTDIPLQSPL 333
Cdd:cd07118 278 FVAAVV-ARSRKvrVGDPLDPETKVGAIINEAQLAKITDYVDAGraegaTLLLGGERLAsaAGLFYQPTIFTDVTPDMAI 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 334 LTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTAngNLPFGGIGNSGM 413
Cdd:cd07118 357 AREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSP--ELPFGGFKQSGI 434
|
330
....*....|....*...
gi 2552840633 414 GAYHGRESFETFSYCRSI 431
Cdd:cd07118 435 GRELGRYGVEEYTELKTV 452
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
14-432 |
1.75e-53 |
|
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: 185.62 E-value: 1.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 14 QKAFFNEHITREIPFRLCALDRLAEALVSREKQLGEALHADLGKSAFESyATEIGFLLHEI-------RTIKNHLQSWar 86
Cdd:cd07120 29 RRAFDETDWAHDPRLRARVLLELADAFEANAERLARLLALENGKILGEA-RFEISGAISELryyaglaRTEAGRMIEP-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 87 drrRPtplflfGSKSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC------ 160
Cdd:cd07120 106 ---EP------GSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEIpslpag 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 161 ----FEEEYIAVTDAdretteLLLQERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIV 236
Cdd:cd07120 177 vvnlFTESGSEGAAH------LVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 237 WGKFLNCGQTCVAPDYLMVHH----KVQDKLTEYIcdeitRQYGENPQQSP--DYPRIVNARHFDRLSALLSHG------ 304
Cdd:cd07120 251 RALTIFAGQFCMAGSRVLVQRsiadEVRDRLAARL-----AAVKVGPGLDPasDMGPLIDRANVDRVDRMVERAiaagae 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 305 TILCGGTSD---PADRYIAPTLLTDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMI 381
Cdd:cd07120 326 VVLRGGPVTeglAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVA 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2552840633 382 QHTTSGGACINDTIVQTANGNlpFGGIGNSGMGAYHGRESFETFSYCRSIV 432
Cdd:cd07120 406 RAIRAGTVWINDWNKLFAEAE--EGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
33-415 |
3.11e-53 |
|
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: 186.27 E-value: 3.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 33 LDRLAEALVSREKQLGEALHADLGKSAFESYA--TE-IGFLLHEIRtiknHLQSWARDRRRPTPlflfGSKSRIHYEPYG 109
Cdd:cd07124 97 LLRAAALLRRRRFELAAWMVLEVGKNWAEADAdvAEaIDFLEYYAR----EMLRLRGFPVEMVP----GEDNRYVYRPLG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 110 CALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQElideCFEEEYIA------VTDADRETTELLLQE- 182
Cdd:cd07124 169 VGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVE----ILEEAGLPpgvvnfLPGPGEEVGDYLVEHp 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 183 RFDYIFYTGGVEYGRHVMQAASR------HLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVH 256
Cdd:cd07124 245 DVRFIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVH 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 257 HKVQDKLTEYICdEITR--QYGENPQQSPDYPRIVNARHFDR----LSALLSHGTILCGG-TSDPADR--YIAPTLLTDI 327
Cdd:cd07124 325 ESVYDEFLERLV-ERTKalKVGDPEDPEVYMGPVIDKGARDRirryIEIGKSEGRLLLGGeVLELAAEgyFVQPTIFADV 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 328 PLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTANGNLPFGG 407
Cdd:cd07124 404 PPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQPFGG 483
|
....*...
gi 2552840633 408 IGNSGMGA 415
Cdd:cd07124 484 FKMSGTGS 491
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
33-432 |
2.12e-52 |
|
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: 2.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 33 LDRLAEALVSREKQLGEALHADLGKSAFESyateIGFLLHEIRTIKnHLQSWARDRRRPTPLF--LFGSKSRIHY---EP 107
Cdd:cd07145 49 LMKVAELIERRKEELAKLLTIEVGKPIKQS----RVEVERTIRLFK-LAAEEAKVLRGETIPVdaYEYNERRIAFtvrEP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 108 YGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVTDADRETT--ELLLQERF 184
Cdd:cd07145 124 IGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPGVINVVTGYGSEVgdEIVTNPKV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 185 DYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQDKLT 264
Cdd:cd07145 204 NMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 265 EYICDEITRQYGENP-QQSPDYPRIVNARHFDRLSALLSH-----GTILCGGTSDPADrYIAPTLLTDIPLQSPLLTDEI 338
Cdd:cd07145 284 KLLVEKVKKLKVGDPlDESTDLGPLISPEAVERMENLVNDavekgGKILYGGKRDEGS-FFPPTVLENDTPDMIVMKEEV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 339 FGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACIND-TIVQTanGNLPFGGIGNSGMGAYH 417
Cdd:cd07145 363 FGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDsTRFRW--DNLPFGGFKKSGIGREG 440
|
410
....*....|....*
gi 2552840633 418 GRESFETFSYCRSIV 432
Cdd:cd07145 441 VRYTMLEMTEEKTIV 455
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
106-431 |
5.45e-52 |
|
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: 181.73 E-value: 5.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 106 EPYG-CALIIApWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDE------CFEeeyiaVTDADRETTEL 178
Cdd:cd07090 115 EPLGvCAGIGA-WNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEaglpdgVFN-----VVQGGGETGQL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 179 LLQE-RFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHH 257
Cdd:cd07090 189 LCEHpDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQR 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 258 KVQDKLTEYICDEITRQYGENP-QQSPDYPRIVNARHFDRLSALLSHG-----TILCGGTSDPADR------YIAPTLLT 325
Cdd:cd07090 269 SIKDEFTERLVERTKKIRIGDPlDEDTQMGALISEEHLEKVLGYIESAkqegaKVLCGGERVVPEDglengfYVSPCVLT 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 326 DIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVqtANGNLPF 405
Cdd:cd07090 349 DCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINTYNI--SPVEVPF 426
|
330 340
....*....|....*....|....*.
gi 2552840633 406 GGIGNSGMGAYHGRESFETFSYCRSI 431
Cdd:cd07090 427 GGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
27-435 |
6.23e-52 |
|
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: 182.16 E-value: 6.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 27 PFRLCALDRLAEALVSREKQLGEALHADLGKSAFESYAteigfllhEIRTIKNHLQSWARDRRRP----TPLFLFGSKSR 102
Cdd:cd07131 59 PRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRG--------DVQEAIDMAQYAAGEGRRLfgetVPSELPNKDAM 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 103 IHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQE-LIDECFEEEYI-AVTDADRETTELLL 180
Cdd:cd07131 131 TRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVElFAEAGLPPGVVnVVHGRGEEVGEALV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 181 QE-RFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKV 259
Cdd:cd07131 211 EHpDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 260 QDKLTEYICDEITR-QYGENPQQSPDYPRIVNARHFDRLSALL----SHG-TILCGGTSDPADRY-----IAPTLLTDIP 328
Cdd:cd07131 291 YDEFLKRFVERAKRlRVGDGLDEETDMGPLINEAQLEKVLNYNeigkEEGaTLLLGGERLTGGGYekgyfVEPTVFTDVT 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 329 LQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACIN-DTIvqTANGNLPFGG 407
Cdd:cd07131 371 PDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNaPTI--GAEVHLPFGG 448
|
410 420 430
....*....|....*....|....*....|..
gi 2552840633 408 IGNSGMGayH---GRESFETFSYCRSI-VDSS 435
Cdd:cd07131 449 VKKSGNG--HreaGTTALDAFTEWKAVyVDYS 478
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
106-414 |
8.84e-52 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 182.20 E-value: 8.84e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 106 EPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVT--DADRETTELLLQE 182
Cdd:PLN02278 159 QPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAgIPPGVLNVVmgDAPEIGDALLASP 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 183 RFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQDK 262
Cdd:PLN02278 239 KVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDK 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 263 LTEYICDEITR-QYG----ENPQQSPdyprIVNARHFDRLSAL----LSHGT-ILCGGTS-DPADRYIAPTLLTDIPLQS 331
Cdd:PLN02278 319 FAEAFSKAVQKlVVGdgfeEGVTQGP----LINEAAVQKVESHvqdaVSKGAkVLLGGKRhSLGGTFYEPTVLGDVTEDM 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 332 PLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTANGnlPFGGIGNS 411
Cdd:PLN02278 395 LIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGGVKQS 472
|
...
gi 2552840633 412 GMG 414
Cdd:PLN02278 473 GLG 475
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
33-427 |
2.85e-51 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 180.14 E-value: 2.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 33 LDRLAEALVSREKQLGEALHADLGK-------------SAFESYATEIgfllheIRTIKNHLQSwardrRRPtplflfGS 99
Cdd:cd07097 65 LDKAGDELEARKEELARLLTREEGKtlpeargevtragQIFRYYAGEA------LRLSGETLPS-----TRP------GV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 100 KSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC------FEeeyiAVTDADR 173
Cdd:cd07097 128 EVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAglpagvFN----LVMGSGS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 174 ETTELLLQ-ERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDY 252
Cdd:cd07097 204 EVGQALVEhPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSR 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 253 LMVHHKVQDKLTEYICDEITR-QYGENPQQSPDYPRIVNARHFDRLSALLSHG-----TILCGGtsDPADR-----YIAP 321
Cdd:cd07097 284 LIVTEGIHDRFVEALVERTKAlKVGDALDEGVDIGPVVSERQLEKDLRYIEIArsegaKLVYGG--ERLKRpdegyYLAP 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 322 TLLTDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTANg 401
Cdd:cd07097 362 ALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDY- 440
|
410 420
....*....|....*....|....*..
gi 2552840633 402 NLPFGGIGNSGMGAY-HGRESFETFSY 427
Cdd:cd07097 441 HVPFGGRKGSSYGPReQGEAALEFYTT 467
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
106-432 |
4.89e-51 |
|
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: 179.69 E-value: 4.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 106 EPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQE-LIDECFEEEYIA-VTDADRETTELLLQ-E 182
Cdd:cd07082 140 EPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEaFHDAGFPKGVVNvVTGRGREIGDPLVThG 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 183 RFDYIFYTGGVEYGRHVMQAASRhlTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQDK 262
Cdd:cd07082 220 RIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 263 LTEYICDEITRQYGENPQQ-SPDYPRIVNARHFDRLSALL----SHG-TILCGGTSDpADRYIAPTLLTDIPLQSPLLTD 336
Cdd:cd07082 298 LVELLKEEVAKLKVGMPWDnGVDITPLIDPKSADFVEGLIddavAKGaTVLNGGGRE-GGNLIYPTLLDPVTPDMRLAWE 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 337 EIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDtivQTANG--NLPFGGIGNSGMG 414
Cdd:cd07082 377 EPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINS---KCQRGpdHFPFLGRKDSGIG 453
|
330
....*....|....*...
gi 2552840633 415 AYHGRESFETFSYCRSIV 432
Cdd:cd07082 454 TQGIGDALRSMTRRKGIV 471
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
33-431 |
5.06e-51 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 179.91 E-value: 5.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 33 LDRLAEaLVSREKQLGEALHA-DLGKSAFESYATEIGFLLHEIRtiknHLQSWArDRrrptplfLFG-----SKSRIHY- 105
Cdd:cd07144 74 LDKLAD-LVEKNRDLLAAIEAlDSGKPYHSNALGDLDEIIAVIR----YYAGWA-DK-------IQGktiptSPNKLAYt 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 106 --EPYG-CALIIaPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVTDADRETTELLLQ 181
Cdd:cd07144 141 lhEPYGvCGQII-PWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVNIIPGYGAVAGSALA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 182 ER--FDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKV 259
Cdd:cd07144 220 EHpdVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESI 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 260 QDKLTEYICDEITRQY------GENPQQSPdyprIVNARHFDRLSALLSHG-----TILCGGTSDPADR----YIAPTLL 324
Cdd:cd07144 300 YDKFVEKFVEHVKQNYkvgspfDDDTVVGP----QVSKTQYDRVLSYIEKGkkegaKLVYGGEKAPEGLgkgyFIPPTIF 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 325 TDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTivQTANGNLP 404
Cdd:cd07144 376 TDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSS--NDSDVGVP 453
|
410 420
....*....|....*....|....*..
gi 2552840633 405 FGGIGNSGMGAYHGRESFETFSYCRSI 431
Cdd:cd07144 454 FGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
103-414 |
1.27e-50 |
|
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: 178.18 E-value: 1.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 103 IHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEcfeeeyiA---------VTDADR 173
Cdd:cd07112 120 ITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALE-------AglpagvlnvVPGFGH 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 174 ETTELL-LQERFDYIFYTGGVEYGRHVMQAASR-HLTPVTLELGGKSPCIVDDDA-DLKATARRIVWGKFLNCGQTCVAP 250
Cdd:cd07112 193 TAGEALgLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAG 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 251 DYLMVHHKVQDKLTEYICDEITRQYGENPQqSPDYP--RIVNARHFDRLSALLSHG-----TILCGGTSDPADR---YIA 320
Cdd:cd07112 273 SRLLVHESIKDEFLEKVVAAAREWKPGDPL-DPATRmgALVSEAHFDKVLGYIESGkaegaRLVAGGKRVLTETggfFVE 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 321 PTLLTDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACIN-----DTI 395
Cdd:cd07112 352 PTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVNcfdegDIT 431
|
330
....*....|....*....
gi 2552840633 396 VqtangnlPFGGIGNSGMG 414
Cdd:cd07112 432 T-------PFGGFKQSGNG 443
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
105-431 |
2.82e-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: 174.49 E-value: 2.82e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 105 YEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECFEEEYIAVTDADRETTELLLQERF 184
Cdd:cd07107 114 REPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREVLPPGVFNILPGDGATAGAALVRHP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 185 DY--IFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWG-KFLNCGQTCVAPDYLMVHHKVQD 261
Cdd:cd07107 194 DVkrIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYD 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 262 KLTEYICDEITRQYGENPqQSPDYPR--IVNARHFDR----LSALLSHGTILCGGTSDPADR------YIAPTLLTDIPL 329
Cdd:cd07107 274 EVLARVVERVAAIKVGDP-TDPATTMgpLVSRQQYDRvmhyIDSAKREGARLVTGGGRPEGPaleggfYVEPTVFADVTP 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 330 QSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDtiVQTANGNLPFGGIG 409
Cdd:cd07107 353 GMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVWING--SSRHFLGAPFGGVK 430
|
330 340
....*....|....*....|..
gi 2552840633 410 NSGMGAYHGRESFETFSYCRSI 431
Cdd:cd07107 431 NSGIGREECLEELLSYTQEKNV 452
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
107-414 |
4.97e-49 |
|
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: 173.59 E-value: 4.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 107 PYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVTDADRETTELLLQ-ERF 184
Cdd:cd07147 123 PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETgLPKGAFSVLPCSRDDADLLVTdERI 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 185 DYIFYTGGVEYGRHVMQAASRHltPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQDKLT 264
Cdd:cd07147 203 KLLSFTGSPAVGWDLKARAGKK--KVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFK 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 265 EYICDEITRQYGENP-QQSPDYPRIVNARHFDRL-----SALLSHGTILCGGTSDPAdrYIAPTLLTDIPLQSPLLTDEI 338
Cdd:cd07147 281 SRLVARVKALKTGDPkDDATDVGPMISESEAERVegwvnEAVDAGAKLLTGGKRDGA--LLEPTILEDVPPDMEVNCEEV 358
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2552840633 339 FGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDtiVQTAN-GNLPFGGIGNSGMG 414
Cdd:cd07147 359 FGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVIND--VPTFRvDHMPYGGVKDSGIG 433
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
98-432 |
2.63e-48 |
|
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: 171.77 E-value: 2.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 98 GSKSRI---HYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVT--DA 171
Cdd:cd07146 108 NGKARKiftLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAgLPPDMLSVVtgEP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 172 DRETTELLLQERFDYIFYTGGVEYGRHVmqAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPD 251
Cdd:cd07146 188 GEIGDELITHPDVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVK 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 252 YLMVHHKVQDKLTEYICdEITRQY--GENPQQSPDYPRIVN---ARHFDR--LSALLSHGTILCGGTSDPAdrYIAPTLL 324
Cdd:cd07146 266 RILVHESVADEFVDLLV-EKSAALvvGDPMDPATDMGTVIDeeaAIQIENrvEEAIAQGARVLLGNQRQGA--LYAPTVL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 325 TDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDtIVQTANGNLP 404
Cdd:cd07146 343 DHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNE-VPGFRSELSP 421
|
330 340
....*....|....*....|....*....
gi 2552840633 405 FGGIGNSGMGAYHG-RESFETFSYCRSIV 432
Cdd:cd07146 422 FGGVKDSGLGGKEGvREAMKEMTNVKTYS 450
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
105-431 |
1.34e-47 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 170.40 E-value: 1.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 105 YEPYG-CALIIaPWNYPLqLALSPLIG-AIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVTDADRETTELLLQ 181
Cdd:cd07143 142 HEPIGvCGQII-PWNFPL-LMCAWKIApALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGYGRTCGNAIS 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 182 E--RFDYIFYTGGVEYGRHVMQAASR-HLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHK 258
Cdd:cd07143 220 ShmDIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEG 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 259 VQDKLTEYICDEITR-----QYGENPQQSPDypriVNARHFDRLSALLSHG-----TILCGGTSDPADRY-IAPTLLTDI 327
Cdd:cd07143 300 IYDKFVKRFKEKAKKlkvgdPFAEDTFQGPQ----VSQIQYERIMSYIESGkaegaTVETGGKRHGNEGYfIEPTIFTDV 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 328 PLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDtiVQTANGNLPFGG 407
Cdd:cd07143 376 TEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNC--YNLLHHQVPFGG 453
|
330 340
....*....|....*....|....
gi 2552840633 408 IGNSGMGAYHGRESFETFSYCRSI 431
Cdd:cd07143 454 YKQSGIGRELGEYALENYTQIKAV 477
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
33-425 |
7.78e-47 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 166.84 E-value: 7.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 33 LDRLAEALVSREKQLGEALHADLGKSAfESYATEIGFLLHEIrtikNHLQSWAR---------DRRRPTpLFLFGSksri 103
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQ-QLAEVEVAFTADYI----DYMAEWARryegeiiqsDRPGEN-ILLFKR---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 104 hyePYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVTDADRET--TELLL 180
Cdd:PRK10090 71 ---ALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETvgQELAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 181 QERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQ 260
Cdd:PRK10090 148 NPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 261 DKLTEYICDEITR-QYGeNP--QQSPDYPRIVNARHFDRLSALLSH-----GTILCGGTSDPADRYI-APTLLTDIPLQS 331
Cdd:PRK10090 228 DQFVNRLGEAMQAvQFG-NPaeRNDIAMGPLINAAALERVEQKVARaveegARVALGGKAVEGKGYYyPPTLLLDVRQEM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 332 PLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTANGnlpF-GGIGN 410
Cdd:PRK10090 307 SIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQG---FhAGWRK 383
|
410
....*....|....*
gi 2552840633 411 SGMGAYHGRESFETF 425
Cdd:PRK10090 384 SGIGGADGKHGLHEY 398
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
107-429 |
1.46e-46 |
|
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: 167.74 E-value: 1.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 107 PYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECFEEE-----YIAVTDADRETTELLLQ 181
Cdd:cd07086 133 PLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLEKNglppgVVNLVTGGGDGGELLVH 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 182 -ERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQ 260
Cdd:cd07086 213 dPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVY 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 261 DKLTEyicdEITRQYGE----NP-QQSPDYPRIVNARHFDR-LSAL----LSHGTILCGG---TSDPADRYIAPTLLTDI 327
Cdd:cd07086 293 DEFLE----RLVKAYKQvrigDPlDEGTLVGPLINQAAVEKyLNAIeiakSQGGTVLTGGkriDGGEPGNYVEPTIVTGV 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 328 PLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTS--GGACIN-DTIvqTANGNLP 404
Cdd:cd07086 369 TDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKGSdcGIVNVNiPTS--GAEIGGA 446
|
330 340
....*....|....*....|....*
gi 2552840633 405 FGGIGNSGMGAYHGRESFEtfSYCR 429
Cdd:cd07086 447 FGGEKETGGGRESGSDAWK--QYMR 469
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
106-431 |
1.61e-46 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 167.75 E-value: 1.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 106 EPYG-CALIIApWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC------FEeeyiaVTDADRETTEL 178
Cdd:PRK13252 141 EPLGvCAGIGA-WNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAglpdgvFN-----VVQGDGRVGAW 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 179 LLQ-ERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHH 257
Cdd:PRK13252 215 LTEhPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQK 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 258 KVQDKLTEYICDEITRQYGENPQQ-SPDYPRIVNARHFDRLSALLSHG-----TILCGGT-----SDPADRYIAPTLLTD 326
Cdd:PRK13252 295 SIKAAFEARLLERVERIRIGDPMDpATNFGPLVSFAHRDKVLGYIEKGkaegaRLLCGGErltegGFANGAFVAPTVFTD 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 327 IPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIqHTTSGGAC-IN---DTIVQtangn 402
Cdd:PRK13252 375 CTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVI-HQLEAGICwINtwgESPAE----- 448
|
330 340
....*....|....*....|....*....
gi 2552840633 403 LPFGGIGNSGMGAYHGRESFETFSYCRSI 431
Cdd:PRK13252 449 MPVGGYKQSGIGRENGIATLEHYTQIKSV 477
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
33-432 |
2.18e-46 |
|
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: 167.14 E-value: 2.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 33 LDRLAEaLVSREKQLGEALHA-DLGKSAFESYATEIGFLLHEIR-----TIKNHLQSWARDrrrpTPLFLFGSKsrihyE 106
Cdd:cd07141 75 LNKLAD-LIERDRAYLASLETlDNGKPFSKSYLVDLPGAIKVLRyyagwADKIHGKTIPMD----GDFFTYTRH-----E 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 107 PYG-CALIIaPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVTDADRETTELLLQER- 183
Cdd:cd07141 145 PVGvCGQII-PWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAgFPPGVVNVVPGYGPTAGAAISSHp 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 184 -FDYIFYTGGVEYGRHVMQAASR-HLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQD 261
Cdd:cd07141 224 dIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYD 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 262 KLTEYICDEITRQYGENP-----QQSPDypriVNARHFDRLSALLSHGT-----ILCGGtSDPADR--YIAPTLLTDIPL 329
Cdd:cd07141 304 EFVKRSVERAKKRVVGNPfdpktEQGPQ----IDEEQFKKILELIESGKkegakLECGG-KRHGDKgyFIQPTVFSDVTD 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 330 QSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGA---CINDTIVQTangnlPFG 406
Cdd:cd07141 379 DMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVwvnCYNVVSPQA-----PFG 453
|
410 420
....*....|....*....|....*.
gi 2552840633 407 GIGNSGMGAYHGRESFETFSYCRSIV 432
Cdd:cd07141 454 GYKMSGNGRELGEYGLQEYTEVKTVT 479
|
|
| ABALDH |
TIGR03374 |
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1. ... |
95-432 |
4.87e-45 |
|
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1.35), also called gamma-aminobutyraldehyde dehydrogenase. This enzyme can follow putrescine transaminase (EC 2.6.1.82) for a two-step conversion of putrescine to gamma-aminobutyric acid (GABA). The member from Escherichia coli is characterized as a homotetramer that binds one NADH per momomer. This enzyme belongs to the medium-chain aldehyde dehydrogenases, and is quite similar in sequence to the betaine aldehyde dehydrogenase (EC 1.2.1.8) family.
Pssm-ID: 132417 Cd Length: 472 Bit Score: 163.25 E-value: 4.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 95 FLFGSKSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECFEEEYIAVTDADRE 174
Cdd:TIGR03374 125 YLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVVNILFGRGK 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 175 TT--ELLLQERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDY 252
Cdd:TIGR03374 205 TVgdPLTGHEKVRMVSLTGSIATGEHILSHTAPSIKRTHMELGGKAPVIVFDDADIDAVVEGVRTFGFYNAGQDCTAACR 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 253 LMVHHKVQDKLTEYICDEI-TRQYGENPQQSPDYPRIVNARHFDRLSAL------LSHGTILCGGTSDPAD-RYIAPTLL 324
Cdd:TIGR03374 285 IYAQRGIYDTLVEKLGAAVaTLKSGAPDDESTELGPLSSLAHLERVMKAveeakaLGHIKVITGGEKRKGNgYYFAPTLL 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 325 TDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTAngNLP 404
Cdd:TIGR03374 365 AGAKQDDAIVQKEVFGPVVSITSFDDEEQVVNWANDSQYGLASSVWTKDVGRAHRLSARLQYGCTWVNTHFMLVS--EMP 442
|
330 340
....*....|....*....|....*...
gi 2552840633 405 FGGIGNSGMGAYHGRESFETFSYCRSIV 432
Cdd:TIGR03374 443 HGGQKLSGYGKDMSLYGLEDYTVVRHIM 470
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
100-420 |
5.32e-45 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 163.75 E-value: 5.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 100 KSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAaalQELIDECFEEEYIA-----VTDADRE 174
Cdd:PLN02467 144 KGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTC---LELADICREVGLPPgvlnvVTGLGTE 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 175 T-TELLLQERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYL 253
Cdd:PLN02467 221 AgAPLASHPGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 254 MVHHKV----QDKLTEY-----ICDEITrqygENPQQSPdyprIVNARHFDR----LSALLSHG-TILCGGTSDPADR-- 317
Cdd:PLN02467 301 LVHERIasefLEKLVKWaknikISDPLE----EGCRLGP----VVSEGQYEKvlkfISTAKSEGaTILCGGKRPEHLKkg 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 318 -YIAPTLLTDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTiv 396
Cdd:PLN02467 373 fFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCS-- 450
|
330 340
....*....|....*....|....
gi 2552840633 397 QTANGNLPFGGIGNSGmgayHGRE 420
Cdd:PLN02467 451 QPCFCQAPWGGIKRSG----FGRE 470
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
98-418 |
5.42e-44 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 161.19 E-value: 5.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 98 GSKSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECFEEEYIA--VTDADRET 175
Cdd:TIGR01237 158 GETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVqfVPGSGSEV 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 176 TELLLQE-RFDYIFYTGGVEYGRHV------MQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCV 248
Cdd:TIGR01237 238 GDYLVDHpKTSLITFTGSREVGTRIferaakVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 249 APDYLMVHHKVQDKLTEYICdEITRQYGENPQQSPD--YPRIVNARHFDRLSALL----SHGTILCGGTSDPADRY-IAP 321
Cdd:TIGR01237 318 AGSRAVVHEKVYDEVVERFV-EITESLKVGPPDSADvyVGPVIDQKSFNKIMEYIeigkAEGRLVSGGCGDDSKGYfIGP 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 322 TLLTDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTANG 401
Cdd:TIGR01237 397 TIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVG 476
|
330
....*....|....*..
gi 2552840633 402 NLPFGGIGNSGMGAYHG 418
Cdd:TIGR01237 477 YQPFGGFKMSGTDSKAG 493
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
105-414 |
6.20e-44 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 160.59 E-value: 6.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 105 YEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECFEEEYI-AVTDADRETTELLL-QE 182
Cdd:cd07559 134 HEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVnVVTGFGSEAGKPLAsHP 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 183 RFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDA-----DLKATARRIVWGKFLNCGQTCVAPDYLMVHH 257
Cdd:cd07559 214 RIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 258 KVQDKLTEYICDEITRQYGENPQqspDYPRIVNAR-HFDRLSALLSH--------GTILCGG-----TSDPADRYIAPTL 323
Cdd:cd07559 294 SIYDEFIERAVERFEAIKVGNPL---DPETMMGAQvSKDQLEKILSYvdigkeegAEVLTGGerltlGGLDKGYFYEPTL 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 324 LTDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTANGnl 403
Cdd:cd07559 371 IKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHA-- 448
|
330
....*....|.
gi 2552840633 404 PFGGIGNSGMG 414
Cdd:cd07559 449 PFGGYKKSGIG 459
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
101-414 |
1.28e-42 |
|
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: 156.85 E-value: 1.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 101 SRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECFEEEYI-AVTDADRETTELL 179
Cdd:cd07117 130 SIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVnIVTGKGSKSGEYL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 180 LQER-FDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHK 258
Cdd:cd07117 210 LNHPgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEG 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 259 VQDKLTEYICDEITRQYGENPQQsPD--YPRIVNARHFDRL-----SALLSHGTILCGG---TSDPADR--YIAPTLLTD 326
Cdd:cd07117 290 IYDEFVAKLKEKFENVKVGNPLD-PDtqMGAQVNKDQLDKIlsyvdIAKEEGAKILTGGhrlTENGLDKgfFIEPTLIVN 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 327 IPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINdTIVQTANGnLPFG 406
Cdd:cd07117 369 VTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVN-TYNQIPAG-APFG 446
|
....*...
gi 2552840633 407 GIGNSGMG 414
Cdd:cd07117 447 GYKKSGIG 454
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
98-412 |
4.01e-42 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 156.25 E-value: 4.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 98 GSKSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC--------FeeeyiaVT 169
Cdd:PRK03137 162 GEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAglpagvvnF------VP 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 170 DADRETTELLLQE-RFDYIFYTGGVEYGRHVMQAASR------HLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLN 242
Cdd:PRK03137 236 GSGSEVGDYLVDHpKTRFITFTGSREVGLRIYERAAKvqpgqiWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGF 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 243 CGQTCVAPDYLMVHHKVQDKLTEYICdEITRQYGENPQQSPDY--PrIVNARHFDRLSALL----SHGTILCGGTSDPAD 316
Cdd:PRK03137 316 SGQKCSACSRAIVHEDVYDEVLEKVV-ELTKELTVGNPEDNAYmgP-VINQASFDKIMSYIeigkEEGRLVLGGEGDDSK 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 317 RY-IAPTLLTDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTI 395
Cdd:PRK03137 394 GYfIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGC 473
|
330
....*....|....*..
gi 2552840633 396 VQTANGNLPFGGIGNSG 412
Cdd:PRK03137 474 TGAIVGYHPFGGFNMSG 490
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
105-432 |
4.62e-41 |
|
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: 152.65 E-value: 4.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 105 YEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVTDADRETTELLLQER 183
Cdd:cd07142 139 HEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAgLPDGVLNIVTGFGPTAGAAIASH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 184 FDY--IFYTGGVEYGRHVMQAASR-HLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQ 260
Cdd:cd07142 219 MDVdkVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIY 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 261 DKLTE---------YICDEITRQYGENPQqspdypriVNARHFDRLSALLSHG-----TILCGGtsdpaDR------YIA 320
Cdd:cd07142 299 DEFVEkakaralkrVVGDPFRKGVEQGPQ--------VDKEQFEKILSYIEHGkeegaTLITGG-----DRigskgyYIQ 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 321 PTLLTDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTAn 400
Cdd:cd07142 366 PTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDA- 444
|
330 340 350
....*....|....*....|....*....|..
gi 2552840633 401 gNLPFGGIGNSGMGAYHGRESFETFSYCRSIV 432
Cdd:cd07142 445 -SIPFGGYKMSGIGREKGIYALNNYLQVKAVV 475
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
106-431 |
6.43e-40 |
|
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: 149.51 E-value: 6.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 106 EPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVTDADRETTELLLQE-R 183
Cdd:cd07113 141 EPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAgIPDGVLNVVNGKGAVGAQLISHpD 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 184 FDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQDKL 263
Cdd:cd07113 221 VAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDEL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 264 TEYICDEITR-QYGENPQQSPDYPRIVNARHFDRLSALL-----SHGTILCGGTSDPADRY-IAPTLLTDIPLQSPLLTD 336
Cdd:cd07113 301 VTKLKQALSSfQVGSPMDESVMFGPLANQPHFDKVCSYLddaraEGDEIVRGGEALAGEGYfVQPTLVLARSADSRLMRE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 337 EIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACIN-DTIVqtaNGNLPFGGIGNSGMGA 415
Cdd:cd07113 381 ETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNmHTFL---DPAVPFGGMKQSGIGR 457
|
330
....*....|....*.
gi 2552840633 416 YHGRESFETFSYCRSI 431
Cdd:cd07113 458 EFGSAFIDDYTELKSV 473
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
106-414 |
3.30e-38 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 145.05 E-value: 3.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 106 EPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC--FEEEYIAVTDADRET-TELLLQE 182
Cdd:PRK11241 145 QPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAgiPAGVFNVVTGSAGAVgGELTSNP 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 183 RFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQDK 262
Cdd:PRK11241 225 LVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDR 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 263 LTEYICDEITR-QYGENPQQSPDYPRIVNARHFDRLS-----ALLSHGTILCGGTSDP-ADRYIAPTLLTDIPLQSPLLT 335
Cdd:PRK11241 305 FAEKLQQAVSKlHIGDGLEKGVTIGPLIDEKAVAKVEehiadALEKGARVVCGGKAHElGGNFFQPTILVDVPANAKVAK 384
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2552840633 336 DEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVqtANGNLPFGGIGNSGMG 414
Cdd:PRK11241 385 EETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGII--SNEVAPFGGIKASGLG 461
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
29-418 |
5.02e-38 |
|
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: 144.64 E-value: 5.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 29 RLCALDRLAEALVSREKQLGEALHADLGKS---AFESYATEIGFLLHEIRtiknhlqsWARDRRRPTPLFLF--GSKSRI 103
Cdd:cd07083 79 RARLLLKAADLLRRRRRELIATLTYEVGKNwveAIDDVAEAIDFIRYYAR--------AALRLRYPAVEVVPypGEDNES 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 104 HYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVTDADRET--TELLL 180
Cdd:cd07083 151 FYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAgFPPGVVQFLPGVGEEvgAYLTE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 181 QERFDYIFYTGGVEYGRHVMQAASRHLT------PVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLM 254
Cdd:cd07083 231 HERIRGINFTGSLETGKKIYEAAARLAPgqtwfkRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLI 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 255 VHHKVQDKLTEYICDEITRQYGENPQQ-SPDYPRIVNARHFDRLSALLSH----GTILCGGTSDPADRY-IAPTLLTDIP 328
Cdd:cd07083 311 LTQGAYEPVLERLLKRAERLSVGPPEEnGTDLGPVIDAEQEAKVLSYIEHgkneGQLVLGGKRLEGEGYfVAPTVVEEVP 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 329 LQSPLLTDEIFGPILPVL--PFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTANGNLPFG 406
Cdd:cd07083 391 PKARIAQEEIFGPVLSVIryKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFG 470
|
410
....*....|..
gi 2552840633 407 GIGNSGMGAYHG 418
Cdd:cd07083 471 GFKLSGTNAKTG 482
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
28-412 |
3.19e-37 |
|
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: 141.25 E-value: 3.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 28 FRLCALDRLAEALVSREKQLGEALHADLGKSAFESyATEIGFLLHEIR-TIKNHlQSWARDRRRPTPlflfGSKSRIHYE 106
Cdd:cd07095 23 ERAAILRRFAELLKANKEELARLISRETGKPLWEA-QTEVAAMAGKIDiSIKAY-HERTGERATPMA----QGRAVLRHR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 107 PYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAaalqELIDECFEE-----EYIAVTDADRETTE-LLL 180
Cdd:cd07095 97 PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVA----ELMVELWEEaglppGVLNLVQGGRETGEaLAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 181 QERFDYIFYTGGVEYGRHVMQAASRHltP---VTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHH 257
Cdd:cd07095 173 HEGIDGLLFTGSAATGLLLHRQFAGR--PgkiLALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLIVPD 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 258 KVQ-DKLTEYICDEITR----QYGENPQqsPDYPRIVNARHFDRLSA---LLSHG-TILCGGTSDPADR-YIAPTLL--T 325
Cdd:cd07095 251 GAVgDAFLERLVEAAKRlrigAPDAEPP--FMGPLIIAAAAARYLLAqqdLLALGgEPLLAMERLVAGTaFLSPGIIdvT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 326 DIplqSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVqTANGNLPF 405
Cdd:cd07095 329 DA---ADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTT-GASSTAPF 404
|
....*..
gi 2552840633 406 GGIGNSG 412
Cdd:cd07095 405 GGVGLSG 411
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
106-432 |
1.51e-36 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 140.73 E-value: 1.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 106 EPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVTDADRETTELLLQERF 184
Cdd:PLN02766 157 EPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAgVPDGVINVVTGFGPTAGAAIASHM 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 185 DY--IFYTGGVEYGRHVMQAASR-HLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQD 261
Cdd:PLN02766 237 DVdkVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYD 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 262 KLTEYIC------------DEITRQygeNPQqspdypriVNARHFDRLSALLSHG-----TILCGGTSdPADR--YIAPT 322
Cdd:PLN02766 317 EFVKKLVekakdwvvgdpfDPRARQ---GPQ--------VDKQQFEKILSYIEHGkregaTLLTGGKP-CGDKgyYIEPT 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 323 LLTDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVqtANGN 402
Cdd:PLN02766 385 IFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFA--FDPD 462
|
330 340 350
....*....|....*....|....*....|
gi 2552840633 403 LPFGGIGNSGMGAYHGRESFETFSYCRSIV 432
Cdd:PLN02766 463 CPFGGYKMSGFGRDQGMDALDKYLQVKSVV 492
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
99-422 |
1.01e-35 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 137.56 E-value: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 99 SKSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELI------DECFEEEYIAVTDAD 172
Cdd:PRK09406 115 SRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFrragfpDGCFQTLLVGSGAVE 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 173 RetteLLLQERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDY 252
Cdd:PRK09406 195 A----ILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKR 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 253 LMVHHKVQDKLTEYICDEI-TRQYGENPQQSPDYPRIVNARHFDRLSALL-----SHGTILCGGTsdPADR---YIAPTL 323
Cdd:PRK09406 271 FIVHADVYDAFAEKFVARMaALRVGDPTDPDTDVGPLATEQGRDEVEKQVddavaAGATILCGGK--RPDGpgwFYPPTV 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 324 LTDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDtiVQTANGNL 403
Cdd:PRK09406 349 ITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFING--MTVSYPEL 426
|
330 340
....*....|....*....|..
gi 2552840633 404 PFGGIGNSGMG---AYHGRESF 422
Cdd:PRK09406 427 PFGGVKRSGYGrelSAHGIREF 448
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
106-421 |
8.04e-35 |
|
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: 135.32 E-value: 8.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 106 EPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQEL-IDECFEEEYIAVTDADRETTELLLQERF 184
Cdd:cd07140 146 EPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELtVKAGFPKGVINILPGSGSLVGQRLSDHP 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 185 DY--IFYTGGVEYGRHVMQ-AASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQD 261
Cdd:cd07140 226 DVrkLGFTGSTPIGKHIMKsCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHD 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 262 KLTEYICDEITR-QYGENPQQSPDYPRIVNARHFDRL-----SALLSHGTILCGGTS-DPADRYIAPTLLTDIPLQSPLL 334
Cdd:cd07140 306 EFVRRVVEEVKKmKIGDPLDRSTDHGPQNHKAHLDKLveyceRGVKEGATLVYGGKQvDRPGFFFEPTVFTDVEDHMFIA 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 335 TDEIFGPILPVLPFD--DIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINdtIVQTANGNLPFGGIGNSG 412
Cdd:cd07140 386 KEESFGPIMIISKFDdgDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVN--TYNKTDVAAPFGGFKQSG 463
|
....*....
gi 2552840633 413 MGAYHGRES 421
Cdd:cd07140 464 FGKDLGEEA 472
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
103-431 |
9.75e-35 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 135.41 E-value: 9.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 103 IHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECFEEEYI--AVTDADRETTELL- 179
Cdd:PRK09847 153 IVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVlnVVTGFGHEAGQALs 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 180 LQERFDYIFYTGGVEYGRHVMQ-AASRHLTPVTLELGGKSPCIVDDDA-DLKATARRIVWGKFLNCGQTCVAPDYLMVHH 257
Cdd:PRK09847 233 RHNDIDAIAFTGSTRTGKQLLKdAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 258 KVQDKLTEYICDEITR-QYGENPQQSPDYPRIVNARHFDRLSALL----SHGTILCGGTSDPADRYIAPTLLTDIPLQSP 332
Cdd:PRK09847 313 SIADEFLALLKQQAQNwQPGHPLDPATTMGTLIDCAHADSVHSFIregeSKGQLLLDGRNAGLAAAIGPTIFVDVDPNAS 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 333 LLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDtiVQTANGNLPFGGIGNSG 412
Cdd:PRK09847 393 LSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNN--YNDGDMTVPFGGYKQSG 470
|
330
....*....|....*....
gi 2552840633 413 MGAYHGRESFETFSYCRSI 431
Cdd:PRK09847 471 NGRDKSLHALEKFTELKTI 489
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
105-432 |
1.49e-33 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 132.62 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 105 YEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVTDADRETTELLLQER 183
Cdd:PLN02466 193 HEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAgLPPGVLNVVSGFGPTAGAALASH 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 184 FDY--IFYTGGVEYGRHVMQAASR-HLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQ 260
Cdd:PLN02466 273 MDVdkLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVY 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 261 DKLTEYICDEITRQYGENP-----QQSPDypriVNARHFDRL-----SALLSHGTILCGGtsdpaDR------YIAPTLL 324
Cdd:PLN02466 353 DEFVEKAKARALKRVVGDPfkkgvEQGPQ----IDSEQFEKIlryikSGVESGATLECGG-----DRfgskgyYIQPTVF 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 325 TDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTAngNLP 404
Cdd:PLN02466 424 SNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDA--AIP 501
|
330 340
....*....|....*....|....*...
gi 2552840633 405 FGGIGNSGMGAYHGRESFETFSYCRSIV 432
Cdd:PLN02466 502 FGGYKMSGIGREKGIYSLNNYLQVKAVV 529
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
105-420 |
4.05e-33 |
|
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: 130.59 E-value: 4.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 105 YEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC--FEEEYIAVTDADRETTELLLQE 182
Cdd:cd07111 145 WKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAglPPGVLNIVTGNGSFGSALANHP 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 183 RFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQDK 262
Cdd:cd07111 225 GVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 263 LTEYICDEITR-QYGENPQQSPDYPRIVNARHFDRLSALLSHGT-----ILCGGTSDPADR-YIAPTLLTDIPLQSPLLT 335
Cdd:cd07111 305 LIRKLKERMSHlRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRaegadVFQPGADLPSKGpFYPPTLFTNVPPASRIAQ 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 336 DEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTivqtangNL-----PFGGIGN 410
Cdd:cd07111 385 EEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGH-------NLfdaaaGFGGYRE 457
|
330
....*....|
gi 2552840633 411 SGMGAYHGRE 420
Cdd:cd07111 458 SGFGREGGKE 467
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
99-414 |
8.65e-33 |
|
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: 129.46 E-value: 8.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 99 SKSRIHY---EPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVTDADRE 174
Cdd:cd07148 113 SAGRIAFttrEPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAgLPEGWCQAVPCENA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 175 TTELLLQE-RFDYIFYTGGVEYGRHVMQAASRHlTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYL 253
Cdd:cd07148 193 VAEKLVTDpRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRV 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 254 MVHHKVQDKLTEYICDEITRQYGENP-----QQSPdyprIVNARHFDRLS-----ALLSHGTILCGGtSDPADRYIAPTL 323
Cdd:cd07148 272 FVPAEIADDFAQRLAAAAEKLVVGDPtdpdtEVGP----LIRPREVDRVEewvneAVAAGARLLCGG-KRLSDTTYAPTV 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 324 LTDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDtivQTA--NG 401
Cdd:cd07148 347 LLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVND---HTAfrVD 423
|
330
....*....|...
gi 2552840633 402 NLPFGGIGNSGMG 414
Cdd:cd07148 424 WMPFAGRRQSGYG 436
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
105-414 |
1.53e-32 |
|
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: 129.11 E-value: 1.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 105 YEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECFEEEYIAVTD-ADRETTE-LLLQE 182
Cdd:cd07116 134 HEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNgFGLEAGKpLASSK 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 183 RFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIV-------DDDADLKATARRIVWGkfLNCGQTCVAPDYLMV 255
Cdd:cd07116 214 RIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPNIFfadvmdaDDAFFDKALEGFVMFA--LNQGEVCTCPSRALI 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 256 HHKVQDKLTEYICDEITRQYGENPQqspDYPRIVNAR-HFDRLSALLSH--------GTILCGG-----TSDPADRYIAP 321
Cdd:cd07116 292 QESIYDRFMERALERVKAIKQGNPL---DTETMIGAQaSLEQLEKILSYidigkeegAEVLTGGernelGGLLGGGYYVP 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 322 TLLTDiPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTANG 401
Cdd:cd07116 369 TTFKG-GNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHA 447
|
330
....*....|...
gi 2552840633 402 nlPFGGIGNSGMG 414
Cdd:cd07116 448 --AFGGYKQSGIG 458
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
105-422 |
2.82e-32 |
|
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: 128.02 E-value: 2.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 105 YEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVTDADRETTELLLQE- 182
Cdd:cd07085 134 RQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAgLPDGVLNVVHGGKEAVNALLDHp 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 183 RFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQDK 262
Cdd:cd07085 214 DIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 263 LTEYICDEITR-QYGENPQQSPDYPRIVNARHFDRLSALLSHG-----TILCGGTSDPADRY-----IAPTLLTDIPLQS 331
Cdd:cd07085 294 WIPKLVERAKKlKVGAGDDPGADMGPVISPAAKERIEGLIESGveegaKLVLDGRGVKVPGYengnfVGPTILDNVTPDM 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 332 PLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTI-VQTAngNLPFGGIGN 410
Cdd:cd07085 374 KIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIpVPLA--FFSFGGWKG 451
|
330
....*....|....
gi 2552840633 411 SGMGAYH--GRESF 422
Cdd:cd07085 452 SFFGDLHfyGKDGV 465
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
11-414 |
3.70e-29 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 119.20 E-value: 3.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 11 VKLQKAFFNEHITREIPFRLCALDRLAEALVSREKQLGEALHADLGKSAFESYAteigfllhEIRTIKNhLQSWARDR-- 88
Cdd:PRK13968 35 LQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARA--------EVAKSAN-LCDWYAEHgp 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 89 --RRPTPLFLFGSKSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPsgeAPRTAAALQeLIDECFEEEYI 166
Cdd:PRK13968 106 amLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKH---APNVMGCAQ-LIAQVFKDAGI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 167 A-----VTDADRETTELLLQE-RFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKF 240
Cdd:PRK13968 182 PqgvygWLNADNDGVSQMINDsRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 241 LNCGQTCVAPDYLMVHHKVQDKLTEYICDEITRQYGENPQQSPDY--PRivnARhFD-------RLSALLSHG-TILCGG 310
Cdd:PRK13968 262 QNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENAlgPM---AR-FDlrdelhhQVEATLAEGaRLLLGG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 311 TS-DPADRYIAPTLLTDIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGA 389
Cdd:PRK13968 338 EKiAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGV 417
|
410 420
....*....|....*....|....*
gi 2552840633 390 CINDtiVQTANGNLPFGGIGNSGMG 414
Cdd:PRK13968 418 FING--YCASDARVAFGGVKKSGFG 440
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
91-415 |
2.68e-28 |
|
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: 117.30 E-value: 2.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 91 PTPLFLFGSKSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVT 169
Cdd:cd07125 151 PELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAgVPRDVLQLV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 170 DADRETT--ELLLQERFDYIFYTGGVEYGRHVMQA-ASRH--LTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCG 244
Cdd:cd07125 231 PGDGEEIgeALVAHPRIDGVIFTGSTETAKLINRAlAERDgpILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAG 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 245 QTCVAPDYLMVHHKVQDKLTEYICDEITrqygenpQQSPDYPR--------IVNARHFDRLSALL----SHGTILCGGTS 312
Cdd:cd07125 311 QRCSALRLLYLQEEIAERFIEMLKGAMA-------SLKVGDPWdlstdvgpLIDKPAGKLLRAHTelmrGEAWLIAPAPL 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 313 DPAD-RYIAPTLLTDIplQSPLLTDEIFGPILPVLPFD--DIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGA 389
Cdd:cd07125 384 DDGNgYFVAPGIIEIV--GIFDLTTEVFGPILHVIRFKaeDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNL 461
|
330 340
....*....|....*....|....*.
gi 2552840633 390 CINDTIVQTANGNLPFGGIGNSGMGA 415
Cdd:cd07125 462 YINRNITGAIVGRQPFGGWGLSGTGP 487
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
105-377 |
1.22e-27 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 115.00 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 105 YEPYGCALIIAPWNYPL-----QLALspligAIAAGNCAIVKPSGEAPRTAAALQELIDECFEEEYI-----AVTDADRE 174
Cdd:cd07130 130 WNPLGVVGVITAFNFPVavwgwNAAI-----ALVCGNVVVWKPSPTTPLTAIAVTKIVARVLEKNGLpgaiaSLVCGGAD 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 175 TTELLLQ-ERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYL 253
Cdd:cd07130 205 VGEALVKdPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 254 MVHHKVQDKLTEyicdEITRQYGE----NP-QQSPDYPRIVNARHFDRLSALL-----SHGTILCGGTS-DPADRYIAPT 322
Cdd:cd07130 285 IVHESIYDEVLE----RLKKAYKQvrigDPlDDGTLVGPLHTKAAVDNYLAAIeeaksQGGTVLFGGKViDGPGNYVEPT 360
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2552840633 323 LLTdIPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRA 377
Cdd:cd07130 361 IVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNA 414
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
107-432 |
1.06e-26 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 112.16 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 107 PYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPsgeaPRTAAALQELIDECFEEEYI------AVTDADRETTELLL 180
Cdd:PLN00412 158 PLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKP----PTQGAVAALHMVHCFHLAGFpkglisCVTGKGSEIGDFLT 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 181 QER-FDYIFYTGGvEYGRHVMQAASrhLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKV 259
Cdd:PLN00412 234 MHPgVNCISFTGG-DTGIAISKKAG--MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 260 QDKLTEYICDEITRQYGENPQQSPDYPRIVNARHFDRLSALL----SHGTILCGGTSDPADrYIAPTLLTDIPLQSPLLT 335
Cdd:PLN00412 311 ADALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVmdakEKGATFCQEWKREGN-LIWPLLLDNVRPDMRIAW 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 336 DEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTivqTANG--NLPFGGIGNSGM 413
Cdd:PLN00412 390 EEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSA---PARGpdHFPFQGLKDSGI 466
|
330
....*....|....*....
gi 2552840633 414 GAYHGRESFETFSYCRSIV 432
Cdd:PLN00412 467 GSQGITNSINMMTKVKSTV 485
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
29-418 |
6.88e-25 |
|
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: 106.92 E-value: 6.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 29 RLCALDRLAEALVSREKQLGEALHADLGKSAFESYAteigfllhEIRTIKNHLQSWARDRRRPTPLFlfgsksriHYEPY 108
Cdd:TIGR01238 98 RAAKLDRLADLLELHMPELMALCVREAGKTIHNAIA--------EVREAVDFCRYYAKQVRDVLGEF--------SVESR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 109 GCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVTDADRET--TELLLQERFD 185
Cdd:TIGR01238 162 GVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAgFPAGTIQLLPGRGADvgAALTSDPRIA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 186 YIFYTGGVEYGRHVMQA-ASRHLTPVTL--ELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQDK 262
Cdd:TIGR01238 242 GVAFTGSTEVAQLINQTlAQREDAPVPLiaETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADR 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 263 LTEYICDEITRQYGENP-QQSPDYPRIVNA-------RHFDRLSALLS--HGTILCGGTSDPADRYIAPTLLTDIPLQSp 332
Cdd:TIGR01238 322 VLTMIQGAMQELKVGVPhLLTTDVGPVIDAeakqnllAHIEHMSQTQKkiAQLTLDDSRACQHGTFVAPTLFELDDIAE- 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 333 lLTDEIFGPILPVLPF--DDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTANGNLPFGGIGN 410
Cdd:TIGR01238 401 -LSEEVFGPVLHVVRYkaRELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFGGQGL 479
|
....*...
gi 2552840633 411 SGMGAYHG 418
Cdd:TIGR01238 480 SGTGPKAG 487
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
98-418 |
4.05e-24 |
|
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: 104.24 E-value: 4.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 98 GSKSRIHYE--PYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC--FEEEYIAVTDADR 173
Cdd:cd07084 89 GLKQQSHGYrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAglLPPEDVTLINGDG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 174 ETTE-LLLQERFDYIFYTGGVEYGRHVmqAASRHLTPVTLELGGKSPCIVDDDAD-LKATARRIVWGKFLNCGQTCVAPD 251
Cdd:cd07084 169 KTMQaLLLHPNPKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQS 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 252 YLMVHHKVQ-DKLTEYICDEITRQYGEN----PQQSPDYPRIVNARHFDRLSALLSHGTILcggTSDPADRYIAPTLLTD 326
Cdd:cd07084 247 MLFVPENWSkTPLVEKLKALLARRKLEDlllgPVQTFTTLAMIAHMENLLGSVLLFSGKEL---KNHSIPSIYGACVASA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 327 IPLQS-------PLLTDEIFGPILPVlpfddiddcVEYVNDREkPLALyyftrskKRARYMIQHTTSGGACINDTIVQ-- 397
Cdd:cd07084 324 LFVPIdeilktyELVTEEIFGPFAIV---------VEYKKDQL-ALVL-------ELLERMHGSLTAAIYSNDPIFLQel 386
|
330 340
....*....|....*....|....*..
gi 2552840633 398 ----TANGNLPFGGIGNSGM--GAYHG 418
Cdd:cd07084 387 ignlWVAGRTYAILRGRTGVapNQNHG 413
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
29-412 |
3.77e-23 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 101.57 E-value: 3.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 29 RLCALDRLAEALVSREKQLGEALHADLGKSAFESyATEIGFLlheIRTIKNHLQSWAR---DRRRPTPlflfGSKSRIHY 105
Cdd:PRK09457 61 RQAIVERFAALLEENKEELAEVIARETGKPLWEA-ATEVTAM---INKIAISIQAYHErtgEKRSEMA----DGAAVLRH 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 106 EPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAaalqELIDECFEE-----EYIAVTDADRETTELLL 180
Cdd:PRK09457 133 RPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVA----ELTVKLWQQaglpaGVLNLVQGGRETGKALA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 181 QER-FDYIFYTGGVEYGRHV-MQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHK 258
Cdd:PRK09457 209 AHPdIDGLLFTGSANTGYLLhRQFAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 259 VQ-----DKLTEyICDEIT-RQYGENPQqsPDYPRIVNARHFDRLSA----LLSHG--TILCGGTSDPADRYIAPTLLtD 326
Cdd:PRK09457 289 AQgdaflARLVA-VAKRLTvGRWDAEPQ--PFMGAVISEQAAQGLVAaqaqLLALGgkSLLEMTQLQAGTGLLTPGII-D 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 327 IPLQSPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGgacindtIV----QT--AN 400
Cdd:PRK09457 365 VTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAG-------IVnwnkPLtgAS 437
|
410
....*....|..
gi 2552840633 401 GNLPFGGIGNSG 412
Cdd:PRK09457 438 SAAPFGGVGASG 449
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
98-414 |
1.53e-18 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 88.72 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 98 GSKSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVTDADRETT 176
Cdd:PRK11904 675 GESNELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAgIPKDVLQLLPGDGATV 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 177 --ELLLQERFDYIFYTGGVEYGRHVMQA-ASRHLTPVTL--ELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPD 251
Cdd:PRK11904 755 gaALTADPRIAGVAFTGSTETARIINRTlAARDGPIVPLiaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALR 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 252 YLMVHHKVQDKLTEYIC---DEITrqYGeNPQQ-SPDYPRIVNARHFDRLSALLSH----GTILCGGTSDPADR---YIA 320
Cdd:PRK11904 835 VLFVQEDIADRVIEMLKgamAELK--VG-DPRLlSTDVGPVIDAEAKANLDAHIERmkreARLLAQLPLPAGTEnghFVA 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 321 PTLltdIPLQSP-LLTDEIFGPILPVLPF--DDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQ 397
Cdd:PRK11904 912 PTA---FEIDSIsQLEREVFGPILHVIRYkaSDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIG 988
|
330
....*....|....*..
gi 2552840633 398 TANGNLPFGGIGNSGMG 414
Cdd:PRK11904 989 AVVGVQPFGGQGLSGTG 1005
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
105-425 |
1.05e-15 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 79.11 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 105 YEPYGCALIIAPWNYPLQ-LALSPLIgAIAAGNCAIVKPSGEAPRTAAALQELIDECFEEE------YIAVTDADRETTE 177
Cdd:PLN02315 152 WNPLGIVGVITAFNFPCAvLGWNACI-ALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNnlpgaiFTSFCGGAEIGEA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 178 LLLQERFDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHH 257
Cdd:PLN02315 231 IAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 258 KVQDKLTEYICDEITRQYGENPQQS-----PDYPRIVNARHFDRLSALLSHG-TILCGGTS-DPADRYIAPTLLtDIPLQ 330
Cdd:PLN02315 311 SIYDDVLEQLLTVYKQVKIGDPLEKgtllgPLHTPESKKNFEKGIEIIKSQGgKILTGGSAiESEGNFVQPTIV-EISPD 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 331 SPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTI-VQTANGNLPFGGIG 409
Cdd:PLN02315 390 ADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVNVNIpTNGAEIGGAFGGEK 469
|
330
....*....|....*.
gi 2552840633 410 NSGMGAYHGRESFETF 425
Cdd:PLN02315 470 ATGGGREAGSDSWKQY 485
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
105-414 |
2.23e-14 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 75.78 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 105 YEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAA-ALQELIDECFEEEYIAVTDADRET--TELLLQ 181
Cdd:PRK11809 766 HRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAqAVRILLEAGVPAGVVQLLPGRGETvgAALVAD 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 182 ERFDYIFYTGGVEYGRHVMQA-ASR-----HLTPVTLELGGKSPCIVDDDA-------DLKATArrivwgkFLNCGQTCV 248
Cdd:PRK11809 846 ARVRGVMFTGSTEVARLLQRNlAGRldpqgRPIPLIAETGGQNAMIVDSSAlteqvvaDVLASA-------FDSAGQRCS 918
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 249 APDYLMVHHKVQDKLTEYICDEITRQYGENPQQ-SPDYPRIVNA-------RHFDRL--------------SALLSHGTi 306
Cdd:PRK11809 919 ALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRlSTDIGPVIDAeakanieRHIQAMrakgrpvfqaarenSEDWQSGT- 997
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 307 lcggtsdpadrYIAPTLltdIPLQS-PLLTDEIFGPILPVLPF--DDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQH 383
Cdd:PRK11809 998 -----------FVPPTL---IELDSfDELKREVFGPVLHVVRYnrNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGS 1063
|
330 340 350
....*....|....*....|....*....|.
gi 2552840633 384 TTSGGACINDTIVQTANGNLPFGGIGNSGMG 414
Cdd:PRK11809 1064 AHVGNLYVNRNMVGAVVGVQPFGGEGLSGTG 1094
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
106-431 |
7.29e-14 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 73.63 E-value: 7.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 106 EPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDEC-FEEEYIAVTDADRETTELLL-QER 183
Cdd:PLN02419 248 EPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAgLPDGVLNIVHGTNDTVNAICdDED 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 184 FDYIFYTGGVEYGRHVMQAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMV---HHKVQ 260
Cdd:PLN02419 328 IRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFvgdAKSWE 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 261 DKLTEYiCDEITRQYGENPqqSPDYPRIVNARHFDRLSALLSHGT-----ILCGGTSDPADRY-----IAPTLLTDIPLQ 330
Cdd:PLN02419 408 DKLVER-AKALKVTCGSEP--DADLGPVISKQAKERICRLIQSGVddgakLLLDGRDIVVPGYekgnfIGPTILSGVTPD 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 331 SPLLTDEIFGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGACINDTIVQTangnLPFGGI-G 409
Cdd:PLN02419 485 MECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVP----LPFFSFtG 560
|
330 340
....*....|....*....|....*.
gi 2552840633 410 NSGMGA----YHGRESFETFSYCRSI 431
Cdd:PLN02419 561 NKASFAgdlnFYGKAGVDFFTQIKLV 586
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
84-356 |
2.40e-13 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 72.13 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 84 WARDRRRPTPLFLfgsKSRIHYEPYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECFEE 163
Cdd:cd07127 173 WEKPQGKHDPLAM---EKTFTVVPRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAAILPLAITVQVAREVLAE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 164 --------EYIAVTDADRETTELLLQERFDYIFYTGGVEYGRHVMQAASRHLtpVTLELGGKSPCIVDDDADLKATARRI 235
Cdd:cd07127 250 agfdpnlvTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANARQAQ--VYTEKAGVNTVVVDSTDDLKAMLRNL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 236 VWGKFLNCGQTCVAPDYLMV---------HHKVQDKLTEYICDEITRQYGENPQQSPDYPRIVNARHFDRLSALLSHGTI 306
Cdd:cd07127 328 AFSLSLYSGQMCTTPQNIYVprdgiqtddGRKSFDEVAADLAAAIDGLLADPARAAALLGAIQSPDTLARIAEARQLGEV 407
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2552840633 307 LCGGTSD-----PADRYIAPTLLTDIPLQSPLLTDEIFGPILPVLPFDDIDDCVE 356
Cdd:cd07127 408 LLASEAVahpefPDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIE 462
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
98-412 |
2.10e-12 |
|
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: 68.77 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 98 GSKSRIHYEPY-GCALIIAPWNYP---LQLALSPLIgaiaAGNCAIVKPSGeaprTAAALQELIDECFEEeyiA------ 167
Cdd:cd07123 160 GVWNRLEYRPLeGFVYAVSPFNFTaigGNLAGAPAL----MGNVVLWKPSD----TAVLSNYLVYKILEE---Aglppgv 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 168 ---VTDADRETTELLLQ-ERFDYIFYTGGVEYGRHVMQAASRHLT-----P-VTLELGGKSPCIVDDDADLKATARRIVW 237
Cdd:cd07123 229 infVPGDGPVVGDTVLAsPHLAGLHFTGSTPTFKSLWKQIGENLDryrtyPrIVGETGGKNFHLVHPSADVDSLVTATVR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 238 GKFLNCGQTCVAPDYLMVHHKVQDKLTEYICDEITR-QYGeNPQqspDYPRIVNA----RHFDRLSALLSH------GTI 306
Cdd:cd07123 309 GAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEiKMG-DPD---DFSNFMGAvideKAFDRIKGYIDHaksdpeAEI 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 307 LCGGTSDPADRY-IAPT-LLTDIPlQSPLLTDEIFGPILPVLPFDD---------IDDCVEY-------VNDREkplALY 368
Cdd:cd07123 385 IAGGKCDDSVGYfVEPTvIETTDP-KHKLMTEEIFGPVLTVYVYPDsdfeetlelVDTTSPYaltgaifAQDRK---AIR 460
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2552840633 369 yftRSKKRARYmiqhtTSGGACIND----TIVqtanGNLPFGGIGNSG 412
Cdd:cd07123 461 ---EATDALRN-----AAGNFYINDkptgAVV----GQQPFGGARASG 496
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
106-414 |
7.56e-12 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 67.58 E-value: 7.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 106 EPYGCALIIAPWNYPL-----QLAlspliGAIAAGNCAIVKPSGEAPRTAA--------------ALQelidecfeeeyi 166
Cdd:PRK11905 675 KPLGPVVCISPWNFPLaiftgQIA-----AALVAGNTVLAKPAEQTPLIAAravrllheagvpkdALQ------------ 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 167 AVTDADRETTELLLQ-ERFDYIFYTGGVEYGRHVMQA-ASRHLTPVTL--ELGGKSPCIVDDDA-------DLKATArri 235
Cdd:PRK11905 738 LLPGDGRTVGAALVAdPRIAGVMFTGSTEVARLIQRTlAKRSGPPVPLiaETGGQNAMIVDSSAlpeqvvaDVIASA--- 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 236 vwgkFLNCGQTCVAPDYLMVHHKVQDKLTEYIC---DEITrqYGeNPQQ-SPDY-PRI-VNAR-----HFDRLSAllsHG 304
Cdd:PRK11905 815 ----FDSAGQRCSALRVLCLQEDVADRVLTMLKgamDELR--IG-DPWRlSTDVgPVIdAEAQanieaHIEAMRA---AG 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 305 TIL---------CGGTsdpadrYIAPTL--LTDIPLqsplLTDEIFGPILPVLPF--DDIDDCVEYVNDREKPLALYYFT 371
Cdd:PRK11905 885 RLVhqlplpaetEKGT------FVAPTLieIDSISD----LEREVFGPVLHVVRFkaDELDRVIDDINATGYGLTFGLHS 954
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2552840633 372 RSKKRARYMIQHTTSGGACINDTIVQTANGNLPFGGIGNSGMG 414
Cdd:PRK11905 955 RIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTG 997
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
102-414 |
1.74e-11 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 66.50 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 102 RIHYEPYGCALIIAPWNYPL-----QLAlspliGAIAAGNCAIVKPSGEAPRTAA--------------ALQELIdecfe 162
Cdd:COG4230 675 PTVLRGRGVFVCISPWNFPLaiftgQVA-----AALAAGNTVLAKPAEQTPLIAAravrllheagvpadVLQLLP----- 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 163 eeyiavtdADRETT--ELLLQERFDYIFYTGGVEYGRHVMQA-ASRHLTPVTL--ELGGKSPCIVDddadlkATA----- 232
Cdd:COG4230 745 --------GDGETVgaALVADPRIAGVAFTGSTETARLINRTlAARDGPIVPLiaETGGQNAMIVD------SSAlpeqv 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 233 -RRIVWGKFLNCGQTCVAPDYLMVHHKVQDKLTEYIC---DEITrqYGeNPQQ-SPDY-PRI-VNAR-----HFDR---- 296
Cdd:COG4230 811 vDDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKgamAELR--VG-DPADlSTDVgPVIdAEARanleaHIERmrae 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 297 --------LSALLSHGTilcggtsdpadrYIAPTLltdIPLQSP-LLTDEIFGPILPVLPF--DDIDDCVEYVNDREKPL 365
Cdd:COG4230 888 grlvhqlpLPEECANGT------------FVAPTL---IEIDSIsDLEREVFGPVLHVVRYkaDELDKVIDAINATGYGL 952
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2552840633 366 ALYYFTRSKKRARYMIQHTTSGGACIN-DTI-----VQtangnlPFGGIGNSGMG 414
Cdd:COG4230 953 TLGVHSRIDETIDRVAARARVGNVYVNrNIIgavvgVQ------PFGGEGLSGTG 1001
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
36-269 |
2.26e-11 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 65.32 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 36 LAEALVSREKQLGEALHADLGKSAFESYATEIGFL-LHEIRTIKNH---LQSWARDRRRPTPLFLFGSKSRIHYEPYGCA 111
Cdd:cd07077 25 IANALYDTRQRLASEAVSERGAYIRSLIANWIAMMgCSESKLYKNIdteRGITASVGHIQDVLLPDNGETYVRAFPIGVT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 112 LIIAPWNYPLQLALSPLIGaIAAGNCAIVKPSGEAPRTAAALQELIDECF-----EEEYIAVTDADRETTELLLQ-ERFD 185
Cdd:cd07077 105 MHILPSTNPLSGITSALRG-IATRNQCIFRPHPSAPFTNRALALLFQAADaahgpKILVLYVPHPSDELAEELLShPKID 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 186 YIFYTGgveyGRHVMQAASRH--LTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNcGQTCVAPDYLMVHHKVQDKL 263
Cdd:cd07077 184 LIVATG----GRDAVDAAVKHspHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFD-QNACASEQNLYVVDDVLDPL 258
|
....*.
gi 2552840633 264 TEYICD 269
Cdd:cd07077 259 YEEFKL 264
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
54-389 |
2.95e-09 |
|
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: 58.82 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 54 DLGKSAfesyATEIGFLLHEIRTIKNHLQS---WARDRRRPTPLFLFGSK---SRIHYEPYGCALIIAPWNYPLQLALSP 127
Cdd:cd07081 40 DLAKLA----VSETGMGRVEDKVIKNHFAAeyiYNVYKDEKTCGVLTGDEnggTLIIAEPIGVVASITPSTNPTSTVIFK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 128 LIGAIAAGNCAIVKPSGEAPRTA--AA---LQELIDECFEEEYIA-VTDADRETTELLLQE-RFDYIFYTGGveygRHVM 200
Cdd:cd07081 116 SLISLKTRNSIIFSPHPRAKKVTqrAAtllLQAAVAAGAPENLIGwIDNPSIELAQRLMKFpGIGLLLATGG----PAVV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 201 QAASRHLTPVTLELGGKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQDKLTeyicDEITRQYGenpq 280
Cdd:cd07081 192 KAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDSVYDEVM----RLFEGQGA---- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 281 qspdypRIVNARHFDRLS-ALLSHGTILCGGTSDPADRyIAPTLLTDIPLQSPLLTDEI-------------FGPILPVL 346
Cdd:cd07081 264 ------YKLTAEELQQVQpVILKNGDVNRDIVGQDAYK-IAAAAGLKVPQETRILIGEVtslaehepfahekLSPVLAMY 336
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 347 PFDDIDDCVE-----------------YVNDREKPLALYYFTRSKKRARYMIQHTTSGGA 389
Cdd:cd07081 337 RAANFADADAkalalkleggcghtsamYSDNIKAIENMNQFANAMKTSRFVKNGPCSQGG 396
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
54-357 |
5.26e-07 |
|
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: 51.85 E-value: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 54 DLGKSAFESyaTEIGFLLHEIrtIKNHLQSwardRRRPTPLFLF-------GSKSRIHYEPYGCALIIAPWNYPLQLALS 126
Cdd:cd07121 45 ELAEMAVEE--TGMGRVEDKI--AKNHLAA----EKTPGTEDLTttawsgdNGLTLVEYAPFGVIGAITPSTNPTETIIN 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 127 PLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECFEEE------YIAVTDADRETTELLLQ-ERFDYIFYTGGVEYGRHV 199
Cdd:cd07121 117 NSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAIAEAggpdnlVVTVEEPTIETTNELMAhPDINLLVVTGGPAVVKAA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 200 MQAASRhltpvtlELG---GKSPCIVDDDADLKATARRIVWGKFLNCGQTCVAPDYLMVHHKVQDKLTEYICDE----IT 272
Cdd:cd07121 197 LSSGKK-------AIGagaGNPPVVVDETADIEKAARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAAMQRNgayvLN 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 273 RQYGENPQQS--PDYPRIVNARHFDRLSAllshGTIL--CGGTSDPADRYIaptlLTDIPLQSPLLTDEIFGPILPVLPF 348
Cdd:cd07121 270 DEQAEQLLEVvlLTNKGATPNKKWVGKDA----SKILkaAGIEVPADIRLI----IVETDKDHPFVVEEQMMPILPVVRV 341
|
....*....
gi 2552840633 349 DDIDDCVEY 357
Cdd:cd07121 342 KNFDEAIEL 350
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
107-350 |
1.19e-04 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 44.41 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 107 PYGCALIIAPWNYPLQLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECfeeeYIAVTDAD------RETTELLL 180
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLC----GMPATDVDlihsdgPTMNKILL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 181 QERFDYIFYTGGveygrhvmQAASRHLTPVT-----LELGGKSPCIVDDD-ADLKATARRIVWGKFLNCGQTCVAPDYLM 254
Cdd:cd07126 218 EANPRMTLFTGS--------SKVAERLALELhgkvkLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILF 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 255 VHHK-VQDKLTEYICDEITRQYGEN----PQQSPDYPRIVNarHFDRLSA------------LLSHGTILCGGTSDPADR 317
Cdd:cd07126 290 AHENwVQAGILDKLKALAEQRKLEDltigPVLTWTTERILD--HVDKLLAipgakvlfggkpLTNHSIPSIYGAYEPTAV 367
|
250 260 270
....*....|....*....|....*....|...
gi 2552840633 318 YIaPTLLTDIPLQSPLLTDEIFGPILPVLPFDD 350
Cdd:cd07126 368 FV-PLEEIAIEENFELVTTEVFGPFQVVTEYKD 399
|
|
| LuxC |
pfam05893 |
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ... |
101-389 |
1.87e-04 |
|
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) proteins. The channelling of fatty acids into the fatty aldehyde substrate for the bacterial bioluminescence reaction is catalyzed by a fatty acid reductase multienzyme complex, which channels fatty acids through the thioesterase (LuxD), synthetase (LuxE) and reductase (LuxC) components.
Pssm-ID: 399113 Cd Length: 401 Bit Score: 43.58 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 101 SRIHYEPYGCALIIAPWNYPLqLALSPLIGAIAAGNCAIVKPSGEAPRTAAA-LQELIDECFEEE---YIAVTDADRETT 176
Cdd:pfam05893 82 SYEKAFPPGLVFHVLSGNVPL-LPVMSILMGLLVKNVNLLKVSSSDPFTAAAlLASFADLDPTHPladSLSVVYWDGGST 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 177 EL--LLQERFDYIFYTGgveyGRHVMQAASRHLTPVT--LELGGK-SPCIVDDDADLKATARRI-----VWGKflncgQT 246
Cdd:pfam05893 161 QLedLIVANADVVIAWG----GEDAINAIRECLKPGKqwIDFGAKiSFAVVDREAALDKAAERAaddicVFDQ-----QA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 247 CVAPDYLMVH-------HKVQDKLTEYIcDEITRQYgenPQQSPDY---PRIVNARHFDRLSALLSHGTilcGGTSDPAD 316
Cdd:pfam05893 232 CLSPQTVFVEsddkitpDEFAERLAAAL-AKRARIL---PKAVLDIdeaAKISSDRAECKLDYAFAGER---GVWSDFHQ 304
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2552840633 317 RYIAPTLLTDIPLQSPLltdeifGPILPVLPFDDIDDCVEYVNDREKPLALYYFTRSKKRARYMIQHTTSGGA 389
Cdd:pfam05893 305 RWTVIWSDGQEELNSPL------NRTVNVVPVPSLSDVVRYVSENRTYLQTCGLAPYSGRLPYLDRKLALAGV 371
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
295-419 |
3.98e-04 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 42.64 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 295 DRLSALLSHGTILCGGTSDP----ADR----YIAPTLLT-DIPLQSPLLTD-EIFGPILPVLPFDDIDDCVEYVNDREKP 364
Cdd:cd07128 345 AAVATLLAEAEVVFGGPDRFevvgADAekgaFFPPTLLLcDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGS 424
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2552840633 365 LALYYFTRSKKRARYMIQhttsggacindtivqtangnlpfggignsGMGAYHGR 419
Cdd:cd07128 425 LVASVVTNDPAFARELVL-----------------------------GAAPYHGR 450
|
|
| ALDH_Acyl-CoA-Red_LuxC |
cd07080 |
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase ... |
87-359 |
1.72e-03 |
|
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase enzyme responsible for synthesis of the aldehyde substrate for the luminescent reaction catalyzed by luciferase. The fatty acid reductase, a luminescence-specific, multienzyme complex (LuxCDE), reduces myristic acid to generate the long chain fatty aldehyde required for the luciferase-catalyzed reaction resulting in the emission of blue-green light. Mutational studies of conserved cysteines of LuxC revealed that the cysteine which aligns with the catalytic cysteine conserved throughout the ALDH superfamily is the LuxC acylation site. This CD is composed of mainly bacterial sequences but also includes a few archaeal sequences similar to the Methanospirillum hungateiacyl acyl-CoA reductase RfbN.
Pssm-ID: 143399 Cd Length: 422 Bit Score: 40.72 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 87 DRRRPTplflfGSKSRIHYEPYGCALIIAPWNYPLqLALSPLIGAIAAGNCAIVKPSGEAPRTAAALQELIDECFEEEYI 166
Cdd:cd07080 97 DEWVPP-----GRGGYIRAQPRGLVVHIIAGNVPL-LPVWSIVRGLLVKNVNLLKMSSSDPLTATALLRSLADVDPNHPL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 167 A---------VTDADRETTELLLQerfDYIFYTGGVEYGRHVMQaasrhLTPVTLEL---GGK-SPCIVDDDA----DLK 229
Cdd:cd07080 171 TdsisvvywpGGDAELEERILASA---DAVVAWGGEEAVKAIRS-----LLPPGCRLidfGPKySFAVIDREAleseKLA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2552840633 230 ATARRIVWG-KFLNcGQTCVAPDYLMVhhkvqDKLTEYICDEITRQYG---ENPQQSPDYPRIVNARH----FDRLSALL 301
Cdd:cd07080 243 EVADALAEDiCRYD-QQACSSPQVVFV-----EKDDDEELREFAEALAaalERLPRRYPALSLSAAESakiaRARLEAEF 316
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2552840633 302 SHGTilcGGTSDPADRYIAptLLTDIPLQSPLLTDEIFgpilpVLPFDDIDDCVEYVN 359
Cdd:cd07080 317 YELK---GGVSRDLGWTVI--ISDEIGLEASPLNRTVN-----VKPVASLDDVLRPVT 364
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
297-358 |
2.75e-03 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 40.07 E-value: 2.75e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2552840633 297 LSALLSHGTILCGGT------SDPADRY-IAPTLL-TDIPLQSPLLTD-EIFGPILPVLPFDDIDDCVEYV 358
Cdd:PRK11903 351 LAALRAQAEVLFDGGgfalvdADPAVAAcVGPTLLgASDPDAATAVHDvEVFGPVATLLPYRDAAHALALA 421
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