|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
5-444 |
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: 833.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEWVTAKPV 84
Cdd:cd07132 4 VRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKPEPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 85 KKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVIN 164
Cdd:cd07132 84 KKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYPVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 165 GGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAP 244
Cdd:cd07132 164 GGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 245 DYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLEGQKIAFGGETDEATRYIAPTVLTDVDPK 324
Cdd:cd07132 244 DYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVLTDVKPS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 325 TKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGS 404
Cdd:cd07132 324 DPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGGVGN 403
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1595488123 405 SGMGAYHGKHSFDTFSHQRPCLLKSLKREGANKLRYPPNS 444
Cdd:cd07132 404 SGMGAYHGKYSFDTFSHKRSCLVKSLNMEKLNSLRYPPYS 443
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
5-426 |
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: 721.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEWVTAKPV 84
Cdd:cd07087 4 VARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKPRRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 85 KKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVIN 164
Cdd:cd07087 84 SVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVAVVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 165 GGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAP 244
Cdd:cd07087 164 GGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 245 DYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLEGQKIAFGGETDEATRYIAPTVLTDVDPK 324
Cdd:cd07087 244 DYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGKVVIGGQVDKEERYIAPTILDDVSPD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 325 TKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGS 404
Cdd:cd07087 324 SPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGGVGN 403
|
410 420
....*....|....*....|..
gi 1595488123 405 SGMGAYHGKHSFDTFSHQRPCL 426
Cdd:cd07087 404 SGMGAYHGKAGFDTFSHLKSVL 425
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
5-458 |
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: 656.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEWVTAKPV 84
Cdd:cd07136 4 VEKQRAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKPKRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 85 KKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVIN 164
Cdd:cd07136 84 KTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVAVVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 165 GGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAP 244
Cdd:cd07136 164 GGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 245 DYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLEGQKIAFGGETDEATRYIAPTVLTDVDPK 324
Cdd:cd07136 244 DYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGKIVFGGNTDRETLYIEPTILDNVTWD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 325 TKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGS 404
Cdd:cd07136 324 DPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYLPFGGVGN 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1595488123 405 SGMGAYHGKHSFDTFSHQRPCLLKSLKREgaNKLRYPPNSqskvdwGKFFLLKR 458
Cdd:cd07136 404 SGMGSYHGKYSFDTFSHKKSILKKSTWFD--LPLRYPPYK------GKKKKLKK 449
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
5-447 |
0e+00 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 649.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEWVTAKPV 84
Cdd:PTZ00381 13 VKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEYLKPEKV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 85 KKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVIN 164
Cdd:PTZ00381 93 DTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPSYVRVIE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 165 GGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAP 244
Cdd:PTZ00381 173 GGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 245 DYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLE--GQKIAFGGETDEATRYIAPTVLTDVD 322
Cdd:PTZ00381 253 DYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKdhGGKVVYGGEVDIENKYVAPTIIVNPD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 323 PKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGV 402
Cdd:PTZ00381 333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGGV 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1595488123 403 GSSGMGAYHGKHSFDTFSHQRPCLLKSLKREGANKLRYPPNSQSK 447
Cdd:PTZ00381 413 GNSGMGAYHGKYGFDTFSHPKPVLNKSTGNSFDLSLRYPPYTSFK 457
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
5-424 |
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: 613.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEWVTAKPV 84
Cdd:cd07135 11 HSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKKWAKDEKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 85 KKNVLT-MLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVI 163
Cdd:cd07135 91 KDGPLAfMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLDPDAFQVV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 164 NGGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIA 243
Cdd:cd07135 171 QGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 244 PDYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLE--GQKIAFGGETDEATRYIAPTVLTDV 321
Cdd:cd07135 251 PDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDttKGKVVIGGEMDEATRFIPPTIVSDV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 322 DPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGG 401
Cdd:cd07135 331 SWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAPFGG 410
|
410 420
....*....|....*....|...
gi 1595488123 402 VGSSGMGAYHGKHSFDTFSHQRP 424
Cdd:cd07135 411 VGDSGYGAYHGKYGFDTFTHERT 433
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
9-426 |
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: 545.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 9 RQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEWVTAKPVKKNV 88
Cdd:cd07134 8 QAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKPKRVRTPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 89 LTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVINGGVE 168
Cdd:cd07134 88 LLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFEGDAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 169 ETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYIL 248
Cdd:cd07134 168 VAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 249 CEASLQNQIVWKIKETVKEFYGEN--IKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEATRYIAPTVLTDV 321
Cdd:cd07134 248 VHESVKDAFVEHLKAEIEKFYGKDaaRKASPDLARIVNDRHFDRLKGLLDdavakGAKVEFGGQFDAAQRYIAPTVLTNV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 322 DPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGG 401
Cdd:cd07134 328 TPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNPNLPFGG 407
|
410 420
....*....|....*....|....*
gi 1595488123 402 VGSSGMGAYHGKHSFDTFSHQRPCL 426
Cdd:cd07134 408 VNNSGIGSYHGVYGFKAFSHERAVL 432
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
2-426 |
0e+00 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 529.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 2 ELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEWVTA 81
Cdd:cd07137 2 PRLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 82 KPVKKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYI 161
Cdd:cd07137 82 EKVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 162 VINGGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNC-GQT 240
Cdd:cd07137 162 VIEGGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCNnGQA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 241 CIAPDYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLE----GQKIAFGGETDEATRYIAPT 316
Cdd:cd07137 242 CIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDdpsvADKIVHGGERDEKNLYIEPT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 317 VLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNS 396
Cdd:cd07137 322 ILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDT 401
|
410 420 430
....*....|....*....|....*....|
gi 1595488123 397 FPFGGVGSSGMGAYHGKHSFDTFSHQRPCL 426
Cdd:cd07137 402 LPFGGVGESGFGAYHGKFSFDAFSHKKAVL 431
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
7-424 |
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: 525.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 7 RVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADL-CKSEFNVYSQEVITVLGEIDFMLENLPEWVTAKPVK 85
Cdd:cd07133 6 RQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFgHRSRHETLLAEILPSIAGIKHARKHLKKWMKPSRRH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 86 KNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVING 165
Cdd:cd07133 86 VGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEVAVVTG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 166 GVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPD 245
Cdd:cd07133 166 GADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 246 YILCEASLQNQIVWKIKETVKEFYGeNIKESPDYERIINLRHFKRILSLLE-----GQKI---AFGGETDEATRYIAPTV 317
Cdd:cd07133 246 YVLVPEDKLEEFVAAAKAAVAKMYP-TLADNPDYTSIINERHYARLQGLLEdarakGARVielNPAGEDFAATRKLPPTL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 318 LTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSF 397
Cdd:cd07133 325 VLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHVAQDDL 404
|
410 420
....*....|....*....|....*..
gi 1595488123 398 PFGGVGSSGMGAYHGKHSFDTFSHQRP 424
Cdd:cd07133 405 PFGGVGASGMGAYHGKEGFLTFSHAKP 431
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
5-448 |
3.37e-160 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 462.66 E-value: 3.37e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEWVTAKPV 84
Cdd:PLN02203 12 VAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSNLKKWMAPKKA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 85 KKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVIN 164
Cdd:PLN02203 92 KLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAVKVIE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 165 GGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYID---KDCDLDIVCRRITWGKYMNC-GQT 240
Cdd:PLN02203 172 GGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGSCaGQA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 241 CIAPDYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLEGQKIA----FGGETDEATRYIAPT 316
Cdd:PLN02203 252 CIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAasivHGGSIDEKKLFIEPT 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 317 VLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNS 396
Cdd:PLN02203 332 ILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYACDS 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1595488123 397 FPFGGVGSSGMGAYHGKHSFDTFSHQRPCLLKSLKREgaNKLRYPPNSQSKV 448
Cdd:PLN02203 412 LPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSLLTE--FEFRYPPWNDFKL 461
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
5-427 |
4.35e-139 |
|
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: 406.98 E-value: 4.35e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSefnvysqeVITVLGEIDFMLENL---PEWVTA 81
Cdd:cd07078 4 VAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKP--------IEEALGEVARAADTFryyAGLARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 82 KPVKKNVLTMLD-EAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDL 159
Cdd:cd07078 76 LHGEVIPSPDPGeLAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLPPGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 160 YIVINGGVEET-TELLKQ-RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNC 237
Cdd:cd07078 156 LNVVTGDGDEVgAALASHpRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 238 GQTCIAPDYILCEASLQNQIVWKIKETVKEFYGEN-IKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEAT- 310
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKVGNpLDPDTDMGPLISAAQLDRVLAYIEdakaeGAKLLCGGKRLEGGk 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 311 -RYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVI 389
Cdd:cd07078 316 gYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYS 395
|
410 420 430
....*....|....*....|....*....|....*...
gi 1595488123 390 MHFTLNsFPFGGVGSSGMGAYHGKHSFDTFSHQRPCLL 427
Cdd:cd07078 396 VGAEPS-APFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
5-457 |
8.33e-139 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 408.28 E-value: 8.33e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEWVTAKPV 84
Cdd:PLN02174 16 VTELRRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 85 KKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVIN 164
Cdd:PLN02174 96 KTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 165 GGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKY-MNCGQTCIA 243
Cdd:PLN02174 176 GAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACIS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 244 PDYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLE----GQKIAFGGETDEATRYIAPTVLT 319
Cdd:PLN02174 256 PDYILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDekevSDKIVYGGEKDRENLKIAPTILL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 320 DVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPF 399
Cdd:PLN02174 336 DVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPF 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1595488123 400 GGVGSSGMGAYHGKHSFDTFSHQRPCLLKSLKreGANKLRYPPNSQskvdwGKFFLLK 457
Cdd:PLN02174 416 GGVGESGMGAYHGKFSFDAFSHKKAVLYRSLF--GDSAVRYPPYSR-----GKLRLLK 466
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
6-427 |
2.18e-114 |
|
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: 341.52 E-value: 2.18e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 6 RRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEfnvysqevITVLGEIDFMLENL---PEWVTAK 82
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPI--------EEALGEVARAIDTFryaAGLADKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 83 PVKKNVLTMLD-EAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLY 160
Cdd:cd06534 73 GGPELPSPDPGgEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 161 IVING-GVEETTELLKQ-RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCG 238
Cdd:cd06534 153 NVVPGgGDEVGAALLSHpRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 239 QTCIAPDYILCEASLQNQIVWKIKetvkefygenikespdyeriinlrhfkrilsllegqkiafggetdeatryiapTVL 318
Cdd:cd06534 233 QICTAASRLLVHESIYDEFVEKLV-----------------------------------------------------TVL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 319 TDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSfP 398
Cdd:cd06534 260 VDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEA-P 338
|
410 420
....*....|....*....|....*....
gi 1595488123 399 FGGVGSSGMGAYHGKHSFDTFSHQRPCLL 427
Cdd:cd06534 339 FGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
5-423 |
2.29e-106 |
|
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: 324.77 E-value: 2.29e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSefnvysqeVITVLGEIDFMLENLpEWV--TAK 82
Cdd:COG1012 49 VAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKP--------LAEARGEVDRAADFL-RYYagEAR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 83 PVKKNVLTMLD---EAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQD 158
Cdd:COG1012 120 RLYGETIPSDApgtRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAgLPAG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 159 LYIVINGGVEETTELLKQ--RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMN 236
Cdd:COG1012 200 VLNVVTGDGSEVGAALVAhpDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGN 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 237 CGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGE--TDE 308
Cdd:COG1012 280 AGQRCTAASRLLVHESIYDEFVERLVAAAKALkVGDPLDPGTDMGPLISEAQLERVLAYIedavaEGAELLTGGRrpDGE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 309 ATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDV 388
Cdd:COG1012 360 GGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDG 439
|
410 420 430
....*....|....*....|....*....|....*
gi 1595488123 389 IMHFTLNsFPFGGVGSSGMGAYHGKHSFDTFSHQR 423
Cdd:COG1012 440 TTGAVPQ-APFGGVKQSGIGREGGREGLEEYTETK 473
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
5-423 |
2.29e-92 |
|
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: 288.28 E-value: 2.29e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSefnvysqeVITVLGEIDFMLENLPEWVTA--- 81
Cdd:pfam00171 35 IAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKP--------LAEARGEVDRAIDVLRYYAGLarr 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 82 -----KPVKKNVLtmldeAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-L 155
Cdd:pfam00171 107 ldgetLPSDPGRL-----AYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAgL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 156 DQDLYIVINGGVEETTELLKQ--RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGK 233
Cdd:pfam00171 182 PAGVLNVVTGSGAEVGEALVEhpDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 234 YMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGETD 307
Cdd:pfam00171 262 FGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLkVGDPLDPDTDMGPLISKAQLERVLKYVedakeEGAKLLTGGEAG 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 308 EAT-RYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGN 386
Cdd:pfam00171 342 LDNgYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWIN 421
|
410 420 430
....*....|....*....|....*....|....*..
gi 1595488123 387 DVIMhFTLNSFPFGGVGSSGMGAYHGKHSFDTFSHQR 423
Cdd:pfam00171 422 DYTT-GDADGLPFGGFKQSGFGREGGPYGLEEYTEVK 457
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
5-423 |
7.53e-90 |
|
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: 281.42 E-value: 7.53e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEfNVYSQEVITVLGEIDFMLENLPEWVTAKPV 84
Cdd:cd07099 24 VARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPR-ADAGLEVLLALEAIDWAARNAPRVLAPRKV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 85 KKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVI 163
Cdd:cd07099 103 PTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAgPPQGVLQVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 164 NGGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIA 243
Cdd:cd07099 183 TGDGATGAALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCIS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 244 PDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGE-TDEATRYIAPT 316
Cdd:cd07099 263 VERVYVHESVYDEFVARLVAKARALrPGADDIGDADIGPMTTARQLDIVRRHVDdavakGAKALTGGArSNGGGPFYEPT 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 317 VLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNS 396
Cdd:cd07099 343 VLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIPA 422
|
410 420
....*....|....*....|....*..
gi 1595488123 397 FPFGGVGSSGMGAYHGKHSFDTFSHQR 423
Cdd:cd07099 423 LPFGGVKDSGGGRRHGAEGLREFCRPK 449
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
5-413 |
6.03e-74 |
|
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: 240.66 E-value: 6.03e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEWVTAKPV 84
Cdd:cd07098 24 IAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEILVTCEKIRWTLKHGEKALRPESR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 85 KKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSEL----SENTAKILAKLLPQY-LDQDL 159
Cdd:cd07098 104 PGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQvawsSGFFLSIIRECLAACgHDPDL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 160 YIVINGgVEETTELLKQ--RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNC 237
Cdd:cd07098 184 VQLVTC-LPETAEALTShpVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 238 GQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGE-----T 306
Cdd:cd07098 263 GQNCIGIERVIVHEKIYDKLLEILTDRVQALrQGPPLDGDVDVGAMISPARFDRLEELVadaveKGARLLAGGKryphpE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 307 DEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGN 386
Cdd:cd07098 343 YPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAIN 422
|
410 420
....*....|....*....|....*..
gi 1595488123 387 DVIMHFTLNSFPFGGVGSSGMGAYHGK 413
Cdd:cd07098 423 DFGVNYYVQQLPFGGVKGSGFGRFAGE 449
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
9-419 |
6.80e-67 |
|
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: 222.14 E-value: 6.80e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 9 RQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSefnvYSQEVITVLGEIDFMlENLPEWvtAKPVKKNV 88
Cdd:cd07088 45 EAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKT----LSLARVEVEFTADYI-DYMAEW--ARRIEGEI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 89 LTMLDEA---YIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVIN 164
Cdd:cd07088 118 IPSDRPNeniFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAgLPAGVLNIVT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 165 GGVEETTELL--KQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCI 242
Cdd:cd07088 198 GRGSVVGDALvaHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCT 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 243 APDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEATR--YIA 314
Cdd:cd07088 278 CAERVYVHEDIYDEFMEKLVEKMKAVkVGDPFDAATDMGPLVNEAALDKVEEMVEraveaGATLLTGGKRPEGEKgyFYE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 315 PTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGV----TGNDVIM 390
Cdd:cd07088 358 PTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETyinrENFEAMQ 437
|
410 420
....*....|....*....|....*....
gi 1595488123 391 HFtlnsfpFGGVGSSGMGAYHGKHSFDTF 419
Cdd:cd07088 438 GF------HAGWKKSGLGGADGKHGLEEY 460
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
94-423 |
5.56e-65 |
|
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: 216.24 E-value: 5.56e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 94 EAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAK-ILAKL-----LPQyldqDLYIVINGGV 167
Cdd:cd07104 91 ESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGlLIAEIfeeagLPK----GVLNVVPGGG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 168 EETTELL--KQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPD 245
Cdd:cd07104 167 SEIGDALveHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 246 YILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEatRYIAPTVLT 319
Cdd:cd07104 247 RILVHESVYDEFVEKLVAKAKALpVGDPRDPDTVIGPLINERQVDRVHAIVEdavaaGARLLTGGTYEG--LFYQPTVLS 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 320 DVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVimhfTLNS--- 396
Cdd:cd07104 325 DVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQ----TVNDeph 400
|
330 340
....*....|....*....|....*..
gi 1595488123 397 FPFGGVGSSGMGAYHGKHSFDTFSHQR 423
Cdd:cd07104 401 VPFGGVKASGGGRFGGPASLEEFTEWQ 427
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
7-421 |
8.00e-64 |
|
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: 213.65 E-value: 8.00e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 7 RVRQAFLSGRSRPLRFRLqqlEALRRMVqerekDILTAIAADLCKS-------EFNVYSQEVITVLGEIDFMLENLPEWV 79
Cdd:cd07102 26 RARAAQKGWRAVPLEERK---AIVTRAV-----ELLAANTDEIAEEltwqmgrPIAQAGGEIRGMLERARYMISIAEEAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 80 TAKPV--KKNVltmldEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LD 156
Cdd:cd07102 98 ADIRVpeKDGF-----ERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAgLP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 157 QDLYIVINGGVEETTELLKQ-RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYM 235
Cdd:cd07102 173 EGVFQVLHLSHETSAALIADpRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 236 NCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGET--- 306
Cdd:cd07102 253 NSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYkLGDPLDPSTTLGPVVSARAADFVRAQIAdaiakGARALIDGALfpe 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 307 -DEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTG 385
Cdd:cd07102 333 dKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFM 412
|
410 420 430
....*....|....*....|....*....|....*...
gi 1595488123 386 N--DvimhFTLNSFPFGGVGSSGMGAYHGKHSFDTFSH 421
Cdd:cd07102 413 NrcD----YLDPALAWTGVKDSGRGVTLSRLGYDQLTR 446
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
96-423 |
2.05e-63 |
|
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: 212.81 E-value: 2.05e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 96 YIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLpqyLDQDL----YIVINGGVEETT 171
Cdd:cd07093 112 YVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELA---NEAGLppgvVNVVHGFGPEAG 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 172 ELLKQ--RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILC 249
Cdd:cd07093 189 AALVAhpDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILV 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 250 EASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGETDEATR-----YIAPTVL 318
Cdd:cd07093 269 QRSIYDEFLERFVERAKALkVGDPLDPDTEVGPLISKEHLEKVLGYVelaraEGATILTGGGRPELPDleggyFVEPTVI 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 319 TDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVtgndvimhfTLNSF- 397
Cdd:cd07093 349 TGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTV---------WVNCWl 419
|
330 340 350
....*....|....*....|....*....|..
gi 1595488123 398 ------PFGGVGSSGMGAYHGKHSFDTFSHQR 423
Cdd:cd07093 420 vrdlrtPFGGVKASGIGREGGDYSLEFYTELK 451
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
100-423 |
2.23e-63 |
|
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: 212.57 E-value: 2.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 100 QPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVINGGVEETTELLKQ-- 176
Cdd:cd07150 118 RPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAgLPKGVFNVVTGGGAEVGDELVDdp 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 177 RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQ 256
Cdd:cd07150 198 RVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 257 IVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDeaTRYIAPTVLTDVDPKTKVMQE 330
Cdd:cd07150 278 FVKKFVARASKLkVGDPRDPDTVIGPLISPRQVERIKRQVEdavakGAKLLTGGKYD--GNFYQPTVLTDVTPDMRIFRE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 331 EIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHN-HKLIKrMIDETSSGGVTGNDVIMHFTLNSfPFGGVGSSGMGA 409
Cdd:cd07150 356 ETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDlQRAFK-LAERLESGMVHINDPTILDEAHV-PFGGVKASGFGR 433
|
330
....*....|....
gi 1595488123 410 YHGKHSFDTFSHQR 423
Cdd:cd07150 434 EGGEWSMEEFTELK 447
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
10-419 |
5.31e-62 |
|
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: 208.83 E-value: 5.31e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 10 QAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSefnvYSQevitVLGEIDFMLENLpEW----------- 78
Cdd:cd07103 30 AAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKP----LAE----ARGEVDYAASFL-EWfaeearriygr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 79 -VTAKPVKKNVLTMldeayiqPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LD 156
Cdd:cd07103 101 tIPSPAPGKRILVI-------KQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEAgLP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 157 QDLYIVINGGVEETTELLKQRFD--HIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKY 234
Cdd:cd07103 174 AGVLNVVTGSPAEIGEALCASPRvrKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 235 MNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDE 308
Cdd:cd07103 254 RNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLkVGNGLDEGTDMGPLINERAVEKVEALVEdavakGAKVLTGGKRLG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 309 AT-RYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGND 387
Cdd:cd07103 334 LGgYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINT 413
|
410 420 430
....*....|....*....|....*....|..
gi 1595488123 388 VIMhfTLNSFPFGGVGSSGMGAYHGKHSFDTF 419
Cdd:cd07103 414 GLI--SDAEAPFGGVKESGLGREGGKEGLEEY 443
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
95-419 |
2.83e-60 |
|
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: 205.33 E-value: 2.83e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 95 AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVINGGVEETTEL 173
Cdd:cd07144 138 AYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVNIIPGYGAVAGSA 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 174 LKQR--FDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEA 251
Cdd:cd07144 218 LAEHpdVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 252 SLQNQIVWKIKETVKEFY--GENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGE----TDEATRYIAPTVLTD 320
Cdd:cd07144 298 SIYDKFVEKFVEHVKQNYkvGSPFDDDTVVGPQVSKTQYDRVLSYIEkgkkeGAKLVYGGEkapeGLGKGYFIPPTIFTD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 321 VDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGV---TGNDviMHFTLnsf 397
Cdd:cd07144 378 VPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVwinSSND--SDVGV--- 452
|
330 340
....*....|....*....|..
gi 1595488123 398 PFGGVGSSGMGAYHGKHSFDTF 419
Cdd:cd07144 453 PFGGFKMSGIGRELGEYGLETY 474
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
101-420 |
1.48e-59 |
|
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: 202.46 E-value: 1.48e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 101 PLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVING-GVEETTELLKQR- 177
Cdd:cd07109 117 PHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAgLPAGALNVVTGlGAEAGAALVAHPg 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 178 FDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQI 257
Cdd:cd07109 197 VDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEV 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 258 VWKIKETVKEF---YGEnikESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEATR----YIAPTVLTDVDPKT 325
Cdd:cd07109 277 LERLVERFRALrvgPGL---EDPDLGPLISAKQLDRVEGFVArararGARIVAGGRIAEGAPaggyFVAPTLLDDVPPDS 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 326 KVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGND------VIMhftlnsfPF 399
Cdd:cd07109 354 RLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNygagggIEL-------PF 426
|
330 340
....*....|....*....|.
gi 1595488123 400 GGVGSSGMGAYHGKHSFDTFS 420
Cdd:cd07109 427 GGVKKSGHGREKGLEALYNYT 447
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
100-420 |
2.39e-59 |
|
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: 201.27 E-value: 2.39e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 100 QPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLpqyLDQDL----YIVINGGVEETTELLK 175
Cdd:cd07105 97 EPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVF---HEAGLpkgvLNVVTHSPEDAPEVVE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 176 QRFDH-----IFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCE 250
Cdd:cd07105 174 ALIAHpavrkVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIVH 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 251 ASLQNQIVWKIKETVKEfygenIKESPDYERI-INLRHFKRILSLLE-----GQKIAFGGETD--EATRYIAPTVLTDVD 322
Cdd:cd07105 254 ESIADEFVEKLKAAAEK-----LFAGPVVLGSlVSAAAADRVKELVDdalskGAKLVVGGLADesPSGTSMPPTILDNVT 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 323 PKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMH--FTLnsfPFG 400
Cdd:cd07105 329 PDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVHdePTL---PHG 405
|
330 340
....*....|....*....|
gi 1595488123 401 GVGSSGMGAYHGKHSFDTFS 420
Cdd:cd07105 406 GVKSSGYGRFNGKWGIDEFT 425
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
100-413 |
2.65e-59 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 201.60 E-value: 2.65e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 100 QPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVINGGvEETTELLKQ--R 177
Cdd:cd07106 113 KPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEVLPPGVLNVVSGG-DELGPALTShpD 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 178 FDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQI 257
Cdd:cd07106 192 IRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEF 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 258 VWKIKETVKEFY-GENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEATRY-IAPTVLTDVDPKTKVMQE 330
Cdd:cd07106 272 CEALVALAKAAVvGDGLDPGTTLGPVQNKMQYDKVKELVEdakakGAKVLAGGEPLDGPGYfIPPTIVDDPPEGSRIVDE 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 331 EIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNdviMHFTLN-SFPFGGVGSSGMGA 409
Cdd:cd07106 352 EQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWIN---THGALDpDAPFGGHKQSGIGV 428
|
....
gi 1595488123 410 YHGK 413
Cdd:cd07106 429 EFGI 432
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
9-423 |
7.05e-59 |
|
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: 200.93 E-value: 7.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 9 RQAFLSG-RSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLP--EWVTAKPVK 85
Cdd:cd07089 29 RRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQVDGPIGHLRYFADLADsfPWEFDLPVP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 86 kNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKL-----LPQYldqdly 160
Cdd:cd07089 109 -ALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIiaetdLPAG------ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 161 iVIN---GGVEETTELLKQ--RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYM 235
Cdd:cd07089 182 -VVNvvtGSDNAVGEALTTdpRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMH 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 236 NCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGETDEA 309
Cdd:cd07089 261 NAGQGCALTTRLLVPRSRYDEVVEALAAAFEALpVGDPADPGTVMGPLISAAQRDRVEGYIargrdEGARLVTGGGRPAG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 310 TR---YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGN 386
Cdd:cd07089 341 LDkgfYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGIN 420
|
410 420 430
....*....|....*....|....*....|....*..
gi 1595488123 387 DViMHFTLNSfPFGGVGSSGMGAYHGKHSFDTFSHQR 423
Cdd:cd07089 421 GG-GGYGPDA-PFGGYKQSGLGRENGIEGLEEFLETK 455
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
100-423 |
2.98e-58 |
|
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: 199.10 E-value: 2.98e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 100 QPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVINGGVEETTELL--KQ 176
Cdd:cd07118 118 EPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAgLPAGVVNIVTGYGATVGQAMteHP 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 177 RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQ 256
Cdd:cd07118 198 DVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 257 IVWKIKE-TVKEFYGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGETDE--ATRYIAPTVLTDVDPKTKVM 328
Cdd:cd07118 278 FVAAVVArSRKVRVGDPLDPETKVGAIINEAQLAKITDYVdagraEGATLLLGGERLAsaAGLFYQPTIFTDVTPDMAIA 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 329 QEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTlnSFPFGGVGSSGMG 408
Cdd:cd07118 358 REEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSP--ELPFGGFKQSGIG 435
|
330
....*....|....*
gi 1595488123 409 AYHGKHSFDTFSHQR 423
Cdd:cd07118 436 RELGRYGVEEYTELK 450
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
5-423 |
3.45e-58 |
|
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: 198.93 E-value: 3.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 5 VRRVRQAFLSGRSRPL----RFRLqqleaLRRMVqerekDILTAIAADLCKSEfnvySQEVITVLGEIDFMLENLPEW-- 78
Cdd:cd07114 25 VAAARAAFEGGAWRKLtpteRGKL-----LRRLA-----DLIEANAEELAELE----TRDNGKLIRETRAQVRYLAEWyr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 79 ------------VTakPV-KKNVLtmldeAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAK 145
Cdd:cd07114 91 yyagladkiegaVI--PVdKGDYL-----NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 146 ILAKL-----LPQYLDQdlyiVINGGVEETTELLKQ--RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDK 218
Cdd:cd07114 164 ELAKLaeeagFPPGVVN----VVTGFGPETGEALVEhpLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 219 DCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKefygeNIK-ESPDYER-----IINLRHFKRIL 292
Cdd:cd07114 240 DADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARAR-----AIRvGDPLDPEtqmgpLATERQLEKVE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 293 SLL-----EGQKIAFGGET-----DEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALY 362
Cdd:cd07114 315 RYVarareEGARVLTGGERpsgadLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAG 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1595488123 363 VFSHNHKLIKRMIDETSSGGVTGNDvimhFTLNSF--PFGGVGSSGMGAYHGKHSFDTFSHQR 423
Cdd:cd07114 395 IWTRDLARAHRVARAIEAGTVWVNT----YRALSPssPFGGFKDSGIGRENGIEAIREYTQTK 453
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
96-408 |
2.51e-57 |
|
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: 196.39 E-value: 2.51e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 96 YIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVINGGVEETTELL- 174
Cdd:cd07092 113 MIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGVVNVVCGGGASAGDALv 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 175 -KQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASL 253
Cdd:cd07092 193 aHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 254 QNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE----GQKIAFGGETDEATRY-IAPTVLTDVDPKTKV 327
Cdd:cd07092 273 YDEFVAALVEAVSAIrVGDPDDEDTEMGPLNSAAQRERVAGFVErapaHARVLTGGRRAEGPGYfYEPTVVAGVAQDDEI 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 328 MQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDvimHFTL-NSFPFGGVGSSG 406
Cdd:cd07092 353 VQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNT---HIPLaAEMPHGGFKQSG 429
|
..
gi 1595488123 407 MG 408
Cdd:cd07092 430 YG 431
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
95-408 |
4.04e-57 |
|
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: 196.66 E-value: 4.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 95 AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYI-VING-----GVE 168
Cdd:cd07091 135 AYTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVnIVPGfgptaGAA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 169 ETTELlkqRFDHIFYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYI 247
Cdd:cd07091 215 ISSHM---DVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRI 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 248 LCEASLQNQIVWKIKETVKEFY-GENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGET-DEATRYIAPTVLTD 320
Cdd:cd07091 292 FVQESIYDEFVEKFKARAEKRVvGDPFDPDTFQGPQVSKAQFDKILSYIesgkkEGATLLTGGERhGSKGYFIQPTVFTD 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 321 VDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNdvimhfTLNSF--- 397
Cdd:cd07091 372 VKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVN------TYNVFdaa 445
|
330
....*....|..
gi 1595488123 398 -PFGGVGSSGMG 408
Cdd:cd07091 446 vPFGGFKQSGFG 457
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
101-408 |
6.64e-57 |
|
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: 195.51 E-value: 6.64e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 101 PLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQ-YLDQDLYIVINGGVEET-TELLK-QR 177
Cdd:cd07149 123 PIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEaGLPKGALNVVTGSGETVgDALVTdPR 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 178 FDHIFYTGNTAVGKIVMEAAAkhLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQI 257
Cdd:cd07149 203 VRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEF 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 258 VWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEAtrYIAPTVLTDVDPKTKVMQEE 331
Cdd:cd07149 281 LERFVAATKKLvVGDPLDEDTDVGPMISEAEAERIEEWVEeavegGARLLTGGKRDGA--ILEPTVLTDVPPDMKVVCEE 358
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595488123 332 IFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDvIMHFTLNSFPFGGVGSSGMG 408
Cdd:cd07149 359 VFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMIND-SSTFRVDHMPYGGVKESGTG 434
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
5-408 |
9.81e-55 |
|
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: 189.88 E-value: 9.81e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEwvtAK-- 82
Cdd:cd07108 25 VAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPEAAVLADLFRYFGGLAGE---LKge 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 83 --PVKKNVLTmldeaYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLY 160
Cdd:cd07108 102 tlPFGPDVLT-----YTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQVLPAGVL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 161 IVINGGVEETTELLKQR--FDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWG-KYMNC 237
Cdd:cd07108 177 NVITGYGEECGAALVDHpdVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGAIAGmRFTRQ 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 238 GQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE------GQKIAFGGETDEAT 310
Cdd:cd07108 257 GQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLkIGDPLDEATDIGAIISEKQFAKVCGYIDlglstsGATVLRGGPLPGEG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 311 R-----YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTG 385
Cdd:cd07108 337 PladgfFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQV 416
|
410 420
....*....|....*....|...
gi 1595488123 386 NDviMHFTLNSFPFGGVGSSGMG 408
Cdd:cd07108 417 NQ--GGGQQPGQSYGGFKQSGLG 437
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
83-420 |
1.18e-54 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 189.74 E-value: 1.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 83 PVKKNVLtmldeAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKL-----LPqylDQ 157
Cdd:cd07112 111 PTGPDAL-----ALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELaleagLP---AG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 158 DLYIVINGGVEETTEL-LKQRFDHIFYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDKDC-DLDIVCRRITWGKY 234
Cdd:cd07112 183 VLNVVPGFGHTAGEALgLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIF 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 235 MNCGQTCIAPDYILCEASLQNQIVWKIKETVKEFY-GENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGETDE 308
Cdd:cd07112 263 WNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKpGDPLDPATRMGALVSEAHFDKVLGYIesgkaEGARLVAGGKRVL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 309 ATR---YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTG 385
Cdd:cd07112 343 TETggfFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWV 422
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1595488123 386 N-----DVIMhftlnsfPFGGVGSSGMGAYHGKHSFDTFS 420
Cdd:cd07112 423 NcfdegDITT-------PFGGFKQSGNGRDKSLHALDKYT 455
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
89-408 |
2.00e-54 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 189.48 E-value: 2.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 89 LTMLDE---AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVING 165
Cdd:cd07559 121 LSEIDEdtlSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVNVVTG 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 166 GVEETTELLK--QRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYI-----DKDCDLDIVCRRITWGKYMNCG 238
Cdd:cd07559 201 FGSEAGKPLAshPRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFfddamDADDDFDDKAEEGQLGFAFNQG 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 239 QTCIAPDYILCEASLQNQIVWKIKETVkefygENIKE-SP-DYERII----NLRHFKRILSLL-----EGQKIAFGGE-- 305
Cdd:cd07559 281 EVCTCPSRALVQESIYDEFIERAVERF-----EAIKVgNPlDPETMMgaqvSKDQLEKILSYVdigkeEGAEVLTGGErl 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 306 ---TDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGG 382
Cdd:cd07559 356 tlgGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGR 435
|
330 340 350
....*....|....*....|....*....|
gi 1595488123 383 VTGNdvimhfTLNSFP----FGGVGSSGMG 408
Cdd:cd07559 436 VWVN------CYHQYPahapFGGYKKSGIG 459
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
9-419 |
4.12e-54 |
|
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: 188.10 E-value: 4.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 9 RQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADL-CKSEFNVYSQeVITVLGEIDFMLENLPEWVTAKPVKKN 87
Cdd:cd07138 46 RRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMgAPITLARAAQ-VGLGIGHLRAAADALKDFEFEERRGNS 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 88 VLTMldeayiqpQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLpqyLDQDL----YIVI 163
Cdd:cd07138 125 LVVR--------EPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEIL---DEAGLpagvFNLV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 164 NGGVEETTELLK--QRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDivcRRITWG---KYMNCG 238
Cdd:cd07138 194 NGDGPVVGEALSahPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLE---KAVPRGvaaCFANSG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 239 QTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGG----ETDE 308
Cdd:cd07138 271 QSCNAPTRMLVPRSRYAEAEEIAAAAAEAYvVGDPRDPATTLGPLASAAQFDRVQGYIqkgieEGARLVAGGpgrpEGLE 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 309 ATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHN----HKLIKRMidetSSGGVT 384
Cdd:cd07138 351 RGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADperaRAVARRL----RAGQVH 426
|
410 420 430
....*....|....*....|....*....|....*
gi 1595488123 385 GNDVIMHFtlnSFPFGGVGSSGMGAYHGKHSFDTF 419
Cdd:cd07138 427 INGAAFNP---GAPFGGYKQSGNGREWGRYGLEEF 458
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
95-429 |
5.85e-54 |
|
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: 187.51 E-value: 5.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 95 AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVINGGvEETTEL 173
Cdd:cd07090 110 AYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAgLPDGVFNVVQGG-GETGQL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 174 LKQRFD--HIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEA 251
Cdd:cd07090 189 LCEHPDvaKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQR 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 252 SLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGE----TD--EATRYIAPTVLT 319
Cdd:cd07090 269 SIKDEFTERLVERTKKIrIGDPLDEDTQMGALISEEHLEKVLGYIesakqEGAKVLCGGErvvpEDglENGFYVSPCVLT 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 320 DVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDvimhFTLNS--F 397
Cdd:cd07090 349 DCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINT----YNISPveV 424
|
330 340 350
....*....|....*....|....*....|..
gi 1595488123 398 PFGGVGSSGMGAYHGKHSFDTFSHqrpclLKS 429
Cdd:cd07090 425 PFGGYKQSGFGRENGTAALEHYTQ-----LKT 451
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
83-420 |
1.39e-53 |
|
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: 186.49 E-value: 1.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 83 PVKKNVLTmldeaYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYI 161
Cdd:cd07115 104 PVRGPFLN-----YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAgFPAGVLN 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 162 VINGGVEETTELLKQR--FDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQ 239
Cdd:cd07115 179 VVTGFGEVAGAALVEHpdVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQ 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 240 TCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGETDEATR-Y 312
Cdd:cd07115 259 MCTAGSRLLVHESIYDEFLERFTSLARSLrPGDPLDPKTQMGPLVSQAQFDRVLDYVdvgreEGARLLTGGKRPGARGfF 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 313 IAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNdvimhf 392
Cdd:cd07115 339 VEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWIN------ 412
|
330 340 350
....*....|....*....|....*....|..
gi 1595488123 393 TLNSF----PFGGVGSSGMGAYHGKHSFDTFS 420
Cdd:cd07115 413 TYNRFdpgsPFGGYKQSGFGREMGREALDEYT 444
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
101-423 |
6.00e-53 |
|
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: 184.42 E-value: 6.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 101 PLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAK-ILAKLLPQY-LDQDLYIVINGGVEETTELLK-QR 177
Cdd:cd07152 110 PLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGvVIARLFEEAgLPAGVLHVLPGGADAGEALVEdPN 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 178 FDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQI 257
Cdd:cd07152 190 VAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAY 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 258 VWKIKETVKEF-----YGENIKESPdyerIINLRHFKRILSLLE-----GQKIAFGGETDEatRYIAPTVLTDVDPKTKV 327
Cdd:cd07152 270 TAKLAAKAKHLpvgdpATGQVALGP----LINARQLDRVHAIVDdsvaaGARLEAGGTYDG--LFYRPTVLSGVKPGMPA 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 328 MQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVimhfTLNS---FPFGGVGS 404
Cdd:cd07152 344 FDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQ----TVNDephNPFGGMGA 419
|
330 340
....*....|....*....|
gi 1595488123 405 SGMGAYHG-KHSFDTFSHQR 423
Cdd:cd07152 420 SGNGSRFGgPANWEEFTQWQ 439
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
94-420 |
8.59e-53 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 185.21 E-value: 8.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 94 EAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKL-----LPQYLDQdlyIVINGGVE 168
Cdd:cd07119 127 ISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELieeagLPAGVVN---LVTGSGAT 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 169 ETTEL-LKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYI 247
Cdd:cd07119 204 VGAELaESPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 248 LCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGE--TDEATR---YIAPT 316
Cdd:cd07119 284 LVEESIHDKFVAALAERAKKIkLGNGLDADTEMGPLVSAEHREKVLSYIqlgkeEGARLVCGGKrpTGDELAkgyFVEPT 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 317 VLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDviMHFTLNS 396
Cdd:cd07119 364 IFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIND--YHPYFAE 441
|
330 340
....*....|....*....|....
gi 1595488123 397 FPFGGVGSSGMGAYHGKHSFDTFS 420
Cdd:cd07119 442 APWGGYKQSGIGRELGPTGLEEYQ 465
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
5-412 |
1.62e-52 |
|
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: 183.71 E-value: 1.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 5 VRRVRQAFLSGRSRPLRF-RLQQLEALRRMVQEREKDILTAIAAD--LCKSEFNVYSQEVITVL-----------GEIdF 70
Cdd:cd07146 23 LREALALAASYRSTLTRYqRSAILNKAAALLEARREEFARLITLEsgLCLKDTRYEVGRAADVLrfaaaealrddGES-F 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 71 MLENLPewvTAKPVKknvltmldeAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKL 150
Cdd:cd07146 102 SCDLTA---NGKARK---------IFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 151 LPQY-LDQDLYIVINGGVEETTELLKQ--RFDHIFYTGNTAVGKIVMEAAA-KHLTpvtLELGGKSPCYIDKDCDLDIVC 226
Cdd:cd07146 170 LYEAgLPPDMLSVVTGEPGEIGDELIThpDVDLVTFTGGVAVGKAIAATAGyKRQL---LELGGNDPLIVMDDADLERAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 227 RRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIIN---LRHF-KRILSLLE-GQKI 300
Cdd:cd07146 247 TLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALvVGDPMDPATDMGTVIDeeaAIQIeNRVEEAIAqGARV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 301 AFGGETDEAtrYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSS 380
Cdd:cd07146 327 LLGNQRQGA--LYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDV 404
|
410 420 430
....*....|....*....|....*....|..
gi 1595488123 381 GGVTGNDViMHFTLNSFPFGGVGSSGMGAYHG 412
Cdd:cd07146 405 GTVNVNEV-PGFRSELSPFGGVKDSGLGGKEG 435
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
100-419 |
2.13e-52 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 184.51 E-value: 2.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 100 QPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVINGGVEETTELL---- 174
Cdd:PLN02278 159 QPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAgIPPGVLNVVMGDAPEIGDALlasp 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 175 KQRfdHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQ 254
Cdd:PLN02278 239 KVR--KITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIY 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 255 NQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGE--TDEATRYiAPTVLTDVDPKTK 326
Cdd:PLN02278 317 DKFAEAFSKAVQKLvVGDGFEEGVTQGPLINEAAVQKVESHVqdavsKGAKVLLGGKrhSLGGTFY-EPTVLGDVTEDML 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 327 VMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTlnSFPFGGVGSSG 406
Cdd:PLN02278 396 IFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTE--VAPFGGVKQSG 473
|
330
....*....|...
gi 1595488123 407 MGAYHGKHSFDTF 419
Cdd:PLN02278 474 LGREGSKYGIDEY 486
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
2-423 |
1.01e-51 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 181.78 E-value: 1.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 2 ELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVySQEVITVLGEIDFMLEnLPEWVTA 81
Cdd:cd07110 22 DAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA-AWDVDDVAGCFEYYAD-LAEQLDA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 82 KpvKKNVLTMLDE---AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAK------LLP 152
Cdd:cd07110 100 K--AERAVPLPSEdfkARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEiaaeagLPP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 153 QYLDqdlyiVINGGVEETTELLKQ--RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRIT 230
Cdd:cd07110 178 GVLN-----VVTGTGDEAGAPLAAhpGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 231 WGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVkefygENIKESPDYER------IINLRHFKRILSLL-----EGQK 299
Cdd:cd07110 253 FGCFWNNGQICSATSRLLVHESIADAFLERLATAA-----EAIRVGDPLEEgvrlgpLVSQAQYEKVLSFIargkeEGAR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 300 IAFGGETDEATR---YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMID 376
Cdd:cd07110 328 LLCGGRRPAHLEkgyFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAE 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1595488123 377 ETSSGGVTGNDVIMHFTlnSFPFGGVGSSGMGAYHGKHSFDTFSHQR 423
Cdd:cd07110 408 ALEAGIVWINCSQPCFP--QAPWGGYKRSGIGRELGEWGLDNYLEVK 452
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
100-419 |
1.69e-51 |
|
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: 181.23 E-value: 1.69e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 100 QPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVINGGVEETTELLKQ-R 177
Cdd:cd07139 136 EPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAgLPPGVVNVVPADREVGEYLVRHpG 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 178 FDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQI 257
Cdd:cd07139 216 VDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEV 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 258 VWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGET-DEATR--YIAPTVLTDVDPKTKVM 328
Cdd:cd07139 296 VEALAAAVAALkVGDPLDPATQIGPLASARQRERVEGYIakgraEGARLVTGGGRpAGLDRgwFVEPTLFADVDNDMRIA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 329 QEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNH----KLIKRMidetSSGGVTGNDVIMHFTLnsfPFGGVGS 404
Cdd:cd07139 376 QEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVerglAVARRI----RTGTVGVNGFRLDFGA---PFGGFKQ 448
|
330
....*....|....*
gi 1595488123 405 SGMGAYHGKHSFDTF 419
Cdd:cd07139 449 SGIGREGGPEGLDAY 463
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
100-421 |
2.02e-51 |
|
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: 181.39 E-value: 2.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 100 QPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVINGGVEETTELLKQ-- 176
Cdd:cd07131 134 QPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAgLPPGVVNVVHGRGEEVGEALVEhp 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 177 RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQ 256
Cdd:cd07131 214 DVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 257 IVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGE-----TDEATRYIAPTVLTDVDPKT 325
Cdd:cd07131 294 FLKRFVERAKRLrVGDGLDEETDMGPLINEAQLEKVLNYNeigkeEGATLLLGGErltggGYEKGYFVEPTVFTDVTPDM 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 326 KVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGN------DVIMhftlnsfPF 399
Cdd:cd07131 374 RIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNaptigaEVHL-------PF 446
|
330 340
....*....|....*....|....*
gi 1595488123 400 GGVGSSGMGayH---GKHSFDTFSH 421
Cdd:cd07131 447 GGVKKSGNG--HreaGTTALDAFTE 469
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
95-408 |
3.09e-51 |
|
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: 180.24 E-value: 3.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 95 AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVINGGVEET-TE 172
Cdd:cd07145 117 AFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPGVINVVTGYGSEVgDE 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 173 LLKQ-RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEA 251
Cdd:cd07145 197 IVTNpKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 252 SLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGETDEATrYIAPTVLTDVDPKT 325
Cdd:cd07145 277 EVYDKFLKLLVEKVKKLkVGDPLDESTDLGPLISPEAVERMENLVndaveKGGKILYGGKRDEGS-FFPPTVLENDTPDM 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 326 KVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMhFTLNSFPFGGVGSS 405
Cdd:cd07145 356 IVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDSTR-FRWDNLPFGGFKKS 434
|
...
gi 1595488123 406 GMG 408
Cdd:cd07145 435 GIG 437
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
2-413 |
5.37e-51 |
|
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: 179.81 E-value: 5.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 2 ELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYsQEVITVLGEIDFMLENLPEWVta 81
Cdd:cd07101 21 EAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAF-EEVLDVAIVARYYARRAERLL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 82 KPVKKN----VLTMLDEAYiqpQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LD 156
Cdd:cd07101 98 KPRRRRgaipVLTRTTVNR---RPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAgLP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 157 QDLYIVINGGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMN 236
Cdd:cd07101 175 RDLWQVVTGPGSEVGGAIVDNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSN 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 237 CGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGET--DE 308
Cdd:cd07101 255 AGQLCVSIERIYVHESVYDEFVRRFVARTRALrLGAALDYGPDMGSLISQAQLDRVTAHVDdavakGATVLAGGRArpDL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 309 ATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDv 388
Cdd:cd07101 335 GPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNE- 413
|
410 420
....*....|....*....|....*..
gi 1595488123 389 IMHFTLNSF--PFGGVGSSGMGAYHGK 413
Cdd:cd07101 414 GYAAAWASIdaPMGGMKDSGLGRRHGA 440
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
95-420 |
1.12e-50 |
|
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: 179.65 E-value: 1.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 95 AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVINGGVEETTEL 173
Cdd:cd07143 138 TYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGYGRTCGNA 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 174 LKQ--RFDHIFYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCE 250
Cdd:cd07143 218 ISShmDIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQ 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 251 ASLQNQIVWKIKETVKEF-----YGENIKESPDYERIinlrHFKRILSLLE-----GQKIAFGGETDEATRY-IAPTVLT 319
Cdd:cd07143 298 EGIYDKFVKRFKEKAKKLkvgdpFAEDTFQGPQVSQI----QYERIMSYIEsgkaeGATVETGGKRHGNEGYfIEPTIFT 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 320 DVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNhklIKRMIdETSSGGVTGNDVIMHFTLNSF-- 397
Cdd:cd07143 374 DVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNN---INNAI-RVANALKAGTVWVNCYNLLHHqv 449
|
330 340
....*....|....*....|...
gi 1595488123 398 PFGGVGSSGMGAYHGKHSFDTFS 420
Cdd:cd07143 450 PFGGYKQSGIGRELGEYALENYT 472
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
93-420 |
3.77e-50 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 177.69 E-value: 3.77e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 93 DEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVINGGVEETT 171
Cdd:TIGR01804 125 SFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAgLPKGVFNVVQGDGAEVG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 172 ELLKQR--FDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILC 249
Cdd:TIGR01804 205 PLLVNHpdVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFV 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 250 EASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGG------ETDEATrYIAPTV 317
Cdd:TIGR01804 285 HKKIKERFLARLVERTERIkLGDPFDEATEMGPLISAAHRDKVLSYIekgkaEGATLATGGgrpenvGLQNGF-FVEPTV 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 318 LTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDviMHFTLNSF 397
Cdd:TIGR01804 364 FADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINT--YNLYPAEA 441
|
330 340
....*....|....*....|...
gi 1595488123 398 PFGGVGSSGMGAYHGKHSFDTFS 420
Cdd:TIGR01804 442 PFGGYKQSGIGRENGKAALAHYT 464
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
95-408 |
4.85e-50 |
|
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: 177.63 E-value: 4.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 95 AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYI-VINGGVEETTEL 173
Cdd:cd07113 136 AFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLnVVNGKGAVGAQL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 174 LKQ-RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEAS 252
Cdd:cd07113 216 ISHpDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRS 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 253 LQNQIVWKIKETVKEFY-GENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGET-DEATRYIAPTVLTDVDPKT 325
Cdd:cd07113 296 KFDELVTKLKQALSSFQvGSPMDESVMFGPLANQPHFDKVCSYLddaraEGDEIVRGGEAlAGEGYFVQPTLVLARSADS 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 326 KVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNdviMHFTLN-SFPFGGVGS 404
Cdd:cd07113 376 RLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN---MHTFLDpAVPFGGMKQ 452
|
....
gi 1595488123 405 SGMG 408
Cdd:cd07113 453 SGIG 456
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
2-412 |
5.86e-50 |
|
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: 176.80 E-value: 5.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 2 ELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADlCKsefNVYSQEVITVLGEIDfMLENLPEWVTA 81
Cdd:cd07107 22 DRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALD-CG---NPVSAMLGDVMVAAA-LLDYFAGLVTE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 82 kpVKKNVLTMLDEA--YIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDL 159
Cdd:cd07107 97 --LKGETIPVGGRNlhYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREVLPPGV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 160 YIVINGGVEETTELLKQRFD--HIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGkyMN- 236
Cdd:cd07107 175 FNILPGDGATAGAALVRHPDvkRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAAVAG--MNf 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 237 --CGQTCIAPDYILCEASLQNQIVWKIKETVKEFY-GENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGG--ET 306
Cdd:cd07107 253 twCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKvGDPTDPATTMGPLVSRQQYDRVMHYIdsakrEGARLVTGGgrPE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 307 DEATR---YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGV 383
Cdd:cd07107 333 GPALEggfYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYV 412
|
410 420
....*....|....*....|....*....
gi 1595488123 384 TGNDVIMHFTlnSFPFGGVGSSGMGAYHG 412
Cdd:cd07107 413 WINGSSRHFL--GAPFGGVKNSGIGREEC 439
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
5-419 |
9.33e-50 |
|
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: 175.73 E-value: 9.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 5 VRRVRQAFLSGRSRPLRFRLQQL----EALRR--------MVQEREKDILTAIA-----ADLCksefnvysqevitvlge 67
Cdd:cd07100 5 LDRAHAAFLAWRKTSFAERAALLrklaDLLRErkdelarlITLEMGKPIAEARAevekcAWIC----------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 68 iDFMLENLPEWVTAKPVKknvlTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKIL 147
Cdd:cd07100 68 -RYYAENAEAFLADEPIE----TDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 148 AKLLPQY-LDQDLYIVINGGVEETTELLK-QRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIV 225
Cdd:cd07100 143 EELFREAgFPEGVFQNLLIDSDQVEAIIAdPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 226 CRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDY---ERiinlrhfKRILSLLEGQ--- 298
Cdd:cd07100 223 VKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALkVGDPMDEDTDLgplAR-------KDLRDELHEQvee 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 299 ------KIAFGGET-DEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLI 371
Cdd:cd07100 296 avaagaTLLLGGKRpDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERA 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1595488123 372 KRMIDETSSGGVTGNDviMHFTLNSFPFGGVGSSGMGAYHGKHSFDTF 419
Cdd:cd07100 376 ERVARRLEAGMVFING--MVKSDPRLPFGGVKRSGYGRELGRFGIREF 421
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
23-420 |
9.47e-50 |
|
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: 176.73 E-value: 9.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 23 RLQQLEALRRMVQEREKDILTAIAADL----CKSEFNVYSQEVIT---------VLGEIdfmlenLPEWVTAKpvkknvl 89
Cdd:cd07151 56 RAEILEKAAQILEERRDEIVEWLIRESgstrIKANIEWGAAMAITreaatfplrMEGRI------LPSDVPGK------- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 90 tmldEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAK-ILAKL-----LPQYLdqdLYIVI 163
Cdd:cd07151 123 ----ENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGlLLAKIfeeagLPKGV---LNVVV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 164 NGGVEETTELLKQ---RFdhIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQT 240
Cdd:cd07151 196 GAGSEIGDAFVEHpvpRL--ISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQI 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 241 CIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEatRYIA 314
Cdd:cd07151 274 CMAINRIIVHEDVYDEFVEKFVERVKALpYGDPSDPDTVVGPLINESQVDGLLDKIEqaveeGATLLVGGEAEG--NVLE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 315 PTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTL 394
Cdd:cd07151 352 PTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEP 431
|
410 420
....*....|....*....|....*.
gi 1595488123 395 NSfPFGGVGSSGMGAYHGKHSFDTFS 420
Cdd:cd07151 432 HV-PFGGEKNSGLGRFNGEWALEEFT 456
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
89-408 |
1.59e-49 |
|
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: 176.11 E-value: 1.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 89 LTMLDE---AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVING 165
Cdd:cd07117 121 ANMIDEdtlSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNIVTG 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 166 GVEETTELLKQR--FDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIA 243
Cdd:cd07117 201 KGSKSGEYLLNHpgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 244 PDYILCEASLQNQIVWKIKEtvkEFygENIK----ESPDYE--RIINLRHFKRILSLL-----EGQKIAFGGE-----TD 307
Cdd:cd07117 281 GSRIFVQEGIYDEFVAKLKE---KF--ENVKvgnpLDPDTQmgAQVNKDQLDKILSYVdiakeEGAKILTGGHrltenGL 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 308 EATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNd 387
Cdd:cd07117 356 DKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVN- 434
|
330 340
....*....|....*....|....*
gi 1595488123 388 vimhfTLNSFP----FGGVGSSGMG 408
Cdd:cd07117 435 -----TYNQIPagapFGGYKKSGIG 454
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
100-419 |
4.58e-49 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 173.38 E-value: 4.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 100 QPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVINGGVEETTELL--KQ 176
Cdd:PRK10090 70 RALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQELagNP 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 177 RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQ 256
Cdd:PRK10090 150 KVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQ 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 257 IVWKIKETVKEF-YGENIKES-PDYERIINLRHFKRILSLL-----EGQKIAFGGETDEATRYI-APTVLTDVDPKTKVM 328
Cdd:PRK10090 230 FVNRLGEAMQAVqFGNPAERNdIAMGPLINAAALERVEQKVaraveEGARVALGGKAVEGKGYYyPPTLLLDVRQEMSIM 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 329 QEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGN----DVIMHFtlnsfpFGGVGS 404
Cdd:PRK10090 310 HEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINrenfEAMQGF------HAGWRK 383
|
330
....*....|....*
gi 1595488123 405 SGMGAYHGKHSFDTF 419
Cdd:PRK10090 384 SGIGGADGKHGLHEY 398
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
8-408 |
7.33e-49 |
|
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: 173.77 E-value: 7.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 8 VRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAAD-------------LCKSEFNVYSQEVITVLGEIdfmlen 74
Cdd:cd07094 30 ARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEggkpikdarvevdRAIDTLRLAAEEAERIRGEE------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 75 LPEWVTAKPVKKNVLTMldeayiqPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLL-PQ 153
Cdd:cd07094 104 IPLDATQGSDNRLAWTI-------REPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILvEA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 154 YLDQDLYIVINGGVEETTELL--KQRFDHIFYTGNTAVGKIVMEAAAKhlTPVTLELGGKSPCYIDKDCDLDIVCRRITW 231
Cdd:cd07094 177 GVPEGVLQVVTGEREVLGDAFaaDERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPVIVDRDADLDAAIEALAK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 232 GKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGE 305
Cdd:cd07094 255 GGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLkVGDPLDEDTDVGPLISEEAAERVERWVEeaveaGARLLCGGE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 306 TDEATRYiaPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTG 385
Cdd:cd07094 335 RDGALFK--PTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMV 412
|
410 420
....*....|....*....|...
gi 1595488123 386 NDViMHFTLNSFPFGGVGSSGMG 408
Cdd:cd07094 413 NDS-SAFRTDWMPFGGVKESGVG 434
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
94-409 |
4.80e-48 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 172.05 E-value: 4.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 94 EAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKL-----LPQYLdqdLYIVINGGVE 168
Cdd:cd07097 128 EVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEIleeagLPAGV---FNLVMGSGSE 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 169 ETTELLK-QRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYI 247
Cdd:cd07097 205 VGQALVEhPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 248 LCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGET-DEATR--YIAPTVL 318
Cdd:cd07097 285 IVTEGIHDRFVEALVERTKALkVGDALDEGVDIGPVVSERQLEKDLRYIeiarsEGAKLVYGGERlKRPDEgyYLAPALF 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 319 TDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGN--DVIMHFTLns 396
Cdd:cd07097 365 AGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlpTAGVDYHV-- 442
|
330
....*....|...
gi 1595488123 397 fPFGGVGSSGMGA 409
Cdd:cd07097 443 -PFGGRKGSSYGP 454
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
5-412 |
4.39e-47 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 170.44 E-value: 4.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYsQEVITVLGEIDFMLENLPEWVTAKPV 84
Cdd:PRK09407 60 FARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAF-EEVLDVALTARYYARRAPKLLAPRRR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 85 KkNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVI 163
Cdd:PRK09407 139 A-GALPVLTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAgLPRDLWQVV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 164 NGGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIA 243
Cdd:PRK09407 218 TGPGPVVGTALVDNADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCIS 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 244 PDYILCEASLQNQIVWKIKETVKefygeNIKESPDYE------RIINLRHFKRILSLLE-----GQKIAFGGET--DEAT 310
Cdd:PRK09407 298 IERIYVHESIYDEFVRAFVAAVR-----AMRLGAGYDysadmgSLISEAQLETVSAHVDdavakGATVLAGGKArpDLGP 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 311 RYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIM 390
Cdd:PRK09407 373 LFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYA 452
|
410 420
....*....|....*....|...
gi 1595488123 391 H-FTLNSFPFGGVGSSGMGAYHG 412
Cdd:PRK09407 453 AaWGSVDAPMGGMKDSGLGRRHG 475
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
96-408 |
4.95e-47 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 169.32 E-value: 4.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 96 YIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVINGGVEETTELL- 174
Cdd:PRK13473 133 MIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDALv 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 175 -KQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASL 253
Cdd:PRK13473 213 gHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGI 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 254 QNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE------GQKIAFGGET-DEATRYIAPTVLTDVDPKT 325
Cdd:PRK13473 293 YDDLVAKLAAAVATLkVGDPDDEDTELGPLISAAHRDRVAGFVErakalgHIRVVTGGEApDGKGYYYEPTLLAGARQDD 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 326 KVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDvimHFTLNS-FPFGGVGS 404
Cdd:PRK13473 373 EIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNT---HFMLVSeMPHGGQKQ 449
|
....
gi 1595488123 405 SGMG 408
Cdd:PRK13473 450 SGYG 453
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
68-406 |
4.80e-46 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 167.42 E-value: 4.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 68 IDFM----LENLpEWVTAKPVkknvLTMLDEA----YIqpqPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSEl 139
Cdd:PRK03137 138 IDFLeyyaRQML-KLADGKPV----ESRPGEHnryfYI---PLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPAS- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 140 seNTAKILAKL--------LPQYldqdlyiVIN---GGVEETTELL----KQRFdhIFYTGNTAVGKIVMEAAAK----- 199
Cdd:PRK03137 209 --DTPVIAAKFvevleeagLPAG-------VVNfvpGSGSEVGDYLvdhpKTRF--ITFTGSREVGLRIYERAAKvqpgq 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 200 -HLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEFYGENIKESPD 278
Cdd:PRK03137 278 iWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNAY 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 279 YERIINLRHFKRILSLLE-GQ---KIAFGGETDEATRY-IAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFIN 353
Cdd:PRK03137 358 MGPVINQASFDKIMSYIEiGKeegRLVLGGEGDDSKGYfIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIAN 437
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1595488123 354 EREKPLALYVFSHNHKLIKRMIDETSSG------GVTGNDVIMHftlnsfPFGGVGSSG 406
Cdd:PRK03137 438 NTEYGLTGAVISNNREHLEKARREFHVGnlyfnrGCTGAIVGYH------PFGGFNMSG 490
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
95-419 |
5.39e-46 |
|
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: 166.52 E-value: 5.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 95 AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKL-----LPqylDQDLYIVINGGVEE 169
Cdd:cd07142 135 VYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLaaeagLP---DGVLNIVTGFGPTA 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 170 TTELLKQR-FDHIFYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYI 247
Cdd:cd07142 212 GAAIASHMdVDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRT 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 248 LCEASLQNQIVWKIKE-----TVKEFYGENIKESPDyeriINLRHFKRILSLL-----EGQKIAFGGE-TDEATRYIAPT 316
Cdd:cd07142 292 FVHESIYDEFVEKAKAralkrVVGDPFRKGVEQGPQ----VDKEQFEKILSYIehgkeEGATLITGGDrIGSKGYYIQPT 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 317 VLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGN--DVimhFTL 394
Cdd:cd07142 368 IFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcyDV---FDA 444
|
330 340
....*....|....*....|....*
gi 1595488123 395 nSFPFGGVGSSGMGAYHGKHSFDTF 419
Cdd:cd07142 445 -SIPFGGYKMSGIGREKGIYALNNY 468
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
5-409 |
2.11e-45 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 165.86 E-value: 2.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 5 VRRVRQAFLSGRSRPLRFRLQQL----EALRR--------MVQE-----REKDILTAIAADLCksefNVYSQEvitvlge 67
Cdd:cd07124 75 VQAARAAFPTWRRTPPEERARLLlraaALLRRrrfelaawMVLEvgknwAEADADVAEAIDFL----EYYARE------- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 68 idfMLENLPEWVTAKPVKKNVLTMldeayiqpQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKIL 147
Cdd:cd07124 144 ---MLRLRGFPVEMVPGEDNRYVY--------RPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 148 AKL-----LPQYldqdlyiVIN---GGVEETTELLKQ--RFDHIFYTGNTAVGKIVMEAAAK------HLTPVTLELGGK 211
Cdd:cd07124 213 VEIleeagLPPG-------VVNflpGPGEEVGDYLVEhpDVRFIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGK 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 212 SPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKR 290
Cdd:cd07124 286 NAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALkVGDPEDPEVYMGPVIDKGARDR 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 291 ILSLLE----GQKIAFGGETDE-ATR--YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYV 363
Cdd:cd07124 366 IRRYIEigksEGRLLLGGEVLElAAEgyFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGV 445
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1595488123 364 FSHNHKLIKRMIDETSSG------GVTGNDVIMHftlnsfPFGGVGSSGMGA 409
Cdd:cd07124 446 FSRSPEHLERARREFEVGnlyanrKITGALVGRQ------PFGGFKMSGTGS 491
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
95-408 |
3.93e-45 |
|
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: 164.27 E-value: 3.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 95 AYIQPQPLGVVLIIGAWNYPFV-----LTIqpligAIAAGNAVIIKPSE----LSENTAKILAKLLPQY-LDQDLYIVIN 164
Cdd:cd07086 127 LMEQWNPLGVVGVITAFNFPVAvpgwnAAI-----ALVCGNTVVWKPSEttplTAIAVTKILAEVLEKNgLPPGVVNLVT 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 165 GGVEETTELLK-QRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIA 243
Cdd:cd07086 202 GGGDGGELLVHdPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTT 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 244 PDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGET---DEATRYIA 314
Cdd:cd07086 282 TRRLIVHESVYDEFLERLVKAYKQVrIGDPLDEGTLVGPLINQAAVEKYLNAIEiaksqGGTVLTGGKRidgGEPGNYVE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 315 PTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSS--------GGVTGN 386
Cdd:cd07086 362 PTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKGSdcgivnvnIPTSGA 441
|
330 340
....*....|....*....|..
gi 1595488123 387 DVIMhftlnsfPFGGVGSSGMG 408
Cdd:cd07086 442 EIGG-------AFGGEKETGGG 456
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
101-408 |
4.19e-45 |
|
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: 163.57 E-value: 4.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 101 PLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLL-PQYLDQDLYIVINGGVEETTELLK-QRF 178
Cdd:cd07147 123 PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLaETGLPKGAFSVLPCSRDDADLLVTdERI 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 179 DHIFYTGNTAVG-KIVMEAAAKHltpVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQI 257
Cdd:cd07147 203 KLLSFTGSPAVGwDLKARAGKKK---VVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEF 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 258 VWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEATryIAPTVLTDVDPKTKVMQEE 331
Cdd:cd07147 280 KSRLVARVKALkTGDPKDDATDVGPMISESEAERVEGWVNeavdaGAKLLTGGKRDGAL--LEPTILEDVPPDMEVNCEE 357
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595488123 332 IFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDViMHFTLNSFPFGGVGSSGMG 408
Cdd:cd07147 358 VFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINDV-PTFRVDHMPYGGVKDSGIG 433
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
94-408 |
2.21e-44 |
|
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: 162.36 E-value: 2.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 94 EAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVINGGVEETTE 172
Cdd:cd07082 134 IAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAgFPKGVVNVVTGRGREIGD 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 173 LL--KQRFDHIFYTGNTAVGKIVMEAAAKhlTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCE 250
Cdd:cd07082 214 PLvtHGRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVH 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 251 ASLQNQIVWKIKETVkefygENIK------ESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEATrYIAPTVLT 319
Cdd:cd07082 292 ESVADELVELLKEEV-----AKLKvgmpwdNGVDITPLIDPKSADFVEGLIDdavakGATVLNGGGREGGN-LIYPTLLD 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 320 DVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTlNSFPF 399
Cdd:cd07082 366 PVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGP-DHFPF 444
|
....*....
gi 1595488123 400 GGVGSSGMG 408
Cdd:cd07082 445 LGRKDSGIG 453
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
2-423 |
1.31e-43 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 160.67 E-value: 1.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 2 ELEVRRVRQAFLSGRSR-----PLRFRLQQLEALRRMVQEReKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLEnLP 76
Cdd:PLN02467 48 DAAVEAARKAFKRNKGKdwartTGAVRAKYLRAIAAKITER-KSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYAD-LA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 77 EWVTAK---PVKknvLTMLD-EAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKL-- 150
Cdd:PLN02467 126 EALDAKqkaPVS---LPMETfKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADIcr 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 151 ---LPQYLdqdLYIVINGGVEETTELLKQ-RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVC 226
Cdd:PLN02467 203 evgLPPGV---LNVVTGLGTEAGAPLASHpGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 227 RRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKefygeNIKESPDYER------IINLRHFKRILSLL----- 295
Cdd:PLN02467 280 EWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAK-----NIKISDPLEEgcrlgpVVSEGQYEKVLKFIstaks 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 296 EGQKIAFGGETDEATR---YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIK 372
Cdd:PLN02467 355 EGATILCGGKRPEHLKkgfFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCE 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1595488123 373 RMIDETSSGGVTGNDVIMHFTlnSFPFGGVGSSGMGAYHGKHSFDTFSHQR 423
Cdd:PLN02467 435 RVSEAFQAGIVWINCSQPCFC--QAPWGGIKRSGFGRELGEWGLENYLSVK 483
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
100-420 |
1.38e-42 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 157.12 E-value: 1.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 100 QPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQ--YLDQDLYIVINGGVEETTELL--K 175
Cdd:cd07120 116 EPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEipSLPAGVVNLFTESGSEGAAHLvaS 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 176 QRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQN 255
Cdd:cd07120 196 PDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIAD 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 256 QIVWKIKEtvkefYGENIKESPDYER------IINLRHFKRILSLLE------GQKIAFGGETDEATR---YIAPTVLTD 320
Cdd:cd07120 276 EVRDRLAA-----RLAAVKVGPGLDPasdmgpLIDRANVDRVDRMVEraiaagAEVVLRGGPVTEGLAkgaFLRPTLLEV 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 321 VDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDvimHFTL-NSFPF 399
Cdd:cd07120 351 DDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWIND---WNKLfAEAEE 427
|
330 340
....*....|....*....|.
gi 1595488123 400 GGVGSSGMGAYHGKHSFDTFS 420
Cdd:cd07120 428 GGYRQSGLGRLHGVAALEDFI 448
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
95-420 |
2.70e-42 |
|
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: 156.74 E-value: 2.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 95 AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLL------PQyldqdlyiVIN--GG 166
Cdd:cd07141 139 TYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIkeagfpPG--------VVNvvPG 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 167 VEETTELL---KQRFDHIFYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCI 242
Cdd:cd07141 211 YGPTAGAAissHPDIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCC 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 243 APDYILCEASLQNQIVWKI-----KETVKEFYGENIKESPDyeriINLRHFKRILSLL-----EGQKIAFGGET-DEATR 311
Cdd:cd07141 291 AGSRTFVQESIYDEFVKRSverakKRVVGNPFDPKTEQGPQ----IDEEQFKKILELIesgkkEGAKLECGGKRhGDKGY 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 312 YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNhklIKRMIdeTSSGGVTGNDVIMH 391
Cdd:cd07141 367 FIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKD---IDKAI--TFSNALRAGTVWVN 441
|
330 340 350
....*....|....*....|....*....|...
gi 1595488123 392 fTLNSF----PFGGVGSSGMGAYHGKHSFDTFS 420
Cdd:cd07141 442 -CYNVVspqaPFGGYKMSGNGRELGEYGLQEYT 473
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
94-421 |
1.37e-40 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 152.28 E-value: 1.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 94 EAYIQPQPLGVVLIIGAWNYP---FVLTIQPligAIAAGNAVIIKPSE---LSENTAKILAKL--LPqylDQDLYIVING 165
Cdd:PLN02766 151 QGYTLKEPIGVVGHIIPWNFPstmFFMKVAP---ALAAGCTMVVKPAEqtpLSALFYAHLAKLagVP---DGVINVVTGF 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 166 GVEETTELLKQR-FDHIFYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIA 243
Cdd:PLN02766 225 GPTAGAAIASHMdVDKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 244 PDYILCEASLQNQIVWKIKETVKEF-----YGENIKESPDYERiinlRHFKRILSLL-----EGQKIAFGGE-TDEATRY 312
Cdd:PLN02766 305 SSRVYVQEGIYDEFVKKLVEKAKDWvvgdpFDPRARQGPQVDK----QQFEKILSYIehgkrEGATLLTGGKpCGDKGYY 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 313 IAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNdviMHF 392
Cdd:PLN02766 381 IEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN---CYF 457
|
330 340 350
....*....|....*....|....*....|
gi 1595488123 393 TL-NSFPFGGVGSSGMGAYHGKHSFDTFSH 421
Cdd:PLN02766 458 AFdPDCPFGGYKMSGFGRDQGMDALDKYLQ 487
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
95-420 |
1.79e-39 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 149.28 E-value: 1.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 95 AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKL-----LPqylDQDLYIVINGGVEE 169
Cdd:PRK09847 151 AMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLakeagLP---DGVLNVVTGFGHEA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 170 TTEL-LKQRFDHIFYTGNTAVGKIVM-EAAAKHLTPVTLELGGKSPCYIDKDC-DLDIVCRRITWGKYMNCGQTCIAPDY 246
Cdd:PRK09847 228 GQALsRHNDIDAIAFTGSTRTGKQLLkDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTR 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 247 ILCEASLQNQIVWKIKETVKEFY-GENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEATrYIAPTVLTD 320
Cdd:PRK09847 308 LLLEESIADEFLALLKQQAQNWQpGHPLDPATTMGTLIDCAHADSVHSFIRegeskGQLLLDGRNAGLAA-AIGPTIFVD 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 321 VDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGV---TGNDVIMhftlnSF 397
Cdd:PRK09847 387 VDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVfvnNYNDGDM-----TV 461
|
330 340
....*....|....*....|...
gi 1595488123 398 PFGGVGSSGMGAYHGKHSFDTFS 420
Cdd:PRK09847 462 PFGGYKQSGNGRDKSLHALEKFT 484
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
1-419 |
6.04e-39 |
|
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: 147.28 E-value: 6.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 1 MELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKsefnVYSQ---EVITVLGEIDF------- 70
Cdd:cd07085 40 VDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGK----TLADargDVLRGLEVVEFacsiphl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 71 -MLENLPEwvtakpVKKNVltmldEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAK 149
Cdd:cd07085 116 lKGEYLEN------VARGI-----DTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 150 LLPQY-LDQDLYIVINGGVEETTELLkqrfDH-----IFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLD 223
Cdd:cd07085 185 LLQEAgLPDGVLNVVHGGKEAVNALL----DHpdikaVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 224 IVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EG 297
Cdd:cd07085 261 QTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLkVGAGDDPGADMGPVISPAAKERIEGLIesgveEG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 298 QKIAFGGETDEATRY-----IAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIK 372
Cdd:cd07085 341 AKLVLDGRGVKVPGYengnfVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAAR 420
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1595488123 373 RMIDETSSGGVtGNDVIMHFTLNSFPFGGVGSSGMGAYH--GKHSFDTF 419
Cdd:cd07085 421 KFQREVDAGMV-GINVPIPVPLAFFSFGGWKGSFFGDLHfyGKDGVRFY 468
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
96-408 |
5.44e-38 |
|
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: 144.95 E-value: 5.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 96 YIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKL-----LPQYldqdlyiVINGgVEET 170
Cdd:cd07140 142 LTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELtvkagFPKG-------VINI-LPGS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 171 TELLKQRF-DH-----IFYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIA 243
Cdd:cd07140 214 GSLVGQRLsDHpdvrkLGFTGSTPIGKHIMKSCAVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIA 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 244 PDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRIL-----SLLEGQKIAFGG-ETDEATRYIAPT 316
Cdd:cd07140 294 AGRLFVEESIHDEFVRRVVEEVKKMkIGDPLDRSTDHGPQNHKAHLDKLVeycerGVKEGATLVYGGkQVDRPGFFFEPT 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 317 VLTDVDPKTKVMQEEIFGPILPIVPVKN--VDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNdvimhfTL 394
Cdd:cd07140 374 VFTDVEDHMFIAKEESFGPIMIISKFDDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVN------TY 447
|
330
....*....|....*...
gi 1595488123 395 N----SFPFGGVGSSGMG 408
Cdd:cd07140 448 NktdvAAPFGGFKQSGFG 465
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
2-414 |
8.96e-38 |
|
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: 144.08 E-value: 8.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 2 ELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVL-------GEIDFMLEN 74
Cdd:cd07111 62 DAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESRDCDIPLVArhfyhhaGWAQLLDTE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 75 LPEWvtakpvkknvltmldeayiqpQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY 154
Cdd:cd07111 142 LAGW---------------------KPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 155 -LDQDLYIVINGGVEETTELLKQ-RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWG 232
Cdd:cd07111 201 gLPPGVLNIVTGNGSFGSALANHpGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 233 KYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLEGQKiAFGGETDEATR 311
Cdd:cd07111 281 IWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLrVGDPLDKAIDMGAIVDPAQLKRIRELVEEGR-AEGADVFQPGA 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 312 -------YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVT 384
Cdd:cd07111 360 dlpskgpFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVW 439
|
410 420 430
....*....|....*....|....*....|....
gi 1595488123 385 GNdvimhfTLNSF----PFGGVGSSGMGAYHGKH 414
Cdd:cd07111 440 IN------GHNLFdaaaGFGGYRESGFGREGGKE 467
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
100-419 |
9.81e-38 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 144.95 E-value: 9.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 100 QPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKL-----LPqylDQDLYIVINGGVEETTELL 174
Cdd:PLN02466 194 EPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLlheagLP---PGVLNVVSGFGPTAGAALA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 175 KQR-FDHIFYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEAS 252
Cdd:PLN02466 271 SHMdVDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHER 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 253 LQNQIVWK-----IKETVKEFYGENIKESPDyeriINLRHFKRILSLLE-----GQKIAFGGETDEATRY-IAPTVLTDV 321
Cdd:PLN02466 351 VYDEFVEKakaraLKRVVGDPFKKGVEQGPQ----IDSEQFEKILRYIKsgvesGATLECGGDRFGSKGYyIQPTVFSNV 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 322 DPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGN--DVIMhftlNSFPF 399
Cdd:PLN02466 427 QDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfDVFD----AAIPF 502
|
330 340
....*....|....*....|
gi 1595488123 400 GGVGSSGMGAYHGKHSFDTF 419
Cdd:PLN02466 503 GGYKMSGIGREKGIYSLNNY 522
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
93-408 |
3.47e-36 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 139.63 E-value: 3.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 93 DEAYIQPQPLGVVLIIGAWNYPfvltIQ-------PligAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVIN 164
Cdd:PRK13252 134 SFVYTRREPLGVCAGIGAWNYP----IQiacwksaP---ALAAGNAMIFKPSEVTPLTALKLAEIYTEAgLPDGVFNVVQ 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 165 GgVEETTELLKQ--RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCI 242
Cdd:PRK13252 207 G-DGRVGAWLTEhpDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCT 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 243 APDYILCEASLQNQIVWKIKETVKEFY-GENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGGE--TDEATR--- 311
Cdd:PRK13252 286 NGTRVFVQKSIKAAFEARLLERVERIRiGDPMDPATNFGPLVSFAHRDKVLGYIekgkaEGARLLCGGErlTEGGFAnga 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 312 YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVtgndvimh 391
Cdd:PRK13252 366 FVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGIC-------- 437
|
330 340
....*....|....*....|....
gi 1595488123 392 fTLNSF-------PFGGVGSSGMG 408
Cdd:PRK13252 438 -WINTWgespaemPVGGYKQSGIG 460
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
11-412 |
1.12e-34 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 135.78 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 11 AFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSefnvYSQEVITVLGEIDFM---------LENLPEWVTA 81
Cdd:cd07083 67 AFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKN----WVEAIDDVAEAIDFIryyaraalrLRYPAVEVVP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 82 KPVKKNVLTMldeayiqpQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSE----LSENTAKIL--AKLLP--- 152
Cdd:cd07083 143 YPGEDNESFY--------VGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEdavvVGYKVFEIFheAGFPPgvv 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 153 QYLDQDLYIVINGGVEEttellkQRFDHIFYTGNTAVGKIVMEAAAKHLT------PVTLELGGKSPCYIDKDCDLDIVC 226
Cdd:cd07083 215 QFLPGVGEEVGAYLTEH------ERIRGINFTGSLETGKKIYEAAARLAPgqtwfkRLYVETGGKNAIIVDETADFELVV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 227 RRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLEGQK----IA 301
Cdd:cd07083 289 EGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLsVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKnegqLV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 302 FGGETDEATRY-IAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVD--EAINFINEREKPLALYVFSHNHKLIKRMIDET 378
Cdd:cd07083 369 LGGKRLEGEGYfVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREF 448
|
410 420 430
....*....|....*....|....*....|....
gi 1595488123 379 SSGGVTGNDVIMHFTLNSFPFGGVGSSGMGAYHG 412
Cdd:cd07083 449 HVGNLYINRKITGALVGVQPFGGFKLSGTNAKTG 482
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
1-416 |
1.27e-34 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 134.99 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 1 MELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSeFNVYSQEVITVLGEIDFMLENLPEWVT 80
Cdd:PRK13968 31 IENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKP-INQARAEVAKSANLCDWYAEHGPAMLK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 81 AKPVkknvLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDL 159
Cdd:PRK13968 110 AEPT----LVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDAgIPQGV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 160 YIVINGGVEETTELLKQ-RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCG 238
Cdd:PRK13968 186 YGWLNADNDGVSQMINDsRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 239 QTCIAPDYILCEASLQNQIVWKIKETVKEF-YGENIKESPDYERI--INLR---HFKRILSLLEGQKIAFGGETDE-ATR 311
Cdd:PRK13968 266 QVCAAAKRFIIEEGIASAFTERFVAAAAALkMGDPRDEENALGPMarFDLRdelHHQVEATLAEGARLLLGGEKIAgAGN 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 312 YIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVtgndvimh 391
Cdd:PRK13968 346 YYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGV-------- 417
|
410 420 430
....*....|....*....|....*....|....*
gi 1595488123 392 fTLNSF-------PFGGVGSSGMG---AYHGKHSF 416
Cdd:PRK13968 418 -FINGYcasdarvAFGGVKKSGFGrelSHFGLHEF 451
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
89-429 |
1.05e-33 |
|
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: 132.58 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 89 LTMLDE---AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVING 165
Cdd:cd07116 121 ISEIDEntvAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNG 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 166 -GVEETTELL-KQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSP-----CYIDKDcdlDIVCRRITWGKYM--- 235
Cdd:cd07116 201 fGLEAGKPLAsSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPniffaDVMDAD---DAFFDKALEGFVMfal 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 236 NCGQTCIAPDYILCEASLQNQIVWKIKETVKEFygenIKESP-DYERII----NLRHFKRILSLL-----EGQKIAFGGE 305
Cdd:cd07116 278 NQGEVCTCPSRALIQESIYDRFMERALERVKAI----KQGNPlDTETMIgaqaSLEQLEKILSYIdigkeEGAEVLTGGE 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 306 -----TDEATRYIAPTVLTDVDpKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSS 380
Cdd:cd07116 354 rnelgGLLGGGYYVPTTFKGGN-KMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQA 432
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1595488123 381 GGVTGNdvIMHFTLNSFPFGGVGSSGMGAYHGKHSFDTFSHQRpCLLKS 429
Cdd:cd07116 433 GRVWTN--CYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK-NLLVS 478
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
100-419 |
1.50e-33 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 132.34 E-value: 1.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 100 QPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY-LDQDLYIVING-----GVEETTEL 173
Cdd:PRK11241 145 QPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAgIPAGVFNVVTGsagavGGELTSNP 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 174 LKQRFDhifYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASL 253
Cdd:PRK11241 225 LVRKLS---FTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGV 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 254 QNQIVWKIKETVKEFY-GENIKESPDYERIINLRHFKRIL-----SLLEGQKIAFGGETDE-ATRYIAPTVLTDVDPKTK 326
Cdd:PRK11241 302 YDRFAEKLQQAVSKLHiGDGLEKGVTIGPLIDEKAVAKVEehiadALEKGARVVCGGKAHElGGNFFQPTILVDVPANAK 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 327 VMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNsfPFGGVGSSG 406
Cdd:PRK11241 382 VAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA--PFGGIKASG 459
|
330
....*....|...
gi 1595488123 407 MGAYHGKHSFDTF 419
Cdd:PRK11241 460 LGREGSKYGIEDY 472
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
5-406 |
5.05e-33 |
|
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: 130.08 E-value: 5.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNvySQ-EVITVLGEIDFML----ENLPEWV 79
Cdd:cd07095 6 VAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWE--AQtEVAAMAGKIDISIkayhERTGERA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 80 TAKPVKKNVLTMldeayiqpQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLL-PQYLDQD 158
Cdd:cd07095 84 TPMAQGRAVLRH--------RPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWeEAGLPPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 159 LYIVINGGVEETTELLKQ-RFDHIFYTGNTAVGKIVMEAAAKHltP---VTLELGGKSPCYIDKDCDLDIVCRRITWGKY 234
Cdd:cd07095 156 VLNLVQGGRETGEALAAHeGIDGLLFTGSAATGLLLHRQFAGR--PgkiLALEMGGNNPLVVWDVADIDAAAYLIVQSAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 235 MNCGQTC------IAPDYILCEASLQnQIVWKIKETV-------KEFYGENI--KESPDYERIINLRHFKRILSLLEGQK 299
Cdd:cd07095 234 LTAGQRCtcarrlIVPDGAVGDAFLE-RLVEAAKRLRigapdaePPFMGPLIiaAAAARYLLAQQDLLALGGEPLLAMER 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 300 IafggetDEATRYIAPTVLtDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETS 379
Cdd:cd07095 313 L------VAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIR 385
|
410 420
....*....|....*....|....*..
gi 1595488123 380 SGGVTGNDVIMhFTLNSFPFGGVGSSG 406
Cdd:cd07095 386 AGIVNWNRPTT-GASSTAPFGGVGLSG 411
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
1-411 |
6.74e-29 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 118.83 E-value: 6.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 1 MELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVysqevitvLGEIDFMLE------N 74
Cdd:TIGR01722 40 VDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDA--------LGDVARGLEvvehacG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 75 LPEWVTAKPVKkNVLTMLDEAYIQpQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQY 154
Cdd:TIGR01722 112 VNSLLKGETST-QVATRVDVYSIR-QPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 155 -LDQDLYIVINGGVEETTELLKQ-RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWG 232
Cdd:TIGR01722 190 gAPDGVLNVVHGDKEAVDRLLEHpDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 233 KYMNCGQTCIAPDYILCEASLQnQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLL-----EGQKIAFGG-- 304
Cdd:TIGR01722 270 AYGAAGQRCMAISAAVLVGAAD-EWVPEIRERAEKIrIGPGDDPGAEMGPLITPQAKDRVASLIaggaaEGAEVLLDGrg 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 305 ---ETDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSG 381
Cdd:TIGR01722 349 ykvDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVG 428
|
410 420 430
....*....|....*....|....*....|
gi 1595488123 382 GVtGNDVIMHFTLNSFPFGGVGSSGMGAYH 411
Cdd:TIGR01722 429 QV-GVNVPIPVPLPYFSFTGWKDSFFGDHH 457
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
98-380 |
1.83e-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: 114.61 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 98 QPQPLGVVLIIGAWNYPF-VLTIQPLIGAIAaGNAVIIKPSELSENTA----KILAKLLPQY-LDQDLYIVINGGVEETT 171
Cdd:cd07130 129 QWNPLGVVGVITAFNFPVaVWGWNAAIALVC-GNVVVWKPSPTTPLTAiavtKIVARVLEKNgLPGAIASLVCGGADVGE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 172 ELLK-QRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILce 250
Cdd:cd07130 208 ALVKdPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLI-- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 251 asLQNQIVWKIKETVKEFY-----GENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGE-TDEATRYIAPTVLT 319
Cdd:cd07130 286 --VHESIYDEVLERLKKAYkqvriGDPLDDGTLVGPLHTKAAVDNYLAAIEeaksqGGTVLFGGKvIDGPGNYVEPTIVE 363
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1595488123 320 dVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSS 380
Cdd:cd07130 364 -GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGS 423
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
95-408 |
4.40e-27 |
|
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: 113.28 E-value: 4.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 95 AYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKL-----LPQYLDQDLYIVINGGVEE 169
Cdd:cd07148 118 AFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLlheagLPEGWCQAVPCENAVAEKL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 170 TTEllkQRFDHIFYTGNTAVGKIVMEAAAKHlTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILC 249
Cdd:cd07148 198 VTD---PRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFV 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 250 EASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGETDEATRYiAPTVLTDVDP 323
Cdd:cd07148 274 PAEIADDFAQRLAAAAEKLvVGDPTDPDTEVGPLIRPREVDRVEEWVNeavaaGARLLCGGKRLSDTTY-APTVLLDPPR 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 324 KTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDvimH--FTLNSFPFGG 401
Cdd:cd07148 353 DAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVND---HtaFRVDWMPFAG 429
|
....*..
gi 1595488123 402 VGSSGMG 408
Cdd:cd07148 430 RRQSGYG 436
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
94-416 |
1.20e-26 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 112.14 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 94 EAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLL-----PQYLDQDLyIVINGGVE 168
Cdd:PRK09406 116 RAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFrragfPDGCFQTL-LVGSGAVE 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 169 ETteLLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYIL 248
Cdd:PRK09406 195 AI--LRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFI 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 249 CEASLQNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLE-----GQKIAFGGET-DEATRYIAPTVLTDV 321
Cdd:PRK09406 273 VHADVYDAFAEKFVARMAALrVGDPTDPDTDVGPLATEQGRDEVEKQVDdavaaGATILCGGKRpDGPGWFYPPTVITDI 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 322 DPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDviMHFTLNSFPFGG 401
Cdd:PRK09406 353 TPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFING--MTVSYPELPFGG 430
|
330
....*....|....*...
gi 1595488123 402 VGSSGMG---AYHGKHSF 416
Cdd:PRK09406 431 VKRSGYGrelSAHGIREF 448
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
101-384 |
7.44e-25 |
|
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: 106.55 E-value: 7.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 101 PLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQ--YLDQDLYIVINGGVEETTELLKQ-R 177
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYagLLPPEDVTLINGDGKTMQALLLHpN 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 178 FDHIFYTGNTAVGKIVmeAAAKHLTPVTLELGGKSPCYIDKDCD-LDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQ 256
Cdd:cd07084 180 PKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMLFVPENWSKT 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 257 ivwKIKETVKEFYGENIKESPDYERIINLRHFKRILSL--LEGQKIAFGGETDEATRY-------IAPTVLTDVDP---K 324
Cdd:cd07084 258 ---PLVEKLKALLARRKLEDLLLGPVQTFTTLAMIAHMenLLGSVLLFSGKELKNHSIpsiygacVASALFVPIDEilkT 334
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1595488123 325 TKVMQEEIFGPILPIVPVKNVDEA-INFINEREK-PLALYVFSHNHKLIKRMIDETSSGGVT 384
Cdd:cd07084 335 YELVTEEIFGPFAIVVEYKKDQLAlVLELLERMHgSLTAAIYSNDPIFLQELIGNLWVAGRT 396
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
101-409 |
1.14e-23 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 103.68 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 101 PLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKL-----LPQYLDQdlyiVINGGVEETTELLK 175
Cdd:PLN00412 158 PLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCfhlagFPKGLIS----CVTGKGSEIGDFLT 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 176 QR--FDHIFYTGNTAVGKIVMEAAakhLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASL 253
Cdd:PLN00412 234 MHpgVNCISFTGGDTGIAISKKAG---MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 254 QNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLEG--QKIA-FGGETDEATRYIAPTVLTDVDPKTKVMQE 330
Cdd:PLN00412 311 ADALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVMDakEKGAtFCQEWKREGNLIWPLLLDNVRPDMRIAWE 390
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595488123 331 EIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTlNSFPFGGVGSSGMGA 409
Cdd:PLN00412 391 EPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGP-DHFPFQGLKDSGIGS 468
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
2-406 |
7.10e-23 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 101.19 E-value: 7.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 2 ELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSqEVITVLGEIDFML----ENLPE 77
Cdd:PRK09457 40 DAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAAT-EVTAMINKIAISIqayhERTGE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 78 WVTAKPVKKNVLtmldeayiQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKL-----LP 152
Cdd:PRK09457 119 KRSEMADGAAVL--------RHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLwqqagLP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 153 QYldqdlyiVIN---GGVEETTELLKQR-FDHIFYTGNTAVGKIVMEAAAKHltP---VTLELGGKSPCYIDKDCDLDIV 225
Cdd:PRK09457 191 AG-------VLNlvqGGRETGKALAAHPdIDGLLFTGSANTGYLLHRQFAGQ--PekiLALEMGGNNPLVIDEVADIDAA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 226 CRRITWGKYMNCGQTCIAPDYILCEASLQNQ-IVWKIKETVK-----EFYGEnikESPDYERIINLRHFKRilsLLEGQK 299
Cdd:PRK09457 262 VHLIIQSAFISAGQRCTCARRLLVPQGAQGDaFLARLVAVAKrltvgRWDAE---PQPFMGAVISEQAAQG---LVAAQA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 300 --IAFGGET-------DEATRYIAPTVLtDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKL 370
Cdd:PRK09457 336 qlLALGGKSllemtqlQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDRED 414
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1595488123 371 IKRMIDETSSGGVTGNDvimhfTLN----SFPFGGVGSSG 406
Cdd:PRK09457 415 YDQFLLEIRAGIVNWNK-----PLTgassAAPFGGVGASG 449
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
5-409 |
9.32e-20 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 91.87 E-value: 9.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 5 VRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSefnvysqeVITVLGE----IDF-------MLE 73
Cdd:cd07125 75 LAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKT--------LADADAEvreaIDFcryyaaqARE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 74 NLPEWVTAKPV-KKNVLTMldeayiqpQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLL- 151
Cdd:cd07125 147 LFSDPELPGPTgELNGLEL--------HGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLh 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 152 ----PQYLdqdLYIVINGGVEETTELLKQ-RFDHIFYTGNTAVGKIVMEAAAKH---LTPVTLELGGKSPCYIDKDCDLD 223
Cdd:cd07125 219 eagvPRDV---LQLVPGDGEEIGEALVAHpRIDGVIFTGSTETAKLINRALAERdgpILPLIAETGGKNAMIVDSTALPE 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 224 IVCRRITWGKYMNCGQTC-----------IAPDYI--LCEASLQNQI--VWKIKETVkefyGENIKESpdyeriiNLRHF 288
Cdd:cd07125 296 QAVKDVVQSAFGSAGQRCsalrllylqeeIAERFIemLKGAMASLKVgdPWDLSTDV----GPLIDKP-------AGKLL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 289 KRILSLLEGQK--IAFGGETDEATRYIAPTVLTDVdpKTKVMQEEIFGPILPIV--PVKNVDEAINFINEREKPLALYVF 364
Cdd:cd07125 365 RAHTELMRGEAwlIAPAPLDDGNGYFVAPGIIEIV--GIFDLTTEVFGPILHVIrfKAEDLDEAIEDINATGYGLTLGIH 442
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1595488123 365 SHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMGA 409
Cdd:cd07125 443 SRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGP 487
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
5-421 |
3.96e-19 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 90.19 E-value: 3.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 5 VRRVRQAFLSGRSRPL----RFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVY-SQEVIT-VLGEIDF-MLENLPe 77
Cdd:PLN02419 157 VSAAKQAFPLWRNTPIttrqRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFrGLEVVEhACGMATLqMGEYLP- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 78 wvtakpvkkNVLTMLDEAYIQpQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQ 157
Cdd:PLN02419 236 ---------NVSNGVDTYSIR-EPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLP 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 158 DLYIVINGGVEETTELL--KQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYM 235
Cdd:PLN02419 306 DGVLNIVHGTNDTVNAIcdDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFG 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 236 NCGQTCIAPDYILC---EASLQNQIVWKIKeTVKEFYGEniKESPDYERIINLRHFKRILSLLE-----GQKIAFGGET- 306
Cdd:PLN02419 386 AAGQRCMALSTVVFvgdAKSWEDKLVERAK-ALKVTCGS--EPDADLGPVISKQAKERICRLIQsgvddGAKLLLDGRDi 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 307 ----DEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGG 382
Cdd:PLN02419 463 vvpgYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQ 542
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1595488123 383 VtGNDVIMHFTLNSFPFGGVGSSGMG--AYHGKHSFDTFSH 421
Cdd:PLN02419 543 I-GINVPIPVPLPFFSFTGNKASFAGdlNFYGKAGVDFFTQ 582
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
101-425 |
1.47e-17 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 85.27 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 101 PLGVVLIIGAWNYP-FVLTIQPLIgAIAAGNAVIIK--PSE--LSENTAKILAKLLPQY-LDQDLYIVINGGVEETTELL 174
Cdd:PLN02315 154 PLGIVGVITAFNFPcAVLGWNACI-ALVCGNCVVWKgaPTTplITIAMTKLVAEVLEKNnLPGAIFTSFCGGAEIGEAIA 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 175 KQ-RFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASL 253
Cdd:PLN02315 233 KDtRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 254 QNQIVWKIKETVKEF-YGENIKES----PDYERIiNLRHFKRILSLLEGQ--KIAFGGETDEAT-RYIAPTVLtDVDPKT 325
Cdd:PLN02315 313 YDDVLEQLLTVYKQVkIGDPLEKGtllgPLHTPE-SKKNFEKGIEIIKSQggKILTGGSAIESEgNFVQPTIV-EISPDA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 326 KVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSG-GVTGNDVIMHFTLNSFPFGGVGS 404
Cdd:PLN02315 391 DVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDcGIVNVNIPTNGAEIGGAFGGEKA 470
|
330 340
....*....|....*....|.
gi 1595488123 405 SGMGAYHGKHSFDTFSHQRPC 425
Cdd:PLN02315 471 TGGGREAGSDSWKQYMRRSTC 491
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
100-412 |
2.61e-17 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 84.19 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 100 QPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQ--YLDQDLYIVINGGVEETTELLK-Q 176
Cdd:TIGR01238 159 ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEagFPAGTIQLLPGRGADVGAALTSdP 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 177 RFDHIFYTGNTAVGKIVMEAAAKHL---TPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASL 253
Cdd:TIGR01238 239 RIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDV 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 254 QNQIVWKIKETVKEF-YGENIKESPDYERIINLRHFKRILSLLEGQKiAFGGETDEATR----------YIAPTV--LTD 320
Cdd:TIGR01238 319 ADRVLTMIQGAMQELkVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMS-QTQKKIAQLTLddsracqhgtFVAPTLfeLDD 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 321 VDPktkvMQEEIFGPILPIVPVK--NVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFP 398
Cdd:TIGR01238 398 IAE----LSEEVFGPVLHVVRYKarELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQP 473
|
330
....*....|....
gi 1595488123 399 FGGVGSSGMGAYHG 412
Cdd:TIGR01238 474 FGGQGLSGTGPKAG 487
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
98-406 |
1.96e-13 |
|
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: 72.23 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 98 QPQPLGVVliIGAWN---Y-P---FVLTIQPL-IGAIAA---------GNAVIIKPSelseNTAkilakLLPQYLDQDLY 160
Cdd:cd07123 151 AQQPLSSP--AGVWNrleYrPlegFVYAVSPFnFTAIGGnlagapalmGNVVLWKPS----DTA-----VLSNYLVYKIL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 161 I-------VIN---GGVEETTELLKQR--FDHIFYTGNTAVGKIVMEAAAKHLT-----P-VTLELGGKSPCYIDKDCDL 222
Cdd:cd07123 220 EeaglppgVINfvpGDGPVVGDTVLASphLAGLHFTGSTPTFKSLWKQIGENLDryrtyPrIVGETGGKNFHLVHPSADV 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 223 DIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEfygenIKESPDYE------RIINLRHFKRILSLLE 296
Cdd:cd07123 300 DSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKE-----IKMGDPDDfsnfmgAVIDEKAFDRIKGYID 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 297 ------GQKIAFGGETDEATRY-IAPTVLTDVDPKTKVMQEEIFGPILPI--VPVKNVDEAINFINEREkPLALY--VFS 365
Cdd:cd07123 375 haksdpEAEIIAGGKCDDSVGYfVEPTVIETTDPKHKLMTEEIFGPVLTVyvYPDSDFEETLELVDTTS-PYALTgaIFA 453
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1595488123 366 HNHKLIKRM------------IDETSSGGVTGNDvimhftlnsfPFGGVGSSG 406
Cdd:cd07123 454 QDRKAIREAtdalrnaagnfyINDKPTGAVVGQQ----------PFGGARASG 496
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
94-349 |
2.26e-09 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 59.16 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 94 EAYIQPQPLGVVLIIGAWNYPfVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLpqyldQDlyIVINGGVEETTEL 173
Cdd:cd07077 93 ETYVRAFPIGVTMHILPSTNP-LSGITSALRGIATRNQCIFRPHPSAPFTNRALALLF-----QA--ADAAHGPKILVLY 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 174 LKQR-------------FDHIFYTGntavGKIVMEAAAKH--LTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMncg 238
Cdd:cd07077 165 VPHPsdelaeellshpkIDLIVATG----GRDAVDAAVKHspHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFF--- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 239 qtciapDYILCeASLQNQIVwkiketVKEFYgenikeSPDYERIInLRHFKRILSLLEGQKIAFGGETDEATryiaPTVL 318
Cdd:cd07077 238 ------DQNAC-ASEQNLYV------VDDVL------DPLYEEFK-LKLVVEGLKVPQETKPLSKETTPSFD----DEAL 293
|
250 260 270
....*....|....*....|....*....|.
gi 1595488123 319 tdvdpktkvmqeEIFGPILPIVPVKNVDEAI 349
Cdd:cd07077 294 ------------ESMTPLECQFRVLDVISAV 312
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
101-408 |
2.68e-08 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 56.52 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 101 PLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPselSENTAKILAkllpqyldQDLYIVINGGV-EETTELL----- 174
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKP---AEQTPLIAA--------QAVRILLEAGVpAGVVQLLpgrge 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 175 --------KQRFDHIFYTGNTAVGKIVMEAAAKHL------TPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQT 240
Cdd:PRK11809 837 tvgaalvaDARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQR 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 241 CIAPDyILCeasLQNQIVWKIKETVKEFYGENIKESPDY-----------ERIINL-RHFKRILSllEGQKI---AFGGE 305
Cdd:PRK11809 917 CSALR-VLC---LQDDVADRTLKMLRGAMAECRMGNPDRlstdigpvidaEAKANIeRHIQAMRA--KGRPVfqaARENS 990
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 306 TDEAT-RYIAPTV--LTDVDPktkvMQEEIFGPILPIV--PVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSS 380
Cdd:PRK11809 991 EDWQSgTFVPPTLieLDSFDE----LKREVFGPVLHVVryNRNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHV 1066
|
330 340
....*....|....*....|....*...
gi 1595488123 381 GGVTGNDVIMHFTLNSFPFGGVGSSGMG 408
Cdd:PRK11809 1067 GNLYVNRNMVGAVVGVQPFGGEGLSGTG 1094
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
77-383 |
2.04e-07 |
|
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: 53.25 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 77 EWVtaKPVKKNVLTMLDEAYiQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELS----ENTAKILAKLLP 152
Cdd:cd07127 172 EWE--KPQGKHDPLAMEKTF-TVVPRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAAilplAITVQVAREVLA 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 153 QY-LDQDLYIVInggVEETTELLKQRF-DH-----IFYTGNTAVGKIvMEAAAKHLTPVTlELGGKSPCYIDKDCDLDIV 225
Cdd:cd07127 249 EAgFDPNLVTLA---ADTPEEPIAQTLaTRpevriIDFTGSNAFGDW-LEANARQAQVYT-EKAGVNTVVVDSTDDLKAM 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 226 CRRITWGKYMNCGQTCIAPDYILCEAS-LQNQIVWK--------IKETVKEFYGENIK--------ESPD-YERIINLRH 287
Cdd:cd07127 324 LRNLAFSLSLYSGQMCTTPQNIYVPRDgIQTDDGRKsfdevaadLAAAIDGLLADPARaaallgaiQSPDtLARIAEARQ 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 288 FKRIlsLLEGQKIAFGGETDEATRyiAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINE--REK-PLALYVF 364
Cdd:cd07127 404 LGEV--LLASEAVAHPEFPDARVR--TPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELAREsvREHgAMTVGVY 479
|
330
....*....|....*....
gi 1595488123 365 SHNHKLIKRMIDETSSGGV 383
Cdd:cd07127 480 STDPEVVERVQEAALDAGV 498
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
101-356 |
2.12e-07 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 53.31 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 101 PLGVVLIIGAWNYPFVLTIqplIG-----AIAAGNAVIIK--PS--ELSENTAK-ILAKLLPQYLDQDLYIVINGGVEET 170
Cdd:cd07129 105 PLGPVAVFGASNFPLAFSV---AGgdtasALAAGCPVVVKahPAhpGTSELVARaIRAALRATGLPAGVFSLLQGGGREV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 171 TELLKQrfdH-----IFYTGNTAVGKIVMEAAAKHLT--PVTLELGGKSPCYI-------DKDCDLDIVCRRITwgkyMN 236
Cdd:cd07129 182 GVALVK---HpaikaVGFTGSRRGGRALFDAAAARPEpiPFYAELGSVNPVFIlpgalaeRGEAIAQGFVGSLT----LG 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 237 CGQTC------IAPDYILCEASLQnqivwKIKETVKEFYG-----ENIKESpdYERIINlrhfkRILSLLEGQKIAFGGE 305
Cdd:cd07129 255 AGQFCtnpglvLVPAGPAGDAFIA-----ALAEALAAAPAqtmltPGIAEA--YRQGVE-----ALAAAPGVRVLAGGAA 322
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1595488123 306 TDEATRYiAPTVL-TDVDP--KTKVMQEEIFGPILPIVPVKNVDEAINFINERE 356
Cdd:cd07129 323 AEGGNQA-APTLFkVDAAAflADPALQEEVFGPASLVVRYDDAAELLAVAEALE 375
|
|
| ALDH_F18-19_ProA-GPR |
cd07079 |
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; ... |
6-354 |
1.47e-06 |
|
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; Gamma-glutamyl phosphate reductase (GPR), a L-proline biosynthetic pathway (PBP) enzyme that catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The glutamate route of the PBP involves two enzymatic steps catalyzed by gamma-glutamyl kinase (GK, EC 2.7.2.11) and GPR (EC 1.2.1.41). These enzymes are fused into the bifunctional enzyme, ProA or delta(1)-pyrroline-5-carboxylate synthetase (P5CS) in plants and animals, whereas they are separate enzymes in bacteria and yeast. In humans, the P5CS (ALDH18A1), an inner mitochondrial membrane enzyme, is essential to the de novo synthesis of the amino acids proline and arginine. Tomato (Lycopersicon esculentum) has both the prokaryotic-like polycistronic operons encoding GK and GPR (PRO1, ALDH19) and the full-length, bifunctional P5CS (PRO2, ALDH18B1).
Pssm-ID: 143398 Cd Length: 406 Bit Score: 50.51 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 6 RRVRQAFLsgrsrplrfRLQQL------EALRRM---VQEREKDILTAIAADLCKSEFNVYSQEVIT--VLGE--IDFML 72
Cdd:cd07079 5 KRAKAASR---------ALATLsteqknAALLAIadaLEANRDEILEANAKDLAAAREAGLSEALLDrlLLTPerIEAMA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 73 E------NLPEwvtakPVKKnVLTM--LD---EAYIQPQPLGVVLIIgawnY---PFVlTIQPLIGAIAAGNAVIIKPSE 138
Cdd:cd07079 76 EglrqvaALPD-----PVGE-VLRGwtLPnglQIEKVRVPLGVIGII----YesrPNV-TVDAAALCLKSGNAVILRGGS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 139 LSENTAKILAKLLPQ-----YLDQDLYIVI-NGGVEETTELLKQRfDH----IFYTGNTAVGKIVMEAaakhLTPVtLEl 208
Cdd:cd07079 145 EALHSNRALVEIIQEaleeaGLPEDAVQLIpDTDREAVQELLKLD-DYidliIPRGGAGLIRFVVENA----TIPV-IK- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 209 GGKSPC--YIDKDCDLDIVCRRITWGKYMNCGqTCIAPDYILCEASLQNQIVWKIKETVKEfygENIKespdyeriinLR 286
Cdd:cd07079 218 HGDGNChvYVDESADLEMAVRIVVNAKTQRPS-VCNALETLLVHRDIAEEFLPKLAEALRE---AGVE----------LR 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595488123 287 HFKRILSLLEGQKIAfgGETDEATRYIAptvltdvdpktkvmqeeifgPILPIVPVKNVDEAINFINE 354
Cdd:cd07079 284 GDEETLAILPGAKPA--TEEDWGTEYLD--------------------LILAVKVVDSLDEAIAHINR 329
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
101-381 |
1.58e-06 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 50.57 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 101 PLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKP----SELSENTAKILAKL-LPQyldQDLYIVINGGVEETTELLK 175
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVdskvSVVMEQFLRLLHLCgMPA---TDVDLIHSDGPTMNKILLE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 176 QRFDHIFYTGNTAV---------GKIVMEAAA---KHLTPVTLELGgkspcYIDKDCDLDivcrritwgKYMNCGQTCIA 243
Cdd:cd07126 219 ANPRMTLFTGSSKVaerlalelhGKVKLEDAGfdwKILGPDVSDVD-----YVAWQCDQD---------AYACSGQKCSA 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 244 PDYILC-EASLQNQIVWKIKETVKEFYGENIKESP----DYERIINlrHFKRILSlLEGQKIAFGGEtdEATRYIAPTVL 318
Cdd:cd07126 285 QSILFAhENWVQAGILDKLKALAEQRKLEDLTIGPvltwTTERILD--HVDKLLA-IPGAKVLFGGK--PLTNHSIPSIY 359
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595488123 319 TDVDP-------KTKVMQE-------EIFGPILPIVPVKNVDEAINF-INER-EKPLALYVFSHNHKLIKRMIDETSSG 381
Cdd:cd07126 360 GAYEPtavfvplEEIAIEEnfelvttEVFGPFQVVTEYKDEQLPLVLeALERmHAHLTAAVVSNDIRFLQEVLANTVNG 438
|
|
| LuxC |
pfam05893 |
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ... |
93-383 |
2.34e-06 |
|
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: 49.75 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 93 DEAYIQPQPLGVVLIIGAWNYPfVLTIQPLIGAIAAGNAVIIKPSElSEN--TAKILAKLLPQYLDQDL--YIVI---NG 165
Cdd:pfam05893 80 KPSYEKAFPPGLVFHVLSGNVP-LLPVMSILMGLLVKNVNLLKVSS-SDPftAAALLASFADLDPTHPLadSLSVvywDG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 166 GVEETTELLKQRFDHIF-YTGNTAVgkivmEAAAKHLTPVT--LELGGK-SPCYIDKDCDLDIVCRRI-----TWGKymn 236
Cdd:pfam05893 158 GSTQLEDLIVANADVVIaWGGEDAI-----NAIRECLKPGKqwIDFGAKiSFAVVDREAALDKAAERAaddicVFDQ--- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 237 cgQTCIAPDYILCEASLQNQivwkIKETVKEFYGENIKESPDYER----------IINLRHFKRILSLLEGQkiaFGGET 306
Cdd:pfam05893 230 --QACLSPQTVFVESDDKIT----PDEFAERLAAALAKRARILPKavldideaakISSDRAECKLDYAFAGE---RGVWS 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 307 DEATRYiapTVLTDVDpktkvmQEEIFGPI---LPIVPVKNVDEAINFINEREKPL---ALYVFSHNhklIKRMIDETSS 380
Cdd:pfam05893 301 DFHQRW---TVIWSDG------QEELNSPLnrtVNVVPVPSLSDVVRYVSENRTYLqtcGLAPYSGR---LPYLDRKLAL 368
|
...
gi 1595488123 381 GGV 383
Cdd:pfam05893 369 AGV 371
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
103-375 |
8.36e-06 |
|
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: 48.03 E-value: 8.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 103 GVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKP----SELSENTAKIL--AKLLPQYLDQdlyiVINGGVEETTELLkQ 176
Cdd:cd07128 146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPatatAYLTEAVVKDIveSGLLPEGALQ----LICGSVGDLLDHL-G 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 177 RFDHIFYTGNTAVGKI--VMEAAAKHLTPVTLELGGKSPCYIDKDC-------DLDI--VCRRITwgkyMNCGQTCIAPD 245
Cdd:cd07128 221 EQDVVAFTGSAATAAKlrAHPNIVARSIRFNAEADSLNAAILGPDAtpgtpefDLFVkeVAREMT----VKAGQKCTAIR 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 246 YILCEASLQNQIVWKIKE-TVKEFYGENIKESPDYERIINLRHF----KRILSLLEGQKIAFGGETDEATR--------Y 312
Cdd:cd07128 297 RAFVPEARVDAVIEALKArLAKVVVGDPRLEGVRMGPLVSREQRedvrAAVATLLAEAEVVFGGPDRFEVVgadaekgaF 376
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1595488123 313 IAPTVLT--DVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMI 375
Cdd:cd07128 377 FPPTLLLcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELV 441
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
100-138 |
1.08e-05 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 48.01 E-value: 1.08e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1595488123 100 QPLGVVLIIGAWNYPfvLTIqpLIG----AIAAGNAVIIKPSE 138
Cdd:COG4230 679 RGRGVFVCISPWNFP--LAI--FTGqvaaALAAGNTVLAKPAE 717
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
97-349 |
2.19e-05 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 46.88 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 97 IQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYL-----DQDLYIVINGGVEETT 171
Cdd:cd07081 91 IIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAvaagaPENLIGWIDNPSIELA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 172 ELLKQR--FDHIFYTGntavGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILC 249
Cdd:cd07081 171 QRLMKFpgIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 250 EASLQNQIV--------WKIK----ETVKEFYGENIKESPDyerIINLRHFKriLSLLEGQKIAfggetdEATR--YIAP 315
Cdd:cd07081 247 VDSVYDEVMrlfegqgaYKLTaeelQQVQPVILKNGDVNRD---IVGQDAYK--IAAAAGLKVP------QETRilIGEV 315
|
250 260 270
....*....|....*....|....*....|....
gi 1595488123 316 TVLTDVDPktkvMQEEIFGPILPIVPVKNVDEAI 349
Cdd:cd07081 316 TSLAEHEP----FAHEKLSPVLAMYRAANFADAD 345
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
100-138 |
1.20e-04 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 44.86 E-value: 1.20e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1595488123 100 QPLGVVLIIGAWNYPfvLTIqpLIG----AIAAGNAVIIKPSE 138
Cdd:PRK11905 675 KPLGPVVCISPWNFP--LAI--FTGqiaaALVAGNTVLAKPAE 713
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
123-357 |
4.73e-04 |
|
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: 42.61 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 123 IGAIAAGNAVIIKPSELSENTAKILAKLLPQYldqdlyIVINGG-------VEE-TTELLKQRFDH-----IFYTGNTAV 189
Cdd:cd07121 119 ISMLAAGNAVVFNPHPGAKKVSAYAVELINKA------IAEAGGpdnlvvtVEEpTIETTNELMAHpdinlLVVTGGPAV 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 190 GKIVMEAAAKhltpvtlELG---GKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKEtVK 266
Cdd:cd07121 193 VKAALSSGKK-------AIGagaGNPPVVVDETADIEKAARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAAMQR-NG 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 267 EFYGENIKESPDYERIINLRHFKRILSLLEGQ---KIA--FGGETDEATRYIaptvLTDVDPKTKVMQEEIFGPILPIVP 341
Cdd:cd07121 265 AYVLNDEQAEQLLEVVLLTNKGATPNKKWVGKdasKILkaAGIEVPADIRLI----IVETDKDHPFVVEEQMMPILPVVR 340
|
250
....*....|....*.
gi 1595488123 342 VKNVDEAINFINEREK 357
Cdd:cd07121 341 VKNFDEAIELAVELEH 356
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
100-138 |
2.51e-03 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 40.57 E-value: 2.51e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1595488123 100 QPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSE 138
Cdd:PRK11904 683 HGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAE 721
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
301-349 |
3.95e-03 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 39.50 E-value: 3.95e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1595488123 301 AFGGETDEATRYIaptvLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAI 349
Cdd:PRK15398 334 AAGINVPKDTRLL----IVETDANHPFVVTELMMPVLPVVRVKDVDEAI 378
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
99-258 |
6.10e-03 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 39.01 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 99 PQPLGVVL-IIGAWNyPFVLTIQPLIGAIAAGNAVIIKPS----ELSENTAKILAKLLPQY-LDQDLYIVI-NGGVEETT 171
Cdd:cd07122 93 AEPVGVIAaLIPSTN-PTSTAIFKALIALKTRNAIIFSPHprakKCSIEAAKIMREAAVAAgAPEGLIQWIeEPSIELTQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595488123 172 ELLKQR-FDHIFYTGNTAVGKivmeAAAKHLTPVtleLG---GKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYI 247
Cdd:cd07122 172 ELMKHPdVDLILATGGPGMVK----AAYSSGKPA---IGvgpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASEQSV 244
|
170
....*....|.
gi 1595488123 248 LCEASLQNQIV 258
Cdd:cd07122 245 IVDDEIYDEVR 255
|
|
| |
