|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
6-449 |
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: 846.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 6 DTLQRARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIISALEADLRRPKQESLIVETEFMKNDIRHILFQLDEWVQSE 85
Cdd:cd07132 2 EAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 86 KPPKSFVNMMDDVQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVIPKYLDNDCYPV 165
Cdd:cd07132 82 PVKKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 166 VCGGPSETAELLNQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCI 245
Cdd:cd07132 162 VLGGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 246 APDYILCSKEVQEKFIVEAKDVLKEWYGENIQSSPDLSRVINANNFQRLLGLMKSGRVAVGGNYDASERFIEPTILVDVK 325
Cdd:cd07132 242 APDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVLTDVK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 326 ETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNETIMHCGVDVLPFGGV 405
Cdd:cd07132 322 PSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGGV 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 442622748 406 GMSGMGRYHGKYGFETFTHKKSCLGKDLSplGEKLSSARYPPYS 449
Cdd:cd07132 402 GNSGMGAYHGKYSFDTFSHKRSCLVKSLN--MEKLNSLRYPPYS 443
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
5-429 |
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: 643.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 5 DDTLQRARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIISALEADLRRPKQESLIVETEFMKNDIRHILFQLDEWVQS 84
Cdd:cd07087 1 AELVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 85 EKPPKSFVNMMDDVQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVIPKYLDNDCYP 164
Cdd:cd07087 81 RRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 165 VVCGGPSETAELLNQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTC 244
Cdd:cd07087 161 VVEGGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 245 IAPDYILCSKEVQEKFIVEAKDVLKEWYGENIQSSPDLSRVINANNFQRLLGLMKSGRVAVGGNYDASERFIEPTILVDV 324
Cdd:cd07087 241 IAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGKVVIGGQVDKEERYIAPTILDDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 325 KETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNETIMHCGVDVLPFGG 404
Cdd:cd07087 321 SPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGG 400
|
410 420
....*....|....*....|....*
gi 442622748 405 VGMSGMGRYHGKYGFETFTHKKSCL 429
Cdd:cd07087 401 VGNSGMGAYHGKAGFDTFSHLKSVL 425
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
2-481 |
0e+00 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 589.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 2 ANFDDTLQRARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIISALEADLRRPKQESLIVETEFMKNDIRHILFQLDEW 81
Cdd:PTZ00381 7 EIIPPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 82 VQSEKPPKSFVNMMDDVQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVIPKYLDND 161
Cdd:PTZ00381 87 LKPEKVDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 162 CYPVVCGGPSETAELLNQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCG 241
Cdd:PTZ00381 167 YVRVIEGGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 242 QTCIAPDYILCSKEVQEKFIVEAKDVLKEWYGENIQSSPDLSRVINANNFQRLLGLMKS--GRVAVGGNYDASERFIEPT 319
Cdd:PTZ00381 247 QTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKDhgGKVVYGGEVDIENKYVAPT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 320 ILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNETIMHCGVDV 399
Cdd:PTZ00381 327 IIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPN 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 400 LPFGGVGMSGMGRYHGKYGFETFTHKKSCLGKdlSPLGEKLSSARYPPYSDRKGSLLSFLLrkrrPLPNLHLSHVLAIGL 479
Cdd:PTZ00381 407 LPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNK--STGNSFDLSLRYPPYTSFKSWVLSFLL----KLSIPVQSEVLKSRL 480
|
..
gi 442622748 480 GV 481
Cdd:PTZ00381 481 FV 482
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
6-452 |
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: 584.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 6 DTLQRARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIISALEADLRRPKQESLIVETEFMKNDIRHILFQLDEWVQSE 85
Cdd:cd07136 2 SLVEKQRAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKPK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 86 KPPKSFVNMMDDVQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVIPKYLDNDCYPV 165
Cdd:cd07136 82 RVKTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 166 VCGGPSETAELLNQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCI 245
Cdd:cd07136 162 VEGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 246 APDYILCSKEVQEKFIVEAKDVLKEWYGENIQSSPDLSRVINANNFQRLLGLMKSGRVAVGGNYDASERFIEPTILVDVK 325
Cdd:cd07136 242 APDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGKIVFGGNTDRETLYIEPTILDNVT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 326 ETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNETIMHCGVDVLPFGGV 405
Cdd:cd07136 322 WDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYLPFGGV 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 442622748 406 GMSGMGRYHGKYGFETFTHKKSCLGK----DLsPLgeklssaRYPPYSDRK 452
Cdd:cd07136 402 GNSGMGSYHGKYSFDTFSHKKSILKKstwfDL-PL-------RYPPYKGKK 444
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
1-427 |
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: 576.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 1 MANFDDTLQRARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIISALEADLRRPKQESLIVETEFMKNDIRHILFQLDE 80
Cdd:cd07135 4 LDEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 81 WVQSEKPPKSFV-NMMDDVQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVIPKYLD 159
Cdd:cd07135 84 WAKDEKVKDGPLaFMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 160 NDCYPVVCGGPSETAELLNQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLIN 239
Cdd:cd07135 164 PDAFQVVQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 240 CGQTCIAPDYILCSKEVQEKFIVEAKDVLKEWYGENIQSSPDLSRVINANNFQRLLGLMKS--GRVAVGGNYDASERFIE 317
Cdd:cd07135 244 AGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDTtkGKVVIGGEMDEATRFIP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 318 PTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNETIMHCGV 397
Cdd:cd07135 324 PTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGV 403
|
410 420 430
....*....|....*....|....*....|
gi 442622748 398 DVLPFGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:cd07135 404 DNAPFGGVGDSGYGAYHGKYGFDTFTHERT 433
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
7-429 |
1.04e-164 |
|
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: 472.67 E-value: 1.04e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 7 TLQRARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIISALEADLRRPKQESLIVETEFMKNDIRHILFQLDEWVQSEK 86
Cdd:cd07137 4 LVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMAPEK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 87 PPKSFVNMMDDVQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVIPKYLDNDCYPVV 166
Cdd:cd07137 84 VKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIKVI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 167 CGGPSETAELLNQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINC-GQTCI 245
Cdd:cd07137 164 EGGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCNnGQACI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 246 APDYILCSKEVQEKFIVEAKDVLKEWYGENIQSSPDLSRVINANNFQRLLGLMKSGRVAV----GGNYDASERFIEPTIL 321
Cdd:cd07137 244 APDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADkivhGGERDEKNLYIEPTIL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 322 VDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNETIMHCGVDVLP 401
Cdd:cd07137 324 LDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTLP 403
|
410 420
....*....|....*....|....*...
gi 442622748 402 FGGVGMSGMGRYHGKYGFETFTHKKSCL 429
Cdd:cd07137 404 FGGVGESGFGAYHGKFSFDAFSHKKAVL 431
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
26-429 |
8.61e-157 |
|
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: 452.45 E-value: 8.61e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 26 RRKQLENLLRCYEEHENEIISALEADLRRPKQESLIVETEFMKNDIRHILFQLDEWVQSEKPPKSFVNMMDDVQIYNDPF 105
Cdd:cd07134 22 RIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKPKRVRTPLLLFGTKSKIRYEPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 106 GVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVIPKYLDNDCYPVVCGGPSETAELLNQRFDYIF 185
Cdd:cd07134 102 GVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFEGDAEVAQALLELPFDHIF 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 186 YTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCSKEVQEKFIVEAK 265
Cdd:cd07134 182 FTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 266 DVLKEWYGEN--IQSSPDLSRVINANNFQRLLGLM-----KSGRVAVGGNYDASERFIEPTILVDVKETDPIMEEEIFGP 338
Cdd:cd07134 262 AEIEKFYGKDaaRKASPDLARIVNDRHFDRLKGLLddavaKGAKVEFGGQFDAAQRYIAPTVLTNVTPDMKIMQEEIFGP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 339 ILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNETIMHCGVDVLPFGGVGMSGMGRYHGKYG 418
Cdd:cd07134 342 VLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNPNLPFGGVNNSGIGSYHGVYG 421
|
410
....*....|.
gi 442622748 419 FETFTHKKSCL 429
Cdd:cd07134 422 FKAFSHERAVL 432
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
5-427 |
2.28e-152 |
|
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: 441.54 E-value: 2.28e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 5 DDTLQRARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIISALEADL-RRPKQESLIVETEFMKNDIRHILFQLDEWVQ 83
Cdd:cd07133 1 QALLERQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFgHRSRHETLLAEILPSIAGIKHARKHLKKWMK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 84 SEKPPKSFVNMMDDVQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVIPKYLDNDCY 163
Cdd:cd07133 81 PSRRHVGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 164 PVVCGGPSETAELLNQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQT 243
Cdd:cd07133 161 AVVTGGADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 244 CIAPDYILCSKEVQEKFIVEAKDVLKEWYGeNIQSSPDLSRVINANNFQRLLGLMKSGR--------VAVGGNYDASERF 315
Cdd:cd07133 241 CVAPDYVLVPEDKLEEFVAAAKAAVAKMYP-TLADNPDYTSIINERHYARLQGLLEDARakgarvieLNPAGEDFAATRK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 316 IEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNETIMHC 395
Cdd:cd07133 320 LPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHV 399
|
410 420 430
....*....|....*....|....*....|..
gi 442622748 396 GVDVLPFGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:cd07133 400 AQDDLPFGGVGASGMGAYHGKEGFLTFSHAKP 431
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
1-461 |
5.25e-149 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 434.92 E-value: 5.25e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 1 MANFDDTLQRARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIISALEADLRRPKQESLIVETEFMKNDIRHILFQLDE 80
Cdd:PLN02203 5 GETLEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSNLKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 81 WVQSEKPPKSFVNMMDDVQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVIPKYLDN 160
Cdd:PLN02203 85 WMAPKKAKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 161 DCYPVVCGGPSETAELLNQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYID---KSVDMRTAVKRILWGKL 237
Cdd:PLN02203 165 KAVKVIEGGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKW 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 238 INC-GQTCIAPDYILcskeVQEKF---IVEA-KDVLKEWYGENIQSSPDLSRVINANNFQRLLGLMKSGRVAV----GGN 308
Cdd:PLN02203 245 GSCaGQACIAIDYVL----VEERFapiLIELlKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAAsivhGGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 309 YDASERFIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSS 388
Cdd:PLN02203 321 IDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTF 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442622748 389 NETIMHCGVDVLPFGGVGMSGMGRYHGKYGFETFTHKKSCLGKDLSPLGEklssARYPPYSDRKGSLLSFLLR 461
Cdd:PLN02203 401 NDAIIQYACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSLLTEFE----FRYPPWNDFKLGFLRLVYR 469
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
12-460 |
2.58e-122 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 366.68 E-value: 2.58e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 12 RLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIISALEADLRRPKQESLIVETEFMKNDIRHILFQLDEWVQSEKPPKSF 91
Cdd:PLN02174 20 RRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEKAKTSL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 92 VNMMDDVQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVIPKYLDNDCYPVVCGGPS 171
Cdd:PLN02174 100 TTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVEGAVT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 172 ETAELLNQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKL-INCGQTCIAPDYI 250
Cdd:PLN02174 180 ETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 251 LCSKEVQEKFIVEAKDVLKEWYGENIQSSPDLSRVINANNFQRLLGLMK----SGRVAVGGNYDASERFIEPTILVDVKE 326
Cdd:PLN02174 260 LTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDekevSDKIVYGGEKDRENLKIAPTILLDVPL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 327 TDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNETIMHCGVDVLPFGGVG 406
Cdd:PLN02174 340 DSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVG 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 442622748 407 MSGMGRYHGKYGFETFTHKKSCLGKDLspLGEklSSARYPPYSDRKGSLLSFLL 460
Cdd:PLN02174 420 ESGMGAYHGKFSFDAFSHKKAVLYRSL--FGD--SAVRYPPYSRGKLRLLKALV 469
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
5-429 |
1.87e-119 |
|
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: 357.29 E-value: 1.87e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 5 DDTLQRARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIISALEADLRRPKQESLiVETEFMKNDIRHILFQLDEWVQS 84
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEAL-GEVARAADTFRYYAGLARRLHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 85 EKPPksfvnMMDDVQIYN--DPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVIPKY-LDND 161
Cdd:cd07078 80 VIPS-----PDPGELAIVrrEPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLPPG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 162 CYPVVCGGPSETAELL--NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLIN 239
Cdd:cd07078 155 VLNVVTGDGDEVGAALasHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 240 CGQTCIAPDYILCSKEVQEKFIVEAKDVLKEWYGEN-IQSSPDLSRVINANNFQRLLGLM-----KSGRVAVGGNYDASE 313
Cdd:cd07078 235 AGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNpLDPDTDMGPLISAAQLDRVLAYIedakaEGAKLLCGGKRLEGG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 314 --RFIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNET 391
Cdd:cd07078 315 kgYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDY 394
|
410 420 430
....*....|....*....|....*....|....*...
gi 442622748 392 IMHcGVDVLPFGGVGMSGMGRYHGKYGFETFTHKKSCL 429
Cdd:cd07078 395 SVG-AEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVT 431
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
9-429 |
8.32e-98 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 299.53 E-value: 8.32e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 9 QRARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIISALEADLRRPKQESLiVETEFMKNDIRHILFQLDEWVQSEKPP 88
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEAL-GEVARAIDTFRYAAGLADKLGGPELPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 89 ksfvnMMDDVQIY--NDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVIPKY-LDNDCYPV 165
Cdd:cd06534 80 -----PDPGGEAYvrREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVVNV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 166 VCGGPSETAELL--NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQT 243
Cdd:cd06534 155 VPGGGDEVGAALlsHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 244 CIAPDYILCSKEVQEKFIveakdvlkewygeniqsspdlsrvinannfqrllglmksgrvavggnydasERFIepTILVD 323
Cdd:cd06534 235 CTAASRLLVHESIYDEFV---------------------------------------------------EKLV--TVLVD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 324 VKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNETIMHCGvDVLPFG 403
Cdd:cd06534 262 VDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVG-PEAPFG 340
|
410 420
....*....|....*....|....*.
gi 442622748 404 GVGMSGMGRYHGKYGFETFTHKKSCL 429
Cdd:cd06534 341 GVKNSGIGREGGPYGLEEYTRTKTVV 366
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
5-427 |
4.63e-95 |
|
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: 296.27 E-value: 4.63e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 5 DDTLQRARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIISALEADLRRPKQESLiVETEFMkndIRHILFQLDEW--V 82
Cdd:COG1012 46 DAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEAR-GEVDRA---ADFLRYYAGEArrL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 83 QSEKPPKSFVNMmdDVQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVI-----PKY 157
Cdd:COG1012 122 YGETIPSDAPGT--RAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLeeaglPAG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 158 LDNdcypVVCGGPSETAELL--NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWG 235
Cdd:COG1012 200 VLN----VVTGDGSEVGAALvaHPDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 236 KLINCGQTCIAPDYILCSKEVQEKFIVEAKDVLKEW-YGENIQSSPDLSRVINANNFQRLLGLMKSG-----RVAVGGNY 309
Cdd:COG1012 276 AFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALkVGDPLDPGTDMGPLISEAQLERVLAYIEDAvaegaELLTGGRR 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 310 DASER--FIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFS 387
Cdd:COG1012 356 PDGEGgyFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVW 435
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 442622748 388 SNETIMHcGVDVLPFGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:COG1012 436 INDGTTG-AVPQAPFGGVKQSGIGREGGREGLEEYTETKT 474
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
2-427 |
1.92e-82 |
|
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: 262.85 E-value: 1.92e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 2 ANFDDTLQRARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIISALEADLRRPKQESLIvetefmknDIRHILFQLDEW 81
Cdd:pfam00171 29 EDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARG--------EVDRAIDVLRYY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 82 V-QSEKPPKSFVNMMDDVQIY--NDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVI---- 154
Cdd:pfam00171 101 AgLARRLDGETLPSDPGRLAYtrREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFeeag 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 155 -PKYLDNdcypVVCGGPSETAELL--NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKR 231
Cdd:pfam00171 181 lPAGVLN----VVTGSGAEVGEALveHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 232 ILWGKLINCGQTCIAPDYILCSKEVQEKFIVEAKDVLKEW-YGENIQSSPDLSRVINANNFQRLLGLMKSG-----RVAV 305
Cdd:pfam00171 257 AVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLkVGDPLDPDTDMGPLISKAQLERVLKYVEDAkeegaKLLT 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 306 GGNYDASE-RFIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSG 384
Cdd:pfam00171 337 GGEAGLDNgYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAG 416
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 442622748 385 GFSSNETIMHcGVDVLPFGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:pfam00171 417 MVWINDYTTG-DADGLPFGGFKQSGFGREGGPYGLEEYTEVKT 458
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
6-427 |
1.95e-77 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 249.83 E-value: 1.95e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 6 DTLQRARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIISALEADLRRPKQESLIvetefmknDIRHILFQLDEWV--- 82
Cdd:cd07099 22 AAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGL--------EVLLALEAIDWAArna 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 83 ----QSEKPPKSFVNMMDDVQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVIPKY- 157
Cdd:cd07099 94 prvlAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAg 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 158 LDNDCYPVVCGGPSETAELLNQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKL 237
Cdd:cd07099 174 PPQGVLQVVTGDGATGAALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAM 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 238 INCGQTCIAPDYILCSKEVQEKFI---VEAKDVLKEWYGENIQSspDLSRVINANNF---QRLLG--LMKSGRVAVGG-N 308
Cdd:cd07099 254 VNAGQTCISVERVYVHESVYDEFVarlVAKARALRPGADDIGDA--DIGPMTTARQLdivRRHVDdaVAKGAKALTGGaR 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 309 YDASERFIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSS 388
Cdd:cd07099 332 SNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSI 411
|
410 420 430
....*....|....*....|....*....|....*....
gi 442622748 389 NETIMHCGVDVLPFGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:cd07099 412 NDVLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKA 450
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
5-426 |
2.91e-64 |
|
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: 214.70 E-value: 2.91e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 5 DDTLQRARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIISAL--EADLRRPKQEsliVETEFMKNDIRH---ILFQLD 79
Cdd:cd07104 3 DRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLirESGSTRPKAA---FEVGAAIAILREaagLPRRPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 80 -EWVQSEKPPKsfVNMmddvqIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKF-IADV---- 153
Cdd:cd07104 80 gEILPSDVPGK--ESM-----VRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLlIAEIfeea 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 154 -IPKYLDNdcypVVCGGPSETAELL--NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVK 230
Cdd:cd07104 153 gLPKGVLN----VVPGGGSEIGDALveHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 231 RILWGKLINCGQTCIAPDYILCSKEVQEKFI---VEAKDVLKewYGEniQSSPD--LSRVINANNFQRLLGLM-----KS 300
Cdd:cd07104 229 AAAFGAFLHQGQICMAAGRILVHESVYDEFVeklVAKAKALP--VGD--PRDPDtvIGPLINERQVDRVHAIVedavaAG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 301 GRVAVGGNYDasERFIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRS 380
Cdd:cd07104 305 ARLLTGGTYE--GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAER 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 442622748 381 TTSGGFSSNETIMHCGVDVlPFGGVGMSGMGRYHGKYGFETFTHKK 426
Cdd:cd07104 383 LETGMVHINDQTVNDEPHV-PFGGVKASGGGRFGGPASLEEFTEWQ 427
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
5-427 |
4.80e-64 |
|
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: 214.86 E-value: 4.80e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 5 DDTLQRARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIISALEADLRRPKQESLIVETEFMKNDIRHILFQLDEWVQS 84
Cdd:cd07098 21 DEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEILVTCEKIRWTLKHGEKALRP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 85 EKPPKSFVNMMDDVQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVIPKYLDNDCYP 164
Cdd:cd07098 101 ESRPGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIRECLAACGHD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 165 -----VVCGGPsETAELL--NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKL 237
Cdd:cd07098 181 pdlvqLVTCLP-ETAEALtsHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 238 INCGQTCIAPDYILCSKEVQEKFIVEAKD-VLKEWYGENIQSSPDLSRVINANNFQRLLGLMKS-----GRVAVGGNY-- 309
Cdd:cd07098 260 QSSGQNCIGIERVIVHEKIYDKLLEILTDrVQALRQGPPLDGDVDVGAMISPARFDRLEELVADavekgARLLAGGKRyp 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 310 ---DASERFIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGF 386
Cdd:cd07098 340 hpeYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMV 419
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 442622748 387 SSNE-TIMHCGVDvLPFGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:cd07098 420 AINDfGVNYYVQQ-LPFGGVKGSGFGRFAGEEGLRGLCNPKS 460
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
104-426 |
8.69e-59 |
|
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: 200.63 E-value: 8.69e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 104 PFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADV-----IPKYLDNdcypVVCGGPSETAELL- 177
Cdd:cd07150 119 PLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEImeeagLPKGVFN----VVTGGGAEVGDELv 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 178 -NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCSKEV 256
Cdd:cd07150 195 dDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPV 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 257 QEKFI---VEAKDVLKewYGENIQSSPDLSRVINANNFQRLLG-----LMKSGRVAVGGNYDAseRFIEPTILVDVKETD 328
Cdd:cd07150 275 YDEFVkkfVARASKLK--VGDPRDPDTVIGPLISPRQVERIKRqvedaVAKGAKLLTGGKYDG--NFYQPTVLTDVTPDM 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 329 PIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNETIMHCGVDVlPFGGVGMS 408
Cdd:cd07150 351 RIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHINDPTILDEAHV-PFGGVKAS 429
|
330
....*....|....*...
gi 442622748 409 GMGRYHGKYGFETFTHKK 426
Cdd:cd07150 430 GFGREGGEWSMEEFTELK 447
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
104-426 |
6.44e-58 |
|
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: 198.43 E-value: 6.44e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 104 PFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADV-----IPKyldnDCYPVVCGGPSETAELLN 178
Cdd:cd07103 117 PVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELaeeagLPA----GVLNVVTGSPAEIGEALC 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 179 QRFDY--IFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCSKEV 256
Cdd:cd07103 193 ASPRVrkISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESI 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 257 QEKFI---VEAKDVLKewYGENIQSSPDLSRVINANNFQRLLGLM-----KSGRVAVGGNYDASE-RFIEPTILVDVKET 327
Cdd:cd07103 273 YDEFVeklVERVKKLK--VGNGLDEGTDMGPLINERAVEKVEALVedavaKGAKVLTGGKRLGLGgYFYEPTVLTDVTDD 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 328 DPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNETIMhcGVDVLPFGGVGM 407
Cdd:cd07103 351 MLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLI--SDAEAPFGGVKE 428
|
330
....*....|....*....
gi 442622748 408 SGMGRYHGKYGFETFTHKK 426
Cdd:cd07103 429 SGLGREGGKEGLEEYLETK 447
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
11-430 |
2.07e-57 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 197.34 E-value: 2.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 11 ARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIISALEADLRRPKQESLIVETEFMKNDIRHILFQLDEWVQSEKPPKS 90
Cdd:cd07138 45 ARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPITLARAAQVGLGIGHLRAAADALKDFEFEERRGNS 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 91 FVNMmddvqiynDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVI-----PKYLDNdcypV 165
Cdd:cd07138 125 LVVR--------EPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILdeaglPAGVFN----L 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 166 VCGGPSETAELL--NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQT 243
Cdd:cd07138 193 VNGDGPVVGEALsaHPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQS 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 244 CIAPDYILCSKEVQEKFIVEAKDVLKEW-YGENIQSSPDLSRVINANNFQRLLGLMKSG-----RVAVGGnydaSER--- 314
Cdd:cd07138 273 CNAPTRMLVPRSRYAEAEEIAAAAAEAYvVGDPRDPATTLGPLASAAQFDRVQGYIQKGieegaRLVAGG----PGRpeg 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 315 -----FIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSN 389
Cdd:cd07138 349 lergyFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN 428
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 442622748 390 ETimhcGVDVL-PFGGVGMSGMGRYHGKYGFETFTHKKSCLG 430
Cdd:cd07138 429 GA----AFNPGaPFGGYKQSGNGREWGRYGLEEFLEVKSIQG 466
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
38-426 |
1.78e-56 |
|
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: 195.18 E-value: 1.78e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 38 EEHENEIISALEADLRRPKQESLiVETEFMKNDIRHILfqldEW--------VQSEKPPKSfvnmmddVQIYNDPFGVVL 109
Cdd:cd07088 71 RENADELAKLIVEEQGKTLSLAR-VEVEFTADYIDYMA----EWarriegeiIPSDRPNEN-------IFIFKVPIGVVA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 110 VIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANC----AKFIADV-IPKYLDNdcypVVCGGPSETAELL--NQRFD 182
Cdd:cd07088 139 GILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNalefAELVDEAgLPAGVLN----IVTGRGSVVGDALvaHPKVG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 183 YIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCSKEVQEKFI- 261
Cdd:cd07088 215 MISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMe 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 262 --VEAKDVLKewYGENIQSSPDLSRVINANNFQRLLGLMK-----SGRVAVGGNYDASER--FIEPTILVDVKETDPIME 332
Cdd:cd07088 295 klVEKMKAVK--VGDPFDAATDMGPLVNEAALDKVEEMVEraveaGATLLTGGKRPEGEKgyFYEPTVLTNVRQDMEIVQ 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 333 EEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGgfssnETIMHCGvdvlPF-------GGV 405
Cdd:cd07088 373 EEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFG-----ETYINRE----NFeamqgfhAGW 443
|
410 420
....*....|....*....|.
gi 442622748 406 GMSGMGRYHGKYGFETFTHKK 426
Cdd:cd07088 444 KKSGLGGADGKHGLEEYLQTK 464
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
7-427 |
5.85e-55 |
|
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: 190.53 E-value: 5.85e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 7 TLQRARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIISALEADLRRPKQESLiVETEFMKNDIRHILFQLDEWVQSEK 86
Cdd:cd07102 23 ALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAG-GEIRGMLERARYMISIAEEALADIR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 87 PPKSfvnmmDDVQ--IYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVIPKY-LDNDCY 163
Cdd:cd07102 102 VPEK-----DGFEryIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAgLPEGVF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 164 PVVCGGPSETAELLNQ-RFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQ 242
Cdd:cd07102 177 QVLHLSHETSAALIADpRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQ 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 243 TCIAPDYILCSKEVQEKFIVEAKDVLKEW-YGENIQSSPDLSRVINANNFQRLLGLM-----KSGRVAVGGN----YDAS 312
Cdd:cd07102 257 SCCSIERIYVHESIYDAFVEAFVAVVKGYkLGDPLDPSTTLGPVVSARAADFVRAQIadaiaKGARALIDGAlfpeDKAG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 313 ERFIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFssnetI 392
Cdd:cd07102 337 GAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTV-----F 411
|
410 420 430
....*....|....*....|....*....|....*...
gi 442622748 393 MHCG--VD-VLPFGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:cd07102 412 MNRCdyLDpALAWTGVKDSGRGVTLSRLGYDQLTRPKS 449
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
11-427 |
4.14e-54 |
|
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: 187.78 E-value: 4.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 11 ARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIISAL--EADLRRPKQEsliVETEFMKNDIRHILFQLDEwVQSEKPP 88
Cdd:cd07105 9 AAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMmeETGATAAWAG---FNVDLAAGMLREAASLITQ-IIGGSIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 89 KSFVNMMddVQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADV-----IPKyldnDCY 163
Cdd:cd07105 85 SDKPGTL--AMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVfheagLPK----GVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 164 PVVCGGPSETAELLNQ-------RFdyIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGK 236
Cdd:cd07105 159 NVVTHSPEDAPEVVEAliahpavRK--VNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 237 LINCGQTCIAPDYILCSKEVQEKFIVEAKDVLKEwygenIQSSPD-LSRVINANNFQRLLGLM-----KSGRVAVGGNYD 310
Cdd:cd07105 237 FLNSGQICMSTERIIVHESIADEFVEKLKAAAEK-----LFAGPVvLGSLVSAAAADRVKELVddalsKGAKLVVGGLAD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 311 ASER--FIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSnSNkLVKEFR--RSTTSGGF 386
Cdd:cd07105 312 ESPSgtSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFT-RD-LARALAvaKRIESGAV 389
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 442622748 387 SSNETIMHcgvD--VLPFGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:cd07105 390 HINGMTVH---DepTLPHGGVKSSGYGRFNGKWGIDEFTETKW 429
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
103-427 |
5.81e-54 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 187.93 E-value: 5.81e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 103 DPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADV-----IPKYLDNdcypVVCGGPSETAELL 177
Cdd:cd07118 118 EPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELlieagLPAGVVN----IVTGYGATVGQAM 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 178 --NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCSKE 255
Cdd:cd07118 194 teHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHES 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 256 VQEKFIVEAKDVLKEW-YGENIQSSPDLSRVINANNFQRLLGLMKSGR-----VAVGGNYDASE--RFIEPTILVDVKET 327
Cdd:cd07118 274 IADAFVAAVVARSRKVrVGDPLDPETKVGAIINEAQLAKITDYVDAGRaegatLLLGGERLASAagLFYQPTIFTDVTPD 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 328 DPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNeTIMHCGVDvLPFGGVGM 407
Cdd:cd07118 354 MAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVN-TFLDGSPE-LPFGGFKQ 431
|
330 340
....*....|....*....|
gi 442622748 408 SGMGRYHGKYGFETFTHKKS 427
Cdd:cd07118 432 SGIGRELGRYGVEEYTELKT 451
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
11-427 |
1.22e-52 |
|
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: 184.37 E-value: 1.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 11 ARLAFSSGK-TRNVSFRRKQLENLLRCYEEHENEIISALEADLRRPkqeSLIVETEFMKNDIRHILFQLD-----EWVQS 84
Cdd:cd07089 28 ARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAP---VMTARAMQVDGPIGHLRYFADladsfPWEFD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 85 -EKPPKSFVNMMDDVQiyNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVI-----PKYL 158
Cdd:cd07089 105 lPVPALRGGPGRRVVR--REPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIaetdlPAGV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 159 DNdcypVVCGGPSETAELL--NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGK 236
Cdd:cd07089 183 VN----VVTGSDNAVGEALttDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVC 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 237 LINCGQTCIAPDYILCSKEVQEKFIVEAKDVLKEW-YGENIQSSPDLSRVINANNFQRLLGLMKSG-----RVAVGGnyd 310
Cdd:cd07089 259 MHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALpVGDPADPGTVMGPLISAAQRDRVEGYIARGrdegaRLVTGG--- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 311 asER--------FIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSnkLVKEFR--RS 380
Cdd:cd07089 336 --GRpagldkgfYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSAD--VDRAYRvaRR 411
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 442622748 381 TTSGGFSSNeTIMHCGVDVlPFGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:cd07089 412 IRTGSVGIN-GGGGYGPDA-PFGGYKQSGLGRENGIEGLEEFLETKS 456
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
102-430 |
2.11e-52 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 184.89 E-value: 2.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 102 NDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEI-------AANCAKfIADVIPKYLDndcypVVCGGPSETA 174
Cdd:PLN02278 158 KQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELtpltalaAAELAL-QAGIPPGVLN-----VVMGDAPEIG 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 175 ELL--NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILC 252
Cdd:PLN02278 232 DALlaSPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILV 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 253 SKEVQEKFiVEA--KDVLKEWYGENIQSSPDLSRVINANNFQRLL-----GLMKSGRVAVGGN-YDASERFIEPTILVDV 324
Cdd:PLN02278 312 QEGIYDKF-AEAfsKAVQKLVVGDGFEEGVTQGPLINEAAVQKVEshvqdAVSKGAKVLLGGKrHSLGGTFYEPTVLGDV 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 325 KETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNETIMhcGVDVLPFGG 404
Cdd:PLN02278 391 TEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLI--STEVAPFGG 468
|
330 340
....*....|....*....|....*..
gi 442622748 405 VGMSGMGRYHGKYGFETFTHKKS-CLG 430
Cdd:PLN02278 469 VKQSGLGREGSKYGIDEYLEIKYvCLG 495
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
92-427 |
3.97e-52 |
|
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: 182.82 E-value: 3.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 92 VNMMDDVQIYN--DPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVIPKY-LDNDCYPVVCG 168
Cdd:cd07109 103 IPLGPGYFVYTvrEPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAgLPAGALNVVTG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 169 -GPSETAELLNQR-FDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIA 246
Cdd:cd07109 183 lGAEAGAALVAHPgVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSA 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 247 PDYILCSKEVQEKFI---VEAKDVLKEWYGEniqSSPDLSRVINANNFQRLLGLM-----KSGRVAVGGNY--DASER-- 314
Cdd:cd07109 263 GSRLLVHRSIYDEVLerlVERFRALRVGPGL---EDPDLGPLISAKQLDRVEGFVararaRGARIVAGGRIaeGAPAGgy 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 315 FIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNETIMH 394
Cdd:cd07109 340 FVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNYGAG 419
|
330 340 350
....*....|....*....|....*....|...
gi 442622748 395 CGVDvLPFGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:cd07109 420 GGIE-LPFGGVKKSGHGREKGLEALYNYTQTKT 451
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
2-427 |
1.15e-51 |
|
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: 181.57 E-value: 1.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 2 ANFDDTLQRARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIISALEADLRRPKQESlIVETEFMKNDIRHIL-FQLDE 80
Cdd:cd07106 19 AQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEA-QFEVGGAVAWLRYTAsLDLPD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 81 WVQSEKPPKSfvnmmddVQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCA----KFIADVIPK 156
Cdd:cd07106 98 EVIEDDDTRR-------VELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTlklgELAQEVLPP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 157 YLDNdcypVVCG----GPSETAellNQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRI 232
Cdd:cd07106 171 GVLN----VVSGgdelGPALTS---HPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 233 LWGKLINCGQTCIAPDYILCSKEVQEKFIVEAKDVLKEWY-GENIQSSPDLSRVINANNFQRLLGLM-----KSGRVAVG 306
Cdd:cd07106 244 FWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVvGDGLDPGTTLGPVQNKMQYDKVKELVedakaKGAKVLAG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 307 GNYDASE-RFIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGG 385
Cdd:cd07106 324 GEPLDGPgYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGT 403
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 442622748 386 FSSNEtimHCGVDV-LPFGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:cd07106 404 VWINT---HGALDPdAPFGGHKQSGIGVEFGIEGLKEYTQTQV 443
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
5-427 |
1.53e-51 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 182.22 E-value: 1.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 5 DDTLQRARLAFSSGKTRNVSFRRKQ-LENLLRCYEEHEnEIISALEA-DLRRPKQESLivetefmKNDIRHILFQLD--- 79
Cdd:cd07144 48 DKAVKAARKAFESWWSKVTGEERGElLDKLADLVEKNR-DLLAAIEAlDSGKPYHSNA-------LGDLDEIIAVIRyya 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 80 ---EWVQSEKPPKSFVNMMDDVQiynDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVI-- 154
Cdd:cd07144 120 gwaDKIQGKTIPTSPNKLAYTLH---EPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVke 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 155 ---PKYLDNdcypVVCG-GPSETAELLNQ-RFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAV 229
Cdd:cd07144 197 agfPPGVVN----IIPGyGAVAGSALAEHpDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 230 KRILWGKLINCGQTCIAPDYILCSKEVQEKFIVEAKDVLKEWY--GENIQSSPDLSRVINANNFQRLLGLMKSG-----R 302
Cdd:cd07144 273 KWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYkvGSPFDDDTVVGPQVSKTQYDRVLSYIEKGkkegaK 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 303 VAVGG----NYDASERFIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFR 378
Cdd:cd07144 353 LVYGGekapEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVA 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 442622748 379 RSTTSGGF---SSNETIMHcgvdvLPFGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:cd07144 433 RELEAGMVwinSSNDSDVG-----VPFGGFKMSGIGRELGEYGLETYTQTKA 479
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
104-427 |
1.85e-51 |
|
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: 181.64 E-value: 1.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 104 PFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVIPKYLdndcYP-----VVCG-GPSETAELL 177
Cdd:cd07091 141 PIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAG----FPpgvvnIVPGfGPTAGAAIS 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 178 NQ-RFDYIFYTGSTRVGKII-HAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCSKE 255
Cdd:cd07091 217 SHmDVDKIAFTGSTAVGRTImEAAAKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQES 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 256 VQEKFIVEAKDVLKEWY-GENIQSSPDLSRVINANNFQRLLGLMKSG-----RVAVGGNYDASE-RFIEPTILVDVKETD 328
Cdd:cd07091 297 IYDEFVEKFKARAEKRVvGDPFDPDTFQGPQVSKAQFDKILSYIESGkkegaTLLTGGERHGSKgYFIQPTVFTDVKDDM 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 329 PIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSN----SNKLVKEFRRST----TSGGFSSNetimhcgvdvL 400
Cdd:cd07091 377 KIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKdinkALRVSRALKAGTvwvnTYNVFDAA----------V 446
|
330 340
....*....|....*....|....*..
gi 442622748 401 PFGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:cd07091 447 PFGGFKQSGFGRELGEEGLEEYTQVKA 473
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
104-426 |
5.05e-50 |
|
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: 177.40 E-value: 5.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 104 PFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVIPK-YLDNDCYPVVCGGPSETAELL--NQR 180
Cdd:cd07149 123 PIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEaGLPKGALNVVTGSGETVGDALvtDPR 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 181 FDYIFYTGSTRVGKIIHAAAnkYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCSKEVQEKF 260
Cdd:cd07149 203 VRMISFTGSPAVGEAIARKA--GLKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEF 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 261 I---VEAKDVLKewYGENIQSSPDLSRVINANNFQRLLGL----MKSG-RVAVGGNYDasERFIEPTILVDVKETDPIME 332
Cdd:cd07149 281 LerfVAATKKLV--VGDPLDEDTDVGPMISEAEAERIEEWveeaVEGGaRLLTGGKRD--GAILEPTVLTDVPPDMKVVC 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 333 EEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNEtIMHCGVDVLPFGGVGMSGMGR 412
Cdd:cd07149 357 EEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMIND-SSTFRVDHMPYGGVKESGTGR 435
|
330
....*....|....
gi 442622748 413 YHGKYGFETFTHKK 426
Cdd:cd07149 436 EGPRYAIEEMTEIK 449
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
103-427 |
7.33e-50 |
|
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: 176.99 E-value: 7.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 103 DPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEI----AANCAKFIADV-IPKYLDNdcypVVCGGPSETAELL 177
Cdd:cd07093 116 QPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWtpltAWLLAELANEAgLPPGVVN----VVHGFGPEAGAAL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 178 --NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCSKE 255
Cdd:cd07093 192 vaHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRS 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 256 VQEKFI---VEAKDVLKewYGENIQSSPDLSRVINANNFQRLLGLMKSGR-----VAVGGNYDASER-----FIEPTILV 322
Cdd:cd07093 272 IYDEFLerfVERAKALK--VGDPLDPDTEVGPLISKEHLEKVLGYVELARaegatILTGGGRPELPDleggyFVEPTVIT 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 323 DVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNETIMHcgvDV-LP 401
Cdd:cd07093 350 GLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNCWLVR---DLrTP 426
|
330 340
....*....|....*....|....*.
gi 442622748 402 FGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:cd07093 427 FGGVKASGIGREGGDYSLEFYTELKN 452
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
2-426 |
1.20e-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: 176.47 E-value: 1.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 2 ANFDDTLQRARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIISALEADLRRPKQESLiVETEFMKNDIRHILFQLDEw 81
Cdd:cd07094 21 ADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR-VEVDRAIDTLRLAAEEAER- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 82 VQSEKPPKSFVNMMDDVQIY--NDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVI-PKYL 158
Cdd:cd07094 99 IRGEEIPLDATQGSDNRLAWtiREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILvEAGV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 159 DNDCYPVVCGGPSETAELL--NQRFDYIFYTGSTRVGKIIHAAANKylTPTTLELGGKSPCYIDKSVDMRTAVKRILWGK 236
Cdd:cd07094 179 PEGVLQVVTGEREVLGDAFaaDERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPVIVDRDADLDAAIEALAKGG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 237 LINCGQTCIAPDYILCSKEVQEKFI---VEAKDVLKewYGENIQSSPDLSRVINANNFQRLL-----GLMKSGRVAVGGN 308
Cdd:cd07094 257 FYHAGQVCISVQRIYVHEELYDEFIeafVAAVKKLK--VGDPLDEDTDVGPLISEEAAERVErwveeAVEAGARLLCGGE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 309 YDAseRFIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSN-SNKLVKEFRRsTTSGGFS 387
Cdd:cd07094 335 RDG--ALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRdLNVAFKAAEK-LEVGGVM 411
|
410 420 430
....*....|....*....|....*....|....*....
gi 442622748 388 SNETiMHCGVDVLPFGGVGMSGMGRYHGKYGFETFTHKK 426
Cdd:cd07094 412 VNDS-SAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEK 449
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
5-427 |
2.79e-49 |
|
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: 174.57 E-value: 2.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 5 DDTLQRARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIISALEADLRRPKQESLiVETEFMKNDIRHIL-----FQLD 79
Cdd:cd07100 2 EAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEAR-AEVEKCAWICRYYAenaeaFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 80 EWVQSEkppksfvnmMDDVQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVIPKY-L 158
Cdd:cd07100 81 EPIETD---------AGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAgF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 159 DNDCYPVVCGGPSETAELL-NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKL 237
Cdd:cd07100 152 PEGVFQNLLIDSDQVEAIIaDPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 238 INCGQTCIApdyilcSKevqeKFIVEAK--DVLKEWYGENIQS-------SPD-----LSRVINANNFQRLL--GLMKSG 301
Cdd:cd07100 232 QNAGQSCIA------AK----RFIVHEDvyDEFLEKFVEAMAAlkvgdpmDEDtdlgpLARKDLRDELHEQVeeAVAAGA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 302 RVAVGGN-YDASERFIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRS 380
Cdd:cd07100 302 TLLLGGKrPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARR 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 442622748 381 TTSGGFSSNEtimHCGVDV-LPFGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:cd07100 382 LEAGMVFING---MVKSDPrLPFGGVKRSGYGRELGRFGIREFVNIKT 426
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
5-423 |
5.99e-49 |
|
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: 174.80 E-value: 5.99e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 5 DDTLQRARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIISAL--EADLRRPKQEsliVETEFMKNDIR---HILFQLD 79
Cdd:cd07151 35 DEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLirESGSTRIKAN---IEWGAAMAITReaaTFPLRME 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 80 -EWVQSEKPPKsfvnmmdDVQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAK-FIADV---- 153
Cdd:cd07151 112 gRILPSDVPGK-------ENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGlLLAKIfeea 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 154 -IPKYLDNdcypVVCGGPSETAEllnqRF------DYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMR 226
Cdd:cd07151 185 gLPKGVLN----VVVGAGSEIGD----AFvehpvpRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADID 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 227 TAVKRILWGKLINCGQTCIAPDYILCSKEVQEKFI---VEAKDVLKewYGEniQSSPD--LSRVINANNFQRLLGLMKS- 300
Cdd:cd07151 257 AAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVekfVERVKALP--YGD--PSDPDtvVGPLINESQVDGLLDKIEQa 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 301 ----GRVAVGGnyDASERFIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKE 376
Cdd:cd07151 333 veegATLLVGG--EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQ 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 442622748 377 FRRSTTSGGFSSNETIMHcgvD--VLPFGGVGMSGMGRYHGKYGFETFT 423
Cdd:cd07151 411 FARRIDAGMTHINDQPVN---DepHVPFGGEKNSGLGRFNGEWALEEFT 456
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
103-426 |
1.02e-48 |
|
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: 173.67 E-value: 1.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 103 DPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEI----AANCAKFIADVIPKYLDNdcypVVCGGPSETAELL- 177
Cdd:cd07092 117 EPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETtpltTLLLAELAAEVLPPGVVN----VVCGGGASAGDALv 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 178 -NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCSKEV 256
Cdd:cd07092 193 aHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 257 QEKF---IVEAkdVLKEWYGENIQSSPDLSRVINANNFQRLLGLM----KSGRVAVGGNY-DASERFIEPTILVDVKETD 328
Cdd:cd07092 273 YDEFvaaLVEA--VSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVerapAHARVLTGGRRaEGPGYFYEPTVVAGVAQDD 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 329 PIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVF----SNSNKLVKEFRRSTTsggfSSNETIMHcgVDVLPFGG 404
Cdd:cd07092 351 EIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWtrdvGRAMRLSARLDFGTV----WVNTHIPL--AAEMPHGG 424
|
330 340
....*....|....*....|..
gi 442622748 405 VGMSGMGRYHGKYGFETFTHKK 426
Cdd:cd07092 425 FKQSGYGKDLSIYALEDYTRIK 446
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
2-427 |
1.50e-48 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 174.07 E-value: 1.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 2 ANFDDTLQRARLAFSSG---KTRNVSFRRKQLENLLRCYEEHENEIISaLEA-DLRRPKQESLIVETEFMKNDIRHILFQ 77
Cdd:cd07141 44 ADVDKAVKAARAAFKLGspwRTMDASERGRLLNKLADLIERDRAYLAS-LETlDNGKPFSKSYLVDLPGAIKVLRYYAGW 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 78 LDEWVQSEKPpksfvnmMD-DVQIY--NDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVI 154
Cdd:cd07141 123 ADKIHGKTIP-------MDgDFFTYtrHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLI 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 155 -----PKYLDNdcypVVCG-GPSETAELLN-QRFDYIFYTGSTRVGKIIHAAANKY-LTPTTLELGGKSPCYIDKSVDMR 226
Cdd:cd07141 196 keagfPPGVVN----VVPGyGPTAGAAISShPDIDKVAFTGSTEVGKLIQQAAGKSnLKRVTLELGGKSPNIVFADADLD 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 227 TAVKRILWGKLINCGQTCIAPDYILCSKEVQEKFI---VE--AKDVLKEWYGENIQSSPDlsrvINANNFQRLLGLMKSG 301
Cdd:cd07141 272 YAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVkrsVEraKKRVVGNPFDPKTEQGPQ----IDEEQFKKILELIESG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 302 R------VAVGGNYDASERFIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVK 375
Cdd:cd07141 348 KkegaklECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAI 427
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 442622748 376 EFRRSTTSGGFSSNetIMHCGVDVLPFGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:cd07141 428 TFSNALRAGTVWVN--CYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKT 477
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
11-426 |
2.64e-48 |
|
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: 172.92 E-value: 2.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 11 ARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIISALEADLRRPKQESlIVETEFMKNDIRHILFQLDEwVQSEKPPks 90
Cdd:cd07145 30 AEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS-RVEVERTIRLFKLAAEEAKV-LRGETIP-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 91 fvnmMDDVqIYND---------PFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSE----IAANCAKFIADV-IPK 156
Cdd:cd07145 106 ----VDAY-EYNErriaftvrePIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSntplTAIELAKILEEAgLPP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 157 YLDNdcypVVCGGPSET-AELL-NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILW 234
Cdd:cd07145 181 GVIN----VVTGYGSEVgDEIVtNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 235 GKLINCGQTCIAPDYILCSKEVQEKFI---VEAKDVLKewYGENIQSSPDLSRVINANNFQRLLGLM-----KSGRVAVG 306
Cdd:cd07145 257 GRFENAGQVCNAVKRILVEEEVYDKFLkllVEKVKKLK--VGDPLDESTDLGPLISPEAVERMENLVndaveKGGKILYG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 307 GNYDASErFIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGF 386
Cdd:cd07145 335 GKRDEGS-FFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGV 413
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 442622748 387 SSNETIMhCGVDVLPFGGVGMSGMGRYHGKYGFETFTHKK 426
Cdd:cd07145 414 VINDSTR-FRWDNLPFGGFKKSGIGREGVRYTMLEMTEEK 452
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
102-427 |
3.22e-48 |
|
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: 173.10 E-value: 3.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 102 NDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEI----AANCAKFIADV-IPKYLDNdcypVVCGGPSETAEL 176
Cdd:cd07143 142 HEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELtplsALYMTKLIPEAgFPPGVIN----VVSGYGRTCGNA 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 177 L--NQRFDYIFYTGSTRVG-KIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCS 253
Cdd:cd07143 218 IssHMDIDKVAFTGSTLVGrKVMEAAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQ 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 254 KEVQEKFIVEAKDVLKEW-----YGENIQSSPDLSRVinanNFQRLLGLMKSGR-----VAVGGNYDASE-RFIEPTILV 322
Cdd:cd07143 298 EGIYDKFVKRFKEKAKKLkvgdpFAEDTFQGPQVSQI----QYERIMSYIESGKaegatVETGGKRHGNEgYFIEPTIFT 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 323 DVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNS-NKLVKEFRRSTTSGGFSSNETIMHCGVdvlP 401
Cdd:cd07143 374 DVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNiNNAIRVANALKAGTVWVNCYNLLHHQV---P 450
|
330 340
....*....|....*....|....*.
gi 442622748 402 FGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:cd07143 451 FGGYKQSGIGRELGEYALENYTQIKA 476
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
11-427 |
7.07e-48 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 172.29 E-value: 7.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 11 ARLAFSSGK-TRNVSFRRKQLENLLRCYEEHENEIISALEA-DLRRPKQESLIVETEFMKNDIRHILFQLDEwVQSEKPP 88
Cdd:cd07142 50 ARKAFDEGPwPRMTGYERSRILLRFADLLEKHADELAALETwDNGKPYEQARYAEVPLAARLFRYYAGWADK-IHGMTLP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 89 ksfVNMMDDVQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADV-----IPKYLDNdcy 163
Cdd:cd07142 129 ---ADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLaaeagLPDGVLN--- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 164 pVVCG-GPSETAELLNQR-FDYIFYTGSTRVGKII-HAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINC 240
Cdd:cd07142 203 -IVTGfGPTAGAAIASHMdVDKVAFTGSTEVGKIImQLAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQ 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 241 GQTCIAPDYILCSKEVQEKFIVEAKDVLKEW-YGENIQSSPDLSRVINANNFQRLLGLMKSG-----RVAVGGNYDASE- 313
Cdd:cd07142 282 GQCCCAGSRTFVHESIYDEFVEKAKARALKRvVGDPFRKGVEQGPQVDKEQFEKILSYIEHGkeegaTLITGGDRIGSKg 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 314 RFIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGgfssneTIM 393
Cdd:cd07142 362 YYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAG------TVW 435
|
410 420 430
....*....|....*....|....*....|....*...
gi 442622748 394 HCGVDVL----PFGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:cd07142 436 VNCYDVFdasiPFGGYKMSGIGREKGIYALNNYLQVKA 473
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
103-427 |
2.14e-47 |
|
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: 170.23 E-value: 2.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 103 DPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAA----NCAKFIADVIPKYLDNdcypVVCGGPSETAELLN 178
Cdd:cd07108 116 EPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPlavlLLAEILAQVLPAGVLN----VITGYGEECGAALV 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 179 QR--FDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWG-KLINCGQTCIAPDYILCSKE 255
Cdd:cd07108 192 DHpdVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHED 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 256 VQEKFI---VEAKDVLKewYGENIQSSPDLSRVINANNFQRLLGLMKSG------RVAVGGN-----YDASERFIEPTIL 321
Cdd:cd07108 272 IYDAFLeklVAKLSKLK--IGDPLDEATDIGAIISEKQFAKVCGYIDLGlstsgaTVLRGGPlpgegPLADGFFVQPTIF 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 322 VDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNEtimhcGVDVLP 401
Cdd:cd07108 350 SGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQ-----GGGQQP 424
|
330 340 350
....*....|....*....|....*....|...
gi 442622748 402 ---FGGVGMSGMGRyhgKYGFET----FTHKKS 427
Cdd:cd07108 425 gqsYGGFKQSGLGR---EASLEGmlehFTQKKT 454
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
2-427 |
2.59e-47 |
|
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: 169.93 E-value: 2.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 2 ANFDDTLQRARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIiSALEA-DLRRPKQESLIVetefmknDIRH---ILFQ 77
Cdd:cd07115 19 EDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADEL-ARLESlDTGKPIRAARRL-------DVPRaadTFRY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 78 LDEWVqsEKPPKSFVNMMDDVQIYN--DPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVIP 155
Cdd:cd07115 91 YAGWA--DKIEGEVIPVRGPFLNYTvrEPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 156 KY-LDNDCYPVVCGGPSETAELL--NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRI 232
Cdd:cd07115 169 EAgFPAGVLNVVTGFGEVAGAALveHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 233 LWGKLINCGQTCIAPDYILCSK----EVQEKFIVEAKDVLkewYGENIQSSPDLSRVINANNFQRLLGLMKSGR------ 302
Cdd:cd07115 249 ATGIFYNQGQMCTAGSRLLVHEsiydEFLERFTSLARSLR---PGDPLDPKTQMGPLVSQAQFDRVLDYVDVGReegarl 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 303 VAVGGNYDASERFIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTT 382
Cdd:cd07115 326 LTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALK 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 442622748 383 SGGFSSNetiMHCGVDV-LPFGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:cd07115 406 AGTVWIN---TYNRFDPgSPFGGYKQSGFGREMGREALDEYTEVKS 448
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
103-427 |
9.84e-46 |
|
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: 165.61 E-value: 9.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 103 DPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVIPKY-LDNDCYPVVCGGPSETAELLNQ-- 179
Cdd:cd07146 119 EPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAgLPPDMLSVVTGEPGEIGDELIThp 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 180 RFDYIFYTGSTRVGKIIHAAANkyLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCSKEVQEK 259
Cdd:cd07146 199 DVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 260 F---IVEAKDVLKewYGENIQSSPDLSRVIN---ANNFQ-RLLGLMKSG-RVAVGGNYDASerFIEPTILVDVKETDPIM 331
Cdd:cd07146 277 FvdlLVEKSAALV--VGDPMDPATDMGTVIDeeaAIQIEnRVEEAIAQGaRVLLGNQRQGA--LYAPTVLDHVPPDAELV 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 332 EEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNEtIMHCGVDVLPFGGVGMSGMG 411
Cdd:cd07146 353 TEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNE-VPGFRSELSPFGGVKDSGLG 431
|
330
....*....|....*..
gi 442622748 412 RYHG-KYGFETFTHKKS 427
Cdd:cd07146 432 GKEGvREAMKEMTNVKT 448
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
104-411 |
1.07e-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: 167.01 E-value: 1.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 104 PFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADV-----IPKyldnDCYPVVCGGPSETAELL- 177
Cdd:cd07124 166 PLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEIleeagLPP----GVVNFLPGPGEEVGDYLv 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 178 -NQRFDYIFYTGSTRVG-KIIHAAAN-----KYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIApdyi 250
Cdd:cd07124 242 eHPDVRFIAFTGSREVGlRIYERAAKvqpgqKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSA---- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 251 lCS-----KEVQEKFI---VEAKDVLKewYGENIQSSPDLSRVINANNFQRLLGLM----KSGRVAVGGNYDASER---F 315
Cdd:cd07124 318 -CSrvivhESVYDEFLerlVERTKALK--VGDPEDPEVYMGPVIDKGARDRIRRYIeigkSEGRLLLGGEVLELAAegyF 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 316 IEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNETIMHC 395
Cdd:cd07124 395 VQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGA 474
|
330
....*....|....*.
gi 442622748 396 GVDVLPFGGVGMSGMG 411
Cdd:cd07124 475 LVGRQPFGGFKMSGTG 490
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
104-427 |
1.58e-45 |
|
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: 165.44 E-value: 1.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 104 PFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVI-----PKYLDNdcypVVCGGpSETAELL- 177
Cdd:cd07139 137 PVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAeeaglPPGVVN----VVPAD-REVGEYLv 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 178 -NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCSKEV 256
Cdd:cd07139 212 rHPGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSR 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 257 QEKF---IVEAKDVLKewYGENIQSSPDLSRVINANNFQRLLGLMKSG-----RVAVGGNY-DASER--FIEPTILVDVK 325
Cdd:cd07139 292 YDEVveaLAAAVAALK--VGDPLDPATQIGPLASARQRERVEGYIAKGraegaRLVTGGGRpAGLDRgwFVEPTLFADVD 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 326 ETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNETIMHCGvdvLPFGGV 405
Cdd:cd07139 370 NDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDFG---APFGGF 446
|
330 340
....*....|....*....|..
gi 442622748 406 GMSGMGRYHGKYGFETFTHKKS 427
Cdd:cd07139 447 KQSGIGREGGPEGLDAYLETKS 468
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
98-426 |
2.41e-45 |
|
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: 165.11 E-value: 2.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 98 VQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVI-----PKYLDNdcypVVCGGPSE 172
Cdd:cd07097 129 VETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILeeaglPAGVFN----LVMGSGSE 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 173 TAELL--NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYI 250
Cdd:cd07097 205 VGQALveHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 251 LCSKEVQEKF---IVEAKDVLKewYGENIQSSPDLSRVINANNFQRLLGLMKSGR-----VAVGGnyDASER-----FIE 317
Cdd:cd07097 285 IVTEGIHDRFveaLVERTKALK--VGDALDEGVDIGPVVSERQLEKDLRYIEIARsegakLVYGG--ERLKRpdegyYLA 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 318 PTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNETIMhcGV 397
Cdd:cd07097 361 PALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTA--GV 438
|
330 340 350
....*....|....*....|....*....|.
gi 442622748 398 DV-LPFGGVGMSGMG-RYHGKYGFETFTHKK 426
Cdd:cd07097 439 DYhVPFGGRKGSSYGpREQGEAALEFYTTIK 469
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
2-426 |
3.43e-45 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 164.94 E-value: 3.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 2 ANFDDTLQRARLAFSSGKTRNVSFRRKQLENLLRCYEEHEnEIISALEA-DLRRPKQESLIVETEFMKNDIRH----ILF 76
Cdd:cd07117 38 ADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENK-ELLAMVETlDNGKPIRETRAVDIPLAADHFRYfagvIRA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 77 QLDEwvqsekppksfVNMMDDVQ---IYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAA----NCAKF 149
Cdd:cd07117 117 EEGS-----------ANMIDEDTlsiVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSlsllELAKI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 150 IADVIPKYLDNdcypVVCGGPSETAE-LLNQR-FDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRT 227
Cdd:cd07117 186 IQDVLPKGVVN----IVTGKGSKSGEyLLNHPgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 228 AVKRILWGKLINCGQTCIAPDYILCSKEVQEKFIVEAKDVLKEW-YGENIQSSPDLSRVINANNFQRLLGLMKSG----- 301
Cdd:cd07117 262 ALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVkVGNPLDPDTQMGAQVNKDQLDKILSYVDIAkeega 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 302 RVAVGG------NYDASErFIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFS-NSNKLV 374
Cdd:cd07117 342 KILTGGhrltenGLDKGF-FIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTkDINRAL 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 442622748 375 KEFRRSTTSGGFSSNETIMHCGVdvlPFGGVGMSGMGRYHGKYGFETFTHKK 426
Cdd:cd07117 421 RVARAVETGRVWVNTYNQIPAGA---PFGGYKKSGIGRETHKSMLDAYTQMK 469
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
85-426 |
4.12e-45 |
|
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: 164.79 E-value: 4.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 85 EKPPKSFVNMMDDVQ--IYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEI----AANCAKFIADV-IPKY 157
Cdd:cd07119 113 TKETGEVYDVPPHVIsrTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVtpltTIALFELIEEAgLPAG 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 158 LDNdcypVVCGGPSETAELL--NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWG 235
Cdd:cd07119 193 VVN----LVTGSGATVGAELaeSPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNG 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 236 KLINCGQTCIAPDYILCSKEVQEKFIVE-AKDVLKEWYGENIQSSPDLSRVINANNFQRLLGLMKSG-----RVAVGGN- 308
Cdd:cd07119 269 VFFNAGQVCSAGSRLLVEESIHDKFVAAlAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLGkeegaRLVCGGKr 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 309 YDASE----RFIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNS----NKLVKEFRRS 380
Cdd:cd07119 349 PTGDElakgYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDiaraNRVARRLRAG 428
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 442622748 381 TT---SGGFSSNETimhcgvdvlPFGGVGMSGMGRYHGKYGFETFTHKK 426
Cdd:cd07119 429 TVwinDYHPYFAEA---------PWGGYKQSGIGRELGPTGLEEYQETK 468
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
5-426 |
9.25e-45 |
|
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: 163.29 E-value: 9.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 5 DDTLQRARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIiSALEA-DLRRPKQESLIvetefmknDIRHIL--FQ---- 77
Cdd:cd07110 22 DAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREEL-AELEArDNGKPLDEAAW--------DVDDVAgcFEyyad 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 78 LDEWVQSEKPPKSFVNMMD-DVQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVI-- 154
Cdd:cd07110 93 LAEQLDAKAERAVPLPSEDfKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIAae 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 155 ---PKYLDNdcypVVCGGPSET-AELLNQR-FDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAV 229
Cdd:cd07110 173 aglPPGVLN----VVTGTGDEAgAPLAAHPgIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 230 KRILWGKLINCGQTCIAPDYILCSKEVQEKFIveakDVLKEWyGENIQSSP------DLSRVINANNFQRLLGLMKSG-- 301
Cdd:cd07110 249 EWAMFGCFWNNGQICSATSRLLVHESIADAFL----ERLATA-AEAIRVGDpleegvRLGPLVSQAQYEKVLSFIARGke 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 302 ---RVAVGGNYDASER---FIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVK 375
Cdd:cd07110 324 egaRLLCGGRRPAHLEkgyFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCD 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 442622748 376 EFRRSTTSGGFSSN-ETIMHCGVdvlPFGGVGMSGMGRYHGKYGFETFTHKK 426
Cdd:cd07110 404 RVAEALEAGIVWINcSQPCFPQA---PWGGYKRSGIGRELGEWGLDNYLEVK 452
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
104-424 |
1.87e-44 |
|
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: 162.48 E-value: 1.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 104 PFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADV-IPKYLDNDCYPVVCGGPSETAELLNQRFD 182
Cdd:cd07101 118 PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELlIEAGLPRDLWQVVTGPGSEVGGAIVDNAD 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 183 YIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCSKEVQEKFI- 261
Cdd:cd07101 198 YVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVr 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 262 --VEAKDVLKewYGENIQSSPDLSRVINANNFQRLLGLM-----KSGRVAVGGNY--DASERFIEPTILVDVKETDPIME 332
Cdd:cd07101 278 rfVARTRALR--LGAALDYGPDMGSLISQAQLDRVTAHVddavaKGATVLAGGRArpDLGPYFYEPTVLTGVTEDMELFA 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 333 EEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNE--TIMHCGVDVlPFGGVGMSGM 410
Cdd:cd07101 356 EETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEgyAAAWASIDA-PMGGMKDSGL 434
|
330
....*....|....
gi 442622748 411 GRYHGKYGFETFTH 424
Cdd:cd07101 435 GRRHGAEGLLKYTE 448
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
104-427 |
4.59e-44 |
|
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: 161.18 E-value: 4.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 104 PFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADV-----IPKYLDNdcypVVCGGPSETAELLN 178
Cdd:cd07114 119 PLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLaeeagFPPGVVN----VVTGFGPETGEALV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 179 Q--RFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCSKEV 256
Cdd:cd07114 195 EhpLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSI 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 257 QEKF---IVEAKDVLKewYGENIQSSPDLSRVINANNFQRLLGLMKS-----GRVAVGGNyDASER------FIEPTILV 322
Cdd:cd07114 275 YDEFverLVARARAIR--VGDPLDPETQMGPLATERQLEKVERYVARareegARVLTGGE-RPSGAdlgagyFFEPTILA 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 323 DVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSnkLVKEFR--RSTTSGGFSSNetiMHCGVDV- 399
Cdd:cd07114 352 DVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRD--LARAHRvaRAIEAGTVWVN---TYRALSPs 426
|
330 340
....*....|....*....|....*...
gi 442622748 400 LPFGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:cd07114 427 SPFGGFKDSGIGRENGIEAIREYTQTKS 454
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
104-427 |
1.02e-43 |
|
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: 160.46 E-value: 1.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 104 PFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADV-----IPKYLDNdcypVVCG-GPSETAEL- 176
Cdd:cd07112 124 PLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELaleagLPAGVLN----VVPGfGHTAGEALg 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 177 LNQRFDYIFYTGSTRVGK-IIHAAANKYLTPTTLELGGKSPCYI-DKSVDMRTAVKRILWGKLINCGQTCIAPDYILCSK 254
Cdd:cd07112 200 LHMDVDALAFTGSTEVGRrFLEYSGQSNLKRVWLECGGKSPNIVfADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 255 EVQEKFIVEAKDVLKEWY-GENIQSSPDLSRVINANNFQRLLGLMKSG-----RVAVGGNYDASER---FIEPTILVDVK 325
Cdd:cd07112 280 SIKDEFLEKVVAAAREWKpGDPLDPATRMGALVSEAHFDKVLGYIESGkaegaRLVAGGKRVLTETggfFVEPTVFDGVT 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 326 ETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSnkLVKEFR--RSTTSGGFSSNeTIMHCGVDVlPFG 403
Cdd:cd07112 360 PDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSD--LSRAHRvaRRLRAGTVWVN-CFDEGDITT-PFG 435
|
330 340
....*....|....*....|....
gi 442622748 404 GVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:cd07112 436 GFKQSGNGRDKSLHALDKYTELKT 459
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
97-426 |
4.36e-43 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 159.51 E-value: 4.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 97 DVQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADV-----IPKYLDNdcypVVCG-GP 170
Cdd:PLN02467 144 KGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADIcrevgLPPGVLN----VVTGlGT 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 171 SETAELLNQ-RFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDY 249
Cdd:PLN02467 220 EAGAPLASHpGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSR 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 250 ILCSKEVQEKFIveakDVLKEWyGENIQSSPDLSR------VINANNFQRLLGLMKSGR-----VAVGGNYDASER---F 315
Cdd:PLN02467 300 LLVHERIASEFL----EKLVKW-AKNIKISDPLEEgcrlgpVVSEGQYEKVLKFISTAKsegatILCGGKRPEHLKkgfF 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 316 IEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKlvkefRRSTTSGGFSSNETIMHC 395
Cdd:PLN02467 375 IEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLE-----RCERVSEAFQAGIVWINC 449
|
330 340 350
....*....|....*....|....*....|....
gi 442622748 396 G---VDVLPFGGVGMSGMGRYHGKYGFETFTHKK 426
Cdd:PLN02467 450 SqpcFCQAPWGGIKRSGFGRELGEWGLENYLSVK 483
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
82-427 |
1.04e-42 |
|
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: 157.89 E-value: 1.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 82 VQSEKPPKSfvNMMDDVqiyndPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADV-----IPK 156
Cdd:cd07131 120 VPSELPNKD--AMTRRQ-----PIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELfaeagLPP 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 157 YLDNdcypVVCGGPSETAELL--NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILW 234
Cdd:cd07131 193 GVVN----VVHGRGEEVGEALveHPDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALW 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 235 GKLINCGQTCIAPDYILCSKEVQEKF---IVEAKDVLKewYGENIQSSPDLSRVINANNFQRLLGLMKSGR--------- 302
Cdd:cd07131 269 SAFGTTGQRCTATSRLIVHESVYDEFlkrFVERAKRLR--VGDGLDEETDMGPLINEAQLEKVLNYNEIGKeegatlllg 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 303 --VAVGGNYDASeRFIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRS 380
Cdd:cd07131 347 geRLTGGGYEKG-YFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRD 425
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 442622748 381 TTSG-GFSSNETImhcGVDV-LPFGGVGMSGMG-RYHGKYGFETFTHKKS 427
Cdd:cd07131 426 LEAGiTYVNAPTI---GAEVhLPFGGVKKSGNGhREAGTTALDAFTEWKA 472
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
100-423 |
2.28e-42 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 156.99 E-value: 2.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 100 IYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEI----AANCAKFIADVIPKYLDNdcypVVCG-GPSETA 174
Cdd:PRK13473 134 IRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEItpltALKLAELAADILPPGVLN----VVTGrGATVGD 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 175 ELLNQR-FDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCS 253
Cdd:PRK13473 210 ALVGHPkVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQ 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 254 KEVQEKF---IVEAKDVLKewYGENIQSSPDLSRVINANNFQRLLGLM------KSGRVAVGGN-YDASERFIEPTILVD 323
Cdd:PRK13473 290 RGIYDDLvakLAAAVATLK--VGDPDDEDTELGPLISAAHRDRVAGFVerakalGHIRVVTGGEaPDGKGYYYEPTLLAG 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 324 VKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSN----SNKLVKEFRRSTTsggfSSNETIMHcgVDV 399
Cdd:PRK13473 368 ARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRdvgrAHRVSARLQYGCT----WVNTHFML--VSE 441
|
330 340
....*....|....*....|....
gi 442622748 400 LPFGGVGMSGMGRYHGKYGFETFT 423
Cdd:PRK13473 442 MPHGGQKQSGYGKDMSLYGLEDYT 465
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
104-424 |
2.90e-42 |
|
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: 155.91 E-value: 2.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 104 PFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKF-IADV-----IPKYLdndcYPVVCGGPsETAELL 177
Cdd:cd07152 110 PLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVvIARLfeeagLPAGV----LHVLPGGA-DAGEAL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 178 --NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCSKE 255
Cdd:cd07152 185 veDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHES 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 256 VQEKF---IVEAKDVLKewYGENIQSSPDLSRVINANNFQRLLGLMKS-----GRVAVGGNYDasERFIEPTILVDVKET 327
Cdd:cd07152 265 VADAYtakLAAKAKHLP--VGDPATGQVALGPLINARQLDRVHAIVDDsvaagARLEAGGTYD--GLFYRPTVLSGVKPG 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 328 DPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNS----NKLVKEFRrsttSGGFSSNETIMHCGVdVLPFG 403
Cdd:cd07152 341 MPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDvgraMALADRLR----TGMLHINDQTVNDEP-HNPFG 415
|
330 340
....*....|....*....|..
gi 442622748 404 GVGMSGMG-RYHGKYGFETFTH 424
Cdd:cd07152 416 GMGASGNGsRFGGPANWEEFTQ 437
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
96-426 |
3.51e-42 |
|
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: 156.51 E-value: 3.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 96 DDVQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADV-----IPKYLDNdcypVVCGGP 170
Cdd:TIGR01804 125 SFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEImeeagLPKGVFN----VVQGDG 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 171 SETAELL--NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPD 248
Cdd:TIGR01804 201 AEVGPLLvnHPDVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGT 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 249 YILCSKEVQEKFIVEAKD-----VLKEWYGENIQSSPdlsrVINANNFQRLLGLMKSG-----RVAVGGNYDASER---- 314
Cdd:TIGR01804 281 RVFVHKKIKERFLARLVErteriKLGDPFDEATEMGP----LISAAHRDKVLSYIEKGkaegaTLATGGGRPENVGlqng 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 315 -FIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNeTIM 393
Cdd:TIGR01804 357 fFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWIN-TYN 435
|
330 340 350
....*....|....*....|....*....|...
gi 442622748 394 HCGVDVlPFGGVGMSGMGRYHGKYGFETFTHKK 426
Cdd:TIGR01804 436 LYPAEA-PFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
92-429 |
7.53e-42 |
|
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: 155.58 E-value: 7.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 92 VNMMDD---VQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAA----NCAKFIADVIPKYLDNdcyp 164
Cdd:cd07559 121 LSEIDEdtlSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPlsilVLMELIGDLLPKGVVN---- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 165 VVCGGPSETAELL--NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYI-----DKSVDMRTAVKRILWGKL 237
Cdd:cd07559 197 VVTGFGSEAGKPLasHPRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFfddamDADDDFDDKAEEGQLGFA 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 238 INCGQTCIAPDYILCSKEVQEKFIVEAKDVLkewygENIQSSPDLSRV------INANNFQRLLGLMKSGR-----VAVG 306
Cdd:cd07559 277 FNQGEVCTCPSRALVQESIYDEFIERAVERF-----EAIKVGNPLDPEtmmgaqVSKDQLEKILSYVDIGKeegaeVLTG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 307 G-----NYDASERFIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFS-NSNKLVKeFRRS 380
Cdd:cd07559 352 GerltlGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTrDINRALR-VARG 430
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 442622748 381 TTSGGFSSNetIMHCGVDVLPFGGVGMSGMGRYHGKYGFETFTHKKSCL 429
Cdd:cd07559 431 IQTGRVWVN--CYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNIL 477
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
11-427 |
1.41e-41 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 156.12 E-value: 1.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 11 ARLAFSSGK-TRNVSFRRKQLenLLR---CYEEHENEIiSALEA-DLRRPKQESLIVETEFMKNDIRHILFQLDE----W 81
Cdd:PLN02466 104 ARKAFDEGPwPKMTAYERSRI--LLRfadLLEKHNDEL-AALETwDNGKPYEQSAKAELPMFARLFRYYAGWADKihglT 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 82 VQSEKPpksfvnmmDDVQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADV-----IPK 156
Cdd:PLN02466 181 VPADGP--------HHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLlheagLPP 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 157 YLDNdcypVVCG-GPSETAELLNQR-FDYIFYTGSTRVGKII-HAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRIL 233
Cdd:PLN02466 253 GVLN----VVSGfGPTAGAALASHMdVDKLAFTGSTDTGKIVlELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAH 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 234 WGKLINCGQTCIAPDYILCSKEVQEKFIVEAK-DVLKEWYGENIQSSPDLSRVINANNFQRLLGLMKSG------RVAVG 306
Cdd:PLN02466 329 FALFFNQGQCCCAGSRTFVHERVYDEFVEKAKaRALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGvesgatLECGG 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 307 GNYDASERFIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSN----SNKLVKEFRRSTt 382
Cdd:PLN02466 409 DRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQnldtANTLSRALRVGT- 487
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 442622748 383 sggfssneTIMHCgVDV----LPFGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:PLN02466 488 --------VWVNC-FDVfdaaIPFGGYKMSGIGREKGIYSLNNYLQVKA 527
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
104-427 |
1.51e-41 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 154.38 E-value: 1.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 104 PFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADV-----IPKYLDNdcypVVCGGpSETAELLN 178
Cdd:cd07090 116 PLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEIlteagLPDGVFN----VVQGG-GETGQLLC 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 179 QRFDY--IFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCSKEV 256
Cdd:cd07090 191 EHPDVakVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSI 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 257 QEKFIVE-AKDVLKEWYGENIQSSPDLSRVINANNFQRLLGLMKSG-----RVAVGGNYDASER------FIEPTILVDV 324
Cdd:cd07090 271 KDEFTERlVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAkqegaKVLCGGERVVPEDglengfYVSPCVLTDC 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 325 KETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSN----SNKLVKEFRRSTT---SGGFSSNEtimhcgv 397
Cdd:cd07090 351 TDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRdlqrAHRVIAQLQAGTCwinTYNISPVE------- 423
|
330 340 350
....*....|....*....|....*....|
gi 442622748 398 dvLPFGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:cd07090 424 --VPFGGYKQSGFGRENGTAALEHYTQLKT 451
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
80-370 |
6.25e-41 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 151.81 E-value: 6.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 80 EWVQSEKPPksfvnmmDDVQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVIPKY-L 158
Cdd:PRK10090 54 EIIQSDRPG-------ENILLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 159 DNDCYPVVCGGPSETAELL--NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGK 236
Cdd:PRK10090 127 PKGVFNLVLGRGETVGQELagNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSR 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 237 LINCGQTCIAPDYILCSKEVQEKFIVEAKDVLKE-WYGENIQ-SSPDLSRVINANNFQRLLGLMKS-----GRVAVGGNY 309
Cdd:PRK10090 207 VINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAvQFGNPAErNDIAMGPLINAAALERVEQKVARaveegARVALGGKA 286
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442622748 310 -DASERFIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNS 370
Cdd:PRK10090 287 vEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQN 348
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
103-427 |
2.41e-40 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 151.90 E-value: 2.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 103 DPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADV-----IPKYLDNdcypVVCG-GPSETAEL 176
Cdd:PLN02766 157 EPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLaklagVPDGVIN----VVTGfGPTAGAAI 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 177 LNQR-FDYIFYTGSTRVG-KIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCSK 254
Cdd:PLN02766 233 ASHMdVDKVSFTGSTEVGrKIMQAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 255 EVQEKFIVEAKDVLKEW-YGENIQSSPDLSRVINANNFQRLLGLMKSGR----VAVGGNYDASER--FIEPTILVDVKET 327
Cdd:PLN02766 313 GIYDEFVKKLVEKAKDWvVGDPFDPRARQGPQVDKQQFEKILSYIEHGKregaTLLTGGKPCGDKgyYIEPTIFTDVTED 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 328 DPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNetimhC----GVDVlPFG 403
Cdd:PLN02766 393 MKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN-----CyfafDPDC-PFG 466
|
330 340
....*....|....*....|....
gi 442622748 404 GVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:PLN02766 467 GYKMSGFGRDQGMDALDKYLQVKS 490
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
104-409 |
7.19e-40 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 150.86 E-value: 7.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 104 PFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADV-----IPKYLDNDCYpvvcGGPSETAELL- 177
Cdd:PRK03137 171 PLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVleeagLPAGVVNFVP----GSGSEVGDYLv 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 178 -NQRFDYIFYTGSTRVGKIIHAAANK------YLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIApdyi 250
Cdd:PRK03137 247 dHPKTRFITFTGSREVGLRIYERAAKvqpgqiWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSA---- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 251 lCS-----KEVQEKFIVEAKDVLKEWYGENIQSSPDLSRVINANNFQRLLGLM----KSGRVAVGGNYDASE-RFIEPTI 320
Cdd:PRK03137 323 -CSraivhEDVYDEVLEKVVELTKELTVGNPEDNAYMGPVINQASFDKIMSYIeigkEEGRLVLGGEGDDSKgYFIQPTI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 321 LVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNETIMHCGVDVL 400
Cdd:PRK03137 402 FADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYH 481
|
....*....
gi 442622748 401 PFGGVGMSG 409
Cdd:PRK03137 482 PFGGFNMSG 490
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
99-415 |
9.66e-40 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 150.40 E-value: 9.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 99 QIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADV-----IPKYLDNdcypVVCGGPSET 173
Cdd:TIGR01237 162 QYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEIleeagLPKGVVQ----FVPGSGSEV 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 174 AELL--NQRFDYIFYTGSTRVGKIIHAAA------NKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCI 245
Cdd:TIGR01237 238 GDYLvdHPKTSLITFTGSREVGTRIFERAakvqpgQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 246 APDYILCSKEVQEKFI---VEAKDVLKewYGENIQSSPDLSRVINANNFQRLLGLMK----SGRVAVGGNYDASE-RFIE 317
Cdd:TIGR01237 318 AGSRAVVHEKVYDEVVerfVEITESLK--VGPPDSADVYVGPVIDQKSFNKIMEYIEigkaEGRLVSGGCGDDSKgYFIG 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 318 PTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNETIMHCGV 397
Cdd:TIGR01237 396 PTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIV 475
|
330
....*....|....*...
gi 442622748 398 DVLPFGGVGMSGMGRYHG 415
Cdd:TIGR01237 476 GYQPFGGFKMSGTDSKAG 493
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
104-427 |
2.07e-39 |
|
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: 148.55 E-value: 2.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 104 PFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVI-----PKyldnDCYPVV-CggPSETAELL 177
Cdd:cd07147 123 PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLaetglPK----GAFSVLpC--SRDDADLL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 178 --NQRFDYIFYTGSTRVGKIIHAAANKylTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCSKE 255
Cdd:cd07147 197 vtDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRS 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 256 VQEKFI---VEAKDVLKEwyGENIQSSPDLSRVINANNFQRLLGLMKS-----GRVAVGGNYDASerFIEPTILVDVKET 327
Cdd:cd07147 275 VYDEFKsrlVARVKALKT--GDPKDDATDVGPMISESEAERVEGWVNEavdagAKLLTGGKRDGA--LLEPTILEDVPPD 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 328 DPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFS-NSNKLVKEFRRsttsggfssnetiMHCG---------- 396
Cdd:cd07147 351 MEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTrDLEKALRAWDE-------------LEVGgvvindvptf 417
|
330 340 350
....*....|....*....|....*....|..
gi 442622748 397 -VDVLPFGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:cd07147 418 rVDHMPYGGVKDSGIGREGVRYAIEEMTEPRL 449
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
84-428 |
1.85e-38 |
|
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: 146.17 E-value: 1.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 84 SEKPPKSfvnMMDdvqIYNdPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSE----IAANCAKFIADVIPKY-L 158
Cdd:cd07086 120 SERPGHR---LME---QWN-PLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSEttplTAIAVTKILAEVLEKNgL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 159 DNDCYPVVCGGpSETAELLN--QRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGK 236
Cdd:cd07086 193 PPGVVNLVTGG-GDGGELLVhdPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 237 LINCGQTCIAPDYILCSKEVQEKFiveaKDVLKEWY-----GENIQSSPDLSRVIN---ANNFQRLLGLMKS--GRVAVG 306
Cdd:cd07086 272 VGTAGQRCTTTRRLIVHESVYDEF----LERLVKAYkqvriGDPLDEGTLVGPLINqaaVEKYLNAIEIAKSqgGTVLTG 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 307 GN-YDASER--FIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTS 383
Cdd:cd07086 348 GKrIDGGEPgnYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKGS 427
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 442622748 384 ggfssnetimHCG-VDV----------LPFGGVGMSGMGRYHGKYGFETFTHKKSC 428
Cdd:cd07086 428 ----------DCGiVNVniptsgaeigGAFGGEKETGGGRESGSDAWKQYMRRSTC 473
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
101-423 |
2.14e-37 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 143.87 E-value: 2.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 101 YNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADV-IPKYLDNDCYPVVCGGPSETAELLNQ 179
Cdd:PRK09407 151 LRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELlYEAGLPRDLWQVVTGPGPVVGTALVD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 180 RFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCSKEVQEK 259
Cdd:PRK09407 231 NADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 260 FI---VEAKDVLKewYGENIQSSPDLSRVINANNFQRLLG-----LMKSGRVAVGGNY--DASERFIEPTILVDVKETDP 329
Cdd:PRK09407 311 FVrafVAAVRAMR--LGAGYDYSADMGSLISEAQLETVSAhvddaVAKGATVLAGGKArpDLGPLFYEPTVLTGVTPDME 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 330 IMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNE--TIMHCGVDVlPFGGVGM 407
Cdd:PRK09407 389 LAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEgyAAAWGSVDA-PMGGMKD 467
|
330
....*....|....*.
gi 442622748 408 SGMGRYHGKYGFETFT 423
Cdd:PRK09407 468 SGLGRRHGAEGLLKYT 483
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
5-412 |
3.24e-36 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 138.94 E-value: 3.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 5 DDTLQRARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIISALEADLRRPKQESLiVETEFMKNDIRHILFQLDEWVQS 84
Cdd:cd07095 3 DAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQ-TEVAAMAGKIDISIKAYHERTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 85 EKPPKSFVNMMddvqIYNDPFGVVLVIGAWNYPLQL---LLVPvasAIAAGNCVVIKPSEIAANCAKFIADVI-PKYLDN 160
Cdd:cd07095 82 RATPMAQGRAV----LRHRPHGVMAVFGPFNFPGHLpngHIVP---ALLAGNTVVFKPSELTPAVAELMVELWeEAGLPP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 161 DCYPVVCGGPSETAELLNQ-RFDYIFYTGSTRVGKIIHAA-ANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLI 238
Cdd:cd07095 155 GVLNLVQGGRETGEALAAHeGIDGLLFTGSAATGLLLHRQfAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 239 NCGQTC-IAPDYILCSKEVQEKFIVEAKDVLKE-----WYGENI-----QSSPDLSRVINAnnFQRLLG-----LMKSGR 302
Cdd:cd07095 235 TAGQRCtCARRLIVPDGAVGDAFLERLVEAAKRlrigaPDAEPPfmgplIIAAAAARYLLA--QQDLLAlggepLLAMER 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 303 VAVGGNydaserFIEPTILvDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTT 382
Cdd:cd07095 313 LVAGTA------FLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIR 385
|
410 420 430
....*....|....*....|....*....|....*....
gi 442622748 383 SG---------GFSSNetimhcgvdvLPFGGVGMSGMGR 412
Cdd:cd07095 386 AGivnwnrpttGASST----------APFGGVGLSGNHR 414
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
5-427 |
3.80e-36 |
|
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: 139.63 E-value: 3.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 5 DDTLQRARLAF-SSGKTRNVSFRRKQLENLLRCYEEHENEIISALEADLRRPKQESLiveTEFMK--NDIRHILFQLDEW 81
Cdd:cd07082 41 LEAAETAYDAGrGWWPTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDAL---KEVDRtiDYIRDTIEELKRL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 82 VQSEKPPKSFVNMMDDV-QIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIAdvipKYLDN 160
Cdd:cd07082 118 DGDSLPGDWFPGTKGKIaQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLA----EAFHD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 161 DCYP-----VVCGGPSETAELL--NQRFDYIFYTGSTRVGKIIHAAANKylTPTTLELGGKSPCYIDKSVDMRTAVKRIL 233
Cdd:cd07082 194 AGFPkgvvnVVTGRGREIGDPLvtHGRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 234 WGKLINCGQTCIAPDYILCSKEVQEKFIVE-AKDVLKEWYGENIQSSPDLSRVINANNFQRLLGLM-----KSGRVAVGG 307
Cdd:cd07082 272 KGALSYSGQRCTAIKRVLVHESVADELVELlKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIddavaKGATVLNGG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 308 NYDaSERFIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFS 387
Cdd:cd07082 352 GRE-GGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVN 430
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 442622748 388 SNETIMHcGVDVLPFGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:cd07082 431 INSKCQR-GPDHFPFLGRKDSGIGTQGIGDALRSMTRRKG 469
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
11-426 |
3.29e-34 |
|
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: 134.01 E-value: 3.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 11 ARLAFSSGK-TRNVSFRRKQLENLLRCYEEHENEIISALEADLRRPKQES------LIVETEFMKNDIRHILFQLDEWvq 83
Cdd:cd07120 28 ARRAFDETDwAHDPRLRARVLLELADAFEANAERLARLLALENGKILGEArfeisgAISELRYYAGLARTEAGRMIEP-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 84 sekPPKSFVNMMddvqiyNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKP----SEIAANCAKFIADV--IPKY 157
Cdd:cd07120 106 ---EPGSFSLVL------REPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPagqtAQINAAIIRILAEIpsLPAG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 158 LDNdcypVVCGGPSETAELL--NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWG 235
Cdd:cd07120 177 VVN----LFTESGSEGAAHLvaSPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 236 KLINCGQTCIAPDYILcskeVQEKFIVEAKDVLKEwYGENIQSSP------DLSRVINANNFQRLLG------------L 297
Cdd:cd07120 253 LTIFAGQFCMAGSRVL----VQRSIADEVRDRLAA-RLAAVKVGPgldpasDMGPLIDRANVDRVDRmveraiaagaevV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 298 MKSGRVAVGGNYDAserFIEPTiLVDVKETD-PIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSnkLVKE 376
Cdd:cd07120 328 LRGGPVTEGLAKGA---FLRPT-LLEVDDPDaDIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRD--LARA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 442622748 377 FR--RSTTSGGFSSNEtimHCGV-DVLPFGGVGMSGMGRYHGKYGFETFTHKK 426
Cdd:cd07120 402 MRvaRAIRAGTVWIND---WNKLfAEAEEGGYRQSGLGRLHGVAALEDFIEYK 451
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
104-430 |
3.67e-34 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 134.26 E-value: 3.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 104 PFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADV-----IPKYLDNdcypVVCGGPSETAELL- 177
Cdd:PRK11241 146 PIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELairagIPAGVFN----VVTGSAGAVGGELt 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 178 -NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCSKEV 256
Cdd:PRK11241 222 sNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGV 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 257 QEKFIVEAKD-VLKEWYGENIQSSPDLSRVINANNFQRLL-----GLMKSGRVAVGGNYDASE-RFIEPTILVDVKETDP 329
Cdd:PRK11241 302 YDRFAEKLQQaVSKLHIGDGLEKGVTIGPLIDEKAVAKVEehiadALEKGARVVCGGKAHELGgNFFQPTILVDVPANAK 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 330 IMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSnkLVKEFRRSTT--------SGGFSSNEtimhcgvdVLP 401
Cdd:PRK11241 382 VAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARD--LSRVFRVGEAleygivgiNTGIISNE--------VAP 451
|
330 340 350
....*....|....*....|....*....|
gi 442622748 402 FGGVGMSGMGRYHGKYGFETFTH-KKSCLG 430
Cdd:PRK11241 452 FGGIKASGLGREGSKYGIEDYLEiKYMCIG 481
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
103-427 |
6.37e-34 |
|
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: 133.34 E-value: 6.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 103 DPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADV-----IPKYLDNdcypvVCGGPSETAELL 177
Cdd:cd07113 141 EPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELakeagIPDGVLN-----VVNGKGAVGAQL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 178 NQRFDY--IFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPD--YILCS 253
Cdd:cd07113 216 ISHPDVakVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPErfYVHRS 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 254 K--EVQEKFiveaKDVLKEWY-GENIQSSPDLSRVINANNFQRLLGLM-----KSGRVAVGGN-YDASERFIEPTILVDV 324
Cdd:cd07113 296 KfdELVTKL----KQALSSFQvGSPMDESVMFGPLANQPHFDKVCSYLddaraEGDEIVRGGEaLAGEGYFVQPTLVLAR 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 325 KETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSnkLVKEFRRS--TTSGGFSSNetiMHCGVD-VLP 401
Cdd:cd07113 372 SADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNN--LSKALRYIprIEAGTVWVN---MHTFLDpAVP 446
|
330 340
....*....|....*....|....*.
gi 442622748 402 FGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:cd07113 447 FGGMKQSGIGREFGSAFIDDYTELKS 472
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
104-411 |
1.23e-31 |
|
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: 127.31 E-value: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 104 PFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIA----------ANCAKFIADVIpKYLDNDcypvvcgGPSET 173
Cdd:cd07083 154 GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAvvvgykvfeiFHEAGFPPGVV-QFLPGV-------GEEVG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 174 AELL-NQRFDYIFYTGSTRVGKIIH-AAANKYLTPTTL-----ELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIA 246
Cdd:cd07083 226 AYLTeHERIRGINFTGSLETGKKIYeAAARLAPGQTWFkrlyvETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 247 PDYILCSKEVQEKFI---VEAKDVLKewYGENIQSSPDLSRVINANNFQRLLGLM----KSGRVAVGGNYDASE-RFIEP 318
Cdd:cd07083 306 ASRLILTQGAYEPVLerlLKRAERLS--VGPPEENGTDLGPVIDAEQEAKVLSYIehgkNEGQLVLGGKRLEGEgYFVAP 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 319 TILVDVKETDPIMEEEIFGPILPIFNVESA--YDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNETIMHCG 396
Cdd:cd07083 384 TVVEEVPPKARIAQEEIFGPVLSVIRYKDDdfAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGAL 463
|
330
....*....|....*
gi 442622748 397 VDVLPFGGVGMSGMG 411
Cdd:cd07083 464 VGVQPFGGFKLSGTN 478
|
|
| ABALDH |
TIGR03374 |
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1. ... |
100-423 |
3.91e-31 |
|
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1.35), also called gamma-aminobutyraldehyde dehydrogenase. This enzyme can follow putrescine transaminase (EC 2.6.1.82) for a two-step conversion of putrescine to gamma-aminobutyric acid (GABA). The member from Escherichia coli is characterized as a homotetramer that binds one NADH per momomer. This enzyme belongs to the medium-chain aldehyde dehydrogenases, and is quite similar in sequence to the betaine aldehyde dehydrogenase (EC 1.2.1.8) family.
Pssm-ID: 132417 Cd Length: 472 Bit Score: 125.50 E-value: 3.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 100 IYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEI----AANCAKFIADVIPKYLDNdcypVVCGGPSETAE 175
Cdd:TIGR03374 133 IRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEItpltALKLAELAKDIFPAGVVN----ILFGRGKTVGD 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 176 LL--NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCS 253
Cdd:TIGR03374 209 PLtgHEKVRMVSLTGSIATGEHILSHTAPSIKRTHMELGGKAPVIVFDDADIDAVVEGVRTFGFYNAGQDCTAACRIYAQ 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 254 KEVQEKfIVEA--KDVLKEWYGENIQSSPDLSRVINANNFQRLLGLMKSG------RVAVGGN-YDASERFIEPTILVDV 324
Cdd:TIGR03374 289 RGIYDT-LVEKlgAAVATLKSGAPDDESTELGPLSSLAHLERVMKAVEEAkalghiKVITGGEkRKGNGYYFAPTLLAGA 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 325 KETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNETIMHcgVDVLPFGG 404
Cdd:TIGR03374 368 KQDDAIVQKEVFGPVVSITSFDDEEQVVNWANDSQYGLASSVWTKDVGRAHRLSARLQYGCTWVNTHFML--VSEMPHGG 445
|
330
....*....|....*....
gi 442622748 405 VGMSGMGRYHGKYGFETFT 423
Cdd:TIGR03374 446 QKLSGYGKDMSLYGLEDYT 464
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
103-427 |
3.94e-31 |
|
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: 125.18 E-value: 3.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 103 DPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAA----NCAKFIADVIPKYLDNdcypVVCGGPSETAELLN 178
Cdd:cd07107 115 EPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPlsalRLAELAREVLPPGVFN----ILPGDGATAGAALV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 179 QRFDY--IFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGklIN---CGQTCIAPDYILCS 253
Cdd:cd07107 191 RHPDVkrIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAAVAG--MNftwCGQSCGSTSRLFVH 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 254 KEVQEKFIVEAKDVLKEWY-GENIQSSPDLSRVINANNFQRLLGLMKSG-----RVAVGGNYDASER-----FIEPTILV 322
Cdd:cd07107 269 ESIYDEVLARVVERVAAIKvGDPTDPATTMGPLVSRQQYDRVMHYIDSAkregaRLVTGGGRPEGPAleggfYVEPTVFA 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 323 DVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNETIMH-CGVdvlP 401
Cdd:cd07107 349 DVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVWINGSSRHfLGA---P 425
|
330 340
....*....|....*....|....*.
gi 442622748 402 FGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:cd07107 426 FGGVKNSGIGREECLEELLSYTQEKN 451
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
2-412 |
2.68e-30 |
|
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: 123.37 E-value: 2.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 2 ANFDDTLQRARLAFSSGKTRNVSFRR--KQLENLLRCYEEHENEIISALEADlrrpkqeSLIVETEFMKNdirHILFQLD 79
Cdd:cd07140 43 EDVDRAVAAAKEAFENGEWGKMNARDrgRLMYRLADLMEEHQEELATIESLD-------SGAVYTLALKT---HVGMSIQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 80 EWvqsekppKSFVNMMDDVQ-----IYN------------DPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEI 142
Cdd:cd07140 113 TF-------RYFAGWCDKIQgktipINQarpnrnltltkrEPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 143 AANCAKFIADV-----IPKYLDNdcypVVCGGPSETAELLNQRFDY--IFYTGSTRVGK-IIHAAANKYLTPTTLELGGK 214
Cdd:cd07140 186 TPLTALKFAELtvkagFPKGVIN----ILPGSGSLVGQRLSDHPDVrkLGFTGSTPIGKhIMKSCAVSNLKKVSLELGGK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 215 SPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCSKEVQEKFIVE-AKDVLKEWYGENIQSSPDLSRVINANNFQR 293
Cdd:cd07140 262 SPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRvVEEVKKMKIGDPLDRSTDHGPQNHKAHLDK 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 294 LL-----GLMKSGRVAVGGNY-DASERFIEPTILVDVKETDPIMEEEIFGPILPI--FNVESAYDAIKFINAREKPLVIY 365
Cdd:cd07140 342 LVeycerGVKEGATLVYGGKQvDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIIskFDDGDVDGVLQRANDTEYGLASG 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 442622748 366 VFS-NSNK--LVKEFRRSTTSGGFSSNETimhcgvDVL-PFGGVGMSGMGR 412
Cdd:cd07140 422 VFTkDINKalYVSDKLEAGTVFVNTYNKT------DVAaPFGGFKQSGFGK 466
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
2-427 |
5.64e-30 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 122.31 E-value: 5.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 2 ANFDDTLQRARLAFSSGKTRNVS-FRRKQLENLLRCYEEHENEIISALEA-DLRRPKQESLIVETEFMKNDIRHILFQLD 79
Cdd:PRK09847 57 VDIDRAVSAARGVFERGDWSLSSpAKRKAVLNKLADLMEAHAEELALLETlDTGKPIRHSLRDDIPGAARAIRWYAEAID 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 80 EwVQSEKPPKSFVNMmddVQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADV-----I 154
Cdd:PRK09847 137 K-VYGEVATTSSHEL---AMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLakeagL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 155 PKYLDNdcypVVCGGPSETAELLNQR--FDYIFYTGSTRVGK-IIHAAANKYLTPTTLELGGKSPCYIDKSV-DMRTAVK 230
Cdd:PRK09847 213 PDGVLN----VVTGFGHEAGQALSRHndIDAIAFTGSTRTGKqLLKDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAAS 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 231 RILWGKLINCGQTCIAPDYILCSKEVQEKFIVEAKDVLKEWY-GENIQSSPDLSRVIN---ANNFQRLL--GLMKsGRVA 304
Cdd:PRK09847 289 ATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQpGHPLDPATTMGTLIDcahADSVHSFIreGESK-GQLL 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 305 VGGNYDASERFIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSG 384
Cdd:PRK09847 368 LDGRNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAG 447
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 442622748 385 GFSSNEtiMHCGVDVLPFGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:PRK09847 448 SVFVNN--YNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKT 488
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
104-427 |
2.67e-29 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 120.37 E-value: 2.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 104 PFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADV-----IPKYLDNdcypvVCGGPSETAELLN 178
Cdd:PRK13252 142 PLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIyteagLPDGVFN-----VVQGDGRVGAWLT 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 179 Q--RFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCSKEV 256
Cdd:PRK13252 217 EhpDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 257 QEKFIVE-----AKDVLKEWYGENIQSSPdlsrVINANNFQRLLGLMKSG-----RVAVGG-----NYDASERFIEPTIL 321
Cdd:PRK13252 297 KAAFEARllervERIRIGDPMDPATNFGP----LVSFAHRDKVLGYIEKGkaegaRLLCGGerlteGGFANGAFVAPTVF 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 322 VDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNS----NKLVKEFRRSTT---SGGFSSNEtimh 394
Cdd:PRK13252 373 TDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADlsraHRVIHQLEAGICwinTWGESPAE---- 448
|
330 340 350
....*....|....*....|....*....|...
gi 442622748 395 cgvdvLPFGGVGMSGMGRYHGKYGFETFTHKKS 427
Cdd:PRK13252 449 -----MPVGGYKQSGIGRENGIATLEHYTQIKS 476
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
2-418 |
5.98e-29 |
|
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: 119.42 E-value: 5.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 2 ANFDDTLQRARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIiSALEA-DLRRPKQESLIVETEFMkndIRHiLFQLDE 80
Cdd:cd07111 59 EDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLF-AVLESlDNGKPIRESRDCDIPLV---ARH-FYHHAG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 81 WVQsekppksfvnMMDDVQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVI-----P 155
Cdd:cd07111 134 WAQ----------LLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICaeaglP 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 156 KYLDNdcypVVCGGPSETAELLNQ-RFDYIFYTGSTRVGKIIH---AAANKYLtptTLELGGKSPCYIDKSVDMRTAVKR 231
Cdd:cd07111 204 PGVLN----IVTGNGSFGSALANHpGVDKVAFTGSTEVGRALRratAGTGKKL---SLELGGKSPFIVFDDADLDSAVEG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 232 ILWGKLINCGQTCIAPDYILCSKEVQEKFIVEAKDVLKEW-YGENIQSSPDLSRVINANNFQRLLGLMKSGR------VA 304
Cdd:cd07111 277 IVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLrVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRaegadvFQ 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 305 VGGNYDASERFIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSG 384
Cdd:cd07111 357 PGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAG 436
|
410 420 430
....*....|....*....|....*....|....*
gi 442622748 385 GFSSNETIMHcgvD-VLPFGGVGMSGMGRYHGKYG 418
Cdd:cd07111 437 VVWINGHNLF---DaAAGFGGYRESGFGREGGKEG 468
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
97-426 |
1.86e-28 |
|
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: 117.62 E-value: 1.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 97 DVQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVI-----PKYLDNdcypVVCGGPS 171
Cdd:cd07085 129 DTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLqeaglPDGVLN----VVHGGKE 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 172 ETAELL-NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYI 250
Cdd:cd07085 205 AVNALLdHPDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVA 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 251 LCSKEVQEKF---IVEAKDVLKEWYGenIQSSPDLSRVINANNFQRLLGLMKSG-----RVAVGG-NYDASER----FIE 317
Cdd:cd07085 285 VAVGDEADEWipkLVERAKKLKVGAG--DDPGADMGPVISPAAKERIEGLIESGveegaKLVLDGrGVKVPGYengnFVG 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 318 PTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREkplviY-----VFSNSNKLVKEFRRSTTSGgfssneti 392
Cdd:cd07085 363 PTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANP-----YgngaaIFTRSGAAARKFQREVDAG-------- 429
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 442622748 393 MhCGVDV--------LPFGGVGMSGMGRYH--GKYGFETFTHKK 426
Cdd:cd07085 430 M-VGINVpipvplafFSFGGWKGSFFGDLHfyGKDGVRFYTQTK 472
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
5-422 |
4.10e-26 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 110.72 E-value: 4.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 5 DDTLQRARLAFSSGKTRNVSFRRKQLENLLRCYEEHENEIISALEADLRRPKQESlivETEFMKNDirhilfQLDEWVQS 84
Cdd:PRK13968 32 ENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQA---RAEVAKSA------NLCDWYAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 85 EKPP-----KSFVNMMDDVQIYNdPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADV-----I 154
Cdd:PRK13968 103 HGPAmlkaePTLVENQQAVIEYR-PLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVfkdagI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 155 PKyldnDCYPVVCGGPSETAELLNQ-RFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRIL 233
Cdd:PRK13968 182 PQ----GVYGWLNADNDGVSQMINDsRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 234 WGKLINCGQTCIAPDYILCSKEVQEKF---IVEAKDVLKewYGENIQSSPDLSRVINAN-----NFQRLLGLMKSGRVAV 305
Cdd:PRK13968 258 AGRYQNTGQVCAAAKRFIIEEGIASAFterFVAAAAALK--MGDPRDEENALGPMARFDlrdelHHQVEATLAEGARLLL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 306 GGNYDASE-RFIEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSG 384
Cdd:PRK13968 336 GGEKIAGAgNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECG 415
|
410 420 430
....*....|....*....|....*....|....*....
gi 442622748 385 GFSSNEtimHCGVDV-LPFGGVGMSGMGRYHGKYGFETF 422
Cdd:PRK13968 416 GVFING---YCASDArVAFGGVKKSGFGRELSHFGLHEF 451
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
101-429 |
9.58e-26 |
|
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: 109.85 E-value: 9.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 101 YNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANC----AKFIADVIPKYLDNdcypVVCGGPSETAEL 176
Cdd:cd07116 133 FHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASilvlMELIGDLLPPGVVN----VVNGFGLEAGKP 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 177 L--NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSP------------CYIDKSVDMRTAVKrilwgklINCGQ 242
Cdd:cd07116 209 LasSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPniffadvmdaddAFFDKALEGFVMFA-------LNQGE 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 243 TCIAPDYILCSKEVQEKFIVEAKDVLKEWygenIQSSP-DLSRVINA----NNFQRLLGLMKSGR-----VAVGGNY--- 309
Cdd:cd07116 282 VCTCPSRALIQESIYDRFMERALERVKAI----KQGNPlDTETMIGAqaslEQLEKILSYIDIGKeegaeVLTGGERnel 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 310 --DASERFIEPTILVDVKETDpIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFS 387
Cdd:cd07116 358 ggLLGGGYYVPTTFKGGNKMR-IFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVW 436
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 442622748 388 SNetIMHCGVDVLPFGGVGMSGMGRYHGKYGFETFTHKKSCL 429
Cdd:cd07116 437 TN--CYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLL 476
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
103-411 |
1.21e-25 |
|
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: 109.43 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 103 DPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKP-SEIAANCAKFIADVIPKYLDND-CYPVVCGgpSETAELL--N 178
Cdd:cd07148 123 EPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPaLATPLSCLAFVDLLHEAGLPEGwCQAVPCE--NAVAEKLvtD 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 179 QRFDYIFYTGSTRVGKIIHAAankyLTPTT---LELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCSKE 255
Cdd:cd07148 201 PRVAFFSFIGSARVGWMLRSK----LAPGTrcaLEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 256 VQEKFIVE-AKDVLKEWYGENIQSSPDLSRVINANNFQRLL-----GLMKSGRVAVGGNYdASERFIEPTILVDVKETDP 329
Cdd:cd07148 277 IADDFAQRlAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEewvneAVAAGARLLCGGKR-LSDTTYAPTVLLDPPRDAK 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 330 IMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKL-VKEFRRSTTSGGFSSNETIMHcgVDVLPFGGVGMS 408
Cdd:cd07148 356 VSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVaLKAVRRLDATAVMVNDHTAFR--VDWMPFAGRRQS 433
|
...
gi 442622748 409 GMG 411
Cdd:cd07148 434 GYG 436
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
104-411 |
8.04e-25 |
|
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: 107.28 E-value: 8.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 104 PFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADV-----IPKYLDNdcypVVCGGPSETAELL- 177
Cdd:cd07125 167 GRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELlheagVPRDVLQ----LVPGDGEEIGEALv 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 178 -NQRFDYIFYTGSTRVGKIIH---AAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCS 253
Cdd:cd07125 243 aHPRIDGVIFTGSTETAKLINralAERDGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQ 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 254 KEVQEKFIVEAKDVLKEWygeNIQSSPDLSR----VINANNFQRLLGLMKSGR-----VAVGGNYDASERFIEPTILVDV 324
Cdd:cd07125 323 EEIAERFIEMLKGAMASL---KVGDPWDLSTdvgpLIDKPAGKLLRAHTELMRgeawlIAPAPLDDGNGYFVAPGIIEIV 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 325 KETDpiMEEEIFGPILPI--FNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNETIMHCGVDVLPF 402
Cdd:cd07125 400 GIFD--LTTEVFGPILHVirFKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPF 477
|
....*....
gi 442622748 403 GGVGMSGMG 411
Cdd:cd07125 478 GGWGLSGTG 486
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
82-438 |
1.18e-24 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 106.84 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 82 VQSEKPPksfvNMMddVQIYNdPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIK--PSE--IAANCAKFIADVIPKY 157
Cdd:PLN02315 139 IPSERPN----HMM--MEVWN-PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKgaPTTplITIAMTKLVAEVLEKN 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 158 -LDNDCYPVVCGGpSETAELL--NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILW 234
Cdd:PLN02315 212 nLPGAIFTSFCGG-AEIGEAIakDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLF 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 235 GKLINCGQTCIAPDYILCSKEVQEKFIVEAKDVLKEW-YGENIQSSP---DLSRVINANNFQRLLGLMKS--GRVAVGGN 308
Cdd:PLN02315 291 AAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVkIGDPLEKGTllgPLHTPESKKNFEKGIEIIKSqgGKILTGGS 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 309 YDASE-RFIEPTIlVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFS 387
Cdd:PLN02315 371 AIESEgNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGI 449
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 442622748 388 SNETIMHCGVDV-LPFGGVGMSGMGRYHGKYGFETFTHKKSC---LGKDLsPLGE 438
Cdd:PLN02315 450 VNVNIPTNGAEIgGAFGGEKATGGGREAGSDSWKQYMRRSTCtinYGNEL-PLAQ 503
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
104-427 |
1.62e-24 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 105.98 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 104 PFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVIPKY-LDNDCYPVVCGGPSETAELL-NQRF 181
Cdd:PRK09406 123 PLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAgFPDGCFQTLLVGSGAVEAILrDPRV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 182 DYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCSKEVQEKFI 261
Cdd:PRK09406 203 AAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFA 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 262 ---VEAKDVLKewYGENIQSSPD---LSRVINANNFQRLL--GLMKSGRVAVGGNY-DASERFIEPTILVDVKETDPIME 332
Cdd:PRK09406 283 ekfVARMAALR--VGDPTDPDTDvgpLATEQGRDEVEKQVddAVAAGATILCGGKRpDGPGWFYPPTVITDITPDMRLYT 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 333 EEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGG-FSSNETIMHcgvDVLPFGGVGMSGMG 411
Cdd:PRK09406 361 EEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQvFINGMTVSY---PELPFGGVKRSGYG 437
|
330
....*....|....*.
gi 442622748 412 RYHGKYGFETFTHKKS 427
Cdd:PRK09406 438 RELSAHGIREFCNIKT 453
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
84-357 |
8.26e-24 |
|
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: 104.21 E-value: 8.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 84 SEKPPKSfvnMMDdvqIYNdPFGVVLVIGAWNYPlqlllvpVA-----SAIAA--GNCVVIKPSE----IAANCAKFIAD 152
Cdd:cd07130 119 SERPGHR---MME---QWN-PLGVVGVITAFNFP-------VAvwgwnAAIALvcGNVVVWKPSPttplTAIAVTKIVAR 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 153 VIPKY-LDNDCYPVVCGGpSETAELL--NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAV 229
Cdd:cd07130 185 VLEKNgLPGAIASLVCGG-ADVGEALvkDPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAV 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 230 KRILWGKLINCGQTCIAPDYILcskeVQEKFIVEAKDVLKEWYG---------ENIQSSPDLSRViNANNFQRLLGLMKS 300
Cdd:cd07130 264 RAVLFAAVGTAGQRCTTTRRLI----VHESIYDEVLERLKKAYKqvrigdpldDGTLVGPLHTKA-AVDNYLAAIEEAKS 338
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 301 --GRVAVGGN-YDASERFIEPTIlVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINA 357
Cdd:cd07130 339 qgGTVLFGGKvIDGPGNYVEPTI-VEGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNE 397
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
104-411 |
3.17e-22 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 99.60 E-value: 3.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 104 PFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSE----IAANCAKFIADVipkyldndcypvvcGGPSETAELL-- 177
Cdd:TIGR01238 160 SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEqtslIAYRAVELMQEA--------------GFPAGTIQLLpg 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 178 -----------NQRFDYIFYTGSTRVGKIIHAAANKYL---TPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQT 243
Cdd:TIGR01238 226 rgadvgaaltsDPRIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQR 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 244 CIAPDYILCSKEVQEKFIVEAKDVLKEW-YGENIQSSPDLSRVINANNFQRLL-------GLMKSGRVAVGGNYDASER- 314
Cdd:TIGR01238 306 CSALRVLCVQEDVADRVLTMIQGAMQELkVGVPHLLTTDVGPVIDAEAKQNLLahiehmsQTQKKIAQLTLDDSRACQHg 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 315 -FIEPTILvdvkETDPIME--EEIFGPILPI--FNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSN 389
Cdd:TIGR01238 386 tFVAPTLF----ELDDIAElsEEVFGPVLHVvrYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVN 461
|
330 340
....*....|....*....|..
gi 442622748 390 ETIMHCGVDVLPFGGVGMSGMG 411
Cdd:TIGR01238 462 RNQVGAVVGVQPFGGQGLSGTG 483
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
104-409 |
8.64e-22 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 98.11 E-value: 8.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 104 PFGVVLVIGAWNYPLQL---LLVPvasAIAAGNCVVIKPSEIAANCAKFIADV-----IPKYLDNdcypVVCGGPsETAE 175
Cdd:PRK09457 134 PHGVVAVFGPYNFPGHLpngHIVP---ALLAGNTVVFKPSELTPWVAELTVKLwqqagLPAGVLN----LVQGGR-ETGK 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 176 LL--NQRFDYIFYTGSTRVGKIIHA--AAN--KYLtptTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDY 249
Cdd:PRK09457 206 ALaaHPDIDGLLFTGSANTGYLLHRqfAGQpeKIL---ALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARR 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 250 ILCSKEVQ-EKFIVEAKDVLK-----EWygeNIQSSPDLSRVINAnnfQRLLGLMKSGR--VAVGGN-------YDASER 314
Cdd:PRK09457 283 LLVPQGAQgDAFLARLVAVAKrltvgRW---DAEPQPFMGAVISE---QAAQGLVAAQAqlLALGGKsllemtqLQAGTG 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 315 FIEPTILvDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSG---------G 385
Cdd:PRK09457 357 LLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGivnwnkpltG 435
|
330 340
....*....|....*....|....
gi 442622748 386 FSSNetimhcgvdvLPFGGVGMSG 409
Cdd:PRK09457 436 ASSA----------APFGGVGASG 449
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
104-411 |
1.39e-18 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 88.27 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 104 PFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAK-----FIADVIPKYLDNdcypVVCGGPSETAELLN 178
Cdd:PLN00412 158 PLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALhmvhcFHLAGFPKGLIS----CVTGKGSEIGDFLT 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 179 QR--FDYIFYTGSTrVGkiIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCSKEV 256
Cdd:PLN00412 234 MHpgVNCISFTGGD-TG--IAISKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 257 QEKFI--VEAKdVLKEWYGENiQSSPDLSRVI---NANNFQRLLGLMKSGRVAVGGNYDASERFIEPTILVDVKETDPIM 331
Cdd:PLN00412 311 ADALVekVNAK-VAKLTVGPP-EDDCDITPVVsesSANFIEGLVMDAKEKGATFCQEWKREGNLIWPLLLDNVRPDMRIA 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 332 EEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNS-NKLVKeFRRSTTSGGFSSNETIMHcGVDVLPFGGVGMSGM 410
Cdd:PLN00412 389 WEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDiNKAIL-ISDAMETGTVQINSAPAR-GPDHFPFQGLKDSGI 466
|
.
gi 442622748 411 G 411
Cdd:PLN00412 467 G 467
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
97-420 |
4.65e-18 |
|
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: 86.52 E-value: 4.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 97 DVQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKP-------SEIAANCAKFIADVIPKYLDndcypVVCGG 169
Cdd:cd07084 93 QSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPhtavsivMQIMVRLLHYAGLLPPEDVT-----LINGD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 170 PSETAELLNQ-RFDYIFYTGSTRVGKIIhaAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKL-INCGQTCIAP 247
Cdd:cd07084 168 GKTMQALLLHpNPKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGPDAQAVDYVAWQCVQDMtACSGQKCTAQ 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 248 DYILCSKEVQEKFIVEAkdvLKEWYGENIQSSPDLSRVINANNFQRL--LGLMKSGRVAVGG----NYDASERF---IEP 318
Cdd:cd07084 246 SMLFVPENWSKTPLVEK---LKALLARRKLEDLLLGPVQTFTTLAMIahMENLLGSVLLFSGkelkNHSIPSIYgacVAS 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 319 TILVDVKETD---PIMEEEIFGPILPI--FNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNETIM 393
Cdd:cd07084 323 ALFVPIDEILktyELVTEEIFGPFAIVveYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQELIGNLWVAGRTYAILRG 402
|
330 340
....*....|....*....|....*..
gi 442622748 394 HCGVDVLPFGGVGMSGMGRYHGKYGFE 420
Cdd:cd07084 403 RTGVAPNQNHGGGPAADPRGAGIGGPE 429
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
102-411 |
1.75e-16 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 82.71 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 102 ND---PFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSE----IAANCAKFIADVipkyldndcypvvcGGPSETA 174
Cdd:PRK11809 763 NDthrPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEqtplIAAQAVRILLEA--------------GVPAGVV 828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 175 ELL-------------NQRFDYIFYTGSTRVGKIIHAAANKYL------TPTTLELGGKSPCYIDKSVDMRTAVKRILWG 235
Cdd:PRK11809 829 QLLpgrgetvgaalvaDARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSALTEQVVADVLAS 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 236 KLINCGQTCIAPDyILCSKE-VQEKFIVEAKDVLKEW-YGENIQSSPDLSRVINAN---NFQRLLGLMKS-GRVAVGGNY 309
Cdd:PRK11809 909 AFDSAGQRCSALR-VLCLQDdVADRTLKMLRGAMAECrMGNPDRLSTDIGPVIDAEakaNIERHIQAMRAkGRPVFQAAR 987
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 310 DASER-----FIEPTILvdvkETDPI--MEEEIFGPILPI--FNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRS 380
Cdd:PRK11809 988 ENSEDwqsgtFVPPTLI----ELDSFdeLKREVFGPVLHVvrYNRNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGS 1063
|
330 340 350
....*....|....*....|....*....|.
gi 442622748 381 TTSGGFSSNETIMHCGVDVLPFGGVGMSGMG 411
Cdd:PRK11809 1064 AHVGNLYVNRNMVGAVVGVQPFGGEGLSGTG 1094
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
93-427 |
6.63e-15 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 77.09 E-value: 6.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 93 NMMDDVQIYN--DPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVIPKYLDNDCYPVVCGGP 170
Cdd:PLN02419 236 NVSNGVDTYSirEPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGT 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 171 SETAELL--NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPD 248
Cdd:PLN02419 316 NDTVNAIcdDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALS 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 249 YILCSKEVQ--EKFIVEAKDVLKEWYGEniQSSPDLSRVINANNFQRLLGLMKSG-----------RVAVGGNYDASErF 315
Cdd:PLN02419 396 TVVFVGDAKswEDKLVERAKALKVTCGS--EPDADLGPVISKQAKERICRLIQSGvddgakllldgRDIVVPGYEKGN-F 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 316 IEPTILVDVKETDPIMEEEIFGPILPIFNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNETImHC 395
Cdd:PLN02419 473 IGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPI-PV 551
|
330 340 350
....*....|....*....|....*....|....
gi 442622748 396 GVDVLPFGGVGMSGMG--RYHGKYGFETFTHKKS 427
Cdd:PLN02419 552 PLPFFSFTGNKASFAGdlNFYGKAGVDFFTQIKL 585
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
104-411 |
9.89e-13 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 71.05 E-value: 9.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 104 PFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSE----IAANCAKFIADV-IPKyldnDCYPVVCG-GPSETAELL 177
Cdd:PRK11905 676 PLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEqtplIAARAVRLLHEAgVPK----DALQLLPGdGRTVGAALV 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 178 -NQRFDYIFYTGSTRVGKIIHAAANKYLTPTTL---ELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDyILCS 253
Cdd:PRK11905 752 aDPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPliaETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALR-VLCL 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 254 KE-VQEKFIVEAKDVLKEWY-GENIQSSPDLSRVINANNFQRLLG---LMKS-GRV--AVGGNYDASE-RFIEPTILvdv 324
Cdd:PRK11905 831 QEdVADRVLTMLKGAMDELRiGDPWRLSTDVGPVIDAEAQANIEAhieAMRAaGRLvhQLPLPAETEKgTFVAPTLI--- 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 325 kETDPI--MEEEIFGPILPI--FNVESAYDAIKFINAREKPLVIYVFSNSNKLVKEFRRSTTSGGFSSNETIMHCGVDVL 400
Cdd:PRK11905 908 -EIDSIsdLEREVFGPVLHVvrFKADELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQ 986
|
330
....*....|.
gi 442622748 401 PFGGVGMSGMG 411
Cdd:PRK11905 987 PFGGEGLSGTG 997
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
112-343 |
3.79e-12 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 68.38 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 112 GAWN---Y-PLQLLLVPVA----SAIAA---------GNCVVIKPSEIAANCAKFIADV-----IPKYLDNdcyPVVCGG 169
Cdd:cd07123 160 GVWNrleYrPLEGFVYAVSpfnfTAIGGnlagapalmGNVVLWKPSDTAVLSNYLVYKIleeagLPPGVIN---FVPGDG 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 170 PSETAELLNQR-FDYIFYTGSTRVGKIIHA--AAN--KYLTPTTL--ELGGKSPCYIDKSVDMRTAVKRILWGKLINCGQ 242
Cdd:cd07123 237 PVVGDTVLASPhLAGLHFTGSTPTFKSLWKqiGENldRYRTYPRIvgETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQ 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 243 TCIA------PDYILcsKEVQEKFIVEAKDVLkewYGENIQSSPDLSRVINANNFQRLLGLMKSGR------VAVGGNYD 310
Cdd:cd07123 317 KCSAasrayvPESLW--PEVKERLLEELKEIK---MGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKsdpeaeIIAGGKCD 391
|
250 260 270
....*....|....*....|....*....|....*..
gi 442622748 311 ASE-RFIEPTILVdvkETDP---IMEEEIFGPILPIF 343
Cdd:cd07123 392 DSVgYFVEPTVIE---TTDPkhkLMTEEIFGPVLTVY 425
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
106-411 |
3.66e-09 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 59.44 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 106 GVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSE----IAANCAK-FIADVIPK----YLDNDcypvvcgGPSETAEL 176
Cdd:PRK11904 686 GVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEqtplIAAEAVKlLHEAGIPKdvlqLLPGD-------GATVGAAL 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 177 LNQ-RFDYIFYTGSTRVGKIIHAA-ANKYLTPTTL--ELGGKSPCYIDKS------VD--MRTAVKrilwgkliNCGQTC 244
Cdd:PRK11904 759 TADpRIAGVAFTGSTETARIINRTlAARDGPIVPLiaETGGQNAMIVDSTalpeqvVDdvVTSAFR--------SAGQRC 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 245 IAPDyILCskeVQE-------KFIVEAKDVLKewYGENIQSSPDLSRVINANNFQRLL----GLMKSGRVAVGGNYDASE 313
Cdd:PRK11904 831 SALR-VLF---VQEdiadrviEMLKGAMAELK--VGDPRLLSTDVGPVIDAEAKANLDahieRMKREARLLAQLPLPAGT 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 314 R---FIEPTILvdvkETDPI--MEEEIFGPILPI-----FNVESAYDAikfINAREKPLVIYVFSNSNKLVKEFRRSTTS 383
Cdd:PRK11904 905 EnghFVAPTAF----EIDSIsqLEREVFGPILHVirykaSDLDKVIDA---INATGYGLTLGIHSRIEETADRIADRVRV 977
|
330 340
....*....|....*....|....*...
gi 442622748 384 GGFSSNETIMHCGVDVLPFGGVGMSGMG 411
Cdd:PRK11904 978 GNVYVNRNQIGAVVGVQPFGGQGLSGTG 1005
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
128-266 |
5.42e-07 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 51.72 E-value: 5.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 128 AIAAGNCVVIKPSEIAANC----AKFIADVIPKY-LDNDCYPVVCGGPSE-TAELLNQR-FDYIFYTGSTRVGKiihaAA 200
Cdd:cd07122 119 ALKTRNAIIFSPHPRAKKCsieaAKIMREAAVAAgAPEGLIQWIEEPSIElTQELMKHPdVDLILATGGPGMVK----AA 194
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442622748 201 NKYLTPTtleLG---GKSPCYIDKSVDMRTAVKRILWGKLINCGQTCIAPDYILCSKEVQEKFIVEAKD 266
Cdd:cd07122 195 YSSGKPA---IGvgpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASEQSVIVDDEIYDEVRAELKR 260
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
104-197 |
1.41e-06 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 51.09 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 104 PFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSE----IAANCAKFI------ADV---IPkyldndcypvvcgGP 170
Cdd:COG4230 680 GRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEqtplIAARAVRLLheagvpADVlqlLP-------------GD 746
|
90 100 110
....*....|....*....|....*....|
gi 442622748 171 SET--AELLNQ-RFDYIFYTGSTRVGKIIH 197
Cdd:COG4230 747 GETvgAALVADpRIAGVAFTGSTETARLIN 776
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
26-259 |
7.98e-04 |
|
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: 41.87 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 26 RRKQLENLLRCY-EEHENEIISALE---ADLRRPKQESLIVET-------EFMKNdirhiLFQLDEWVQSEKPPKSFVNM 94
Cdd:cd07081 7 AAKVAQQGLSCKsQEMVDLIFRAAAeaaEDARIDLAKLAVSETgmgrvedKVIKN-----HFAAEYIYNVYKDEKTCGVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 95 MDD----VQIYNDPFGVVLVIGAWNYPLQLLLVPVASAIAAGNCVVIKPSEIAANCAKFIADVIPKYLdndcypVVCGGP 170
Cdd:cd07081 82 TGDenggTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAA------VAAGAP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 171 S-----------ETAELLNQR--FDYIFYTGSTRVGKiihaAANKYLTPTTLELGGKSPCYIDKSVDMRTAVKRILWGKL 237
Cdd:cd07081 156 EnligwidnpsiELAQRLMKFpgIGLLLATGGPAVVK----AAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKT 231
|
250 260
....*....|....*....|..
gi 442622748 238 INCGQTCIAPDYILCSKEVQEK 259
Cdd:cd07081 232 FDNGVICASEQSVIVVDSVYDE 253
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
100-236 |
1.44e-03 |
|
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: 41.05 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 100 IYNDPFGVVLVIGAWNYPLQLLLVpVASAIAAGNCVVIKPSEIAANCAKFIADVIPKYLDNdcypvvcGGPSETAELLNQ 179
Cdd:cd07077 96 VRAFPIGVTMHILPSTNPLSGITS-ALRGIATRNQCIFRPHPSAPFTNRALALLFQAADAA-------HGPKILVLYVPH 167
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442622748 180 R-------------FDYIFYTGSTRVGKIIHAAANKylTPTTLELGGKSPCYIDKSVDMRTAVKRILWGK 236
Cdd:cd07077 168 PsdelaeellshpkIDLIVATGGRDAVDAAVKHSPH--IPVIGFGAGNSPVVVDETADEERASGSVHDSK 235
|
|
| |
