|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
1-374 |
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: 707.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 1 MLGNLPELASARPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAEL 80
Cdd:cd07132 70 AISNLPEWMKPEPVKKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 81 LPQYLDQDLYAIVNGGIPETTELLKQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIA 160
Cdd:cd07132 150 IPKYLDKECYPVVLGGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 161 WGKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVKDFYGENIKASPDYERIINLRHFKRLQSLLKGQKIAFGGEMDEAT 240
Cdd:cd07132 230 WGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 241 RYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIM 320
Cdd:cd07132 310 RYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIM 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1062593943 321 HFTVNSLPFGGVGASGMGAYHGKYSFDTFSHQRPCLLKGLKGESVNKLRYPPNS 374
Cdd:cd07132 390 HYTLDSLPFGGVGNSGMGAYHGKYSFDTFSHKRSCLVKSLNMEKLNSLRYPPYS 443
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
1-356 |
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: 611.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 1 MLGNLPELASARPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAEL 80
Cdd:cd07087 70 ALKHLKKWMKPRRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 81 LPQYLDQDLYAIVNGGIPETTELLKQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIA 160
Cdd:cd07087 150 IPKYFDPEAVAVVEGGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 161 WGKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVKDFYGENIKASPDYERIINLRHFKRLQSLLKGQKIAFGGEMDEAT 240
Cdd:cd07087 230 WGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGKVVIGGQVDKEE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 241 RYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIM 320
Cdd:cd07087 310 RYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLL 389
|
330 340 350
....*....|....*....|....*....|....*.
gi 1062593943 321 HFTVNSLPFGGVGASGMGAYHGKYSFDTFSHQRPCL 356
Cdd:cd07087 390 HAAIPNLPFGGVGNSGMGAYHGKAGFDTFSHLKSVL 425
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
1-412 |
0e+00 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 571.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 1 MLGNLPELASARPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAEL 80
Cdd:PTZ00381 79 LLKHLDEYLKPEKVDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 81 LPQYLDQDLYAIVNGGIPETTELLKQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIA 160
Cdd:PTZ00381 159 LTKYLDPSYVRVIEGGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 161 WGKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVKDFYGENIKASPDYERIINLRHFKRLQSLLK--GQKIAFGGEMDE 238
Cdd:PTZ00381 239 WGKFLNAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKdhGGKVVYGGEVDI 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 239 ATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDV 318
Cdd:PTZ00381 319 ENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDC 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 319 IMHFTVNSLPFGGVGASGMGAYHGKYSFDTFSHQRPCLLKGLKGESVNKLRYPPNSESKVSWAKFFL-LKQFNKGRLGML 397
Cdd:PTZ00381 399 VFHLLNPNLPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNKSTGNSFDLSLRYPPYTSFKSWVLSFLLkLSIPVQSEVLKS 478
|
410
....*....|....*
gi 1062593943 398 LFVCLVAVAAVIVKK 412
Cdd:PTZ00381 479 RLFVSALVFVALLQK 493
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
1-377 |
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: 554.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 1 MLGNLPELASARPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAEL 80
Cdd:cd07136 70 AIKHLKKWMKPKRVKTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 81 LPQYLDQDLYAIVNGGIPETTELLKQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIA 160
Cdd:cd07136 150 IEETFDEEYVAVVEGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIV 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 161 WGKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVKDFYGENIKASPDYERIINLRHFKRLQSLLKGQKIAFGGEMDEAT 240
Cdd:cd07136 230 WGKFLNAGQTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGKIVFGGNTDRET 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 241 RYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIM 320
Cdd:cd07136 310 LYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIM 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1062593943 321 HFTVNSLPFGGVGASGMGAYHGKYSFDTFSHQRPCLLKGLKGESvnKLRYPPNSESK 377
Cdd:cd07136 390 HLANPYLPFGGVGNSGMGSYHGKYSFDTFSHKKSILKKSTWFDL--PLRYPPYKGKK 444
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
1-354 |
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: 526.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 1 MLGNLPELASARPAKKNLLT-MMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAE 79
Cdd:cd07135 77 MLKNLKKWAKDEKVKDGPLAfMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 80 LLPQYLDQDLYAIVNGGIPETTELLKQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRI 159
Cdd:cd07135 157 LVPKYLDPDAFQVVQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRI 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 160 AWGKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVKDFYGENIKASPDYERIINLRHFKRLQSLLK--GQKIAFGGEMD 237
Cdd:cd07135 237 LWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDttKGKVVIGGEMD 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 238 EATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGND 317
Cdd:cd07135 317 EATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVIND 396
|
330 340 350
....*....|....*....|....*....|....*..
gi 1062593943 318 VIMHFTVNSLPFGGVGASGMGAYHGKYSFDTFSHQRP 354
Cdd:cd07135 397 TLIHVGVDNAPFGGVGDSGYGAYHGKYGFDTFTHERT 433
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
5-356 |
1.03e-167 |
|
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: 477.87 E-value: 1.03e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 5 LPELASARPAKKNLLTMM-------------DEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSE 71
Cdd:cd07134 61 LPVLSEINHAIKHLKKWMkpkrvrtplllfgTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTP 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 72 NTAKILAELLPQYLDQDLYAIVNGGIPETTELLKQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCD 151
Cdd:cd07134 141 HTSAVIAKIIREAFDEDEVAVFEGDAEVAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETAD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 152 LDVACRRIAWGKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVKDFYGEN--IKASPDYERIINLRHFKRLQSLL---- 225
Cdd:cd07134 221 LKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFYGKDaaRKASPDLARIVNDRHFDRLKGLLddav 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 226 -KGQKIAFGGEMDEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRV 304
Cdd:cd07134 301 aKGAKVEFGGQFDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKV 380
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1062593943 305 IDETSSGGVTGNDVIMHFTVNSLPFGGVGASGMGAYHGKYSFDTFSHQRPCL 356
Cdd:cd07134 381 LARTSSGGVVVNDVVLHFLNPNLPFGGVNNSGIGSYHGVYGFKAFSHERAVL 432
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
5-354 |
1.38e-164 |
|
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: 470.04 E-value: 1.38e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 5 LPELASARPAKKNL------------LTMMD-EAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSE 71
Cdd:cd07133 62 LPSIAGIKHARKHLkkwmkpsrrhvgLLFLPaKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 72 NTAKILAELLPQYLDQDLYAIVNGGIPETTELLKQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCD 151
Cdd:cd07133 142 RTSALLAELLAEYFDEDEVAVVTGGADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDAD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 152 LDVACRRIAWGKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVKDFYGeNIKASPDYERIINLRHFKRLQSLL-----K 226
Cdd:cd07133 222 LAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYP-TLADNPDYTSIINERHYARLQGLLedaraK 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 227 GQKI---AFGGEMDEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKR 303
Cdd:cd07133 301 GARVielNPAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDR 380
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1062593943 304 VIDETSSGGVTGNDVIMHFTVNSLPFGGVGASGMGAYHGKYSFDTFSHQRP 354
Cdd:cd07133 381 VLRRTHSGGVTINDTLLHVAQDDLPFGGVGASGMGAYHGKEGFLTFSHAKP 431
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
2-356 |
7.20e-157 |
|
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: 450.32 E-value: 7.20e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 2 LGNLPELASARPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELL 81
Cdd:cd07137 72 IKELKKWMAPEKVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLI 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 82 PQYLDQDLYAIVNGGIPETTELLKQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAW 161
Cdd:cd07137 152 PEYLDTKAIKVIEGGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 162 GKYMNC-GQTCIAPDYILCEASLQNQIVQKIKETVKDFYGENIKASPDYERIINLRHFKRLQSLLK----GQKIAFGGEM 236
Cdd:cd07137 232 GKWGCNnGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDdpsvADKIVHGGER 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 237 DEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGN 316
Cdd:cd07137 312 DEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFN 391
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1062593943 317 DVIMHFTVNSLPFGGVGASGMGAYHGKYSFDTFSHQRPCL 356
Cdd:cd07137 392 DTVVQYAIDTLPFGGVGESGFGAYHGKFSFDAFSHKKAVL 431
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
2-398 |
2.58e-135 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 397.56 E-value: 2.58e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 2 LGNLPELASARPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELL 81
Cdd:PLN02203 79 LSNLKKWMAPKKAKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 82 PQYLDQDLYAIVNGGIPETTELLKQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYID---RDCDLDVACRR 158
Cdd:PLN02203 159 PKYLDSKAVKVIEGGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 159 IAWGKYMNC-GQTCIAPDYILCEASLQNQIVQKIKETVKDFYGENIKASPDYERIINLRHFKRLQSLLKGQKIA----FG 233
Cdd:PLN02203 239 IVGGKWGSCaGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAasivHG 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 234 GEMDEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGV 313
Cdd:PLN02203 319 GSIDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSV 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 314 TGNDVIMHFTVNSLPFGGVGASGMGAYHGKYSFDTFSHQRPCLLKGLKGESvnKLRYPPNSESKVSwakfFLLKQFNKGR 393
Cdd:PLN02203 399 TFNDAIIQYACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSLLTEF--EFRYPPWNDFKLG----FLRLVYRFDY 472
|
....*
gi 1062593943 394 LGMLL 398
Cdd:PLN02203 473 FGLLL 477
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
7-357 |
1.22e-118 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 353.05 E-value: 1.22e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 7 ELASARPAKKNLLTMMD-EAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY- 84
Cdd:cd07078 71 GLARRLHGEVIPSPDPGeLAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAg 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 85 LDQDLYAIVNGGIPET-TELLKQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWG 162
Cdd:cd07078 151 LPPGVLNVVTGDGDEVgAALASHpRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFG 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 163 KYMNCGQTCIAPDYILCEASLQNQIVQKIKETVKDFYGEN-IKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGEM 236
Cdd:cd07078 231 AFGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNpLDPDTDMGPLISAAQLDRVLAYIedakaEGAKLLCGGKR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 237 DEAT--RYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVT 314
Cdd:cd07078 311 LEGGkgYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVW 390
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1062593943 315 GNDVIMHFTVNsLPFGGVGASGMGAYHGKYSFDTFSHQRPCLL 357
Cdd:cd07078 391 INDYSVGAEPS-APFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
2-382 |
5.04e-118 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 353.20 E-value: 5.04e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 2 LGNLPELASARPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELL 81
Cdd:PLN02174 83 LKQLKNWMAPEKAKTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 82 PQYLDQDLYAIVNGGIPETTELLKQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAW 161
Cdd:PLN02174 163 EQYLDSSAVRVVEGAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 162 GKY-MNCGQTCIAPDYILCEASLQNQIVQKIKETVKDFYGENIKASPDYERIINLRHFKRLQSLLK----GQKIAFGGEM 236
Cdd:PLN02174 243 GKWgCNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDekevSDKIVYGGEK 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 237 DEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGN 316
Cdd:PLN02174 323 DRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVN 402
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1062593943 317 DVIMHFTVNSLPFGGVGASGMGAYHGKYSFDTFSHQRPCLLKGLKGESVnkLRYPPNSESKVSWAK 382
Cdd:PLN02174 403 DIAVHLALHTLPFGGVGESGMGAYHGKFSFDAFSHKKAVLYRSLFGDSA--VRYPPYSRGKLRLLK 466
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
24-357 |
2.24e-95 |
|
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: 291.06 E-value: 2.24e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 24 EAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPET-T 101
Cdd:cd06534 85 EAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVVNVVPGGGDEVgA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 102 ELLKQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCE 180
Cdd:cd06534 165 ALLSHpRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVH 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 181 ASLQNQIVQKIKetvkdfygenikaspdyeriinlrhfkrlqsllkgqkiafggemdeatrylapTILTDVDPNSKVMQE 260
Cdd:cd06534 245 ESIYDEFVEKLV-----------------------------------------------------TVLVDVDPDMPIAQE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 261 EIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFTVNsLPFGGVGASGMGAY 340
Cdd:cd06534 272 EIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPE-APFGGVKNSGIGRE 350
|
330
....*....|....*..
gi 1062593943 341 HGKYSFDTFSHQRPCLL 357
Cdd:cd06534 351 GGPYGLEEYTRTKTVVI 367
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
24-353 |
1.29e-92 |
|
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: 287.79 E-value: 1.29e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 24 EAYVQPEPLGVVLIIGAWNYPFVLTMQP------------LvgaiaagnaaivKPSELSENTAKILAELLPQY-LDQDLY 90
Cdd:COG1012 134 RAYVRREPLGVVGAITPWNFPLALAAWKlapalaagntvvL------------KPAEQTPLSALLLAELLEEAgLPAGVL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 91 AIVNGGIPETTELLKQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCG 168
Cdd:COG1012 202 NVVTGDGSEVGAALVAhpDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAG 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 169 QTCIAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGE--MDEAT 240
Cdd:COG1012 282 QRCTAASRLLVHESIYDEFVERLVAAAKALkVGDPLDPGTDMGPLISEAQLERVLAYIedavaEGAELLTGGRrpDGEGG 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 241 RYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIM 320
Cdd:COG1012 362 YFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTT 441
|
330 340 350
....*....|....*....|....*....|...
gi 1062593943 321 HFTVNsLPFGGVGASGMGAYHGKYSFDTFSHQR 353
Cdd:COG1012 442 GAVPQ-APFGGVKQSGIGREGGREGLEEYTETK 473
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
24-353 |
2.49e-81 |
|
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: 257.84 E-value: 2.49e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 24 EAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTE 102
Cdd:pfam00171 119 LAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAgLPAGVLNVVTGSGAEVGE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 103 LLKQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCE 180
Cdd:pfam00171 199 ALVEhpDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVH 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 181 ASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGEMDEAT-RYLAPTILTDVDP 253
Cdd:pfam00171 279 ESIYDEFVEKLVEAAKKLkVGDPLDPDTDMGPLISKAQLERVLKYVedakeEGAKLLTGGEAGLDNgYFVEPTVLANVTP 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 254 NSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMhFTVNSLPFGGVG 333
Cdd:pfam00171 359 DMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTT-GDADGLPFGGFK 437
|
330 340
....*....|....*....|
gi 1062593943 334 ASGMGAYHGKYSFDTFSHQR 353
Cdd:pfam00171 438 QSGFGREGGPYGLEEYTEVK 457
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
4-353 |
8.92e-79 |
|
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: 251.37 E-value: 8.92e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 4 NLPELASARPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQ 83
Cdd:cd07099 92 NAPRVLAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 84 Y-LDQDLYAIVNGGIPETTELLKQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWG 162
Cdd:cd07099 172 AgPPQGVLQVVTGDGATGAALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWG 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 163 KYMNCGQTCIAPDYILCEASLQNQIVQKIKETVKDF---YGENIKA------SPDYERIINlRHFKrlQSLLKGQKIAFG 233
Cdd:cd07099 252 AMVNAGQTCISVERVYVHESVYDEFVARLVAKARALrpgADDIGDAdigpmtTARQLDIVR-RHVD--DAVAKGAKALTG 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 234 GE-MDEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGG 312
Cdd:cd07099 329 GArSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGA 408
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1062593943 313 VTGNDVIMHFTVNSLPFGGVGASGMGAYHGKYSFDTFSHQR 353
Cdd:cd07099 409 VSINDVLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPK 449
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
10-343 |
5.62e-69 |
|
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: 226.03 E-value: 5.62e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 10 SARPAkkNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYL---- 85
Cdd:cd07098 101 ESRPG--GLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIRECLaacg 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 86 -DQDLYAIVNGgIPETTELLKQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWG 162
Cdd:cd07098 179 hDPDLVQLVTC-LPETAEALTShpVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRG 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 163 KYMNCGQTCIAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGEM 236
Cdd:cd07098 258 TFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALrQGPPLDGDVDVGAMISPARFDRLEELVadaveKGARLLAGGKR 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 237 -----DEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSG 311
Cdd:cd07098 338 yphpeYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETG 417
|
330 340 350
....*....|....*....|....*....|..
gi 1062593943 312 GVTGNDVIMHFTVNSLPFGGVGASGMGAYHGK 343
Cdd:cd07098 418 MVAINDFGVNYYVQQLPFGGVKGSGFGRFAGE 449
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
8-353 |
4.58e-62 |
|
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: 207.00 E-value: 4.58e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 8 LASARPAKKNlltmmdeaYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENT-----AKILAEL-L 81
Cdd:cd07104 83 LPSDVPGKES--------MVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgglliAEIFEEAgL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 82 PQyldqDLYAIVNGGIPETTELL--KQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRI 159
Cdd:cd07104 155 PK----GVLNVVPGGGSEIGDALveHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 160 AWGKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVKDF-YGEniKASPDYE--RIINLRHFKRLQSLL-----KGQKIA 231
Cdd:cd07104 231 AFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALpVGD--PRDPDTVigPLINERQVDRVHAIVedavaAGARLL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 232 FGGEMDEatRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSG 311
Cdd:cd07104 309 TGGTYEG--LFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETG 386
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1062593943 312 GVTGNDVimhfTVNS---LPFGGVGASGMGAYHGKYSFDTFSHQR 353
Cdd:cd07104 387 MVHINDQ----TVNDephVPFGGVKASGGGRFGGPASLEEFTEWQ 427
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
8-307 |
5.07e-60 |
|
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: 202.50 E-value: 5.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 8 LASARPAKKnlltmmdeAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LD 86
Cdd:cd07088 118 IPSDRPNEN--------IFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAgLP 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 87 QDLYAIVNGGIPETTELL--KQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKY 164
Cdd:cd07088 190 AGVLNIVTGRGSVVGDALvaHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRI 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 165 MNCGQTCIAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLLK-----GQKIAFGGEMDE 238
Cdd:cd07088 270 INCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVkVGDPFDAATDMGPLVNEAALDKVEEMVEraveaGATLLTGGKRPE 349
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1062593943 239 ATR--YLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDE 307
Cdd:cd07088 350 GEKgyFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNE 420
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
26-353 |
8.97e-59 |
|
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: 198.94 E-value: 8.97e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 26 YVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLpqyLDQDL----YAIVNGGIPETT 101
Cdd:cd07093 112 YVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELA---NEAGLppgvVNVVHGFGPEAG 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 102 ELLKQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILC 179
Cdd:cd07093 189 AALVAhpDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILV 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 180 EASLQNQIVQKIKETVKdfygeNIKA----SPDYE--RIINLRHFKRLQSLLK-----GQKIAFGGEMDEATR-----YL 243
Cdd:cd07093 269 QRSIYDEFLERFVERAK-----ALKVgdplDPDTEvgPLISKEHLEKVLGYVElaraeGATILTGGGRPELPDleggyFV 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 244 APTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDvimhFT 323
Cdd:cd07093 344 EPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNC----WL 419
|
330 340 350
....*....|....*....|....*....|..
gi 1062593943 324 VNSL--PFGGVGASGMGAYHGKYSFDTFSHQR 353
Cdd:cd07093 420 VRDLrtPFGGVKASGIGREGGDYSLEFYTELK 451
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
30-353 |
5.72e-58 |
|
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: 196.78 E-value: 5.72e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 30 EPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTELLKQ-- 106
Cdd:cd07150 118 RPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAgLPKGVFNVVTGGGAEVGDELVDdp 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 107 RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEASLQNQ 186
Cdd:cd07150 198 RVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 187 IVQKIKE-----TVKDFYGENIKASPdyerIINLRHFKRLQSLL-----KGQKIAFGGEMDeaTRYLAPTILTDVDPNSK 256
Cdd:cd07150 278 FVKKFVArasklKVGDPRDPDTVIGP----LISPRQVERIKRQVedavaKGAKLLTGGKYD--GNFYQPTVLTDVTPDMR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 257 VMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFTVNsLPFGGVGASG 336
Cdd:cd07150 352 IFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHINDPTILDEAH-VPFGGVKASG 430
|
330
....*....|....*..
gi 1062593943 337 MGAYHGKYSFDTFSHQR 353
Cdd:cd07150 431 FGREGGEWSMEEFTELK 447
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
27-349 |
8.23e-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: 196.50 E-value: 8.23e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 27 VQPEPLGVVLIIGAWNYPFVL-------------TMqplvgaiaagnaaIVKPSELSENTAKILAELLPQY-LDQDLYAI 92
Cdd:cd07103 113 VIKQPVGVVAAITPWNFPAAMitrkiapalaagcTV-------------VLKPAEETPLSALALAELAEEAgLPAGVLNV 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 93 VNGGIPETTELLKQRFD--HILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQT 170
Cdd:cd07103 180 VTGSPAEIGEALCASPRvrKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQT 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 171 CIAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGEMDEAT-RYL 243
Cdd:cd07103 260 CVCANRIYVHESIYDEFVEKLVERVKKLkVGNGLDEGTDMGPLINERAVEKVEALVedavaKGAKVLTGGKRLGLGgYFY 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 244 APTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMhfT 323
Cdd:cd07103 340 EPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLI--S 417
|
330 340
....*....|....*....|....*.
gi 1062593943 324 VNSLPFGGVGASGMGAYHGKYSFDTF 349
Cdd:cd07103 418 DAEAPFGGVKESGLGREGGKEGLEEY 443
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
30-353 |
3.48e-57 |
|
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: 194.86 E-value: 3.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 30 EPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTELL--KQ 106
Cdd:cd07118 118 EPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAgLPAGVVNIVTGYGATVGQAMteHP 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 107 RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEASLQNQ 186
Cdd:cd07118 198 DVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 187 IVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLLK-----GQKIAFGGEMDE--ATRYLAPTILTDVDPNSKVM 258
Cdd:cd07118 278 FVAAVVARSRKVrVGDPLDPETKVGAIINEAQLAKITDYVDagraeGATLLLGGERLAsaAGLFYQPTIFTDVTPDMAIA 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 259 QEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFTvnSLPFGGVGASGMG 338
Cdd:cd07118 358 REEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSP--ELPFGGFKQSGIG 435
|
330
....*....|....*
gi 1062593943 339 AYHGKYSFDTFSHQR 353
Cdd:cd07118 436 RELGRYGVEEYTELK 450
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
25-349 |
7.62e-56 |
|
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: 191.85 E-value: 7.62e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 25 AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTEL 103
Cdd:cd07144 138 AYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVNIIPGYGAVAGSA 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 104 LKQR--FDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEA 181
Cdd:cd07144 218 LAEHpdVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 182 SLQNQIVQKIKETVK------DFYGENIKASP-----DYERIINLRHfkrlQSLLKGQKIAFGGE----MDEATRYLAPT 246
Cdd:cd07144 298 SIYDKFVEKFVEHVKqnykvgSPFDDDTVVGPqvsktQYDRVLSYIE----KGKKEGAKLVYGGEkapeGLGKGYFIPPT 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 247 ILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGV---TGNDviMHFT 323
Cdd:cd07144 374 IFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVwinSSND--SDVG 451
|
330 340
....*....|....*....|....*.
gi 1062593943 324 VnslPFGGVGASGMGAYHGKYSFDTF 349
Cdd:cd07144 452 V---PFGGFKMSGIGRELGEYGLETY 474
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
30-350 |
1.06e-55 |
|
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: 190.48 E-value: 1.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 30 EPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLpqyLDQDLYAivnGGI----------PE 99
Cdd:cd07105 97 EPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVF---HEAGLPK---GVLnvvthspedaPE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 100 TTELLkqrFDH-----ILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAP 174
Cdd:cd07105 171 VVEAL---IAHpavrkVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMST 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 175 DYILCEASLQNQIVQKIKETVkdfygENIKASPDYERI-INLRHFKRLQSLL-----KGQKIAFGG--EMDEATRYLAPT 246
Cdd:cd07105 248 ERIIVHESIADEFVEKLKAAA-----EKLFAGPVVLGSlVSAAAADRVKELVddalsKGAKLVVGGlaDESPSGTSMPPT 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 247 ILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHfTVNS 326
Cdd:cd07105 323 ILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVH-DEPT 401
|
330 340
....*....|....*....|....
gi 1062593943 327 LPFGGVGASGMGAYHGKYSFDTFS 350
Cdd:cd07105 402 LPHGGVKSSGYGRFNGKWGIDEFT 425
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
25-350 |
3.31e-55 |
|
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: 189.75 E-value: 3.31e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 25 AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTEL 103
Cdd:cd07109 111 VYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAgLPAGALNVVTGLGAEAGAA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 104 LKQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEA 181
Cdd:cd07109 191 LVAhpGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHR 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 182 SLQNQIVQKIKETVKDF---YGEnikASPDYERIINLRHFKRLQSLL-----KGQKIAFGGEMDEATR----YLAPTILT 249
Cdd:cd07109 271 SIYDEVLERLVERFRALrvgPGL---EDPDLGPLISAKQLDRVEGFVararaRGARIVAGGRIAEGAPaggyFVAPTLLD 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 250 DVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDvimHFTVN--SL 327
Cdd:cd07109 348 DVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNN---YGAGGgiEL 424
|
330 340
....*....|....*....|...
gi 1062593943 328 PFGGVGASGMGAYHGKYSFDTFS 350
Cdd:cd07109 425 PFGGVKKSGHGREKGLEALYNYT 447
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
25-347 |
1.80e-53 |
|
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: 185.49 E-value: 1.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 25 AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQD-LYAIVNGGIPETTEL 103
Cdd:cd07091 135 AYTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPgVVNIVPGFGPTAGAA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 104 LKQ--RFDHILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCE 180
Cdd:cd07091 215 ISShmDVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQ 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 181 ASLQNQIVQKIKETVKDFY-GENIKASPDYERIINLRHFKRLQSLLK-----GQKIAFGGE-MDEATRYLAPTILTDVDP 253
Cdd:cd07091 295 ESIYDEFVEKFKARAEKRVvGDPFDPDTFQGPQVSKAQFDKILSYIEsgkkeGATLLTGGErHGSKGYFIQPTVFTDVKD 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 254 NSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGN--DVIMHftvnSLPFGG 331
Cdd:cd07091 375 DMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNtyNVFDA----AVPFGG 450
|
330
....*....|....*.
gi 1062593943 332 VGASGMGAYHGKYSFD 347
Cdd:cd07091 451 FKQSGFGRELGEEGLE 466
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
25-353 |
2.83e-53 |
|
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: 184.68 E-value: 2.83e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 25 AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAEL-----LPQyldqDLYAIVNGGIPE 99
Cdd:cd07114 113 NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLaeeagFPP----GVVNVVTGFGPE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 100 TTELLKQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYI 177
Cdd:cd07114 189 TGEALVEhpLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 178 LCEASLQNQIVQKIKETVKdfygeNIK-ASPDYER-----IINLRHFKRLQSLLK-----GQKIAFGGE-MDEATR---- 241
Cdd:cd07114 269 LVQRSIYDEFVERLVARAR-----AIRvGDPLDPEtqmgpLATERQLEKVERYVArareeGARVLTGGErPSGADLgagy 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 242 YLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDviMH 321
Cdd:cd07114 344 FFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNT--YR 421
|
330 340 350
....*....|....*....|....*....|..
gi 1062593943 322 FTVNSLPFGGVGASGMGAYHGKYSFDTFSHQR 353
Cdd:cd07114 422 ALSPSSPFGGFKDSGIGRENGIEAIREYTQTK 453
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
31-344 |
4.11e-53 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 183.88 E-value: 4.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 31 PLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYAIVNGGiPETTELLKQ--RF 108
Cdd:cd07106 114 PLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEVLPPGVLNVVSGG-DELGPALTShpDI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 109 DHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEASLQNQIV 188
Cdd:cd07106 193 RKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFC 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 189 QKIKETVKDFY-GENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGEMDEATRY-LAPTILTDVDPNSKVMQEE 261
Cdd:cd07106 273 EALVALAKAAVvGDGLDPGTTLGPVQNKMQYDKVKELVedakaKGAKVLAGGEPLDGPGYfIPPTIVDDPPEGSRIVDEE 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 262 IFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNdviMHFTVN-SLPFGGVGASGMGAY 340
Cdd:cd07106 353 QFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWIN---THGALDpDAPFGGHKQSGIGVE 429
|
....
gi 1062593943 341 HGKY 344
Cdd:cd07106 430 FGIE 433
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
30-349 |
1.22e-52 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 183.74 E-value: 1.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 30 EPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTELL---- 104
Cdd:PLN02278 159 QPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAgIPPGVLNVVMGDAPEIGDALlasp 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 105 KQRfdHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEASLQ 184
Cdd:PLN02278 239 KVR--KITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIY 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 185 NQIVQKIKETVK-----DFYGENIKASPdyerIINLRHFKRLQSLL-----KGQKIAFGGE-MDEATRYLAPTILTDVDP 253
Cdd:PLN02278 317 DKFAEAFSKAVQklvvgDGFEEGVTQGP----LINEAAVQKVESHVqdavsKGAKVLLGGKrHSLGGTFYEPTVLGDVTE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 254 NSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFTVnsLPFGGVG 333
Cdd:PLN02278 393 DMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEV--APFGGVK 470
|
330
....*....|....*.
gi 1062593943 334 ASGMGAYHGKYSFDTF 349
Cdd:PLN02278 471 QSGLGREGSKYGIDEY 486
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
1-351 |
1.51e-52 |
|
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: 182.45 E-value: 1.51e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 1 MLGNLPE-LASARPAKKNLLtmmdEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELS----ENTAK 75
Cdd:cd07102 89 MISIAEEaLADIRVPEKDGF----ERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTplcgERFAA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 76 ILAE-LLPQyldqDLYAIVNGGIPETTELLKQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLD 153
Cdd:cd07102 165 AFAEaGLPE----GVFQVLHLSHETSAALIADpRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLD 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 154 VACRRIAWGKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRH--FKRLQ---SLLKG 227
Cdd:cd07102 241 AAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYkLGDPLDPSTTLGPVVSARAadFVRAQiadAIAKG 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 228 QKIAFGGEM----DEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKR 303
Cdd:cd07102 321 ARALIDGALfpedKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEA 400
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1062593943 304 VIDETSSGGVTGN--DvimhFTVNSLPFGGVGASGMGAYHGKYSFDTFSH 351
Cdd:cd07102 401 LGEQLETGTVFMNrcD----YLDPALAWTGVKDSGRGVTLSRLGYDQLTR 446
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
31-353 |
1.96e-52 |
|
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: 182.11 E-value: 1.96e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 31 PLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENT-----AKILAEL-LPQYLDQdlyaIVNGGiPETTELL 104
Cdd:cd07152 110 PLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSggvviARLFEEAgLPAGVLH----VLPGG-ADAGEAL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 105 --KQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEAS 182
Cdd:cd07152 185 veDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHES 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 183 LQNQIVQKIKE-----TVKDFYGENIKASPdyerIINLRHFKRLQ-----SLLKGQKIAFGGEMDEatRYLAPTILTDVD 252
Cdd:cd07152 265 VADAYTAKLAAkakhlPVGDPATGQVALGP----LINARQLDRVHaivddSVAAGARLEAGGTYDG--LFYRPTVLSGVK 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 253 PNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVimhfTVNS---LPF 329
Cdd:cd07152 339 PGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQ----TVNDephNPF 414
|
330 340
....*....|....*....|....*
gi 1062593943 330 GGVGASGMGAYHG-KYSFDTFSHQR 353
Cdd:cd07152 415 GGMGASGNGSRFGgPANWEEFTQWQ 439
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
26-350 |
3.08e-52 |
|
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: 181.76 E-value: 3.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 26 YVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYAIVNGGIPETTELL- 104
Cdd:cd07092 113 MIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGVVNVVCGGGASAGDALv 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 105 -KQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEASL 183
Cdd:cd07092 193 aHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 184 QNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLL----KGQKIAFGGEMDEATRY-LAPTILTDVDPNSKV 257
Cdd:cd07092 273 YDEFVAALVEAVSAIrVGDPDDEDTEMGPLNSAAQRERVAGFVerapAHARVLTGGRRAEGPGYfYEPTVVAGVAQDDEI 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 258 MQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDvimHFT-VNSLPFGGVGASG 336
Cdd:cd07092 353 VQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNT---HIPlAAEMPHGGFKQSG 429
|
330
....*....|....
gi 1062593943 337 MGAYHGKYSFDTFS 350
Cdd:cd07092 430 YGKDLSIYALEDYT 443
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
25-338 |
1.82e-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: 177.02 E-value: 1.82e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 25 AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQ-YLDQDLYAIVNGGIPET-TE 102
Cdd:cd07149 117 GFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEaGLPKGALNVVTGSGETVgDA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 103 LLK-QRFDHILYTGNTAVGKIVMEAAAkhLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEA 181
Cdd:cd07149 197 LVTdPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 182 SLQNQIVQKIKETVK-----DFYGENIKASPdyerIINLRHFKRLQSLL-----KGQKIAFGGEMDEAtrYLAPTILTDV 251
Cdd:cd07149 275 DIYDEFLERFVAATKklvvgDPLDEDTDVGP----MISEAEAERIEEWVeeaveGGARLLTGGKRDGA--ILEPTVLTDV 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 252 DPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDvIMHFTVNSLPFGG 331
Cdd:cd07149 349 PPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMIND-SSTFRVDHMPYGG 427
|
....*..
gi 1062593943 332 VGASGMG 338
Cdd:cd07149 428 VKESGTG 434
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
30-353 |
2.14e-50 |
|
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: 177.05 E-value: 2.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 30 EPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLpqyLDQDLYA----IVNGGIPETTELLK 105
Cdd:cd07089 122 EPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEII---AETDLPAgvvnVVTGSDNAVGEALT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 106 Q--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEASL 183
Cdd:cd07089 199 TdpRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSR 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 184 QNQIVQKIKETVkdfygENIK----ASPD--YERIINLRHFKRLQSLLK-----GQKIAFGGEMDEATR---YLAPTILT 249
Cdd:cd07089 279 YDEVVEALAAAF-----EALPvgdpADPGtvMGPLISAAQRDRVEGYIArgrdeGARLVTGGGRPAGLDkgfYVEPTLFA 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 250 DVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDViMHFTVNSlPF 329
Cdd:cd07089 354 DVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINGG-GGYGPDA-PF 431
|
330 340
....*....|....*....|....
gi 1062593943 330 GGVGASGMGAYHGKYSFDTFSHQR 353
Cdd:cd07089 432 GGYKQSGLGRENGIEGLEEFLETK 455
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
25-351 |
9.42e-50 |
|
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: 175.18 E-value: 9.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 25 AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGiPETTEL 103
Cdd:cd07090 110 AYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAgLPDGVFNVVQGG-GETGQL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 104 LKQRFD--HILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEA 181
Cdd:cd07090 189 LCEHPDvaKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQR 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 182 SLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLLK-----GQKIAFGGE---MD---EATRYLAPTILT 249
Cdd:cd07090 269 SIKDEFTERLVERTKKIrIGDPLDEDTQMGALISEEHLEKVLGYIEsakqeGAKVLCGGErvvPEdglENGFYVSPCVLT 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 250 DVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDvimhFTVNS--L 327
Cdd:cd07090 349 DCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINT----YNISPveV 424
|
330 340
....*....|....*....|....
gi 1062593943 328 PFGGVGASGMGAYHGKYSFDTFSH 351
Cdd:cd07090 425 PFGGYKQSGFGRENGTAALEHYTQ 448
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
26-350 |
3.34e-49 |
|
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: 173.78 E-value: 3.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 26 YVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTELL 104
Cdd:cd07115 112 YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAgFPAGVLNVVTGFGEVAGAAL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 105 KQR--FDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEAS 182
Cdd:cd07115 192 VEHpdVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHES 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 183 LQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGEMDEATR-YLAPTILTDVDPNS 255
Cdd:cd07115 272 IYDEFLERFTSLARSLrPGDPLDPKTQMGPLVSQAQFDRVLDYVdvgreEGARLLTGGKRPGARGfFVEPTIFAAVPPEM 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 256 KVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNdvIMHFTVNSLPFGGVGAS 335
Cdd:cd07115 352 RIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWIN--TYNRFDPGSPFGGYKQS 429
|
330
....*....|....*
gi 1062593943 336 GMGAYHGKYSFDTFS 350
Cdd:cd07115 430 GFGREMGREALDEYT 444
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
7-353 |
3.40e-49 |
|
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: 173.69 E-value: 3.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 7 ELASARPAKKNL-LTMMDE---AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAEL-- 80
Cdd:cd07110 92 DLAEQLDAKAERaVPLPSEdfkARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIaa 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 81 ---LPQyldqDLYAIVNGGIPETTELLKQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVA 155
Cdd:cd07110 172 eagLPP----GVLNVVTGTGDEAGAPLAAhpGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 156 CRRIAWGKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVkdfygENIKASPDYER------IINLRHFKRLQSLLK--- 226
Cdd:cd07110 248 VEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAA-----EAIRVGDPLEEgvrlgpLVSQAQYEKVLSFIArgk 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 227 --GQKIAFGGEMDEATR---YLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLI 301
Cdd:cd07110 323 eeGARLLCGGRRPAHLEkgyFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERC 402
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1062593943 302 KRVIDETSSGGVTGNDVIMHFTvnSLPFGGVGASGMGAYHGKYSFDTFSHQR 353
Cdd:cd07110 403 DRVAEALEAGIVWINCSQPCFP--QAPWGGYKRSGIGRELGEWGLDNYLEVK 452
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
27-349 |
4.83e-49 |
|
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: 173.46 E-value: 4.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 27 VQPEPLGVVLIIGAWNYPF-----------------VLtmqplvgaiaagnaaivKPSELSENTAKILAELLpqyLDQDL 89
Cdd:cd07138 126 VVREPIGVCGLITPWNWPLnqivlkvapalaagctvVL-----------------KPSEVAPLSAIILAEIL---DEAGL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 90 YA----IVNGGIPETTELLK--QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGK 163
Cdd:cd07138 186 PAgvfnLVNGDGPVVGEALSahPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAAC 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 164 YMNCGQTCIAPDYILCEASLQNQIVQKIKETVkdfygENIKA-SPDYER-----IINLRHFKRLQSLLK-----GQKIAF 232
Cdd:cd07138 266 FANSGQSCNAPTRMLVPRSRYAEAEEIAAAAA-----EAYVVgDPRDPAttlgpLASAAQFDRVQGYIQkgieeGARLVA 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 233 GG----EMDEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDET 308
Cdd:cd07138 341 GGpgrpEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRL 420
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1062593943 309 SSGGVTGNDVIMHFtvnSLPFGGVGASGMGAYHGKYSFDTF 349
Cdd:cd07138 421 RAGQVHINGAAFNP---GAPFGGYKQSGNGREWGRYGLEEF 458
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
13-338 |
6.09e-49 |
|
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: 172.93 E-value: 6.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 13 PAKKNLLTmmdeaYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYAI 92
Cdd:cd07108 104 PFGPDVLT-----YTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQVLPAGVLNV 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 93 VNGGIPETTELLKQR--FDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRR-IAWGKYMNCGQ 169
Cdd:cd07108 179 ITGYGEECGAALVDHpdVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGaIAGMRFTRQGQ 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 170 TCIAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLL------KGQKIAFGGEMDEATR- 241
Cdd:cd07108 259 SCTAGSRLFVHEDIYDAFLEKLVAKLSKLkIGDPLDEATDIGAIISEKQFAKVCGYIdlglstSGATVLRGGPLPGEGPl 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 242 ----YLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGND 317
Cdd:cd07108 339 adgfFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQ 418
|
330 340
....*....|....*....|.
gi 1062593943 318 viMHFTVNSLPFGGVGASGMG 338
Cdd:cd07108 419 --GGGQQPGQSYGGFKQSGLG 437
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
9-338 |
2.27e-48 |
|
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: 172.14 E-value: 2.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 9 ASARPAKKNLLTMMDE---AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYL 85
Cdd:cd07559 111 AGVIRAQEGSLSEIDEdtlSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 86 DQDLYAIVNGGIPETTELLK--QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYI-----DRDCDLDVACRR 158
Cdd:cd07559 191 PKGVVNVVTGFGSEAGKPLAshPRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFfddamDADDDFDDKAEE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 159 IAWGKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVkdfygENIKA-SP-DYERII----NLRHFKRLQSLLK-----G 227
Cdd:cd07559 271 GQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERF-----EAIKVgNPlDPETMMgaqvSKDQLEKILSYVDigkeeG 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 228 QKIAFGGEM-----DEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIK 302
Cdd:cd07559 346 AEVLTGGERltlggLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRAL 425
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1062593943 303 RVIDETSSGGVTGNdvimhfTVNSLP----FGGVGASGMG 338
Cdd:cd07559 426 RVARGIQTGRVWVN------CYHQYPahapFGGYKKSGIG 459
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
24-350 |
2.96e-47 |
|
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: 168.64 E-value: 2.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 24 EAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENT-----AKILAEL-LPQyldqDLYAIVNGGI 97
Cdd:cd07151 123 ENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITgglllAKIFEEAgLPK----GVLNVVVGAG 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 98 PEttelLKQRF-DH-----ILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTC 171
Cdd:cd07151 199 SE----IGDAFvEHpvprlISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQIC 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 172 IAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLLK-----GQKIAFGGEMDEatRYLAP 245
Cdd:cd07151 275 MAINRIIVHEDVYDEFVEKFVERVKALpYGDPSDPDTVVGPLINESQVDGLLDKIEqaveeGATLLVGGEAEG--NVLEP 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 246 TILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVimhfTVN 325
Cdd:cd07151 353 TVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQ----PVN 428
|
330 340
....*....|....*....|....*...
gi 1062593943 326 S---LPFGGVGASGMGAYHGKYSFDTFS 350
Cdd:cd07151 429 DephVPFGGEKNSGLGRFNGEWALEEFT 456
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
24-350 |
6.05e-47 |
|
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: 168.26 E-value: 6.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 24 EAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTE 102
Cdd:cd07119 127 ISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAgLPAGVVNLVTGSGATVGA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 103 LL--KQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCE 180
Cdd:cd07119 207 ELaeSPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 181 ASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGEM---DEATR--YLAPTILT 249
Cdd:cd07119 287 ESIHDKFVAALAERAKKIkLGNGLDADTEMGPLVSAEHREKVLSYIqlgkeEGARLVCGGKRptgDELAKgyFVEPTIFD 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 250 DVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDviMHFTVNSLPF 329
Cdd:cd07119 367 DVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIND--YHPYFAEAPW 444
|
330 340
....*....|....*....|.
gi 1062593943 330 GGVGASGMGAYHGKYSFDTFS 350
Cdd:cd07119 445 GGYKQSGIGRELGPTGLEEYQ 465
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
23-350 |
3.59e-46 |
|
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: 165.75 E-value: 3.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 23 DEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETT 101
Cdd:TIGR01804 125 SFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAgLPKGVFNVVQGDGAEVG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 102 ELLKQR--FDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILC 179
Cdd:TIGR01804 205 PLLVNHpdVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFV 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 180 EASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLLK-----GQKIAFGG------EMDEATrYLAPTI 247
Cdd:TIGR01804 285 HKKIKERFLARLVERTERIkLGDPFDEATEMGPLISAAHRDKVLSYIEkgkaeGATLATGGgrpenvGLQNGF-FVEPTV 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 248 LTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDviMHFTVNSL 327
Cdd:TIGR01804 364 FADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINT--YNLYPAEA 441
|
330 340
....*....|....*....|...
gi 1062593943 328 PFGGVGASGMGAYHGKYSFDTFS 350
Cdd:TIGR01804 442 PFGGYKQSGIGRENGKAALAHYT 464
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
25-338 |
5.21e-46 |
|
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: 165.21 E-value: 5.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 25 AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPET-TE 102
Cdd:cd07145 117 AFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPGVINVVTGYGSEVgDE 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 103 LLKQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEA 181
Cdd:cd07145 197 IVTNpKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 182 SLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGEMDEATrYLAPTILTDVDPNS 255
Cdd:cd07145 277 EVYDKFLKLLVEKVKKLkVGDPLDESTDLGPLISPEAVERMENLVndaveKGGKILYGGKRDEGS-FFPPTVLENDTPDM 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 256 KVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMhFTVNSLPFGGVGAS 335
Cdd:cd07145 356 IVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDSTR-FRWDNLPFGGFKKS 434
|
...
gi 1062593943 336 GMG 338
Cdd:cd07145 435 GIG 437
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
25-350 |
6.66e-46 |
|
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: 165.08 E-value: 6.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 25 AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAEL-----LPQyldqDLYAIVNGGIPE 99
Cdd:cd07112 118 ALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELaleagLPA----GVLNVVPGFGHT 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 100 TTELL--KQRFDHILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDC-DLDVACRRIAWGKYMNCGQTCIAPD 175
Cdd:cd07112 194 AGEALglHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 176 YILCEASLQNQIVQKIKETVKDFY-GENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGEMDEATR---YLAPT 246
Cdd:cd07112 274 RLLVHESIKDEFLEKVVAAAREWKpGDPLDPATRMGALVSEAHFDKVLGYIesgkaEGARLVAGGKRVLTETggfFVEPT 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 247 ILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNdvimhfTVN- 325
Cdd:cd07112 354 VFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVN------CFDe 427
|
330 340
....*....|....*....|....*...
gi 1062593943 326 ---SLPFGGVGASGMGAYHGKYSFDTFS 350
Cdd:cd07112 428 gdiTTPFGGFKQSGNGRDKSLHALDKYT 455
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
31-351 |
8.17e-46 |
|
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: 165.21 E-value: 8.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 31 PLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTELLKQ--R 107
Cdd:cd07131 135 PIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAgLPPGVVNVVHGRGEEVGEALVEhpD 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 108 FDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEASLQNQI 187
Cdd:cd07131 215 VDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEF 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 188 VQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQ-----------SLLKGQKIAFGGEMDEATrYLAPTILTDVDPNS 255
Cdd:cd07131 295 LKRFVERAKRLrVGDGLDEETDMGPLINEAQLEKVLnyneigkeegaTLLLGGERLTGGGYEKGY-FVEPTVFTDVTPDM 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 256 KVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFTVNsLPFGGVGAS 335
Cdd:cd07131 374 RIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAEVH-LPFGGVKKS 452
|
330
....*....|....*..
gi 1062593943 336 GMGAYHGKYS-FDTFSH 351
Cdd:cd07131 453 GNGHREAGTTaLDAFTE 469
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
25-350 |
8.25e-46 |
|
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: 165.01 E-value: 8.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 25 AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTEL 103
Cdd:cd07143 138 TYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGYGRTCGNA 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 104 LKQ--RFDHILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCE 180
Cdd:cd07143 218 ISShmDIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQ 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 181 ASLQNQIVQKIKETVK-----DFYGENIKASP-----DYERIIN-LRHFKRlqsllKGQKIAFGGEMDEATRY-LAPTIL 248
Cdd:cd07143 298 EGIYDKFVKRFKEKAKklkvgDPFAEDTFQGPqvsqiQYERIMSyIESGKA-----EGATVETGGKRHGNEGYfIEPTIF 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 249 TDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDV-IMHFTVnsl 327
Cdd:cd07143 373 TDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYnLLHHQV--- 449
|
330 340
....*....|....*....|...
gi 1062593943 328 PFGGVGASGMGAYHGKYSFDTFS 350
Cdd:cd07143 450 PFGGYKQSGIGRELGEYALENYT 472
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
21-349 |
3.90e-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: 163.13 E-value: 3.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 21 MMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIpE 99
Cdd:cd07139 127 GGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAgLPPGVVNVVPADR-E 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 100 TTELLKQR--FDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYI 177
Cdd:cd07139 206 VGEYLVRHpgVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRI 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 178 LCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGEM-DEATR--YLAPTIL 248
Cdd:cd07139 286 LVPRSRYDEVVEALAAAVAALkVGDPLDPATQIGPLASARQRERVEGYIakgraEGARLVTGGGRpAGLDRgwFVEPTLF 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 249 TDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFS----RNNKLIKRVidetSSGGVTGNDVIMHFtv 324
Cdd:cd07139 366 ADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTadveRGLAVARRI----RTGTVGVNGFRLDF-- 439
|
330 340
....*....|....*....|....*
gi 1062593943 325 nSLPFGGVGASGMGAYHGKYSFDTF 349
Cdd:cd07139 440 -GAPFGGFKQSGIGREGGPEGLDAY 463
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
26-311 |
1.03e-44 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 160.67 E-value: 1.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 26 YVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTELL 104
Cdd:PRK10090 66 LLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQEL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 105 --KQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEAS 182
Cdd:PRK10090 146 agNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 183 LQNQIVQKIKETVKDF-YGENIKAS-PDYERIINLRHFKRLQSLL-----KGQKIAFGGEMDEATRYL-APTILTDVDPN 254
Cdd:PRK10090 226 IYDQFVNRLGEAMQAVqFGNPAERNdIAMGPLINAAALERVEQKVaraveEGARVALGGKAVEGKGYYyPPTLLLDVRQE 305
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1062593943 255 SKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSG 311
Cdd:PRK10090 306 MSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFG 362
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
18-343 |
1.12e-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: 161.32 E-value: 1.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 18 LLTMMDEAYVqpePLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGG 96
Cdd:cd07101 108 VLTRTTVNRR---PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAgLPRDLWQVVTGP 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 97 IPETTELLKQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDY 176
Cdd:cd07101 185 GSEVGGAIVDNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIER 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 177 ILCEASLQNQIVQKIKETVkdfygENIKASPDYE------RIINLRHFKRLQSLL-----KGQKIAFGGEM--DEATRYL 243
Cdd:cd07101 265 IYVHESVYDEFVRRFVART-----RALRLGAALDygpdmgSLISQAQLDRVTAHVddavaKGATVLAGGRArpDLGPYFY 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 244 APTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDvIMHFT 323
Cdd:cd07101 340 EPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNE-GYAAA 418
|
330 340
....*....|....*....|..
gi 1062593943 324 VNSL--PFGGVGASGMGAYHGK 343
Cdd:cd07101 419 WASIdaPMGGMKDSGLGRRHGA 440
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
20-349 |
1.48e-44 |
|
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: 160.70 E-value: 1.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 20 TMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIP 98
Cdd:cd07100 85 TDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAgFPEGVFQNLLIDSD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 99 ETTELLK-QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYI 177
Cdd:cd07100 165 QVEAIIAdPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRF 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 178 LCEASLQNQIVQKIKETVK-----DFYGENIK----ASPDyeriinLR---HFKRLQSLLKGQKIAFGGE-MDEATRYLA 244
Cdd:cd07100 245 IVHEDVYDEFLEKFVEAMAalkvgDPMDEDTDlgplARKD------LRdelHEQVEEAVAAGATLLLGGKrPDGPGAFYP 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 245 PTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVimhftV 324
Cdd:cd07100 319 PTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGM-----V 393
|
330 340
....*....|....*....|....*...
gi 1062593943 325 NS---LPFGGVGASGMGAYHGKYSFDTF 349
Cdd:cd07100 394 KSdprLPFGGVKRSGYGRELGRFGIREF 421
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
25-350 |
1.67e-44 |
|
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: 160.99 E-value: 1.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 25 AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTEL 103
Cdd:cd07146 114 IFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAgLPPDMLSVVTGEPGEIGDE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 104 LKQ--RFDHILYTGNTAVGKIVMEAAA-KHLTpvtLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCE 180
Cdd:cd07146 194 LIThpDVDLVTFTGGVAVGKAIAATAGyKRQL---LELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVH 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 181 ASLQNQIVQKIKETVKDF-YGENIKASPDYERIIN---LRHFKR--LQSLLKGQKIAFGGEMDEAtrYLAPTILTDVDPN 254
Cdd:cd07146 271 ESVADEFVDLLVEKSAALvVGDPMDPATDMGTVIDeeaAIQIENrvEEAIAQGARVLLGNQRQGA--LYAPTVLDHVPPD 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 255 SKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDViMHFTVNSLPFGGVGA 334
Cdd:cd07146 349 AELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEV-PGFRSELSPFGGVKD 427
|
330
....*....|....*..
gi 1062593943 335 SGMGAYHG-KYSFDTFS 350
Cdd:cd07146 428 SGLGGKEGvREAMKEMT 444
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
9-338 |
2.99e-44 |
|
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: 160.70 E-value: 2.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 9 ASARPAKKNLLTMMDE---AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYL 85
Cdd:cd07117 111 AGVIRAEEGSANMIDEdtlSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDVL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 86 DQDLYAIVNGGIPETTELLKQR--FDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGK 163
Cdd:cd07117 191 PKGVVNIVTGKGSKSGEYLLNHpgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGI 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 164 YMNCGQTCIAPDYILCEASLQNQIVQKIKETVkdfygENIKA----SPDYE--RIINLRHFKRLQSLLK-----GQKIAF 232
Cdd:cd07117 271 LFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKF-----ENVKVgnplDPDTQmgAQVNKDQLDKILSYVDiakeeGAKILT 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 233 GGEM-----DEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDE 307
Cdd:cd07117 346 GGHRltengLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARA 425
|
330 340 350
....*....|....*....|....*....|....*
gi 1062593943 308 TSSGGVTGNdvimhfTVNSLP----FGGVGASGMG 338
Cdd:cd07117 426 VETGRVWVN------TYNQIPagapFGGYKKSGIG 454
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
25-338 |
1.87e-43 |
|
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: 157.98 E-value: 1.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 25 AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELL-PQYLDQDLYAIVNGGIPETTEL 103
Cdd:cd07094 117 AWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILvEAGVPEGVLQVVTGEREVLGDA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 104 L--KQRFDHILYTGNTAVGKIVMEAAAKhlTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEA 181
Cdd:cd07094 197 FaaDERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 182 SLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGEMDEATRYlaPTILTDVDPNS 255
Cdd:cd07094 275 ELYDEFIEAFVAAVKKLkVGDPLDEDTDVGPLISEEAAERVERWVeeaveAGARLLCGGERDGALFK--PTVLEDVPRDT 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 256 KVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRN-NKLIKrVIDETSSGGVTGNDViMHFTVNSLPFGGVGA 334
Cdd:cd07094 353 KLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDlNVAFK-AAEKLEVGGVMVNDS-SAFRTDWMPFGGVKE 430
|
....
gi 1062593943 335 SGMG 338
Cdd:cd07094 431 SGVG 434
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
25-349 |
1.92e-42 |
|
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: 155.73 E-value: 1.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 25 AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTEL 103
Cdd:cd07142 135 VYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAgLPDGVLNIVTGFGPTAGAA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 104 LKQRF--DHILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCE 180
Cdd:cd07142 215 IASHMdvDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVH 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 181 ASLQNQIVQKIKE-----TVKDFYGENIKASPDyeriINLRHFKRLQSLLK-----GQKIAFGGE-MDEATRYLAPTILT 249
Cdd:cd07142 295 ESIYDEFVEKAKAralkrVVGDPFRKGVEQGPQ----VDKEQFEKILSYIEhgkeeGATLITGGDrIGSKGYYIQPTIFS 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 250 DVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGN--DVimhFTVnSL 327
Cdd:cd07142 371 DVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcyDV---FDA-SI 446
|
330 340
....*....|....*....|..
gi 1062593943 328 PFGGVGASGMGAYHGKYSFDTF 349
Cdd:cd07142 447 PFGGYKMSGIGREKGIYALNNY 468
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
24-339 |
2.68e-42 |
|
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: 155.48 E-value: 2.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 24 EAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQyldqdlyaivnGGIPETT-- 101
Cdd:cd07097 128 EVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEE-----------AGLPAGVfn 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 102 -----------ELLK-QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQ 169
Cdd:cd07097 197 lvmgsgsevgqALVEhPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQ 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 170 TCIAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGE-MDEATR- 241
Cdd:cd07097 277 RCTASSRLIVTEGIHDRFVEALVERTKALkVGDALDEGVDIGPVVSERQLEKDLRYIeiarsEGAKLVYGGErLKRPDEg 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 242 -YLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGN--DV 318
Cdd:cd07097 357 yYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlpTA 436
|
330 340
....*....|....*....|.
gi 1062593943 319 IMHFTVnslPFGGVGASGMGA 339
Cdd:cd07097 437 GVDYHV---PFGGRKGSSYGP 454
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
31-338 |
5.18e-42 |
|
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: 154.33 E-value: 5.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 31 PLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELL-PQYLDQDLYAIVNGGIPETTELLK-QRF 108
Cdd:cd07147 123 PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLaETGLPKGAFSVLPCSRDDADLLVTdERI 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 109 DHILYTGNTAVG-KIVMEAAAKHltpVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEASLQNQI 187
Cdd:cd07147 203 KLLSFTGSPAVGwDLKARAGKKK---VVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEF 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 188 VQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLLK-----GQKIAFGGEMDEATryLAPTILTDVDPNSKVMQEE 261
Cdd:cd07147 280 KSRLVARVKALkTGDPKDDATDVGPMISESEAERVEGWVNeavdaGAKLLTGGKRDGAL--LEPTILEDVPPDMEVNCEE 357
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1062593943 262 IFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDViMHFTVNSLPFGGVGASGMG 338
Cdd:cd07147 358 VFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINDV-PTFRVDHMPYGGVKDSGIG 433
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
22-353 |
1.52e-41 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 153.73 E-value: 1.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 22 MDE--AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAE------LLPQYLDqdlyaIV 93
Cdd:PLN02467 140 METfkGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADicrevgLPPGVLN-----VV 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 94 NGGIPETTELLKQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTC 171
Cdd:PLN02467 215 TGLGTEAGAPLAShpGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQIC 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 172 IAPDYILCEASLQNQIVQKIKETVKdfygeNIKASPDYER------IINLRHFKRLQSLL-----KGQKIAFGGEMDEAT 240
Cdd:PLN02467 295 SATSRLLVHERIASEFLEKLVKWAK-----NIKISDPLEEgcrlgpVVSEGQYEKVLKFIstaksEGATILCGGKRPEHL 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 241 R---YLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGND 317
Cdd:PLN02467 370 KkgfFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINC 449
|
330 340 350
....*....|....*....|....*....|....*.
gi 1062593943 318 VIMHFTvnSLPFGGVGASGMGAYHGKYSFDTFSHQR 353
Cdd:PLN02467 450 SQPCFC--QAPWGGIKRSGFGRELGEWGLENYLSVK 483
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
25-338 |
1.53e-41 |
|
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: 153.37 E-value: 1.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 25 AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGgipeTTEL 103
Cdd:cd07113 136 AFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAgIPDGVLNVVNG----KGAV 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 104 LKQRFDH-----ILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYIL 178
Cdd:cd07113 212 GAQLISHpdvakVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 179 CEASLQNQIVQKIKETVKDFY-GENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGE-MDEATRYLAPTILTDV 251
Cdd:cd07113 292 VHRSKFDELVTKLKQALSSFQvGSPMDESVMFGPLANQPHFDKVCSYLddaraEGDEIVRGGEaLAGEGYFVQPTLVLAR 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 252 DPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNdviMHFTVN-SLPFG 330
Cdd:cd07113 372 SADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN---MHTFLDpAVPFG 448
|
....*...
gi 1062593943 331 GVGASGMG 338
Cdd:cd07113 449 GMKQSGIG 456
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
26-347 |
4.18e-41 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 151.99 E-value: 4.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 26 YVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYAIVNGGIPETTELL- 104
Cdd:PRK13473 133 MIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDALv 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 105 -KQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEASL 183
Cdd:PRK13473 213 gHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGI 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 184 QNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSL------LKGQKIAFGGEM-DEATRYLAPTILTDVDPNS 255
Cdd:PRK13473 293 YDDLVAKLAAAVATLkVGDPDDEDTELGPLISAAHRDRVAGFverakaLGHIRVVTGGEApDGKGYYYEPTLLAGARQDD 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 256 KVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMhfTVNSLPFGGVGAS 335
Cdd:PRK13473 373 EIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM--LVSEMPHGGQKQS 450
|
330
....*....|....*.
gi 1062593943 336 GmgayHGK----YSFD 347
Cdd:PRK13473 451 G----YGKdmslYGLE 462
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
31-353 |
1.18e-40 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 151.95 E-value: 1.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 31 PLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTELLKQRFD 109
Cdd:PRK09407 154 PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAgLPRDLWQVVTGPGPVVGTALVDNAD 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 110 HILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEASLQNQIVQ 189
Cdd:PRK09407 234 YLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVR 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 190 KIKETVKDFygeNIKASPDYE----RIINLRHFKRLQS-----LLKGQKIAFGGEM--DEATRYLAPTILTDVDPNSKVM 258
Cdd:PRK09407 314 AFVAAVRAM---RLGAGYDYSadmgSLISEAQLETVSAhvddaVAKGATVLAGGKArpDLGPLFYEPTVLTGVTPDMELA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 259 QEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMH-FTVNSLPFGGVGASGM 337
Cdd:PRK09407 391 REETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAaWGSVDAPMGGMKDSGL 470
|
330 340
....*....|....*....|..
gi 1062593943 338 GAYHG-----KYS-FDTFSHQR 353
Cdd:PRK09407 471 GRRHGaegllKYTeSQTIATQR 492
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
30-342 |
4.65e-40 |
|
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: 149.06 E-value: 4.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 30 EPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYAIVNGGIPETTELLKQRFD 109
Cdd:cd07107 115 EPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREVLPPGVFNILPGDGATAGAALVRHPD 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 110 --HILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGkyMN---CGQTCIAPDYILCEASLQ 184
Cdd:cd07107 195 vkRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAAVAG--MNftwCGQSCGSTSRLFVHESIY 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 185 NQIVQKIKETVKDFY-GENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGG-----EMDEATRYLAPTILTDVDP 253
Cdd:cd07107 273 DEVLARVVERVAAIKvGDPTDPATTMGPLVSRQQYDRVMHYIdsakrEGARLVTGGgrpegPALEGGFYVEPTVFADVTP 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 254 NSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFTvnSLPFGGVG 333
Cdd:cd07107 353 GMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVWINGSSRHFL--GAPFGGVK 430
|
....*....
gi 1062593943 334 ASGMGAYHG 342
Cdd:cd07107 431 NSGIGREEC 439
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
11-338 |
1.42e-39 |
|
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: 148.03 E-value: 1.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 11 ARPaKKNLltmmdeAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELlpqyldqdly 90
Cdd:cd07140 134 ARP-NRNL------TLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAEL---------- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 91 aIVNGGIPE--------TTELLKQRF-DH-----ILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDCDLDVA 155
Cdd:cd07140 197 -TVKAGFPKgvinilpgSGSLVGQRLsDHpdvrkLGFTGSTPIGKHIMKSCAVsNLKKVSLELGGKSPLIIFADCDMDKA 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 156 CRRIAWGKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRL-----QSLLKGQK 229
Cdd:cd07140 276 VRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMkIGDPLDRSTDHGPQNHKAHLDKLveyceRGVKEGAT 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 230 IAFGG-EMDEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKN--VDEAINFINDREKPLALYVFSRNNKLIKRVID 306
Cdd:cd07140 356 LVYGGkQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSD 435
|
330 340 350
....*....|....*....|....*....|..
gi 1062593943 307 ETSSGGVTGNdvIMHFTVNSLPFGGVGASGMG 338
Cdd:cd07140 436 KLEAGTVFVN--TYNKTDVAAPFGGFKQSGFG 465
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
25-350 |
4.80e-39 |
|
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: 146.72 E-value: 4.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 25 AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAEL-------------LPQYLDQDLYA 91
Cdd:cd07141 139 TYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLikeagfppgvvnvVPGYGPTAGAA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 92 IVNggipettellKQRFDHILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQT 170
Cdd:cd07141 219 ISS----------HPDIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQC 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 171 CIAPDYILCEASLQNQIVQKI-----KETVKDFYGENIKASPDyeriINLRHFKRLQSLLK-----GQKIAFGGE-MDEA 239
Cdd:cd07141 289 CCAGSRTFVQESIYDEFVKRSverakKRVVGNPFDPKTEQGPQ----IDEEQFKKILELIEsgkkeGAKLECGGKrHGDK 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 240 TRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNnklIKRVIdeTSSGGVTGNDVI 319
Cdd:cd07141 365 GYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKD---IDKAI--TFSNALRAGTVW 439
|
330 340 350
....*....|....*....|....*....|....*
gi 1062593943 320 M----HFTVNSlPFGGVGASGMGAYHGKYSFDTFS 350
Cdd:cd07141 440 VncynVVSPQA-PFGGYKMSGNGRELGEYGLQEYT 473
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
24-350 |
9.15e-39 |
|
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: 145.79 E-value: 9.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 24 EAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTE 102
Cdd:cd07082 134 IAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAgFPKGVVNVVTGRGREIGD 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 103 LL--KQRFDHILYTGNTAVGKIVMEAAAKhlTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCE 180
Cdd:cd07082 214 PLvtHGRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVH 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 181 ASLQNQIVQKIKE-----TVKDFYGENI-------KASPDYeriinlrhfkrLQSLL-----KGQKIAFGGEMDEATrYL 243
Cdd:cd07082 292 ESVADELVELLKEevaklKVGMPWDNGVditplidPKSADF-----------VEGLIddavaKGATVLNGGGREGGN-LI 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 244 APTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHfT 323
Cdd:cd07082 360 YPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQR-G 438
|
330 340
....*....|....*....|....*..
gi 1062593943 324 VNSLPFGGVGASGMGAYHGKYSFDTFS 350
Cdd:cd07082 439 PDHFPFLGRKDSGIGTQGIGDALRSMT 465
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
8-338 |
1.37e-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: 145.40 E-value: 1.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 8 LASARPAKKnlltMMDeayvQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSE----LSENTAKILAELLPQ 83
Cdd:cd07086 118 IPSERPGHR----LME----QWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSEttplTAIAVTKILAEVLEK 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 84 Y-LDQDLYAIVNGGiPETTELLK--QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIA 160
Cdd:cd07086 190 NgLPPGVVNLVTGG-GDGGELLVhdPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 161 WGKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLLK-----GQKIAFGG 234
Cdd:cd07086 269 FAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVrIGDPLDEGTLVGPLINQAAVEKYLNAIEiaksqGGTVLTGG 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 235 EM---DEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSS- 310
Cdd:cd07086 349 KRidgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKGSd 428
|
330 340 350
....*....|....*....|....*....|....*
gi 1062593943 311 -------GGVTGNDVimhftvnSLPFGGVGASGMG 338
Cdd:cd07086 429 cgivnvnIPTSGAEI-------GGAFGGEKETGGG 456
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
30-339 |
1.62e-38 |
|
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: 145.83 E-value: 1.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 30 EPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLpqyldqdlyaiVNGGIP---------ET 100
Cdd:cd07124 165 RPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEIL-----------EEAGLPpgvvnflpgPG 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 101 TELLKQRFDH-----ILYTGNTAVGKIVMEAAAK------HLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQ 169
Cdd:cd07124 234 EEVGDYLVEHpdvrfIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQ 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 170 TCIAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLL----KGQKIAFGGE-MDEATR-- 241
Cdd:cd07124 314 KCSACSRVIVHESVYDEFLERLVERTKALkVGDPEDPEVYMGPVIDKGARDRIRRYIeigkSEGRLLLGGEvLELAAEgy 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 242 YLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSG------GVTG 315
Cdd:cd07124 394 FVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGnlyanrKITG 473
|
330 340
....*....|....*....|....
gi 1062593943 316 NDVIMHftvnslPFGGVGASGMGA 339
Cdd:cd07124 474 ALVGRQ------PFGGFKMSGTGS 491
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
24-351 |
3.87e-38 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 144.58 E-value: 3.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 24 EAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTE 102
Cdd:PLN02766 151 QGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAgVPDGVINVVTGFGPTAGA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 103 LLKQRFD--HILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILC 179
Cdd:PLN02766 231 AIASHMDvdKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 180 EASLQNQIVQKIKETVKDF-----YGENIKASP-----DYERIIN-LRHFKRL-QSLLKGQKIAFggemdEATRYLAPTI 247
Cdd:PLN02766 311 QEGIYDEFVKKLVEKAKDWvvgdpFDPRARQGPqvdkqQFEKILSyIEHGKREgATLLTGGKPCG-----DKGYYIEPTI 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 248 LTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNdviMHFTV-NS 326
Cdd:PLN02766 386 FTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN---CYFAFdPD 462
|
330 340
....*....|....*....|....*
gi 1062593943 327 LPFGGVGASGMGAYHGKYSFDTFSH 351
Cdd:PLN02766 463 CPFGGYKMSGFGRDQGMDALDKYLQ 487
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
30-336 |
1.89e-37 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 142.77 E-value: 1.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 30 EPLGVVLIIGAWNYPFVL----TMQPLVGAIAAGNaaivKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTELL 104
Cdd:PRK03137 170 IPLGVGVVISPWNFPFAImagmTLAAIVAGNTVLL----KPASDTPVIAAKFVEVLEEAgLPAGVVNFVPGSGSEVGDYL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 105 ----KQRFdhILYTGNTAVGKIVMEAAAK------HLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAP 174
Cdd:PRK03137 246 vdhpKTRF--ITFTGSREVGLRIYERAAKvqpgqiWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSAC 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 175 DYILCEASLQNQIVQKIKETVKDFYGENIKASPDYERIINLRHFKR-LQSLLKGQ---KIAFGGEMDEATRY-LAPTILT 249
Cdd:PRK03137 324 SRAIVHEDVYDEVLEKVVELTKELTVGNPEDNAYMGPVINQASFDKiMSYIEIGKeegRLVLGGEGDDSKGYfIQPTIFA 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 250 DVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSG------GVTGNDVIMHft 323
Cdd:PRK03137 404 DVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGnlyfnrGCTGAIVGYH-- 481
|
330
....*....|...
gi 1062593943 324 vnslPFGGVGASG 336
Cdd:PRK03137 482 ----PFGGFNMSG 490
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
27-349 |
2.16e-37 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 141.97 E-value: 2.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 27 VQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPET-TELL 104
Cdd:PRK11241 142 VIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAgIPAGVFNVVTGSAGAVgGELT 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 105 KQRFDHIL-YTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEASL 183
Cdd:PRK11241 222 SNPLVRKLsFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGV 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 184 QNQIVQKIKETVKDFY-GENIKASPDYERIINLRHFKRLQ-----SLLKGQKIAFGGEMDE-ATRYLAPTILTDVDPNSK 256
Cdd:PRK11241 302 YDRFAEKLQQAVSKLHiGDGLEKGVTIGPLIDEKAVAKVEehiadALEKGARVVCGGKAHElGGNFFQPTILVDVPANAK 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 257 VMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFTVnsLPFGGVGASG 336
Cdd:PRK11241 382 VAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEV--APFGGIKASG 459
|
330
....*....|...
gi 1062593943 337 MGAYHGKYSFDTF 349
Cdd:PRK11241 460 LGREGSKYGIEDY 472
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
30-350 |
4.36e-37 |
|
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: 140.94 E-value: 4.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 30 EPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQ--YLDQDLYAIVNGGIPETTELL--K 105
Cdd:cd07120 116 EPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEipSLPAGVVNLFTESGSEGAAHLvaS 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 106 QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEASLQN 185
Cdd:cd07120 196 PDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIAD 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 186 QIVQKIKEtvkdfYGENIKASPDYER------IINLRHFKRLQSLLK------GQKIAFGGEMDEATR---YLAPTILTD 250
Cdd:cd07120 276 EVRDRLAA-----RLAAVKVGPGLDPasdmgpLIDRANVDRVDRMVEraiaagAEVVLRGGPVTEGLAkgaFLRPTLLEV 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 251 VDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFtvNSLPFG 330
Cdd:cd07120 351 DDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWINDWNKLF--AEAEEG 428
|
330 340
....*....|....*....|
gi 1062593943 331 GVGASGMGAYHGKYSFDTFS 350
Cdd:cd07120 429 GYRQSGLGRLHGVAALEDFI 448
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
25-350 |
3.81e-35 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 136.18 E-value: 3.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 25 AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTEL 103
Cdd:PRK09847 151 AMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGFGHEAGQA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 104 LKQR--FDHILYTGNTAVGKIVM-EAAAKHLTPVTLELGGKSPCYIDRDC-DLDVACRRIAWGKYMNCGQTCIAPDYILC 179
Cdd:PRK09847 231 LSRHndIDAIAFTGSTRTGKQLLkDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLL 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 180 EASLQNQIVQKIKETVKDFY-GENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGEMDEATrYLAPTILTDVDP 253
Cdd:PRK09847 311 EESIADEFLALLKQQAQNWQpGHPLDPATTMGTLIDCAHADSVHSFIregesKGQLLLDGRNAGLAA-AIGPTIFVDVDP 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 254 NSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGV---TGNDVIMhftvnSLPFG 330
Cdd:PRK09847 390 NASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVfvnNYNDGDM-----TVPFG 464
|
330 340
....*....|....*....|
gi 1062593943 331 GVGASGMGAYHGKYSFDTFS 350
Cdd:PRK09847 465 GYKQSGNGRDKSLHALEKFT 484
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
30-349 |
1.51e-34 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 134.94 E-value: 1.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 30 EPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTELLKQRF 108
Cdd:PLN02466 194 EPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAgLPPGVLNVVSGFGPTAGAALASHM 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 109 --DHILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEASLQN 185
Cdd:PLN02466 274 dvDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYD 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 186 QIVQK-----IKETVKDFYGENIKASPDyeriINLRHFKRLQSLLK-----GQKIAFGGE-MDEATRYLAPTILTDVDPN 254
Cdd:PLN02466 354 EFVEKakaraLKRVVGDPFKKGVEQGPQ----IDSEQFEKILRYIKsgvesGATLECGGDrFGSKGYYIQPTVFSNVQDD 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 255 SKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGN--DVimhFTVnSLPFGGV 332
Cdd:PLN02466 430 MLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfDV---FDA-AIPFGGY 505
|
330
....*....|....*..
gi 1062593943 333 GASGMGAYHGKYSFDTF 349
Cdd:PLN02466 506 KMSGIGREKGIYSLNNY 522
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
22-343 |
4.92e-32 |
|
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: 127.13 E-value: 4.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 22 MDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPET 100
Cdd:cd07111 138 LDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAgLPPGVLNIVTGNGSFG 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 101 TELLKQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILC 179
Cdd:cd07111 218 SALANHpGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLV 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 180 EASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLLK------GQKIAFGGEMDEATRYLAPTILTDVD 252
Cdd:cd07111 298 QESVAEELIRKLKERMSHLrVGDPLDKAIDMGAIVDPAQLKRIRELVEegraegADVFQPGADLPSKGPFYPPTLFTNVP 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 253 PNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMhFTVNSlPFGGV 332
Cdd:cd07111 378 PASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNL-FDAAA-GFGGY 455
|
330
....*....|.
gi 1062593943 333 GASGMGAYHGK 343
Cdd:cd07111 456 RESGFGREGGK 466
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
24-349 |
8.76e-31 |
|
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: 123.40 E-value: 8.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 24 EAYVQPEPLGVVLIIGAWNYP-----------------FVLtmqplvgaiaagnaaivKPSELSENTAKILAELLPQY-L 85
Cdd:cd07085 129 DTYSYRQPLGVVAGITPFNFPamiplwmfpmaiacgntFVL-----------------KPSERVPGAAMRLAELLQEAgL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 86 DQDLYAIVNGGIPETTELLkqrfDH-----ILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIA 160
Cdd:cd07085 192 PDGVLNVVHGGKEAVNALL----DHpdikaVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALV 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 161 WGKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLLkGQKIAFGGEM--D 237
Cdd:cd07085 268 GAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLkVGAGDDPGADMGPVISPAAKERIEGLI-ESGVEEGAKLvlD 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 238 ---------EATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDET 308
Cdd:cd07085 347 grgvkvpgyENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREV 426
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1062593943 309 SSGGVTGNDVI-----MHftvnslPFGGVGASGMGAYH--GKYSFDTF 349
Cdd:cd07085 427 DAGMVGINVPIpvplaFF------SFGGWKGSFFGDLHfyGKDGVRFY 468
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
23-338 |
1.01e-30 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 123.45 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 23 DEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNG-GipET 100
Cdd:PRK13252 134 SFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAgLPDGVFNVVQGdG--RV 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 101 TELLKQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYIL 178
Cdd:PRK13252 212 GAWLTEhpDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVF 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 179 CEASLQNQIVQKIKETVK-----DFYGENIKASPdyerIINLRHFKRLQS-----------LLKGQKIAFGGEMDEATrY 242
Cdd:PRK13252 292 VQKSIKAAFEARLLERVEririgDPMDPATNFGP----LVSFAHRDKVLGyiekgkaegarLLCGGERLTEGGFANGA-F 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 243 LAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVtgndvimhf 322
Cdd:PRK13252 367 VAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGIC--------- 437
|
330 340
....*....|....*....|...
gi 1062593943 323 TVNS-------LPFGGVGASGMG 338
Cdd:PRK13252 438 WINTwgespaeMPVGGYKQSGIG 460
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
9-338 |
2.96e-29 |
|
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: 119.09 E-value: 2.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 9 ASARPAKKNLLTMMDE---AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYL 85
Cdd:cd07116 111 AGCIRAQEGSISEIDEntvAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 86 DQDLYAIVNGGIPETTELL--KQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSP-CYIDRDCDLDVA-CRRIAW 161
Cdd:cd07116 191 PPGVVNVVNGFGLEAGKPLasSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPnIFFADVMDADDAfFDKALE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 162 GKYM---NCGQTCIAPDYILCEASLQNQIVQKIKETVKDFygenIKASP-DYERII----NLRHFKRLQSLLK-----GQ 228
Cdd:cd07116 271 GFVMfalNQGEVCTCPSRALIQESIYDRFMERALERVKAI----KQGNPlDTETMIgaqaSLEQLEKILSYIDigkeeGA 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 229 KIAFGGEMDEATR------YLAPTILTdvDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIK 302
Cdd:cd07116 347 EVLTGGERNELGGllgggyYVPTTFKG--GNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAY 424
|
330 340 350
....*....|....*....|....*....|....*.
gi 1062593943 303 RVIDETSSGGVTGNdvIMHFTVNSLPFGGVGASGMG 338
Cdd:cd07116 425 RMGRGIQAGRVWTN--CYHLYPAHAAFGGYKQSGIG 458
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
31-342 |
1.34e-28 |
|
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: 117.68 E-value: 1.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 31 PLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTELL--KQR 107
Cdd:cd07083 154 GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAgFPPGVVQFLPGVGEEVGAYLteHER 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 108 FDHILYTGNTAVGKIVMEAAAKHLT------PVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEA 181
Cdd:cd07083 234 IRGINFTGSLETGKKIYEAAARLAPgqtwfkRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQ 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 182 SLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLLKGQK----IAFGGEMDEATRY-LAPTILTDVDPNS 255
Cdd:cd07083 314 GAYEPVLERLLKRAERLsVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKnegqLVLGGKRLEGEGYfVAPTVVEEVPPKA 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 256 KVMQEEIFGPILPIVSVKNVD--EAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLPFGGVG 333
Cdd:cd07083 394 RIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGVQPFGGFK 473
|
....*....
gi 1062593943 334 ASGMGAYHG 342
Cdd:cd07083 474 LSGTNAKTG 482
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
24-338 |
1.70e-26 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 111.11 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 24 EAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELlpqYLDQDLYAIVNGGIPETTEL 103
Cdd:PRK13968 119 QAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQV---FKDAGIPQGVYGWLNADNDG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 104 LKQ-----RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYIL 178
Cdd:PRK13968 196 VSQmindsRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFI 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 179 CEASLQNQIVQKIKETVKDFygeNIKASPDYERII------NLR---HFKRLQSLLKGQKIAFGGE-MDEATRYLAPTIL 248
Cdd:PRK13968 276 IEEGIASAFTERFVAAAAAL---KMGDPRDEENALgpmarfDLRdelHHQVEATLAEGARLLLGGEkIAGAGNYYAPTVL 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 249 TDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVtgndVIMHFTVNS-- 326
Cdd:PRK13968 353 ANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGV----FINGYCASDar 428
|
330
....*....|..
gi 1062593943 327 LPFGGVGASGMG 338
Cdd:PRK13968 429 VAFGGVKKSGFG 440
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
31-336 |
6.04e-25 |
|
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: 106.20 E-value: 6.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 31 PLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELL-PQYLDQDLYAIVNGGIPETTELLKQ-RF 108
Cdd:cd07095 97 PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWeEAGLPPGVLNLVQGGRETGEALAAHeGI 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 109 DHILYTGNTAVGKIVMEAAAKHltP---VTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTC------IAPDYILC 179
Cdd:cd07095 177 DGLLFTGSAATGLLLHRQFAGR--PgkiLALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCtcarrlIVPDGAVG 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 180 EASLQnQIVQKIKETVKD-------FYGENI--KASPDYERIINLRHFKRLQSLLKGQKiafggeMDEATRYLAPTILtD 250
Cdd:cd07095 255 DAFLE-RLVEAAKRLRIGapdaeppFMGPLIiaAAAARYLLAQQDLLALGGEPLLAMER------LVAGTAFLSPGII-D 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 251 VDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMhFTVNSLPFG 330
Cdd:cd07095 327 VTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRPTT-GASSTAPFG 405
|
....*.
gi 1062593943 331 GVGASG 336
Cdd:cd07095 406 GVGLSG 411
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
24-346 |
8.53e-25 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 105.98 E-value: 8.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 24 EAYVQPEPLGVVLIIGAWNYPFVLTMQplvgaiaagnaaIVKPSELSENTAkIL--AELLPQ---YLdQDLYAivNGGIP 98
Cdd:PRK09406 116 RAYVRYQPLGVVLAVMPWNFPLWQVVR------------FAAPALMAGNVG-LLkhASNVPQtalYL-ADLFR--RAGFP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 99 E---TTELL----------KQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYM 165
Cdd:PRK09406 180 DgcfQTLLVgsgaveailrDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQ 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 166 NCGQTCIAPDYILCEASLQNQIVQKIKE-----TVKDFYGENIKASP--------DYERIINlrhfkrlQSLLKGQKIAF 232
Cdd:PRK09406 260 NNGQSCIAAKRFIVHADVYDAFAEKFVArmaalRVGDPTDPDTDVGPlateqgrdEVEKQVD-------DAVAAGATILC 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 233 GGE-MDEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSG 311
Cdd:PRK09406 333 GGKrPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAG 412
|
330 340 350
....*....|....*....|....*....|....*...
gi 1062593943 312 GVTGNDviMHFTVNSLPFGGVGASGMG---AYHGKYSF 346
Cdd:PRK09406 413 QVFING--MTVSYPELPFGGVKRSGYGrelSAHGIREF 448
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
25-338 |
2.52e-24 |
|
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: 104.81 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 25 AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQyldqdlyaivnGGIPE----- 99
Cdd:cd07148 118 AFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHE-----------AGLPEgwcqa 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 100 ------TTELL--KQRFDHILYTGNTAVGKIVMEAAAKHlTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTC 171
Cdd:cd07148 187 vpcenaVAEKLvtDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVC 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 172 IAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRL-----QSLLKGQKIAFGGEMDEATRYlAP 245
Cdd:cd07148 266 VSVQRVFVPAEIADDFAQRLAAAAEKLvVGDPTDPDTEVGPLIRPREVDRVeewvnEAVAAGARLLCGGKRLSDTTY-AP 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 246 TILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDvimH--FT 323
Cdd:cd07148 345 TVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVND---HtaFR 421
|
330
....*....|....*
gi 1062593943 324 VNSLPFGGVGASGMG 338
Cdd:cd07148 422 VDWMPFAGRRQSGYG 436
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
8-297 |
3.85e-23 |
|
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: 101.13 E-value: 3.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 8 LASARPAKKnlltMMDeayvQPEPLGVVLIIGAWNYP-------FVLTMqplvgaiAAGNAAIVKPSELSENTA----KI 76
Cdd:cd07130 117 IPSERPGHR----MME----QWNPLGVVGVITAFNFPvavwgwnAAIAL-------VCGNVVVWKPSPTTPLTAiavtKI 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 77 LAELLPQY-LDQDLYAIVNGGIPETTELLK-QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDV 154
Cdd:cd07130 182 VARVLEKNgLPGAIASLVCGGADVGEALVKdPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 155 ACRRIAWGKYMNCGQTCIAPDYILceasLQNQIVQKIKETVKDFY-----GENIKASPDYERIINLRHFKRLQSLLK--- 226
Cdd:cd07130 262 AVRAVLFAAVGTAGQRCTTTRRLI----VHESIYDEVLERLKKAYkqvriGDPLDDGTLVGPLHTKAAVDNYLAAIEeak 337
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1062593943 227 --GQKIAFGGE-MDEATRYLAPTILTdVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRN 297
Cdd:cd07130 338 sqGGTVLFGGKvIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTD 410
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
17-341 |
3.03e-20 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 92.64 E-value: 3.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 17 NLLTMMDeAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNG 95
Cdd:TIGR01722 123 QVATRVD-VYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEAgAPDGVLNVVHG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 96 GIPETTELLKQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAP 174
Cdd:TIGR01722 202 DKEAVDRLLEHpDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAI 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 175 DYILCEASLQnQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLLkGQKIAFGGEM-----------DEATRY 242
Cdd:TIGR01722 282 SAAVLVGAAD-EWVPEIRERAEKIrIGPGDDPGAEMGPLITPQAKDRVASLI-AGGAAEGAEVlldgrgykvdgYEEGNW 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 243 LAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVtGNDVIMHF 322
Cdd:TIGR01722 360 VGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQV-GVNVPIPV 438
|
330
....*....|....*....
gi 1062593943 323 TVNSLPFGGVGASGMGAYH 341
Cdd:TIGR01722 439 PLPYFSFTGWKDSFFGDHH 457
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
31-339 |
3.98e-18 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 86.35 E-value: 3.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 31 PLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTELLKQR-- 107
Cdd:PLN00412 158 PLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAgFPKGLISCVTGKGSEIGDFLTMHpg 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 108 FDHILYTGNTAVGKIVMEAAakhLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEASLQNQI 187
Cdd:PLN00412 238 VNCISFTGGDTGIAISKKAG---MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADAL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 188 VQKIKETVKDFYGENIKASPDYERIINLRHFKRLQSLL---KGQKIAFGGEMDEATRYLAPTILTDVDPNSKVMQEEIFG 264
Cdd:PLN00412 315 VEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVmdaKEKGATFCQEWKREGNLIWPLLLDNVRPDMRIAWEEPFG 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 265 PILPIVSVKNVDEAINFINDREKPLALYVFSRN-NKLIkRVIDETSSGGVTGNDVIM----HFtvnslPFGGVGASGMGA 339
Cdd:PLN00412 395 PVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDiNKAI-LISDAMETGTVQINSAPArgpdHF-----PFQGLKDSGIGS 468
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
30-339 |
7.36e-18 |
|
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: 85.71 E-value: 7.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 30 EPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELL-----PQYLdqdLYAIVNGGIPETTELL 104
Cdd:cd07125 166 HGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLheagvPRDV---LQLVPGDGEEIGEALV 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 105 KQ-RFDHILYTGNTAVGKIVMEAAAKH---LTPVTLELGGKSPCYIDRDCDLDVACRRI---AWGkymNCGQTCIAPDyI 177
Cdd:cd07125 243 AHpRIDGVIFTGSTETAKLINRALAERdgpILPLIAETGGKNAMIVDSTALPEQAVKDVvqsAFG---SAGQRCSALR-L 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 178 LCeasLQNQIVQKIKETVKDFY-----GENIKASPDYERIINLRHFKRLQS---LLKGQ-KIAFGGEMDEAT-RYLAPTI 247
Cdd:cd07125 319 LY---LQEEIAERFIEMLKGAMaslkvGDPWDLSTDVGPLIDKPAGKLLRAhteLMRGEaWLIAPAPLDDGNgYFVAPGI 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 248 LTDVdpNSKVMQEEIFGPILPIVSVK--NVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFTVN 325
Cdd:cd07125 396 IEIV--GIFDLTTEVFGPILHVIRFKaeDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVG 473
|
330
....*....|....
gi 1062593943 326 SLPFGGVGASGMGA 339
Cdd:cd07125 474 RQPFGGWGLSGTGP 487
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
31-339 |
9.95e-16 |
|
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: 78.82 E-value: 9.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 31 PLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQ--YLDQDLYAIVNGGIPETTELLKQ-R 107
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYagLLPPEDVTLINGDGKTMQALLLHpN 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 108 FDHILYTGNTAVGKIVmeAAAKHLTPVTLELGGKSPCYIDRDCD-LDVACRRIAWGKYMNCGQTCIAPDYILCEASLQNq 186
Cdd:cd07084 180 PKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMLFVPENWSK- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 187 ivQKIKETVKDFYGENIKASPDYERIINLRHFKRLQSL--LKGQKIAFGGEMDEATRY-------LAPTILTDVDPN--- 254
Cdd:cd07084 257 --TPLVEKLKALLARRKLEDLLLGPVQTFTTLAMIAHMenLLGSVLLFSGKELKNHSIpsiygacVASALFVPIDEIlkt 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 255 SKVMQEEIFGPILPIVSVKNVDEA--INFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFTV--NSLPFG 330
Cdd:cd07084 335 YELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQELIGNLWVAGRTYAILRGRTGVapNQNHGG 414
|
....*....
gi 1062593943 331 GVGASGMGA 339
Cdd:cd07084 415 GPAADPRGA 423
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
24-351 |
8.37e-15 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 76.32 E-value: 8.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 24 EAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAEL-LPQYLDQDLYAIVNGGIPETTE 102
Cdd:PLN02419 242 DTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELaMEAGLPDGVLNIVHGTNDTVNA 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 103 LLK-QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILC-- 179
Cdd:PLN02419 322 ICDdEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFvg 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 180 -EASLQNQIVQKIKeTVKDFYGENIKAS--PDYERIINLRHFKRLQS--------LLKGQKIAFGGEmdEATRYLAPTIL 248
Cdd:PLN02419 402 dAKSWEDKLVERAK-ALKVTCGSEPDADlgPVISKQAKERICRLIQSgvddgaklLLDGRDIVVPGY--EKGNFIGPTIL 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 249 TDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVtGNDVIMHFTVNSLP 328
Cdd:PLN02419 479 SGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQI-GINVPIPVPLPFFS 557
|
330 340
....*....|....*....|....*
gi 1062593943 329 FGGVGASGMG--AYHGKYSFDTFSH 351
Cdd:PLN02419 558 FTGNKASFAGdlNFYGKAGVDFFTQ 582
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
21-355 |
2.78e-14 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 74.49 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 21 MMDEAYvqpEPLGVVLIIGAWNYP-FVLTMQP-LVGAIAAGNAAIVKPSE--LSENTAKILAELLPQY-LDQDLYAIVNG 95
Cdd:PLN02315 147 MMMEVW---NPLGIVGVITAFNFPcAVLGWNAcIALVCGNCVVWKGAPTTplITIAMTKLVAEVLEKNnLPGAIFTSFCG 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 96 GIPETTELLKQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAP 174
Cdd:PLN02315 224 GAEIGEAIAKDtRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTC 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 175 DYILceasLQNQIVQKIKETVKDFYGENIKASP-DYERIINLRH-------FKRLQSLLKGQ--KIAFGGEMDEAT-RYL 243
Cdd:PLN02315 304 RRLL----LHESIYDDVLEQLLTVYKQVKIGDPlEKGTLLGPLHtpeskknFEKGIEIIKSQggKILTGGSAIESEgNFV 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 244 APTILtDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIdetssgGVTGND---VIM 320
Cdd:PLN02315 380 QPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWI------GPLGSDcgiVNV 452
|
330 340 350
....*....|....*....|....*....|....*....
gi 1062593943 321 HFTVNSL----PFGGVGASGMGAYHGKYSFDTFSHQRPC 355
Cdd:PLN02315 453 NIPTNGAeiggAFGGEKATGGGREAGSDSWKQYMRRSTC 491
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
31-336 |
7.67e-14 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 73.07 E-value: 7.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 31 PLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGiPETTELL--KQR 107
Cdd:PRK09457 134 PHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAgLPAGVLNLVQGG-RETGKALaaHPD 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 108 FDHILYTGNTAVGKIVMEAAAKHltP---VTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEASLQ 184
Cdd:PRK09457 213 IDGLLFTGSANTGYLLHRQFAGQ--PekiLALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQ 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 185 NQ-IVQKIKETVKdfygeNIKA-SPDYE------RIINLRHFKRLqslLKGQK--IAFGG----EM---DEATRYLAPTI 247
Cdd:PRK09457 291 GDaFLARLVAVAK-----RLTVgRWDAEpqpfmgAVISEQAAQGL---VAAQAqlLALGGksllEMtqlQAGTGLLTPGI 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 248 LtDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFTvNSL 327
Cdd:PRK09457 363 I-DVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKPLTGAS-SAA 440
|
....*....
gi 1062593943 328 PFGGVGASG 336
Cdd:PRK09457 441 PFGGVGASG 449
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
30-342 |
8.95e-14 |
|
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: 73.02 E-value: 8.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 30 EPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQyldqdlyaivnGGIPETT-ELL---- 104
Cdd:TIGR01238 159 ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQE-----------AGFPAGTiQLLpgrg 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 105 ---------KQRFDHILYTGNTAVGKIVMEAAAKHL---TPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCI 172
Cdd:TIGR01238 228 advgaaltsDPRIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCS 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 173 APDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIIN-------LRHFKRLQSllKGQKIA-FGGEMDEATRY- 242
Cdd:TIGR01238 308 ALRVLCVQEDVADRVLTMIQGAMQELkVGVPHLLTTDVGPVIDaeakqnlLAHIEHMSQ--TQKKIAqLTLDDSRACQHg 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 243 -LAPTILTDVDpNSKVMQEEIFGPILPIVSVK--NVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVI 319
Cdd:TIGR01238 386 tFVAPTLFELD-DIAELSEEVFGPVLHVVRYKarELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQ 464
|
330 340
....*....|....*....|...
gi 1062593943 320 MHFTVNSLPFGGVGASGMGAYHG 342
Cdd:TIGR01238 465 VGAVVGVQPFGGQGLSGTGPKAG 487
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
137-336 |
2.85e-11 |
|
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: 65.30 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 137 ELGGKSPCYIDRDCDLD---VACRRIAWGkYmnCGQTCIAPDYILCEASLQNQIVQKIKETVKDfygenIKASPDYE--- 210
Cdd:cd07123 284 ETGGKNFHLVHPSADVDslvTATVRGAFE-Y--QGQKCSAASRAYVPESLWPEVKERLLEELKE-----IKMGDPDDfsn 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 211 ---RIINLRHFKRLQSLLK------GQKIAFGGEMDEATRY-LAPTILTDVDPNSKVMQEEIFGPILpIVSV---KNVDE 277
Cdd:cd07123 356 fmgAVIDEKAFDRIKGYIDhaksdpEAEIIAGGKCDDSVGYfVEPTVIETTDPKHKLMTEEIFGPVL-TVYVypdSDFEE 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1062593943 278 AINFINDREkPLALY--VFSRNNKLIKRV------------IDETSSGGVTGNDvimhftvnslPFGGVGASG 336
Cdd:cd07123 435 TLELVDTTS-PYALTgaIFAQDRKAIREAtdalrnaagnfyINDKPTGAVVGQQ----------PFGGARASG 496
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
215-338 |
3.21e-08 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 55.98 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 215 LRHFKRLQsllKGQKIAFGGEMDEATR---YLAPTI--LTDVDpnskVMQEEIFGPILPIVSVK--NVDEAINFINDREK 287
Cdd:PRK11904 882 DAHIERMK---REARLLAQLPLPAGTEnghFVAPTAfeIDSIS----QLEREVFGPILHVIRYKasDLDKVIDAINATGY 954
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1062593943 288 PLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLPFGGVGASGMG 338
Cdd:PRK11904 955 GLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTG 1005
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
31-338 |
8.65e-08 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 54.59 E-value: 8.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 31 PLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTA----KILAE---------LLPqyldqdlyaivngGI 97
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAaqavRILLEagvpagvvqLLP-------------GR 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 98 PET--TELLK-QRFDHILYTGNTAVGKIVMEAAAKHL------TPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCG 168
Cdd:PRK11809 835 GETvgAALVAdARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAG 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 169 QTCIAPDyILCeasLQNQIVQKIKETVKDFYGENIKASPDY-----------ERIINL-RHFKRLQSllKGQKIaFGGEM 236
Cdd:PRK11809 915 QRCSALR-VLC---LQDDVADRTLKMLRGAMAECRMGNPDRlstdigpvidaEAKANIeRHIQAMRA--KGRPV-FQAAR 987
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 237 DEATR-----YLAPTI--LTDVDPnskvMQEEIFGPILPIVSVK--NVDEAINFINDREKPLALYVFSRNNKLIKRVIDE 307
Cdd:PRK11809 988 ENSEDwqsgtFVPPTLieLDSFDE----LKREVFGPVLHVVRYNrnQLDELIEQINASGYGLTLGVHTRIDETIAQVTGS 1063
|
330 340 350
....*....|....*....|....*....|.
gi 1062593943 308 TSSGGVTGNDVIMHFTVNSLPFGGVGASGMG 338
Cdd:PRK11809 1064 AHVGNLYVNRNMVGAVVGVQPFGGEGLSGTG 1094
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
215-338 |
1.91e-05 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 47.24 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 215 LRHFKRLQSllKGQKIaFGGEMDEATR---YLAPTI--LTDVDpnskVMQEEIFGPILPIVSVK--NVDEAINFINDREK 287
Cdd:COG4230 878 EAHIERMRA--EGRLV-HQLPLPEECAngtFVAPTLieIDSIS----DLEREVFGPVLHVVRYKadELDKVIDAINATGY 950
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 288 PLALYVFSRNNKLIKRVIDETSsggvTGNdvimhFTVN---------SLPFGGVGASGMG 338
Cdd:COG4230 951 GLTLGVHSRIDETIDRVAARAR----VGN-----VYVNrniigavvgVQPFGGEGLSGTG 1001
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
229-338 |
1.02e-04 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 44.86 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 229 KIAFGGEMDEATrYLAPTILtDVDpNSKVMQEEIFGPILPIVSVK--NVDEAINFINDREKPLALYVFSRNNKLIKRVID 306
Cdd:PRK11905 889 QLPLPAETEKGT-FVAPTLI-EID-SISDLEREVFGPVLHVVRFKadELDRVIDDINATGYGLTFGLHSRIDETIAHVTS 965
|
90 100 110
....*....|....*....|....*....|..
gi 1062593943 307 ETSSGGVTGNDVIMHFTVNSLPFGGVGASGMG 338
Cdd:PRK11905 966 RIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTG 997
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
97-279 |
1.30e-04 |
|
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: 44.02 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 97 IPETTELLKQR-FDHILYTGNTAVGKivmeAAAKHLTPVtleLG---GKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCi 172
Cdd:cd07122 167 IELTQELMKHPdVDLILATGGPGMVK----AAYSSGKPA---IGvgpGNVPAYIDETADIKRAVKDIILSKTFDNGTIC- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 173 apdyilceASLQNQIVQK-IKETVKdfygENIKASPDYerIINLRHFKRLQSLL--------------KGQKIA--FGGE 235
Cdd:cd07122 239 --------ASEQSVIVDDeIYDEVR----AELKRRGAY--FLNEEEKEKLEKALfddggtlnpdivgkSAQKIAelAGIE 304
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1062593943 236 MDEATRYLAPTIlTDVDPNSKVMQEEIFgPILPIVSVKNVDEAI 279
Cdd:cd07122 305 VPEDTKVLVAEE-TGVGPEEPLSREKLS-PVLAFYRAEDFEEAL 346
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
231-359 |
6.90e-04 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 41.81 E-value: 6.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 231 AFGGEMDEATRylapTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINfindrekpLALYV----------FSRN-NK 299
Cdd:PRK15398 334 AAGINVPKDTR----LLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIA--------LAVKLehgnrhtaimHSRNvDN 401
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1062593943 300 LIK--RVIDETssggvtgndvImhFTVNSLPFGGVGASGMGAY---------HGKYSFDTFSHQRPCLLKG 359
Cdd:PRK15398 402 LNKmaRAIQTS----------I--FVKNGPSYAGLGLGGEGFTtftiatptgEGVTSARTFTRRRRCVLVD 460
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
31-339 |
1.15e-03 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 41.33 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 31 PLGVVLIIGAWNYPFVLTMQPLVGAIAAGnaaiVKPSELSENTAKILAELLPQYL--------DQDLyaiVNGGIPETTE 102
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMG----NKPLLKVDSKVSVVMEQFLRLLhlcgmpatDVDL---IHSDGPTMNK 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 103 LLKQ-RFDHILYTGNTAV---------GKIVMEAAA---KHLTPVTLELGgkspcYIDRDCDLDVacrriawgkYMNCGQ 169
Cdd:cd07126 215 ILLEaNPRMTLFTGSSKVaerlalelhGKVKLEDAGfdwKILGPDVSDVD-----YVAWQCDQDA---------YACSGQ 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 170 TCIAPDYILC-EASLQNQIVQKIKETVKDFYGENIKASP----DYERIINlrHFKRLQSlLKGQKIAFGGEmdEATRYLA 244
Cdd:cd07126 281 KCSAQSILFAhENWVQAGILDKLKALAEQRKLEDLTIGPvltwTTERILD--HVDKLLA-IPGAKVLFGGK--PLTNHSI 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 245 PTILTDVDP--------------NSKVMQEEIFGPILPIVSVKNVDEainfindrekPLALYVFSRnnklikrvIDETSS 310
Cdd:cd07126 356 PSIYGAYEPtavfvpleeiaieeNFELVTTEVFGPFQVVTEYKDEQL----------PLVLEALER--------MHAHLT 417
|
330 340 350
....*....|....*....|....*....|....
gi 1062593943 311 GGVTGNDV-----IMHFTVNSLPFGGVGASGMGA 339
Cdd:cd07126 418 AAVVSNDIrflqeVLANTVNGTTYAGIRARTTGA 451
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
247-280 |
2.08e-03 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 40.30 E-value: 2.08e-03
10 20 30
....*....|....*....|....*....|....
gi 1062593943 247 ILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAIN 280
Cdd:cd07121 316 IIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIE 349
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
219-305 |
5.47e-03 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 39.18 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 219 KRLQSLLKGQKIAFGGEMDEATR--------YLAPTILT--DVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKP 288
Cdd:cd07128 345 AAVATLLAEAEVVFGGPDRFEVVgadaekgaFFPPTLLLcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGS 424
|
90
....*....|....*..
gi 1062593943 289 LALYVFSRNNKLIKRVI 305
Cdd:cd07128 425 LVASVVTNDPAFARELV 441
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
12-313 |
6.74e-03 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 38.61 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 12 RPAKKNLLTMMDEAYvQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELS----ENTAKILAELLPQY-LD 86
Cdd:cd07127 175 KPQGKHDPLAMEKTF-TVVPRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAAilplAITVQVAREVLAEAgFD 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 87 QDLYAIV--NGGIPETTEL-LKQRFDHILYTGNTAVGKIvMEAAAKHLTPVTlELGGKSPCYIDRDCDLDVACRRIAWGK 163
Cdd:cd07127 254 PNLVTLAadTPEEPIAQTLaTRPEVRIIDFTGSNAFGDW-LEANARQAQVYT-EKAGVNTVVVDSTDDLKAMLRNLAFSL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 164 YMNCGQTCIAPDYILCEAS-LQN--------QIVQKIKETVKDFYGENIKASPDYERIINLRHFKRLQS-------LLKG 227
Cdd:cd07127 332 SLYSGQMCTTPQNIYVPRDgIQTddgrksfdEVAADLAAAIDGLLADPARAAALLGAIQSPDTLARIAEarqlgevLLAS 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 228 QKIAFGGEMDEATRylAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFIND--REK-PLALYVFSRNNKLIKRV 304
Cdd:cd07127 412 EAVAHPEFPDARVR--TPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELAREsvREHgAMTVGVYSTDPEVVERV 489
|
....*....
gi 1062593943 305 IDETSSGGV 313
Cdd:cd07127 490 QEAALDAGV 498
|
|
| LuxC |
pfam05893 |
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ... |
102-313 |
8.12e-03 |
|
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) proteins. The channelling of fatty acids into the fatty aldehyde substrate for the bacterial bioluminescence reaction is catalyzed by a fatty acid reductase multienzyme complex, which channels fatty acids through the thioesterase (LuxD), synthetase (LuxE) and reductase (LuxC) components.
Pssm-ID: 399113 Cd Length: 401 Bit Score: 38.19 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 102 ELLKQRFDHIL-YTGNTAVgkivmEAAAKHLTPVT--LELGGK-SPCYIDRDCDLDVACRRIA-----WGKymncgQTCI 172
Cdd:pfam05893 164 DLIVANADVVIaWGGEDAI-----NAIRECLKPGKqwIDFGAKiSFAVVDREAALDKAAERAAddicvFDQ-----QACL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062593943 173 APDYILCEASLQNQivqkIKETVKDFYGENIKASPDYER----------IINLRHFKRLQSLLKGQkiaFGGEMDEATRY 242
Cdd:pfam05893 234 SPQTVFVESDDKIT----PDEFAERLAAALAKRARILPKavldideaakISSDRAECKLDYAFAGE---RGVWSDFHQRW 306
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1062593943 243 LapTILTDvdpnskvMQEEIFGPI---LPIVSVKNVDEAINFIN---DREKPLALYVFSRNnklIKRVIDETSSGGV 313
Cdd:pfam05893 307 T--VIWSD-------GQEELNSPLnrtVNVVPVPSLSDVVRYVSenrTYLQTCGLAPYSGR---LPYLDRKLALAGV 371
|
|
| |
