|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
16-444 |
0e+00 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 809.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 16 QQRFQAQREAFMANPMPSADQRIAWLDSLKAALLADQDALVRCISEDFGNRSADETLLAEMLPTVQGIRYARKRLRRWMK 95
Cdd:cd07133 1 QALLERQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFGHRSRHETLLAEILPSIAGIKHARKHLKKWMK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 96 PSRRHVGLAFMPASARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASIFPEELV 175
Cdd:cd07133 81 PSRRHVGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 176 SVVLGEAEIGMAFARLPFDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQT 255
Cdd:cd07133 161 AVVTGGADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 256 CVAPDYVLVPRQRVDDFVDAYRSVVQRFYPQVEGNPDYTSIINARQQQRLQGYLDDARAKGAEVIALTAEATD----RRM 331
Cdd:cd07133 241 CVAPDYVLVPEDKLEEFVAAAKAAVAKMYPTLADNPDYTSIINERHYARLQGLLEDARAKGARVIELNPAGEDfaatRKL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 332 PQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDTLLHVA 411
Cdd:cd07133 321 PPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHVA 400
|
410 420 430
....*....|....*....|....*....|...
gi 2068619660 412 QDDMPFGGIGASGMGHYHGHEGFLTFSKAKGVL 444
Cdd:cd07133 401 QDDLPFGGVGASGMGAYHGKEGFLTFSHAKPVF 433
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
16-445 |
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: 559.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 16 QQRFQAQREAFMANPMPSADQRIAWLDSLKAALLADQDALVRCISEDFGnRSADETLLAEMLPTVQGIRYARKRLRRWMK 95
Cdd:cd07087 1 AELVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLG-KPPAEAYLTEIAVVLGEIDHALKHLKKWMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 96 PSRRHVGLAFMPASARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASIFPEELV 175
Cdd:cd07087 80 PRRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 176 SVVLGEAEIGMAFARLPFDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQT 255
Cdd:cd07087 160 AVVEGGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 256 CVAPDYVLVPRQRVDDFVDAYRSVVQRFY-PQVEGNPDYTSIINARQQQRLQGYLDDAR-AKGAEVialtaEATDRRMPQ 333
Cdd:cd07087 240 CIAPDYVLVHESIKDELIEELKKAIKEFYgEDPKESPDYGRIINERHFDRLASLLDDGKvVIGGQV-----DKEERYIAP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 334 TLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDTLLHVAQD 413
Cdd:cd07087 315 TILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIP 394
|
410 420 430
....*....|....*....|....*....|..
gi 2068619660 414 DMPFGGIGASGMGHYHGHEGFLTFSKAKGVLI 445
Cdd:cd07087 395 NLPFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
16-445 |
0e+00 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 532.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 16 QQRFQAQREAFMANPMPSADQRIAWLDSLKAALLADQDALVRCISEDFGnRSADETLLAEMLPTVQGIRYARKRLRRWMK 95
Cdd:cd07134 1 RRVFAAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFR-KPAAEVDLTEILPVLSEINHAIKHLKKWMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 96 PSRRHVGLAFMPASARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASIFPEELV 175
Cdd:cd07134 80 PKRVRTPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 176 SVVLGEAEIGMAFARLPFDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQT 255
Cdd:cd07134 160 AVFEGDAEVAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 256 CVAPDYVLVPRQRVDDFVDAYRSVVQRFY---PQVEGNPDYTSIINARQQQRLQGYLDDARAKGAEVIA-LTAEATDRRM 331
Cdd:cd07134 240 CIAPDYVFVHESVKDAFVEHLKAEIEKFYgkdAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFgGQFDAAQRYI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 332 PQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDTLLHVA 411
Cdd:cd07134 320 APTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFL 399
|
410 420 430
....*....|....*....|....*....|....
gi 2068619660 412 QDDMPFGGIGASGMGHYHGHEGFLTFSKAKGVLI 445
Cdd:cd07134 400 NPNLPFGGVNNSGIGSYHGVYGFKAFSHERAVLR 433
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
16-467 |
2.93e-180 |
|
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: 512.05 E-value: 2.93e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 16 QQRFQAQREAFMANPMPSADQRIAWLDSLKAALLADQDALVRCISEDFgNRSADETLLAEMLPTVQGIRYARKRLRRWMK 95
Cdd:cd07136 1 ESLVEKQRAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDL-GKSEFEAYMTEIGFVLSEINYAIKHLKKWMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 96 PSRRHVGLAFMPASARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASIFPEELV 175
Cdd:cd07136 80 PKRVKTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 176 SVVLGEAEIGMAFARLPFDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQT 255
Cdd:cd07136 160 AVVEGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 256 CVAPDYVLVPRQRVDDFVDAYRSVVQRFYP-QVEGNPDYTSIINARQQQRLQGYLDDARAkgaeVIALTAEATDRRMPQT 334
Cdd:cd07136 240 CVAPDYVLVHESVKEKFIKELKEEIKKFYGeDPLESPDYGRIINEKHFDRLAGLLDNGKI----VFGGNTDRETLYIEPT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 335 LLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDTLLHVAQDD 414
Cdd:cd07136 316 ILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPY 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2068619660 415 MPFGGIGASGMGHYHGHEGFLTFSKAKGVLiKQ--RLNLArLIYPPYGKALQRLV 467
Cdd:cd07136 396 LPFGGVGNSGMGSYHGKYSFDTFSHKKSIL-KKstWFDLP-LRYPPYKGKKKKLK 448
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
7-471 |
8.17e-156 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 451.41 E-value: 8.17e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 7 PVEQAIAELQQRFQAQREAFMANPMPSADQRIAWLDSLKAALLADQDALVRCISEDFGnRSADETLLAEMLPTVQGIRYA 86
Cdd:PTZ00381 1 QEPDNPEIIPPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLG-RHPFETKMTEVLLTVAEIEHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 87 RKRLRRWMKPSRRHVGLAFMPASARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELL 166
Cdd:PTZ00381 80 LKHLDEYLKPEKVDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 167 ASIFPEELVSVVLGEAEIGMAFARLPFDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAF 246
Cdd:PTZ00381 160 TKYLDPSYVRVIEGGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 247 GKTLNAGQTCVAPDYVLVPRQRVDDFVDAYRSVVQRFY-PQVEGNPDYTSIINARQQQRLQGYLDDarAKGAEVIALTAE 325
Cdd:PTZ00381 240 GKFLNAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEFFgEDPKKSEDYSRIVNEFHTKRLAELIKD--HGGKVVYGGEVD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 326 ATDRRMPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLND 405
Cdd:PTZ00381 318 IENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVIND 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2068619660 406 TLLHVAQDDMPFGGIGASGMGHYHGHEGFLTFSKAKGVLIKQRLN--LARLIYPPYGKALQRLVYKLF 471
Cdd:PTZ00381 398 CVFHLLNPNLPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNKSTGNsfDLSLRYPPYTSFKSWVLSFLL 465
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
3-444 |
7.34e-154 |
|
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: 444.36 E-value: 7.34e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 3 TPFGPVEQAIAELQQRFQAQREAfmanpmpSADQRIAWLDSLKAALLADQDALVRCISEDFGnRSADETLLAEMLPTVQG 82
Cdd:cd07135 2 TPLDEIDSIHSRLRATFRSGKTK-------DLEYRLWQLKQLYWAVKDNEEAIVEALKKDLG-RPPFETLLTEVSGVKND 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 83 IRYARKRLRRWMKPSRRHVG-LAFMPASARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQH 161
Cdd:cd07135 74 ILHMLKNLKKWAKDEKVKDGpLAFMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 162 LKELLASIFPEELVSVVLGEAEIGMAFARLPFDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAA 241
Cdd:cd07135 154 LAELVPKYLDPDAFQVVQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 242 ERIAFGKTLNAGQTCVAPDYVLVPRQRVDDFVDAYRSVVQRFYPQV-EGNPDYTSIINARQQQRLQGYLDdaRAKGAEVI 320
Cdd:cd07135 234 KRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGaNASPDYTRIVNPRHFNRLKSLLD--TTKGKVVI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 321 ALTAEATDRRMPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGG 400
Cdd:cd07135 312 GGEMDEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGG 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2068619660 401 VCLNDTLLHVAQDDMPFGGIGASGMGHYHGHEGFLTFSKAKGVL 444
Cdd:cd07135 392 VVINDTLIHVGVDNAPFGGVGDSGYGAYHGKYGFDTFTHERTVV 435
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
20-459 |
6.63e-139 |
|
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: 406.61 E-value: 6.63e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 20 QAQREAFMANPMPSADQRIAWLDSLKAALLADQDALVRCISEDFgNRSADETLLAEMLPTVQGIRYARKRLRRWMKPSRR 99
Cdd:cd07132 5 RRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDL-RKPKFEAVLSEILLVKNEIKYAISNLPEWMKPEPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 100 HVGLAFMPASARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASIFPEELVSVVL 179
Cdd:cd07132 84 KKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYPVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 180 GEAEIGMAFARLPFDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAP 259
Cdd:cd07132 164 GGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 260 DYVLVPRQRVDDFVDAYRSVVQRFY---PQveGNPDYTSIINARQQQRLQGYLDDAR-AKGAEVialtaEATDRRMPQTL 335
Cdd:cd07132 244 DYVLCTPEVQEKFVEALKKTLKEFYgedPK--ESPDYGRIINDRHFQRLKKLLSGGKvAIGGQT-----DEKERYIAPTV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 336 LLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDTLLHVAQDDM 415
Cdd:cd07132 317 LTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSL 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2068619660 416 PFGGIGASGMGHYHGHEGFLTFSKAKGVLIK----QRLNLARliYPPY 459
Cdd:cd07132 397 PFGGVGNSGMGAYHGKYSFDTFSHKRSCLVKslnmEKLNSLR--YPPY 442
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
16-445 |
1.01e-126 |
|
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: 375.01 E-value: 1.01e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 16 QQRFQAQREAFMANPMPSADQRIAWLDSLKAALLADQDALVRCISEDFGNRSADetLLAEMLPTVQGIRYARKRLRRWMK 95
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEE--ALGEVARAADTFRYYAGLARRLHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 96 PSRRhvgLAFMPASARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASI-FPEEL 174
Cdd:cd07078 79 EVIP---SPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLPPGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 175 VSVVLGEA-EIGMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNA 252
Cdd:cd07078 156 LNVVTGDGdEVGAALASHPrVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 253 GQTCVAPDYVLVPRQRVDDFVDAYRSVVQRFYPqveGNP-----DYTSIINARQQQRLQGYLDDARAKGAEVIALTAEAT 327
Cdd:cd07078 236 GQVCTAASRLLVHESIYDEFVERLVERVKALKV---GNPldpdtDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 328 DRR---MPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLN 404
Cdd:cd07078 313 GGKgyfVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIN 392
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2068619660 405 DTLLHvAQDDMPFGGIGASGMGHYHGHEGFLTFSKAKGVLI 445
Cdd:cd07078 393 DYSVG-AEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
8-444 |
2.20e-117 |
|
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: 351.33 E-value: 2.20e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 8 VEQAIAELqqrfqaqREAFMANPMPSADQRIAWLDSLKAALLADQDALVRCISEDFGNRSAdETLLAEMLPTVQGIRYAR 87
Cdd:cd07137 1 APRLVREL-------RETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSA-ESFRDEVSVLVSSCKLAI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 88 KRLRRWMKPSRRHVGLAFMPASARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQhlkeLLA 167
Cdd:cd07137 73 KELKKWMAPEKVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSA----LLA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 168 SIFPEEL----VSVVLGEAEIGMAFARLPFDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAER 243
Cdd:cd07137 149 KLIPEYLdtkaIKVIEGGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 244 IAFGK-TLNAGQTCVAPDYVLVPRQRVDDFVDAYRSVVQRFYPQvegNP----DYTSIINARQQQRLQGYLDDARAKGAE 318
Cdd:cd07137 229 IAGGKwGCNNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGE---NPkeskDLSRIVNSHHFQRLSRLLDDPSVADKI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 319 VIALTAEATDRRMPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHS 398
Cdd:cd07137 306 VHGGERDEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSS 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2068619660 399 GGVCLNDTLLHVAQDDMPFGGIGASGMGHYHGHEGFLTFSKAKGVL 444
Cdd:cd07137 386 GGVTFNDTVVQYAIDTLPFGGVGESGFGAYHGKFSFDAFSHKKAVL 431
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
8-446 |
2.42e-117 |
|
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: 352.51 E-value: 2.42e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 8 VEQAIAelqqrfqAQREAFMANPMPSADQRIAWLDSLKAALLADQDALVRCISEDFGnRSADETLlAEMLPTVQGIRYAR 87
Cdd:COG1012 45 VDAAVA-------AARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETG-KPLAEAR-GEVDRAADFLRYYA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 88 KRLRRwMKPSRRHVGLAFMpaSARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLA 167
Cdd:COG1012 116 GEARR-LYGETIPSDAPGT--RAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 168 SI-FPEELVSVVLGE-AEIGMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERI 244
Cdd:COG1012 193 EAgLPAGVLNVVTGDgSEVGAALVAHPdVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 245 AFGKTLNAGQTCVAPDYVLVPRQRVDDFVDAYRSVVQRFypQVeGNP-----DYTSIINARQQQRLQGYLDDARAKGAEV 319
Cdd:COG1012 273 VRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKAL--KV-GDPldpgtDMGPLISEAQLERVLAYIEDAVAEGAEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 320 IALTAEATDRR---MPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHS 396
Cdd:COG1012 350 LTGGRRPDGEGgyfVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRL 429
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2068619660 397 HSGGVCLNDTLLHvAQDDMPFGGIGASGMGHYHGHEGFLTFSKAKGVLIK 446
Cdd:COG1012 430 EAGMVWINDGTTG-AVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
1-469 |
2.06e-103 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 317.05 E-value: 2.06e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 1 MVTPFGPVEQAIAELqqrfqaqREAFMANPMPSADQRIAWLDSLKAALLADQDALVRCISEDFGNRSAdETLLAEMLPTV 80
Cdd:PLN02203 1 EEAPGETLEGSVAEL-------RETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRV-EAYRDEVGVLT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 81 QGIRYARKRLRRWMKPSRRHVGLAFMPASARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQ 160
Cdd:PLN02203 73 KSANLALSNLKKWMAPKKAKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 161 HLKELLASIFPEELVSVVLGEAEIGMAFARLPFDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAI---ISADVPL 237
Cdd:PLN02203 153 FLAANIPKYLDSKAVKVIEGGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIvdsLSSSRDT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 238 EHAAERIAFGK-TLNAGQTCVAPDYVLVPRQRVDDFVDAYRSVVQRFYPQVEGNPDYTS-IINARQQQRLQGYLDDARAK 315
Cdd:PLN02203 233 KVAVNRIVGGKwGSCAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMArILNKKHFQRLSNLLKDPRVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 316 GAEVIALTAEATDRRMPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHH 395
Cdd:PLN02203 313 ASIVHGGSIDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068619660 396 SHSGGVCLNDTLLHVAQDDMPFGGIGASGMGHYHGHEGFLTFSKAKGVLIKQRLNLARLIYPPYGK---ALQRLVYK 469
Cdd:PLN02203 393 TSSGSVTFNDAIIQYACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSLLTEFEFRYPPWNDfklGFLRLVYR 469
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
4-445 |
7.66e-103 |
|
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: 314.54 E-value: 7.66e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 4 PFGPV-EQAIAELQQRFQAQREAFMANPMPSADQRIAWLDSLKAALLADQDALVRCISEDFGNRSADetLLAEMLPTVQG 82
Cdd:cd07099 8 VLGEVpVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRAD--AGLEVLLALEA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 83 IRYARKRLRRWMKPSRRHVGLAFMPASARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHL 162
Cdd:cd07099 86 IDWAARNAPRVLAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 163 KELLASI-FPEELVSVVLGEAEIGMAFARLPFDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAA 241
Cdd:cd07099 166 AEAWAAAgPPQGVLQVVTGDGATGAALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 242 ERIAFGKTLNAGQTCVAPDYVLVPRQRVDDFVDAYRSVVQRFYPQVE--GNPDYTSIINARQQQRLQGYLDDARAKGAEV 319
Cdd:cd07099 246 AAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADdiGDADIGPMTTARQLDIVRRHVDDAVAKGAKA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 320 IALTAEATDRRM--PQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSH 397
Cdd:cd07099 326 LTGGARSNGGGPfyEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLE 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2068619660 398 SGGVCLNDTLLHVAQDDMPFGGIGASGMGHYHGHEGFLTFSKAKGVLI 445
Cdd:cd07099 406 AGAVSINDVLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
8-443 |
5.65e-99 |
|
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: 304.84 E-value: 5.65e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 8 VEQAIAelqqrfqAQREAF--MANpMPSAdQRIAWLDSLKAALLADQDALVRCISEDFGnRSADETLlAEMLPTVQGIRY 85
Cdd:pfam00171 31 VDAAIA-------AARAAFpaWRK-TPAA-ERAAILRKAADLLEERKDELAELETLENG-KPLAEAR-GEVDRAIDVLRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 86 ARKRLRR------WMKPSRRhvglafmpasARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTS 159
Cdd:pfam00171 100 YAGLARRldgetlPSDPGRL----------AYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 160 QHLKELLASI-FPEELVSVVLGE-AEIGMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVP 236
Cdd:pfam00171 170 LLLAELFEEAgLPAGVLNVVTGSgAEVGEALVEHPdVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDAD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 237 LEHAAERIAFGKTLNAGQTCVAPDYVLVPRQRVDDFVDAYRSVVQ--RFYPQVEGNPDYTSIINARQQQRLQGYLDDARA 314
Cdd:pfam00171 250 LDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKklKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 315 KGAEVIA--LTAEATDRRMPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHV 392
Cdd:pfam00171 330 EGAKLLTggEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRV 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2068619660 393 LHHSHSGGVCLNDTLLHVAqDDMPFGGIGASGMGHYHGHEGFLTFSKAKGV 443
Cdd:pfam00171 410 ARRLEAGMVWINDYTTGDA-DGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
20-445 |
2.19e-96 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 294.91 E-value: 2.19e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 20 QAQREAFMANPMPSADQRIAWLDSLKAALLADQDALVRCISEDFGNRSadETLLAEMLPTVQGIRYARKRLRRWMKPsrr 99
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPI--EEALGEVARAIDTFRYAAGLADKLGGP--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 100 HVGLAFMPASARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASI-FPEELVSVV 178
Cdd:cd06534 76 ELPSPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVVNVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 179 LGEA-EIGMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTC 256
Cdd:cd06534 156 PGGGdEVGAALLSHPrVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 257 VAPDYVLVPRQRVDDFVDAYrsvvqrfypqvegnpdytsiinarqqqrlqgylddarakgaevialtaeatdrrmpQTLL 336
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKL--------------------------------------------------------VTVL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 337 LNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDTLLHVaQDDMP 416
Cdd:cd06534 260 VDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGV-GPEAP 338
|
410 420
....*....|....*....|....*....
gi 2068619660 417 FGGIGASGMGHYHGHEGFLTFSKAKGVLI 445
Cdd:cd06534 339 FGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
13-444 |
2.25e-92 |
|
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: 288.04 E-value: 2.25e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 13 AELQQRFQAQREAFMANPMPSADQRIAWLDSLKAALLADQDALVRCISEDFGNRSADeTLLAEMLPTVQGIRYARKRLRR 92
Cdd:cd07098 18 EDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVD-ASLGEILVTCEKIRWTLKHGEK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 93 WMKPSRRHVGLAFMPASARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQH----LKELLAS 168
Cdd:cd07098 97 ALRPESRPGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFflsiIRECLAA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 169 I-FPEELVSVVLGEAEIGMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAF 246
Cdd:cd07098 177 CgHDPDLVQLVTCLPETAEALTSHPvIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 247 GKTLNAGQTCVAPDYVLVPRQRVDDFVDAYRSVVQRFY--PQVEGNPDYTSIINARQQQRLQGYLDDARAKGAEVIA--- 321
Cdd:cd07098 257 GTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRqgPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAggk 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 322 ---LTAEATDRRMPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHS 398
Cdd:cd07098 337 rypHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLET 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2068619660 399 GGVCLND-TLLHVAQdDMPFGGIGASGMGHYHGHEGFLTFSKAKGVL 444
Cdd:cd07098 417 GMVAINDfGVNYYVQ-QLPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
83-470 |
4.54e-88 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 277.70 E-value: 4.54e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 83 IRYARKRLRRWMKPSRRHVGLAFMPASARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHL 162
Cdd:PLN02174 79 IKLALKQLKNWMAPEKAKTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 163 KELLASIFPEELVSVVLGEAEIGMAFARLPFDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAE 242
Cdd:PLN02174 159 AKLLEQYLDSSAVRVVEGAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 243 RIAFGK-TLNAGQTCVAPDYVLVPRQRVDDFVDAYRSVVQRFYPQvegNP----DYTSIINARQQQRLQGYLDDARAKGA 317
Cdd:PLN02174 239 RIIAGKwGCNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGK---NPmeskDMSRIVNSTHFDRLSKLLDEKEVSDK 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 318 EVIALTAEATDRRMPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSH 397
Cdd:PLN02174 316 IVYGGEKDRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVS 395
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068619660 398 SGGVCLNDTLLHVAQDDMPFGGIGASGMGHYHGHEGFLTFSKAKGVLIKQRLNLARLIYPPYGKALQRLVYKL 470
Cdd:PLN02174 396 AGGIVVNDIAVHLALHTLPFGGVGESGMGAYHGKFSFDAFSHKKAVLYRSLFGDSAVRYPPYSRGKLRLLKAL 468
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
8-445 |
7.34e-82 |
|
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: 260.97 E-value: 7.34e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 8 VEQAIAelqqrfqAQREAFMANPMP--SADQRIAWLDSLKAALLADQDALVRCISEDFGNRSADETLLAEMLPTVQgIRY 85
Cdd:cd07139 38 VDAAVA-------AARRAFDNGPWPrlSPAERAAVLRRLADALEARADELARLWTAENGMPISWSRRAQGPGPAAL-LRY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 86 ARKRLRRWMKPSRRHvglAFMPASARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKEL 165
Cdd:cd07139 110 YAALARDFPFEERRP---GSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 166 LASI-FPEELVSVVLGEAEIGMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAER 243
Cdd:cd07139 187 AEEAgLPPGVVNVVPADREVGEYLVRHPgVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 244 IAFGKTLNAGQTCVAPDYVLVPRQRVDDFVDAYRSVVQRfypQVEGNP--DYTSI---INARQQQRLQGYLDDARAKGAE 318
Cdd:cd07139 267 LVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAA---LKVGDPldPATQIgplASARQRERVEGYIAKGRAEGAR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 319 VIALTAEATDrrMPQ------TLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHV 392
Cdd:cd07139 344 LVTGGGRPAG--LDRgwfvepTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAV 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2068619660 393 LHHSHSGGVCLNdtllHVAQD-DMPFGGIGASGMGHYHGHEGFLTFSKAKGVLI 445
Cdd:cd07139 422 ARRIRTGTVGVN----GFRLDfGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
112-445 |
3.06e-79 |
|
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: 253.22 E-value: 3.06e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 112 VIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASIFPEELVSVVLGEAEIGMAFARL 191
Cdd:cd07106 110 LRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEVLPPGVLNVVSGGDELGPALTSH 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 192 P-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQRVD 270
Cdd:cd07106 190 PdIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYD 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 271 DFVDAYRSVVQRFY------PQVEGNPdytsIINARQQQRLQGYLDDARAKGAEVIALtAEATDRR---MPQTLLLNVDD 341
Cdd:cd07106 270 EFCEALVALAKAAVvgdgldPGTTLGP----VQNKMQYDKVKELVEDAKAKGAKVLAG-GEPLDGPgyfIPPTIVDDPPE 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 342 SMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDtllHVAQD-DMPFGGI 420
Cdd:cd07106 345 GSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWINT---HGALDpDAPFGGH 421
|
330 340
....*....|....*....|....*
gi 2068619660 421 GASGMGHYHGHEGFLTFSKAKGVLI 445
Cdd:cd07106 422 KQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
8-434 |
9.01e-77 |
|
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: 246.96 E-value: 9.01e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 8 VEQAIAELQQRFQAQREAfmanpmpSADQRIAWLDSLKAALLADQDALVRCISedfgnrsadetllAEM---LPTVQG-I 83
Cdd:cd07103 21 ADAAIDAAAAAFKTWRKT-------TARERAAILRRWADLIRERAEDLARLLT-------------LEQgkpLAEARGeV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 84 RYARKRLRrWMKPSRRHVGLAFMPASA-----RVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQT 158
Cdd:cd07103 81 DYAASFLE-WFAEEARRIYGRTIPSPApgkriLVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 159 SQHLKELLASI-FPEELVSVVLGE-AEIGMAFARLPFDHLL-FTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADV 235
Cdd:cd07103 160 ALALAELAEEAgLPAGVLNVVTGSpAEIGEALCASPRVRKIsFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 236 PLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQRVDDFVDAYRSVVQRFypQVeGNP--DYTSI---INARQQQRLQGYLD 310
Cdd:cd07103 240 DLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKL--KV-GNGldEGTDMgplINERAVEKVEALVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 311 DARAKGAEVIAlTAEATDRR---MPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRR 387
Cdd:cd07103 317 DAVAKGAKVLT-GGKRLGLGgyfYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLA 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2068619660 388 EQQHVLHHSHSGGVCLNDTLLHVAQddMPFGGIGASGMGHYHGHEGF 434
Cdd:cd07103 396 RAWRVAEALEAGMVGINTGLISDAE--APFGGVKESGLGREGGKEGL 440
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
8-441 |
2.17e-76 |
|
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: 246.39 E-value: 2.17e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 8 VEQAIAelqqrfqAQREAFMANPMP-SADQRIAWLDSLKAALLADQDALVRCISEDFGN-RSADETLLAEMLptVQGIRY 85
Cdd:cd07089 21 VDAAIA-------AARRAFDTGDWStDAEERARCLRQLHEALEARKEELRALLVAEVGApVMTARAMQVDGP--IGHLRY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 86 ARKRLRRWMKP-SRRHVGLAFMPASARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKE 164
Cdd:cd07089 92 FADLADSFPWEfDLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 165 LLASI-FPEELVSVVLG-EAEIGMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAA 241
Cdd:cd07089 172 IIAETdLPAGVVNVVTGsDNAVGEALTTDPrVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 242 ERIAFGKTLNAGQTCVAPDYVLVPRQRVDDFVDAyrsvVQRFYPQVE-GNPD-----YTSIINARQQQRLQGYLDDARAK 315
Cdd:cd07089 252 PAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEA----LAAAFEALPvGDPAdpgtvMGPLISAAQRDRVEGYIARGRDE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 316 GAEViaLTAEATDRRMPQ------TLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQ 389
Cdd:cd07089 328 GARL--VTGGGRPAGLDKgfyvepTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRA 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2068619660 390 QHVLHHSHSGGVCLNDTllHVAQDDMPFGGIGASGMGHYHGHEGFLTFSKAK 441
Cdd:cd07089 406 YRVARRIRTGSVGINGG--GGYGPDAPFGGYKQSGLGRENGIEGLEEFLETK 455
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
8-437 |
1.63e-75 |
|
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: 244.33 E-value: 1.63e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 8 VEQAIAelqqrfqAQREAFMANPMPSADQRIAWLDSLKAALLADQDALVRCISEDFGnrsADETLLAEM---LPtVQGIR 84
Cdd:cd07138 38 VDRAVA-------AARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMG---APITLARAAqvgLG-IGHLR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 85 YARKRLRRWmkPSRRHVGlafmpaSARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKE 164
Cdd:cd07138 107 AAADALKDF--EFEERRG------NSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 165 LLASI-FPEELVSVVLGE-AEIGMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAA 241
Cdd:cd07138 179 ILDEAgLPAGVFNLVNGDgPVVGEALSAHPdVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 242 ERIAFGKTLNAGQTCVAPDYVLVPRQRVDDFVDAYRSVVQRFypqVEGNPDYTS-----IINARQQQRLQGYLDDARAKG 316
Cdd:cd07138 259 PRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAY---VVGDPRDPAttlgpLASAAQFDRVQGYIQKGIEEG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 317 AEVIALTAEATDRR------MPqTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQ 390
Cdd:cd07138 336 ARLVAGGPGRPEGLergyfvKP-TVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERAR 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2068619660 391 HVLHHSHSGGVCLNDTLLHVaqdDMPFGGIGASGMGHYHGHEGFLTF 437
Cdd:cd07138 415 AVARRLRAGQVHINGAAFNP---GAPFGGYKQSGNGREWGRYGLEEF 458
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
3-443 |
8.01e-75 |
|
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: 242.21 E-value: 8.01e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 3 TPFGPVEQ-AIAELQQRFQAQREAFMANPMPSADQRIAWLDSLKAALLADQDALVRCISEDFGN--RSADEtllaEMLPT 79
Cdd:cd07101 7 EPLGELPQsTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKarRHAFE----EVLDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 80 VQGIRYARKRLRRWMKPSRRHVGLAFMpASARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTS 159
Cdd:cd07101 83 AIVARYYARRAERLLKPRRRRGAIPVL-TRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 160 QHLKELL-ASIFPEELVSVVLGE-AEIGMAFARlPFDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPL 237
Cdd:cd07101 162 LWAVELLiEAGLPRDLWQVVTGPgSEVGGAIVD-NADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 238 EHAAERIAFGKTLNAGQTCVAPDYVLVPRQRVDDFVDAYRSVVQ--RFYPQVEGNPDYTSIINARQQQRLQGYLDDARAK 315
Cdd:cd07101 241 DKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRalRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 316 GAEVIaltaeATDRRMPQ--------TLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRR 387
Cdd:cd07101 321 GATVL-----AGGRARPDlgpyfyepTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2068619660 388 EQQHVLHHSHSGGVCLNDTLLHV-AQDDMPFGGIGASGMGHYHGHEGFLTFSKAKGV 443
Cdd:cd07101 396 RGRRIAARLRAGTVNVNEGYAAAwASIDAPMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
33-460 |
5.29e-74 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 242.09 E-value: 5.29e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 33 SADQRIAWLDSLKAALLADQDALVRCISEDFGN--RSADEtllaEMLPTVQGIRYARKRLRRWMKPsRRHVGLAFMPASA 110
Cdd:PRK09407 74 PVRERAAVLLRFHDLVLENREELLDLVQLETGKarRHAFE----EVLDVALTARYYARRAPKLLAP-RRRAGALPVLTKT 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 111 RVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASI-FPEELVSVVLGE-AEIGMAF 188
Cdd:PRK09407 149 TELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAgLPRDLWQVVTGPgPVVGTAL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 189 ARLPfDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQR 268
Cdd:PRK09407 229 VDNA-DYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESI 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 269 VDDFVDAYRSVVQRFypQVEGNPDYT----SIINARQQQRLQGYLDDARAKGAEVIaltaeATDRRMPQ--------TLL 336
Cdd:PRK09407 308 YDEFVRAFVAAVRAM--RLGAGYDYSadmgSLISEAQLETVSAHVDDAVAKGATVL-----AGGKARPDlgplfyepTVL 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 337 LNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDTLLHV-AQDDM 415
Cdd:PRK09407 381 TGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAwGSVDA 460
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2068619660 416 PFGGIGASGMGHYHGHEGFLTFSKAKGVLIKQRLNLArliyPPYG 460
Cdd:PRK09407 461 PMGGMKDSGLGRRHGAEGLLKYTESQTIATQRVLPLA----PPPG 501
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
20-445 |
4.86e-70 |
|
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: 229.53 E-value: 4.86e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 20 QAQREAFMANPMP--SADQRIAWLdsLKAA--LLADQDALVRCISEDFGNRSADEtlLAEMLPTVQGIRYARKRLRRWMK 95
Cdd:cd07118 26 AAARKAFDKGPWPrmSGAERAAVL--LKVAdlIRARRERLALIETLESGKPISQA--RGEIEGAADLWRYAASLARTLHG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 96 PSRRHVGLAFMpasARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASI-FPEEL 174
Cdd:cd07118 102 DSYNNLGDDML---GLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAgLPAGV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 175 VSVVLGE-AEIGMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNA 252
Cdd:cd07118 179 VNIVTGYgATVGQAMTEHPdVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 253 GQTCVAPDYVLVPRQRVDDFVDAyrsVVQRFYPQVEGNP-----DYTSIINARQQQRLQGYLDDARAKGAEViALTAEAT 327
Cdd:cd07118 259 GECCNSGSRLLVHESIADAFVAA---VVARSRKVRVGDPldpetKVGAIINEAQLAKITDYVDAGRAEGATL-LLGGERL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 328 DRR----MPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCL 403
Cdd:cd07118 335 ASAaglfYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWV 414
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2068619660 404 NDTLLHVAQddMPFGGIGASGMGHYHGHEGFLTFSKAKGVLI 445
Cdd:cd07118 415 NTFLDGSPE--LPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
112-445 |
2.41e-68 |
|
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: 225.19 E-value: 2.41e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 112 VIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASI-FPEELVSVVLGE-AEIGMAFA 189
Cdd:cd07109 113 TVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAgLPAGALNVVTGLgAEAGAALV 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 190 RLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQR 268
Cdd:cd07109 193 AHPgVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSI 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 269 VDDFVDAyrsVVQRFY-----PQVEgNPDYTSIINARQQQRLQGYLDDARAKGAEVIALTAEATDRR-----MPQTLLLN 338
Cdd:cd07109 273 YDEVLER---LVERFRalrvgPGLE-DPDLGPLISAKQLDRVEGFVARARARGARIVAGGRIAEGAPaggyfVAPTLLDD 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 339 VDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDtLLHVAQDDMPFG 418
Cdd:cd07109 349 VPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNN-YGAGGGIELPFG 427
|
330 340
....*....|....*....|....*..
gi 2068619660 419 GIGASGMGHYHGHEGFLTFSKAKGVLI 445
Cdd:cd07109 428 GVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
111-430 |
5.89e-68 |
|
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: 223.56 E-value: 5.89e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 111 RVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSqhlKELLASIF-----PEELVSVVLGEA-EI 184
Cdd:cd07104 93 MVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTG---GLLIAEIFeeaglPKGVLNVVPGGGsEI 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 185 GMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVL 263
Cdd:cd07104 170 GDALVEHPrVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRIL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 264 VPRQRVDDFVDAYRSVVQRF------YPQVEGNPdytsIINARQQQRLQGYLDDARAKGAEVIALtAEATDRRMPQTLLL 337
Cdd:cd07104 250 VHESVYDEFVEKLVAKAKALpvgdprDPDTVIGP----LINERQVDRVHAIVEDAVAAGARLLTG-GTYEGLFYQPTVLS 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 338 NVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLND-TLLHVAQddMP 416
Cdd:cd07104 325 DVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDqTVNDEPH--VP 402
|
330
....*....|....
gi 2068619660 417 FGGIGASGMGHYHG 430
Cdd:cd07104 403 FGGVKASGGGRFGG 416
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
20-445 |
5.06e-67 |
|
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: 221.66 E-value: 5.06e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 20 QAQREAFMANPMPSAD--QRIAWLDSLKAALLADQDALVRCISEDFGNrsadetLLAEMLPTVQGI----RY----ARKR 89
Cdd:cd07114 26 AAARAAFEGGAWRKLTptERGKLLRRLADLIEANAEELAELETRDNGK------LIRETRAQVRYLaewyRYyaglADKI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 90 LRRWMkPSRRHVGLAFmpasarVIYQPLGVVGIIVPWNYPLFLA---IAPlvgALAAGNRVMLKLSEATPQTSQHLKELL 166
Cdd:cd07114 100 EGAVI-PVDKGDYLNF------TRREPLGVVAAITPWNSPLLLLakkLAP---ALAAGNTVVLKPSEHTPASTLELAKLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 167 ASI-FPEELVSVVLGE-AEIGMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAER 243
Cdd:cd07114 170 EEAgFPPGVVNVVTGFgPETGEALVEHPlVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 244 IAFGKTLNAGQTCVAPDYVLVPRQRVDDFVDAYRSVVQRFypqVEGNP-----DYTSIINARQQQRLQGYLDDARAKGAE 318
Cdd:cd07114 250 VVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAI---RVGDPldpetQMGPLATERQLEKVERYVARAREEGAR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 319 VIALTAEATDRRMPQ------TLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHV 392
Cdd:cd07114 327 VLTGGERPSGADLGAgyffepTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRV 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2068619660 393 LHHSHSGGVCLNDtlLHVAQDDMPFGGIGASGMGHYHGHEGFLTFSKAKGVLI 445
Cdd:cd07114 407 ARAIEAGTVWVNT--YRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
8-445 |
2.34e-66 |
|
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: 219.89 E-value: 2.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 8 VEQAIAELQQRFQAQREAfmanpmpSADQRIAWLdsLKAALLADQDAlvrcisEDFGNRSADE---TLLAEMLPTVQGIR 84
Cdd:cd07150 23 AERAIAAAYDAFPAWAAT-------TPSERERIL--LKAAEIMERRA------DDLIDLLIDEggsTYGKAWFETTFTPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 85 YAR------KRLRRWMKPSRRHvGLAFMpasarVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQT 158
Cdd:cd07150 88 LLRaaagecRRVRGETLPSDSP-GTVSM-----SVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 159 SQHLKELLASI-FPEELVSVVLGE-AEIGMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADV 235
Cdd:cd07150 162 GLKIAEIMEEAgLPKGVFNVVTGGgAEVGDELVDDPrVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 236 PLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQRVDDFVDAYRSVVQRFYpqvEGNP-DYTSI----INARQQQRLQGYLD 310
Cdd:cd07150 242 DLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLK---VGDPrDPDTVigplISPRQVERIKRQVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 311 DARAKGAEVIALTAEATDRRMPqTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQ 390
Cdd:cd07150 319 DAVAKGAKLLTGGKYDGNFYQP-TVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAF 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2068619660 391 HVLHHSHSGGVCLNDTLLHvAQDDMPFGGIGASGMGHYHGHEGFLTFSKAKGVLI 445
Cdd:cd07150 398 KLAERLESGMVHINDPTIL-DEAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
116-445 |
1.24e-65 |
|
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: 217.96 E-value: 1.24e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 116 PLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASIFPEELVSVVLGEAE-IGMAFARLPFD 194
Cdd:cd07092 118 PIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGVVNVVCGGGAsAGDALVAHPRV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 195 HLL-FTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQRVDDFV 273
Cdd:cd07092 198 RMVsLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFV 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 274 DAYRSVVQRF---YPQVEGNpDYTSIINARQQQRLQGYLDDARaKGAEVIAlTAEATDRR---MPQTLLLNVDDSMLVMQ 347
Cdd:cd07092 278 AALVEAVSAIrvgDPDDEDT-EMGPLNSAAQRERVAGFVERAP-AHARVLT-GGRRAEGPgyfYEPTVVAGVAQDDEIVQ 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 348 DEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDTLLHVAqdDMPFGGIGASGMGH 427
Cdd:cd07092 355 EEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNTHIPLAA--EMPHGGFKQSGYGK 432
|
330
....*....|....*...
gi 2068619660 428 YHGHEGFLTFSKAKGVLI 445
Cdd:cd07092 433 DLSIYALEDYTRIKHVMV 450
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
8-445 |
1.38e-64 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 215.51 E-value: 1.38e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 8 VEQAIAelqqrfqAQREAFMANPMPSADQRIAWLdsLKAAlladqDALvrcisedfgNRSADETLLAEMLPTVQGIRYAR 87
Cdd:cd07093 21 VDAAVA-------AAKEAFPGWSRMSPAERARIL--HKVA-----DLI---------EARADELALLESLDTGKPITLAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 88 KR--------LRRWMKPSRRHVGLAF-MPASAR--VIYQPLGVVGIIVPWNYPLFLA---IAPlvgALAAGNRVMLKLSE 153
Cdd:cd07093 78 TRdipraaanFRFFADYILQLDGESYpQDGGALnyVLRQPVGVAGLITPWNLPLMLLtwkIAP---ALAFGNTVVLKPSE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 154 ATPQTSQHLKELLASI-FPEELVSVVLGE-AEIGMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAI 230
Cdd:cd07093 155 WTPLTAWLLAELANEAgLPPGVVNVVHGFgPEAGAALVAHPdVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 231 ISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQRVDDFVDAYRSVVQRFYPQVEGNPDYT--SIINARQQQRLQGY 308
Cdd:cd07093 235 VFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEvgPLISKEHLEKVLGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 309 LDDARAKGAEVIALTAEATDRRMPQ------TLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYF 382
Cdd:cd07093 315 VELARAEGATILTGGGRPELPDLEGgyfvepTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVW 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068619660 383 GYDRREQQHVLHHSHSGGVCLNDTLLHvaqdD--MPFGGIGASGMGHYHGHEGFLTFSKAKGVLI 445
Cdd:cd07093 395 TRDLGRAHRVARRLEAGTVWVNCWLVR----DlrTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
8-445 |
1.47e-64 |
|
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: 215.30 E-value: 1.47e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 8 VEQAIAELQQRFQAQREAfmanpmpSADQRIAWLDSLKAALLADQDALVRCISEDFGN----RSADET-LLAEMLPTVQG 82
Cdd:cd07108 21 VDRAVAAAKAAFPEWAAT-------PARERGKLLARIADALEARSEELARLLALETGNalrtQARPEAaVLADLFRYFGG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 83 IRYARKrlrrwmkpsrrhvGLAFMPASARVIY---QPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTS 159
Cdd:cd07108 94 LAGELK-------------GETLPFGPDVLTYtvrEPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 160 QHLKELLASIFPEELVSVVLGE-AEIGMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPL 237
Cdd:cd07108 161 LLLAEILAQVLPAGVLNVITGYgEECGAALVDHPdVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 238 EHAAERIAFG-KTLNAGQTCVAPDYVLVPRQRVDDFVDAYRSVVQRFypqVEGNP-----DYTSIINARQQQRLQGYLDD 311
Cdd:cd07108 241 DDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKL---KIGDPldeatDIGAIISEKQFAKVCGYIDL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 312 ARA-KGAEVIALTAEATDRRMPQ------TLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGY 384
Cdd:cd07108 318 GLStSGATVLRGGPLPGEGPLADgffvqpTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2068619660 385 DRREQQHVLHHSHSGGVCLNDTllHVAQDDMPFGGIGASGMGHYHGHEGFL-TFSKAKGVLI 445
Cdd:cd07108 398 DLGRALRAAHALEAGWVQVNQG--GGQQPGQSYGGFKQSGLGREASLEGMLeHFTQKKTVNI 457
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
4-443 |
1.99e-64 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 214.80 E-value: 1.99e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 4 PFGPVEQAIAELQQRFQAQREaFMANPMpsaDQRIAWLDSLKAALLADQDALVRCISEDFGnrsadetllaemlptvQGI 83
Cdd:cd07102 13 PLASLEAVRAALERARAAQKG-WRAVPL---EERKAIVTRAVELLAANTDEIAEELTWQMG----------------RPI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 84 RYARKRLR------RWM--------KPSRrhvglafMPASA----RVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGN 145
Cdd:cd07102 73 AQAGGEIRgmleraRYMisiaeealADIR-------VPEKDgferYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 146 RVMLKLSEATPQTSQHLKELLASI-FPEELVSVVLGEAEIGMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLEL 223
Cdd:cd07102 146 AVILKHSPQTPLCGERFAAAFAEAgLPEGVFQVLHLSHETSAALIADPrIDHVSFTGSVAGGRAIQRAAAGRFIKVGLEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 224 GGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQRVDDFVDAYRSVVQRFypqVEGNPDYTS-----IIN 298
Cdd:cd07102 226 GGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGY---KLGDPLDPSttlgpVVS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 299 ARQQQRLQGYLDDARAKGAevIALTAEATDRRMPQ-------TLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYIT 371
Cdd:cd07102 303 ARAADFVRAQIADAIAKGA--RALIDGALFPEDKAggaylapTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMN 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2068619660 372 ARPRPLALYYFGYDRREQQHVLHHSHSGGVCLN--DTLlhvaQDDMPFGGIGASGMGHYHGHEGFLTFSKAKGV 443
Cdd:cd07102 381 DSEYGLTASVWTKDIARAEALGEQLETGTVFMNrcDYL----DPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
21-445 |
6.27e-64 |
|
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: 214.48 E-value: 6.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 21 AQREAFMANPMP--SADQRIAWLDSLKAALLADQDALVRCISEDFGnrsadETLL---AEMLPTVQGIRY----ARKRLR 91
Cdd:cd07119 43 AARRAFDSGEWPhlPAQERAALLFRIADKIREDAEELARLETLNTG-----KTLReseIDIDDVANCFRYyaglATKETG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 92 RwMKPSRRHVglafmpaSARVIYQPLGVVGIIVPWNYPLFLA---IAPlvgALAAGNRVMLKLSEATPQTSQHLKELLAS 168
Cdd:cd07119 118 E-VYDVPPHV-------ISRTVREPVGVCGLITPWNYPLLQAawkLAP---ALAAGNTVVIKPSEVTPLTTIALFELIEE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 169 I-FPEELVSVVLGE-AEIGMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIA 245
Cdd:cd07119 187 AgLPAGVVNLVTGSgATVGAELAESPdVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQAL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 246 FGKTLNAGQTCVAPDYVLVPRQRVDDFVDAyrsVVQRFYPQVEGNPDYTSI-----INARQQQRLQGYLDDARAKGAEVI 320
Cdd:cd07119 267 NGVFFNAGQVCSAGSRLLVEESIHDKFVAA---LAERAKKIKLGNGLDADTemgplVSAEHREKVLSYIQLGKEEGARLV 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 321 ALTAEATDRRMPQ------TLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLH 394
Cdd:cd07119 344 CGGKRPTGDELAKgyfvepTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVAR 423
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2068619660 395 HSHSGGVCLNDtlLHVAQDDMPFGGIGASGMGHYHGHEGFLTFSKAKGVLI 445
Cdd:cd07119 424 RLRAGTVWIND--YHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHINI 472
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
20-445 |
2.15e-63 |
|
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: 212.30 E-value: 2.15e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 20 QAQREAFMA-NPMPSADQ-RIAWldSLKAALLADQDALVRCISEDFGnRSADETLLAEMLPTVQGIRY----ARKrlrrw 93
Cdd:cd07115 26 AAARAAFEAwSAMDPAERgRILW--RLAELILANADELARLESLDTG-KPIRAARRLDVPRAADTFRYyagwADK----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 94 mkpsrrhVGLAFMPASAR----VIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASI 169
Cdd:cd07115 98 -------IEGEVIPVRGPflnyTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 170 -FPEELVSVVLGEAEI-GMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAF 246
Cdd:cd07115 171 gFPAGVLNVVTGFGEVaGAALVEHPdVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAAT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 247 GKTLNAGQTCVAPDYVLVPRQRVDDFVDAYRSVVQRFYPqveGNP-DYTS----IINARQQQRLQGYLDDARAKGAEVIA 321
Cdd:cd07115 251 GIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRP---GDPlDPKTqmgpLVSQAQFDRVLDYVDVGREEGARLLT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 322 LTAEATDRR--MPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSG 399
Cdd:cd07115 328 GGKRPGARGffVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAG 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2068619660 400 GVCLNdtLLHVAQDDMPFGGIGASGMGHYHGHEGFLTFSKAKGVLI 445
Cdd:cd07115 408 TVWIN--TYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWV 451
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
110-445 |
2.73e-63 |
|
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: 212.65 E-value: 2.73e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 110 ARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASI-FPEELVSVVLG-EAEIGMA 187
Cdd:cd07144 138 AYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVNIIPGyGAVAGSA 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 188 FARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPR 266
Cdd:cd07144 218 LAEHPdVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 267 QRVDDFVDAYRSVVQRFYPQVEGNPDYTS---IINARQQQRLQGYLDDARAKGAEVI-----ALTAEATDRRMPQTLLLN 338
Cdd:cd07144 298 SIYDKFVEKFVEHVKQNYKVGSPFDDDTVvgpQVSKTQYDRVLSYIEKGKKEGAKLVyggekAPEGLGKGYFIPPTIFTD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 339 VDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDTllHVAQDDMPFG 418
Cdd:cd07144 378 VPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSS--NDSDVGVPFG 455
|
330 340
....*....|....*....|....*..
gi 2068619660 419 GIGASGMGHYHGHEGFLTFSKAKGVLI 445
Cdd:cd07144 456 GFKMSGIGRELGEYGLETYTQTKAVHI 482
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
111-430 |
4.31e-63 |
|
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: 211.78 E-value: 4.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 111 RVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSqhlKELLASIF-----PEELVSVVLGE-AEI 184
Cdd:cd07151 125 RVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITG---GLLLAKIFeeaglPKGVLNVVVGAgSEI 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 185 GMAFARLPFDHLL-FTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVL 263
Cdd:cd07151 202 GDAFVEHPVPRLIsFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRII 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 264 VPRQRVDDFvdayrsvVQRFYPQVE----GNPDYTS-----IINARQQQRLQGYLDDARAKGAEViALTAEATDRRMPQT 334
Cdd:cd07151 282 VHEDVYDEF-------VEKFVERVKalpyGDPSDPDtvvgpLINESQVDGLLDKIEQAVEEGATL-LVGGEAEGNVLEPT 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 335 LLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDtllHVAQDD 414
Cdd:cd07151 354 VLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHIND---QPVNDE 430
|
330
....*....|....*...
gi 2068619660 415 --MPFGGIGASGMGHYHG 430
Cdd:cd07151 431 phVPFGGEKNSGLGRFNG 448
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
110-445 |
3.23e-62 |
|
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: 209.89 E-value: 3.23e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 110 ARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASIFPEELVSVVLGE-AEIGMAF 188
Cdd:cd07559 130 SYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVNVVTGFgSEAGKPL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 189 ARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEH-----AAERIAFGKTLNAGQTCVAPDYV 262
Cdd:cd07559 210 ASHPrIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFFDDAMDADddfddKAEEGQLGFAFNQGEVCTCPSRA 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 263 LVPRQRVDDFVDAyrsVVQRFYPQVEGNP-DYTSII----NARQQQRLQGYLDDARAKGAEVIA------LTAEATDRRM 331
Cdd:cd07559 290 LVQESIYDEFIER---AVERFEAIKVGNPlDPETMMgaqvSKDQLEKILSYVDIGKEEGAEVLTggerltLGGLDKGYFY 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 332 PQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNdtLLHVA 411
Cdd:cd07559 367 EPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVN--CYHQY 444
|
330 340 350
....*....|....*....|....*....|....*
gi 2068619660 412 QDDMPFGGIGASGMGHyHGHEGFLT-FSKAKGVLI 445
Cdd:cd07559 445 PAHAPFGGYKKSGIGR-ETHKMMLDhYQQTKNILV 478
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
4-369 |
6.24e-62 |
|
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: 208.66 E-value: 6.24e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 4 PFGPVEQAIAELQQRFQAQREAfmaNPMPSAdQRIAWLDSLKAALLADQDALVRCISEDFGNRSADETLlaEMLPTVQGI 83
Cdd:cd07088 30 PAATAEDADRAVDAAEAAQKAW---ERLPAI-ERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARV--EVEFTADYI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 84 RYARKRLRRW---MKPSRRhvglafmpaSARVIY---QPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQ 157
Cdd:cd07088 104 DYMAEWARRIegeIIPSDR---------PNENIFifkVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 158 TSQHLKELLASI-FPEELVSVVLGE-AEIGMAFARLPFDHLL-FTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISAD 234
Cdd:cd07088 175 NALEFAELVDEAgLPAGVLNIVTGRgSVVGDALVAHPKVGMIsLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 235 VPLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQRVDDFVDayrSVVQRFYPQVEGNP-----DYTSIINARQQQRLQGYL 309
Cdd:cd07088 255 ADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFME---KLVEKMKAVKVGDPfdaatDMGPLVNEAALDKVEEMV 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068619660 310 DDARAKGAEVIALTAEATDRR---MPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAY 369
Cdd:cd07088 332 ERAVEAGATLLTGGKRPEGEKgyfYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIEL 394
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
115-443 |
4.11e-60 |
|
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: 203.98 E-value: 4.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 115 QPLGVVGIIVPWNYPLFLA---IAPlvgALAAGNRVMLKLSEATPQTSQHLKELLASI-FPEELVSVVLGE-AEIGMAFA 189
Cdd:cd07091 140 EPIGVCGQIIPWNFPLLMLawkLAP---ALAAGNTVVLKPAEQTPLSALYLAELIKEAgFPPGVVNIVPGFgPTAGAAIS 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 190 RLP-FDHLLFTGATSIGRHVMRAAAD-NLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQ 267
Cdd:cd07091 217 SHMdVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQES 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 268 RVDDFVDAYRSVVQRFypqVEGNPDYTS-----IINARQQQRLQGYLDDARAKGAEVIALTAEATDRR--MPQTLLLNVD 340
Cdd:cd07091 297 IYDEFVEKFKARAEKR---VVGDPFDPDtfqgpQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGyfIQPTVFTDVK 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 341 DSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLND-TLLHVAqddMPFGG 419
Cdd:cd07091 374 DDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTyNVFDAA---VPFGG 450
|
330 340
....*....|....*....|....
gi 2068619660 420 IGASGMGHYHGHEGFLTFSKAKGV 443
Cdd:cd07091 451 FKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
108-445 |
7.22e-60 |
|
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: 203.22 E-value: 7.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 108 ASARVIYQPLGVVGIIVPWNYPLFLA---IAPlvgALAAGNRVMLKLSEATPQTSQHLKEL-LASIFPEELVSVV--LGE 181
Cdd:cd07112 116 ALALITREPLGVVGAVVPWNFPLLMAawkIAP---ALAAGNSVVLKPAEQSPLTALRLAELaLEAGLPAGVLNVVpgFGH 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 182 aEIGMAFARLP-FDHLLFTGATSIGRHVMRAAAD-NLTPVTLELGGKSPAIISADVP-LEHAAERIAFGKTLNAGQTCVA 258
Cdd:cd07112 193 -TAGEALGLHMdVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADAPdLDAAAEAAAAGIFWNQGEVCSA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 259 PDYVLVPRQRVDDFVDAYRSVVQRFYPqveGNP-DYTS----IINARQQQRLQGYLDDARAKGAEVIA----LTAEATDR 329
Cdd:cd07112 272 GSRLLVHESIKDEFLEKVVAAAREWKP---GDPlDPATrmgaLVSEAHFDKVLGYIESGKAEGARLVAggkrVLTETGGF 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 330 RMPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDtllh 409
Cdd:cd07112 349 FVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVNC---- 424
|
330 340 350
....*....|....*....|....*....|....*...
gi 2068619660 410 VAQDDM--PFGGIGASGMGHYHGHEGFLTFSKAKGVLI 445
Cdd:cd07112 425 FDEGDIttPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
116-426 |
9.02e-59 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 200.52 E-value: 9.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 116 PLGVVGIIVPWNYPLFLA---IAPlvgALAAGNRVMLKLSEATPQTSQHLKELLASIFPEELVSVVLGE-AEIGMAFARL 191
Cdd:PRK13473 138 PVGVVASIAPWNYPLMMAawkLAP---ALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRgATVGDALVGH 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 192 P-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQRVD 270
Cdd:PRK13473 215 PkVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYD 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 271 DFVDAYRSVVQ--RFYPQVEGNPDYTSIINARQQQRLQGYLDDARAKGAEVIALTAEATDRR---MPQTLLLNVDDSMLV 345
Cdd:PRK13473 295 DLVAKLAAAVAtlKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGHIRVVTGGEAPDGKgyyYEPTLLAGARQDDEI 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 346 MQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDTLLHVAqdDMPFGGIGASGM 425
Cdd:PRK13473 375 VQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVS--EMPHGGQKQSGY 452
|
.
gi 2068619660 426 G 426
Cdd:PRK13473 453 G 453
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
13-443 |
4.39e-58 |
|
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: 198.34 E-value: 4.39e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 13 AELQQRFQAQREAFMANPMPS-ADQRIAWLDSLKAALLADQDALVRCISEDFGNrsadetLLAEMLPTVQGiryARKRLR 91
Cdd:cd07120 19 AEAEAAIAAARRAFDETDWAHdPRLRARVLLELADAFEANAERLARLLALENGK------ILGEARFEISG---AISELR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 92 RWMKPSRRHVGLAFMPAS---ARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLAS 168
Cdd:cd07120 90 YYAGLARTEAGRMIEPEPgsfSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 169 I--FPEELVSVVLGE-AEIGMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERI 244
Cdd:cd07120 170 IpsLPAGVVNLFTESgSEGAAHLVASPdVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 245 AFGKTLNAGQTCVAPDYVLVPRQRVDDF----VDAYRSVvqRFYPQVEGNPDYTSIINARQQQRLQGYLDDARAKGAEVI 320
Cdd:cd07120 250 ERALTIFAGQFCMAGSRVLVQRSIADEVrdrlAARLAAV--KVGPGLDPASDMGPLIDRANVDRVDRMVERAIAAGAEVV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 321 aLTAEATDRRMPQ------TLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLH 394
Cdd:cd07120 328 -LRGGPVTEGLAKgaflrpTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVAR 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2068619660 395 HSHSGGVCLNDtllHVA-QDDMPFGGIGASGMGHYHGHEGFLTFSKAKGV 443
Cdd:cd07120 407 AIRAGTVWIND---WNKlFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
8-426 |
2.70e-57 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 196.28 E-value: 2.70e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 8 VEQAIAELQQRFQAqreafMANPmpSADQRIAWLDslKAALLADQDAlvrcisEDFGNRSADE------TLLAEMLPTVQ 81
Cdd:cd07149 23 VEKAIAAAKEGAKE-----MKSL--PAYERAEILE--RAAQLLEERR------EEFARTIALEagkpikDARKEVDRAIE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 82 GIRYA---RKRLRRWMKPSRRHVG----LAFmpasarVIYQPLGVVGIIVPWNYPLFLaIAPLVG-ALAAGNRVMLKLSE 153
Cdd:cd07149 88 TLRLSaeeAKRLAGETIPFDASPGgegrIGF------TIREPIGVVAAITPFNFPLNL-VAHKVGpAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 154 ATPQTSQHLKELLA-SIFPEELVSVVLGEAE-IGMAFARLP-FDHLLFTGATSIGRHVMRAAAdnLTPVTLELGGKSPAI 230
Cdd:cd07149 161 QTPLSALKLAELLLeAGLPKGALNVVTGSGEtVGDALVTDPrVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 231 ISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQRVDDFVDAYRSVVQRfypQVEGNP-----DYTSIINARQQQRL 305
Cdd:cd07149 239 VDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKK---LVVGDPldedtDVGPMISEAEAERI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 306 QGYLDDARAKGAEVIAlTAEATDRRMPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYD 385
Cdd:cd07149 316 EEWVEEAVEGGARLLT-GGKRDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTND 394
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2068619660 386 RREQQHVLHHSHSGGVCLNDTLLHVAqDDMPFGGIGASGMG 426
Cdd:cd07149 395 LQKALKAARELEVGGVMINDSSTFRV-DHMPYGGVKESGTG 434
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
109-445 |
3.72e-57 |
|
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: 195.10 E-value: 3.72e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 109 SARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELL-ASIFPEELVSVVLGEAEIGMA 187
Cdd:cd07105 91 LAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFhEAGLPKGVLNVVTHSPEDAPE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 188 FARLPFDHLL-----FTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYV 262
Cdd:cd07105 171 VVEALIAHPAvrkvnFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERI 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 263 LVPRQRVDDFVDAYRSVVQRFypqVEGNPDYTSIINARQQQRLQGYLDDARAKGAEVI---ALTAEATDRRMPQTLLLNV 339
Cdd:cd07105 251 IVHESIADEFVEKLKAAAEKL---FAGPVVLGSLVSAAAADRVKELVDDALSKGAKLVvggLADESPSGTSMPPTILDNV 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 340 DDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDTLLHvaqDD--MPF 417
Cdd:cd07105 328 TPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVH---DEptLPH 404
|
330 340
....*....|....*....|....*...
gi 2068619660 418 GGIGASGMGHYHGHEGFLTFSKAKGVLI 445
Cdd:cd07105 405 GGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
3-426 |
1.35e-56 |
|
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: 194.49 E-value: 1.35e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 3 TPFGPVEQAIAE-LQQRFQAQREAFMANPMPSADQRIAWLDSLKAALLADQDALVRCISEDFGnRSADETLLaEMLPTVQ 81
Cdd:cd07110 8 ATIGEIPAATAEdVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNG-KPLDEAAW-DVDDVAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 82 GIRYARKRLRRWMKPSRRHVGLAFMPASARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQH 161
Cdd:cd07110 86 CFEYYADLAEQLDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 162 LKELLASI-FPEELVSVVLGEA-EIGMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLE 238
Cdd:cd07110 166 LAEIAAEAgLPPGVLNVVTGTGdEAGAPLAAHPgIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 239 HAAERIAFGKTLNAGQTCVAPDYVLVPRQRVDDFVDAyrsVVQRFYPQVEGNP-----DYTSIINARQQQRLQGYLDDAR 313
Cdd:cd07110 246 KAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLER---LATAAEAIRVGDPleegvRLGPLVSQAQYEKVLSFIARGK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 314 AKGAEVIaltaeaTDRRMPQ----------TLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFG 383
Cdd:cd07110 323 EEGARLL------CGGRRPAhlekgyfiapTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVIS 396
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2068619660 384 YDRREQQHVLHHSHSGGVCLNDTLLHVAQddMPFGGIGASGMG 426
Cdd:cd07110 397 RDAERCDRVAEALEAGIVWINCSQPCFPQ--APWGGYKRSGIG 437
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
112-426 |
8.96e-55 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 190.67 E-value: 8.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 112 VIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKEL-LASIFPEELVSVVLGEA-EIGMAFA 189
Cdd:PLN02278 156 VLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELaLQAGIPPGVLNVVMGDApEIGDALL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 190 RLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQR 268
Cdd:PLN02278 236 ASPkVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGI 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 269 VDDFVDAYRSVVQR------FYPQVEGNPdytsIINARQQQRLQGYLDDARAKGAEVIALTAEATDRRM---PqTLLLNV 339
Cdd:PLN02278 316 YDKFAEAFSKAVQKlvvgdgFEEGVTQGP----LINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTfyeP-TVLGDV 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 340 DDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDTLLHVAQddMPFGG 419
Cdd:PLN02278 391 TEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEV--APFGG 468
|
....*..
gi 2068619660 420 IGASGMG 426
Cdd:PLN02278 469 VKQSGLG 475
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
112-445 |
1.09e-54 |
|
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: 189.59 E-value: 1.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 112 VIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASIFPEELVSVVLGE-AEIGMAFAR 190
Cdd:cd07117 132 VLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNIVTGKgSKSGEYLLN 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 191 LP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQRV 269
Cdd:cd07117 212 HPgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 270 DDFVDAyrsVVQRFYPQVEGNP-DYTSI----INARQQQRLQGYLDDARAKGAEVIA----LTAEATDRR--MPQTLLLN 338
Cdd:cd07117 292 DEFVAK---LKEKFENVKVGNPlDPDTQmgaqVNKDQLDKILSYVDIAKEEGAKILTgghrLTENGLDKGffIEPTLIVN 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 339 VDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNdtLLHVAQDDMPFG 418
Cdd:cd07117 369 VTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVN--TYNQIPAGAPFG 446
|
330 340
....*....|....*....|....*...
gi 2068619660 419 GIGASGMGHyHGHEGFLT-FSKAKGVLI 445
Cdd:cd07117 447 GYKKSGIGR-ETHKSMLDaYTQMKNIYI 473
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
116-430 |
5.37e-54 |
|
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: 187.12 E-value: 5.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 116 PLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLkelLASIF-----PEELVSVVLGEAEIGMAFAR 190
Cdd:cd07152 110 PLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVV---IARLFeeaglPAGVLHVLPGGADAGEALVE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 191 LP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQRV 269
Cdd:cd07152 187 DPnVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 270 DDFVDAyrsVVQRFYPQVEGNPdYTS------IINARQQQRLQGYLDDARAKGAEVIAlTAEATDRRMPQTLLLNVDDSM 343
Cdd:cd07152 267 DAYTAK---LAAKAKHLPVGDP-ATGqvalgpLINARQLDRVHAIVDDSVAAGARLEA-GGTYDGLFYRPTVLSGVKPGM 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 344 LVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLND-TLLHVAQddMPFGGIGA 422
Cdd:cd07152 342 PAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDqTVNDEPH--NPFGGMGA 419
|
....*...
gi 2068619660 423 SGMGHYHG 430
Cdd:cd07152 420 SGNGSRFG 427
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
8-443 |
2.71e-53 |
|
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: 184.97 E-value: 2.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 8 VEQAIAELQQRFQAQREAfmanpmpSADQRIAWLDSLKAALLADQDALVRCISEDFGNRSADEtlLAEMLPTVQGIRYAR 87
Cdd:cd07100 1 IEAALDRAHAAFLAWRKT-------SFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA--RAEVEKCAWICRYYA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 88 KRLRRWMKPSRRHVGLAfmpaSARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLA 167
Cdd:cd07100 72 ENAEAFLADEPIETDAG----KAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 168 SI-FPEELVSVVLGEAEigmAFARLPFDHLL----FTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAE 242
Cdd:cd07100 148 EAgFPEGVFQNLLIDSD---QVEAIIADPRVrgvtLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 243 RIAFGKTLNAGQTCVAPDYVLVPRQRVDDFVDAYRSVVQRFYPqveGNP-DYTSIIN--ARQQQR--LQGYLDDARAKGA 317
Cdd:cd07100 225 TAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKV---GDPmDEDTDLGplARKDLRdeLHEQVEEAVAAGA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 318 EVIaLTAEATDRR---MPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLH 394
Cdd:cd07100 302 TLL-LGGKRPDGPgafYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVAR 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2068619660 395 HSHSGGVCLNDtllHVAQD-DMPFGGIGASGMGHYHGHEGFLTFSKAKGV 443
Cdd:cd07100 381 RLEAGMVFING---MVKSDpRLPFGGVKRSGYGRELGRFGIREFVNIKTV 427
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
116-445 |
3.44e-53 |
|
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: 185.20 E-value: 3.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 116 PLGVVGIIVPWNYPLFLA---IAPlvgALAAGNRVMLKLSEATPQTSQhlkeLLASIFPEE-----LVSVVLGEAEIGMA 187
Cdd:cd07090 116 PLGVCAGIGAWNYPIQIAswkSAP---ALACGNAMVYKPSPFTPLTAL----LLAEILTEAglpdgVFNVVQGGGETGQL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 188 FARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPR 266
Cdd:cd07090 189 LCEHPdVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQR 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 267 QRVDDFVDAyrsVVQRFYPQVEGNP-----DYTSIINARQQQRLQGYLDDARAKGAEVIALTAEATDRR-------MPQT 334
Cdd:cd07090 269 SIKDEFTER---LVERTKKIRIGDPldedtQMGALISEEHLEKVLGYIESAKQEGAKVLCGGERVVPEDglengfyVSPC 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 335 LLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDtlLHVAQDD 414
Cdd:cd07090 346 VLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINT--YNISPVE 423
|
330 340 350
....*....|....*....|....*....|.
gi 2068619660 415 MPFGGIGASGMGHYHGHEGFLTFSKAKGVLI 445
Cdd:cd07090 424 VPFGGYKQSGFGRENGTAALEHYTQLKTVYV 454
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
9-444 |
1.38e-52 |
|
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: 184.23 E-value: 1.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 9 EQAIAELQQRFQAQREAFMANPMP--SADQRIAWLDSLKAALLADQDALVRCISEDFGnRSADETLLAEMLPTVQGIRYA 86
Cdd:cd07142 37 EGDAEDVDRAVKAARKAFDEGPWPrmTGYERSRILLRFADLLEKHADELAALETWDNG-KPYEQARYAEVPLAARLFRYY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 87 RKrlrrWMKPSRRHVGLAFMPASARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELL 166
Cdd:cd07142 116 AG----WADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 167 ASI-FPEELVSVVLG-EAEIGMAFAR-LPFDHLLFTGATSIGRHVMRAAAD-NLTPVTLELGGKSPAIISADVPLEHAAE 242
Cdd:cd07142 192 AEAgLPDGVLNIVTGfGPTAGAAIAShMDVDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 243 RIAFGKTLNAGQTCVAPDYVLVPRQRVDDFVD------AYRSVVQRFYPQVEGNPDytsiINARQQQRLQGYLDDARAKG 316
Cdd:cd07142 272 LAHFALFFNQGQCCCAGSRTFVHESIYDEFVEkakaraLKRVVGDPFRKGVEQGPQ----VDKEQFEKILSYIEHGKEEG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 317 AEVIALTAEATDRR---MPqTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVL 393
Cdd:cd07142 348 ATLITGGDRIGSKGyyiQP-TIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLS 426
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2068619660 394 HHSHSGGVCLNdtLLHVAQDDMPFGGIGASGMGHYHGHEGFLTFSKAKGVL 444
Cdd:cd07142 427 RALKAGTVWVN--CYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVV 475
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
115-446 |
4.75e-52 |
|
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: 182.93 E-value: 4.75e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 115 QPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASI-FPEELVSVVLGEAEI-GMAFARLP 192
Cdd:cd07141 144 EPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAgFPPGVVNVVPGYGPTaGAAISSHP 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 193 -FDHLLFTGATSIGRHVMRAAAD-NLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQRVD 270
Cdd:cd07141 224 dIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYD 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 271 DFVdayRSVVQRFYPQVEGNPDYTSI-----INARQQQRLQGYLDDARAKGAEVIALTAEATDRR--MPQTLLLNVDDSM 343
Cdd:cd07141 304 EFV---KRSVERAKKRVVGNPFDPKTeqgpqIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGyfIQPTVFSDVTDDM 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 344 LVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNdTLLHVAQdDMPFGGIGAS 423
Cdd:cd07141 381 RIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVN-CYNVVSP-QAPFGGYKMS 458
|
330 340
....*....|....*....|...
gi 2068619660 424 GMGHYHGHEGFLTFSKAKGVLIK 446
Cdd:cd07141 459 GNGRELGEYGLQEYTEVKTVTIK 481
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
111-426 |
3.62e-51 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 179.85 E-value: 3.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 111 RVIY---QPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASI-FPEELVSVVLGEA-EIG 185
Cdd:cd07145 115 RIAFtvrEPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPGVINVVTGYGsEVG 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 186 MAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLV 264
Cdd:cd07145 195 DEIVTNPkVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILV 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 265 PRQRVDDFVDAYRSVVQRFypqVEGNP-----DYTSIINARQQQRLQGYLDDARAKGAEVIALTAEATDRRMPQTLLLNV 339
Cdd:cd07145 275 EEEVYDKFLKLLVEKVKKL---KVGDPldestDLGPLISPEAVERMENLVNDAVEKGGKILYGGKRDEGSFFPPTVLEND 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 340 DDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDTLLhVAQDDMPFGG 419
Cdd:cd07145 352 TPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDSTR-FRWDNLPFGG 430
|
....*..
gi 2068619660 420 IGASGMG 426
Cdd:cd07145 431 FKKSGIG 437
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
68-446 |
6.68e-51 |
|
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: 179.56 E-value: 6.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 68 ADETLlAEMLPTVQGIRYARKRLRrwmkpsrrhvglafmpasarviyQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRV 147
Cdd:cd07113 118 NGETL-APSIPSMQGERYTAFTRR-----------------------EPVGVVAGIVPWNFSVMIAVWKIGAALATGCTI 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 148 MLKLSEATPQTSQHLKELLASI-FPEELVSVVLGEAEIGMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGG 225
Cdd:cd07113 174 VIKPSEFTPLTLLRVAELAKEAgIPDGVLNVVNGKGAVGAQLISHPdVAKVSFTGSVATGKKIGRQAASDLTRVTLELGG 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 226 KSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQRVDDFVDAYRSVVQRFYPqveGNP-DYTSII----NAR 300
Cdd:cd07113 254 KNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQV---GSPmDESVMFgplaNQP 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 301 QQQRLQGYLDDARAKGAEVIAlTAEATDRR---MPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPL 377
Cdd:cd07113 331 HFDKVCSYLDDARAEGDEIVR-GGEALAGEgyfVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGL 409
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 378 ALYYFGYDRREQQHVLHHSHSGGVCLN-DTLLHVAqddMPFGGIGASGMGHYHGHEGFLTFSKAKGVLIK 446
Cdd:cd07113 410 TASVWTNNLSKALRYIPRIEAGTVWVNmHTFLDPA---VPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
112-368 |
1.17e-50 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 177.24 E-value: 1.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 112 VIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASI-FPEELVSVVLGE-AEIGMAFA 189
Cdd:PRK10090 67 LFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRgETVGQELA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 190 RLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQR 268
Cdd:PRK10090 147 GNPkVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGI 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 269 VDDFVDAYR---SVVQRFYPQVEGNPDYTSIINARQQQRLQGYLDDARAKGAeVIALTAEATDRR---MPQTLLLNVDDS 342
Cdd:PRK10090 227 YDQFVNRLGeamQAVQFGNPAERNDIAMGPLINAAALERVEQKVARAVEEGA-RVALGGKAVEGKgyyYPPTLLLDVRQE 305
|
250 260
....*....|....*....|....*.
gi 2068619660 343 MLVMQDEIFGPLLPVVPYDCLDDALA 368
Cdd:PRK10090 306 MSIMHEETFGPVLPVVAFDTLEEAIA 331
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
8-445 |
1.26e-50 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 178.34 E-value: 1.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 8 VEQAIAelqqrfqAQREAFMANPMPSADQRIAWLDSLKAALLADQDALVRCISEDFGNRSADetLLAEMLPTVQGIRYar 87
Cdd:cd07107 21 VDRAVA-------AARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSA--MLGDVMVAAALLDY-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 88 krlrrwmkpsrrHVGLAFM------PASAR----VIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQ 157
Cdd:cd07107 90 ------------FAGLVTElkgetiPVGGRnlhyTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 158 TSQHLKELLASIFPEELVSVVLGE-AEIGMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADV 235
Cdd:cd07107 158 SALRLAELAREVLPPGVFNILPGDgATAGAALVRHPdVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 236 PLEHAAERIAFGKTLN-AGQTCVAPDYVLVPRQRVDDFVDAYRSVVQRFYPQVEGNPDYT--SIINARQQQRLQGYLDDA 312
Cdd:cd07107 238 DPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTmgPLVSRQQYDRVMHYIDSA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 313 RAKGAEVIALTAEATDRR------MPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDR 386
Cdd:cd07107 318 KREGARLVTGGGRPEGPAleggfyVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDI 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2068619660 387 REQQHVLHHSHSGGVCLNDTLLHVAqdDMPFGGIGASGMGHYHGHEGFLTFSKAKGVLI 445
Cdd:cd07107 398 SQAHRTARRVEAGYVWINGSSRHFL--GAPFGGVKNSGIGREECLEELLSYTQEKNVNV 454
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
20-427 |
5.78e-50 |
|
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: 177.15 E-value: 5.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 20 QAQREAFMANPMPSADQRIAWLDSLKAALLADQDALVRCISEDFGNRSAdETLlAEMLPTVQGIRYARKRLRRwMK---- 95
Cdd:cd07131 44 EAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLA-EGR-GDVQEAIDMAQYAAGEGRR-LFgetv 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 96 PSRRHVGLAFMpasarvIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASI-FPEEL 174
Cdd:cd07131 121 PSELPNKDAMT------RRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAgLPPGV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 175 VSVVLGEAE-IGMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERI---AFGKT 249
Cdd:cd07131 195 VNVVHGRGEeVGEALVEHPdVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGAlwsAFGTT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 250 lnaGQTCVAPDYVLVPRQRVDDFVDAYRSVVQRFypQVeGNP-----DYTSIINARQQQRLQGYLDDARAKGAEVIALTA 324
Cdd:cd07131 275 ---GQRCTATSRLIVHESVYDEFLKRFVERAKRL--RV-GDGldeetDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 325 EATDRRMPQ------TLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHS 398
Cdd:cd07131 349 RLTGGGYEKgyfvepTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEA 428
|
410 420
....*....|....*....|....*....
gi 2068619660 399 GGVCLNDTLLHvAQDDMPFGGIGASGMGH 427
Cdd:cd07131 429 GITYVNAPTIG-AEVHLPFGGVKKSGNGH 456
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
8-426 |
1.28e-49 |
|
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: 176.29 E-value: 1.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 8 VEQAIAelqqrfqAQREAFMANPMPSADQRIAWLDSLKAALLADQDALVRCISedfgnRSADETL---LAEMLPTVQGIR 84
Cdd:cd07097 39 ADAAIA-------AAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLT-----REEGKTLpeaRGEVTRAGQIFR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 85 Y---ARKRLRRWMKPSRRhvglafmP-ASARVIYQPLGVVGIIVPWNYPLFLA---IAPlvgALAAGNRVMLKLSEATPQ 157
Cdd:cd07097 107 YyagEALRLSGETLPSTR-------PgVEVETTREPLGVVGLITPWNFPIAIPawkIAP---ALAYGNTVVFKPAELTPA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 158 TSQHLKELLASI-FPEELVSVVLGE-AEIGMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISAD 234
Cdd:cd07097 177 SAWALVEILEEAgLPAGVFNLVMGSgSEVGQALVEHPdVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 235 VPLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQRVDDFVDAyrsVVQRFYPQVEGNP-----DYTSIINARQQQRLQGYL 309
Cdd:cd07097 257 ADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEA---LVERTKALKVGDAldegvDIGPVVSERQLEKDLRYI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 310 DDARAKGAEVI----ALTAEATDRRMPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYD 385
Cdd:cd07097 334 EIARSEGAKLVyggeRLKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTS 413
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2068619660 386 RREQQHVLHHSHSGGVCLN----DTLLHVaqddmPFGGIGASGMG 426
Cdd:cd07097 414 LKHATHFKRRVEAGVVMVNlptaGVDYHV-----PFGGRKGSSYG 453
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
114-446 |
1.69e-49 |
|
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: 176.18 E-value: 1.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 114 YQPLGVVGIIVPWNYPLFL---AIAPlvgALAAGNRVMLKLSEATPQTSQHLKELLASI-FPEELVSVVLGEAE-IGMAF 188
Cdd:cd07143 142 HEPIGVCGQIIPWNFPLLMcawKIAP---ALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGYGRtCGNAI 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 189 ARLP-FDHLLFTGATSIGRHVMRAAA-DNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPR 266
Cdd:cd07143 219 SSHMdIDKVAFTGSTLVGRKVMEAAAkSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 267 QRVDDFVDAYRSVVQR------FYPQVEGNPDYTSIinarQQQRLQGYLDDARAKGAEVIAltaeATDRR------MPQT 334
Cdd:cd07143 299 GIYDKFVKRFKEKAKKlkvgdpFAEDTFQGPQVSQI----QYERIMSYIESGKAEGATVET----GGKRHgnegyfIEPT 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 335 LLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDTLLHVAQdd 414
Cdd:cd07143 371 IFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQ-- 448
|
330 340 350
....*....|....*....|....*....|..
gi 2068619660 415 MPFGGIGASGMGHYHGHEGFLTFSKAKGVLIK 446
Cdd:cd07143 449 VPFGGYKQSGIGRELGEYALENYTQIKAVHIN 480
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
8-426 |
2.47e-48 |
|
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: 172.04 E-value: 2.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 8 VEQAIAELQQRFQAQREAfmanpmpSADQRIAWLDSLKAALLADQDALVRCISEDFGNRSADETllAEMLPTVQGIRYAR 87
Cdd:cd07147 23 IEEAIAAAVKAFRPMRAL-------PAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDAR--GEVARAIDTFRIAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 88 KRLRRWmkpSRRHVGLAFMPASA-------RViyqPLGVVGIIVPWNYPLFLA---IAPlvgALAAGNRVMLKLSEATPQ 157
Cdd:cd07147 94 EEATRI---YGEVLPLDISARGEgrqglvrRF---PIGPVSAITPFNFPLNLVahkVAP---AIAAGCPFVLKPASRTPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 158 TSQHLKELLA-SIFPEELVSVVLGEAEIGMAFA---RLPFdhLLFTGATSIGRHVMRAAADNltPVTLELGGKSPAIISA 233
Cdd:cd07147 165 SALILGEVLAeTGLPKGAFSVLPCSRDDADLLVtdeRIKL--LSFTGSPAVGWDLKARAGKK--KVVLELGGNAAVIVDS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 234 DVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQRVDDFVDayrSVVQRFYPQVEGNP-----DYTSIINARQQQRLQGY 308
Cdd:cd07147 241 DADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKS---RLVARVKALKTGDPkddatDVGPMISESEAERVEGW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 309 LDDARAKGAEVIAlTAEATDRRMPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRRE 388
Cdd:cd07147 318 VNEAVDAGAKLLT-GGKRDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEK 396
|
410 420 430
....*....|....*....|....*....|....*...
gi 2068619660 389 QQHVLHHSHSGGVCLNDtLLHVAQDDMPFGGIGASGMG 426
Cdd:cd07147 397 ALRAWDELEVGGVVIND-VPTFRVDHMPYGGVKDSGIG 433
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
8-426 |
2.15e-47 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 169.54 E-value: 2.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 8 VEQAIAELQQRFQAQREAfmanpmpSADQRIAWLDSLKAALLADQDALVRCISEDFGNRSADEtlLAEMLPTVQGIRYAR 87
Cdd:cd07094 23 AEEALATARAGAENRRAL-------PPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDA--RVEVDRAIDTLRLAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 88 KRLRRwmkpsRRHVGLAfMPASAR-------VIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQ 160
Cdd:cd07094 94 EEAER-----IRGEEIP-LDATQGsdnrlawTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 161 HLKELLASI-FPEELVSVVLGE-AEIGMAFARLP-FDHLLFTGATSIGRHVMRAAAdnLTPVTLELGGKSPAIISADVPL 237
Cdd:cd07094 168 ELAKILVEAgVPEGVLQVVTGErEVLGDAFAADErVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVIVDRDADL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 238 EHAAERIAFGKTLNAGQTCVAPDYVLVPRQRVDDFVDAyrsvvqrFYPQVE----GNP-----DYTSIINARQQQRLQGY 308
Cdd:cd07094 246 DAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEA-------FVAAVKklkvGDPldedtDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 309 LDDARAKGAEVIaLTAEATDRRMPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRRE 388
Cdd:cd07094 319 VEEAVEAGARLL-CGGERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNV 397
|
410 420 430
....*....|....*....|....*....|....*...
gi 2068619660 389 QQHVLHHSHSGGVCLNDTlLHVAQDDMPFGGIGASGMG 426
Cdd:cd07094 398 AFKAAEKLEVGGVMVNDS-SAFRTDWMPFGGVKESGVG 434
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
100-443 |
2.43e-46 |
|
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: 167.57 E-value: 2.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 100 HVGLAFMPASARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASI-FPEELVSVV 178
Cdd:cd07111 131 HAGWAQLLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAgLPPGVLNIV 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 179 LGEAEIGMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCV 257
Cdd:cd07111 211 TGNGSFGSALANHPgVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCC 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 258 APDYVLVPRQRVDDFVDAYRSVVQRFY--PQVEGNPDYTSIINARQQQRLQGYLDDARAKGAEVIALTAEATDRRM--PQ 333
Cdd:cd07111 291 AGSRLLVQESVAEELIRKLKERMSHLRvgDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPfyPP 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 334 TLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDTLLHVAQd 413
Cdd:cd07111 371 TLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAA- 449
|
330 340 350
....*....|....*....|....*....|
gi 2068619660 414 dMPFGGIGASGMGHYHGHEGFLTFSKAKGV 443
Cdd:cd07111 450 -AGFGGYRESGFGREGGKEGLYEYLRPSWE 478
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
36-446 |
3.23e-46 |
|
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: 166.98 E-value: 3.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 36 QRIAWLDSLKAALLADQDALVRCISEDFGNRSADEtlLAEMLPTVQGIRY---ARKRLRR------WMKPSRRHVGLAfm 106
Cdd:cd07082 62 ERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDA--LKEVDRTIDYIRDtieELKRLDGdslpgdWFPGTKGKIAQV-- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 107 pasARViyqPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASI-FPEELVSVVLGE-AEI 184
Cdd:cd07082 138 ---RRE---PLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAgFPKGVVNVVTGRgREI 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 185 G---MAFARLpfDHLLFTGATSIGRHVMRAAAdnLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDY 261
Cdd:cd07082 212 GdplVTHGRI--DVISFTGSTEVGNRLKKQHP--MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKR 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 262 VLVPRQRVDDFVDAYRSVVQRF---YPQvEGNPDYTSIINARQQQRLQGYLDDARAKGAEVIaltaeATDRRMPQT---- 334
Cdd:cd07082 288 VLVHESVADELVELLKEEVAKLkvgMPW-DNGVDITPLIDPKSADFVEGLIDDAVAKGATVL-----NGGGREGGNliyp 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 335 -LLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDTLLHvAQD 413
Cdd:cd07082 362 tLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQR-GPD 440
|
410 420 430
....*....|....*....|....*....|...
gi 2068619660 414 DMPFGGIGASGMGHYHGHEGFLTFSKAKGVLIK 446
Cdd:cd07082 441 HFPFLGRKDSGIGTQGIGDALRSMTRRKGIVIN 473
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
113-426 |
3.53e-46 |
|
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: 166.86 E-value: 3.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 113 IYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASIFPEELVSVVLG-EAEIGMAFARL 191
Cdd:cd07116 133 FHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGfGLEAGKPLASS 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 192 P-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEH------AAERIAFgKTLNAGQTCVAPDYVLV 264
Cdd:cd07116 213 KrIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPNIFFADVMDADdaffdkALEGFVM-FALNQGEVCTCPSRALI 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 265 PRQRVDDFVDayrSVVQRFYPQVEGNP-DYTSIINAR----QQQRLQGYLDDARAKGAEVIA------LTAEATDRRMPQ 333
Cdd:cd07116 292 QESIYDRFME---RALERVKAIKQGNPlDTETMIGAQasleQLEKILSYIDIGKEEGAEVLTggerneLGGLLGGGYYVP 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 334 TLLLNvDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNdtLLHVAQD 413
Cdd:cd07116 369 TTFKG-GNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN--CYHLYPA 445
|
330
....*....|...
gi 2068619660 414 DMPFGGIGASGMG 426
Cdd:cd07116 446 HAAFGGYKQSGIG 458
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
113-368 |
5.57e-44 |
|
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: 160.81 E-value: 5.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 113 IYQPLGVVGIIVPWNYPLflAI-----APlvgALAAGNRVMLKLSEATPQTSQHLKELLASI-----FPEELVSVVLGEA 182
Cdd:cd07086 130 QWNPLGVVGVITAFNFPV--AVpgwnaAI---ALVCGNTVVWKPSETTPLTAIAVTKILAEVlekngLPPGVVNLVTGGG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 183 EIGMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDY 261
Cdd:cd07086 205 DGGELLVHDPrVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRR 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 262 VLVPRQRVDDFVDAyrsvVQRFYPQVE-GNP-----DYTSIINARQQQRLQGYLDDARAKGAEVIaLTAEATDRRMP--- 332
Cdd:cd07086 285 LIVHESVYDEFLER----LVKAYKQVRiGDPldegtLVGPLINQAAVEKYLNAIEIAKSQGGTVL-TGGKRIDGGEPgny 359
|
250 260 270
....*....|....*....|....*....|....*...
gi 2068619660 333 --QTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALA 368
Cdd:cd07086 360 vePTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIA 397
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
17-424 |
4.16e-42 |
|
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: 154.74 E-value: 4.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 17 QRFQAQREAFMANPMPSADQRIAWLDSLKAALLADQDALVRCISEDFGNRSAD-ETLLAEMLPTVQ-GIRYARKRLrrwm 94
Cdd:cd07095 4 AAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEaQTEVAAMAGKIDiSIKAYHERT---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 95 kpSRRHVGLAFMPASARviYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASI-FPEE 173
Cdd:cd07095 80 --GERATPMAQGRAVLR--HRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAgLPPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 174 LVSVVLGEAEIGMAFARLP-FDHLLFTGATSIGRHVMRAAADNltP---VTLELGGKSPAIISADVPLEHAAERIAFGKT 249
Cdd:cd07095 156 VLNLVQGGRETGEALAAHEgIDGLLFTGSAATGLLLHRQFAGR--PgkiLALEMGGNNPLVVWDVADIDAAAYLIVQSAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 250 LNAGQTCVAPDYVLVPRQRV-DDFVDAYRSVVQRFYPqveGNPD-----YTSIINARQQQRLQGYLDDARAKGAEVI-AL 322
Cdd:cd07095 234 LTAGQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRI---GAPDaeppfMGPLIIAAAAARYLLAQQDLLALGGEPLlAM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 323 TAEATDRRMPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVC 402
Cdd:cd07095 311 ERLVAGTAFLSPGIIDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVN 390
|
410 420
....*....|....*....|..
gi 2068619660 403 LNDTLLHvAQDDMPFGGIGASG 424
Cdd:cd07095 391 WNRPTTG-ASSTAPFGGVGLSG 411
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
62-426 |
4.65e-42 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 156.21 E-value: 4.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 62 DFGNRSADETLLAEMLPTVQGIRYARK-------RLRRWMKPSRRHVGLAFMPAS----ARVIYQPLGVVGIIVPWNYPL 130
Cdd:PRK09847 92 DLMEAHAEELALLETLDTGKPIRHSLRddipgaaRAIRWYAEAIDKVYGEVATTSshelAMIVREPVGVIAAIVPWNFPL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 131 FLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKEL--LASIfPEELVSVVLGEA-EIGMAFARLP-FDHLLFTGATSIGR 206
Cdd:PRK09847 172 LLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLakEAGL-PDGVLNVVTGFGhEAGQALSRHNdIDAIAFTGSTRTGK 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 207 HVMRAAAD-NLTPVTLELGGKSPAIISADVP-LEHAAERIAFGKTLNAGQTCVAPDYVLVPRQRVDDFVDAYRSVVQRFY 284
Cdd:PRK09847 251 QLLKDAGDsNMKRVWLEAGGKSANIVFADCPdLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQ 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 285 PQVEGNPDYT--SIINARQQQRLQGYLDDARAKGAEVIALTAEATDRRMPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDC 362
Cdd:PRK09847 331 PGHPLDPATTmgTLIDCAHADSVHSFIREGESKGQLLLDGRNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTS 410
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068619660 363 LDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDtllhVAQDDM--PFGGIGASGMG 426
Cdd:PRK09847 411 EEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNN----YNDGDMtvPFGGYKQSGNG 472
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
107-433 |
5.16e-42 |
|
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: 155.21 E-value: 5.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 107 PASARVIY---QPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELL-ASIFPEELVSVVLGE- 181
Cdd:cd07146 108 NGKARKIFtlrEPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLyEAGLPPDMLSVVTGEp 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 182 AEIGMAFARLP-FDHLLFTGATSIGRHVmrAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPD 260
Cdd:cd07146 188 GEIGDELITHPdVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVK 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 261 YVLVPRQRVDDFVDAyrsVVQRFYPQVEGNP-----DYTSIINARQQQRLQGYLDDARAKGAEViALTAEATDRRMPQTL 335
Cdd:cd07146 266 RILVHESVADEFVDL---LVEKSAALVVGDPmdpatDMGTVIDEEAAIQIENRVEEAIAQGARV-LLGNQRQGALYAPTV 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 336 LLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLalyyfgydrreqqhvlhhshSGGVCLND--------TL 407
Cdd:cd07146 342 LDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGL--------------------SSGVCTNDldtikrlvER 401
|
330 340 350
....*....|....*....|....*....|....*..
gi 2068619660 408 LHVAQ-----------DDMPFGGIGASGMGhyhGHEG 433
Cdd:cd07146 402 LDVGTvnvnevpgfrsELSPFGGVKDSGLG---GKEG 435
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
111-443 |
6.77e-42 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 155.66 E-value: 6.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 111 RVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASI-FPEELVSVVLGE-AEIGMAF 188
Cdd:PLN02467 146 YVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVgLPPGVLNVVTGLgTEAGAPL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 189 ARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQ 267
Cdd:PLN02467 226 ASHPgVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHER 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 268 RVDDFVDAYRSVVQRFY---PQVEG---NPdytsIINARQQQRLQGYLDDARAKGAEVIALTAEATDRRM----PQTLLL 337
Cdd:PLN02467 306 IASEFLEKLVKWAKNIKisdPLEEGcrlGP----VVSEGQYEKVLKFISTAKSEGATILCGGKRPEHLKKgffiEPTIIT 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 338 NVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDTLLHVAQddMPF 417
Cdd:PLN02467 382 DVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQ--APW 459
|
330 340
....*....|....*....|....*.
gi 2068619660 418 GGIGASGMGHYHGHEGFLTFSKAKGV 443
Cdd:PLN02467 460 GGIKRSGFGRELGEWGLENYLSVKQV 485
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
107-444 |
4.82e-41 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 153.81 E-value: 4.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 107 PASARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASI-FPEELVSVVLG-EAEI 184
Cdd:PLN02466 186 PHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAgLPPGVLNVVSGfGPTA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 185 GMAFA-RLPFDHLLFTGATSIGRHVMRAAA-DNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYV 262
Cdd:PLN02466 266 GAALAsHMDVDKLAFTGSTDTGKIVLELAAkSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRT 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 263 LVPRQRVDDFVD-----AYRSVV-QRFYPQVEGNPDytsiINARQQQRLQGYLDDARAKGAEVIALTAEATDR--RMPQT 334
Cdd:PLN02466 346 FVHERVYDEFVEkakarALKRVVgDPFKKGVEQGPQ----IDSEQFEKILRYIKSGVESGATLECGGDRFGSKgyYIQPT 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 335 LLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNdtLLHVAQDD 414
Cdd:PLN02466 422 VFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVN--CFDVFDAA 499
|
330 340 350
....*....|....*....|....*....|
gi 2068619660 415 MPFGGIGASGMGHYHGHEGFLTFSKAKGVL 444
Cdd:PLN02466 500 IPFGGYKMSGIGREKGIYSLNNYLQVKAVV 529
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
115-446 |
9.72e-41 |
|
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: 152.26 E-value: 9.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 115 QPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASI-FPEELVSVVLGEAE-IGMAFARLP 192
Cdd:cd07140 146 EPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAgFPKGVINILPGSGSlVGQRLSDHP 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 193 -FDHLLFTGATSIGRHVMRAAAD-NLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQRVD 270
Cdd:cd07140 226 dVRKLGFTGSTPIGKHIMKSCAVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHD 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 271 DFVdayRSVVQRFYPQVEGNPDYTSIINARQQQ-----RLQGYLDDARAKGAEVIaLTAEATDRR---MPQTLLLNVDDS 342
Cdd:cd07140 306 EFV---RRVVEEVKKMKIGDPLDRSTDHGPQNHkahldKLVEYCERGVKEGATLV-YGGKQVDRPgffFEPTVFTDVEDH 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 343 MLVMQDEIFGPLLPVVPYDC--LDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLND-TLLHVAQddmPFGG 419
Cdd:cd07140 382 MFIAKEESFGPIMIISKFDDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTyNKTDVAA---PFGG 458
|
330 340
....*....|....*....|....*..
gi 2068619660 420 IGASGMGHYHGHEGFLTFSKAKGVLIK 446
Cdd:cd07140 459 FKQSGFGKDLGEEALNEYLKTKTVTIE 485
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
3-445 |
1.22e-40 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 151.43 E-value: 1.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 3 TPFGP--VEQAIAELQQRFQAQREAFMAnpmpsadQRIAWLDSLKAALLADQDALVRCISEDFGN--RSADetllAEMLP 78
Cdd:PRK09406 18 TALTDdeVDAAIARAHARFRDYRTTTFA-------QRARWANAAADLLEAEADQVAALMTLEMGKtlASAK----AEALK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 79 TVQGIRYARKRLRRWMKPSRRHVGlAFMPASARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQT 158
Cdd:PRK09406 87 CAKGFRYYAEHAEALLADEPADAA-AVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 159 SQHLKELLASI-FPEELVSVVLGEAEIGMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAII--SAD 234
Cdd:PRK09406 166 ALYLADLFRRAgFPDGCFQTLLVGSGAVEAILRDPrVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVmpSAD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 235 vpLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQRVDDFVDAYrsvVQRFYPQVEGNP-DYTSIIN--ARQQQR--LQGYL 309
Cdd:PRK09406 246 --LDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKF---VARMAALRVGDPtDPDTDVGplATEQGRdeVEKQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 310 DDARAKGAEVIAlTAEATDRR---MPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDR 386
Cdd:PRK09406 321 DDAVAAGATILC-GGKRPDGPgwfYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDE 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2068619660 387 REQQHVLHHSHSGGVCLNDtlLHVAQDDMPFGGIGASGMGHYHGHEGFLTFSKAKGVLI 445
Cdd:PRK09406 400 AEQERFIDDLEAGQVFING--MTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVWI 456
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
116-445 |
1.52e-40 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 151.57 E-value: 1.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 116 PLGVVGIIVPWNYPLFLAI---APlvgALAAGNRVMLKLSEATPQTSqhLKelLASIF-----PEELVSVVLGEAEIGMA 187
Cdd:PRK13252 142 PLGVCAGIGAWNYPIQIACwksAP---ALAAGNAMIFKPSEVTPLTA--LK--LAEIYteaglPDGVFNVVQGDGRVGAW 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 188 FARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPR 266
Cdd:PRK13252 215 LTEHPdIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQK 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 267 QRVDDFVDAYRSVVQRFypqVEGNP-----DYTSIINARQQQRLQGYLDDARAKGAEVIALTAEATDRRMPQ------TL 335
Cdd:PRK13252 295 SIKAAFEARLLERVERI---RIGDPmdpatNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANgafvapTV 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 336 LLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDTLLHVAQddM 415
Cdd:PRK13252 372 FTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAE--M 449
|
330 340 350
....*....|....*....|....*....|
gi 2068619660 416 PFGGIGASGMGHYHGHEGFLTFSKAKGVLI 445
Cdd:PRK13252 450 PVGGYKQSGIGRENGIATLEHYTQIKSVQV 479
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
115-444 |
3.82e-40 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 150.74 E-value: 3.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 115 QPLGVVGIIVPWNYP---LFLAIAPlvgALAAGNRVMLKLSEATPQTSQHLKEL--LASIfPEELVSVVLGEAEI-GMAF 188
Cdd:PLN02766 157 EPIGVVGHIIPWNFPstmFFMKVAP---ALAAGCTMVVKPAEQTPLSALFYAHLakLAGV-PDGVINVVTGFGPTaGAAI 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 189 A-RLPFDHLLFTGATSIGRHVMRAAA-DNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPR 266
Cdd:PLN02766 233 AsHMDVDKVSFTGSTEVGRKIMQAAAtSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 267 QRVDDFVdayRSVVQRFYPQVEGNP-DYTS----IINARQQQRLQGYLDDARAKGAEVIALTAEATDR--RMPQTLLLNV 339
Cdd:PLN02766 313 GIYDEFV---KKLVEKAKDWVVGDPfDPRArqgpQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKgyYIEPTIFTDV 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 340 DDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNdtlLHVAQD-DMPFG 418
Cdd:PLN02766 390 TEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN---CYFAFDpDCPFG 466
|
330 340
....*....|....*....|....*.
gi 2068619660 419 GIGASGMGHYHGHEGFLTFSKAKGVL 444
Cdd:PLN02766 467 GYKMSGFGRDQGMDALDKYLQVKSVV 492
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
112-426 |
6.33e-40 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 150.06 E-value: 6.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 112 VIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELL--ASIfPEELVSVVLGEA-EIGMAF 188
Cdd:PRK11241 142 VIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAirAGI-PAGVFNVVTGSAgAVGGEL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 189 ARLPF-DHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQ 267
Cdd:PRK11241 221 TSNPLvRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 268 RVDDFVDAYRSVVQRFY--PQVEGNPDYTSIINARQQQRLQGYLDDARAKGAEVIA---LTAEATDRRMPqTLLLNVDDS 342
Cdd:PRK11241 301 VYDRFAEKLQQAVSKLHigDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCggkAHELGGNFFQP-TILVDVPAN 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 343 MLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDTLlhVAQDDMPFGGIGA 422
Cdd:PRK11241 380 AKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGI--ISNEVAPFGGIKA 457
|
....
gi 2068619660 423 SGMG 426
Cdd:PRK11241 458 SGLG 461
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
12-426 |
1.35e-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: 146.60 E-value: 1.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 12 IAELQQRFQAQREAFMANPMPSADQRIAWLdsLKAAlladqdALVRCISEDFgnrSADETL---------LAEMLPTVQG 82
Cdd:cd07124 68 KEEAEAAVQAARAAFPTWRRTPPEERARLL--LRAA------ALLRRRRFEL---AAWMVLevgknwaeaDADVAEAIDF 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 83 IRYARKRLRRWMKPSRRHVGlafmPASARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHL 162
Cdd:cd07124 137 LEYYAREMLRLRGFPVEMVP----GEDNRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 163 KELLASI-FPEELVSVVLGE-AEIGMAFARLPFDHLL-FTGATSIGRHVMRAAA------DNLTPVTLELGGKSPAIISA 233
Cdd:cd07124 213 VEILEEAgLPPGVVNFLPGPgEEVGDYLVEHPDVRFIaFTGSREVGLRIYERAAkvqpgqKWLKRVIAEMGGKNAIIVDE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 234 DVPLEHAAERI---AFGKtlnAGQTCVAPDYVLVPRQRVDDFVDayrSVVQRFYPQVEGNPDYTS-----IINARQQQRL 305
Cdd:cd07124 293 DADLDEAAEGIvrsAFGF---QGQKCSACSRVIVHESVYDEFLE---RLVERTKALKVGDPEDPEvymgpVIDKGARDRI 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 306 QGYLDDARAKGAEVIALTAEATDRR---MPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYF 382
Cdd:cd07124 367 RRYIEIGKSEGRLLLGGEVLELAAEgyfVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVF 446
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2068619660 383 GYDRREQQHVLHHSHSGGVCLNDTLLHVAQDDMPFGGIGASGMG 426
Cdd:cd07124 447 SRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTG 490
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
8-426 |
3.47e-38 |
|
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: 144.48 E-value: 3.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 8 VEQAIAELQQRFQAQreafmANPMPsADQRIAWLDSLkAALLADQ-DALVRCISEDFGNRSADEtlLAEMLPTVQGIRYA 86
Cdd:cd07148 23 IDKALDTAHALFLDR-----NNWLP-AHERIAILERL-ADLMEERaDELALLIAREGGKPLVDA--KVEVTRAIDGVELA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 87 RKRLRrwmKPSRRHVGLAFMPASA-RVIY---QPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHL 162
Cdd:cd07148 94 ADELG---QLGGREIPMGLTPASAgRIAFttrEPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 163 KELLASI-FPEELVSVVLGEAEIGMAFA---RLPFdhLLFTGATSIGRHvMRAAADNLTPVTLELGGKSPAIISADVPLE 238
Cdd:cd07148 171 VDLLHEAgLPEGWCQAVPCENAVAEKLVtdpRVAF--FSFIGSARVGWM-LRSKLAPGTRCALEHGGAAPVIVDRSADLD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 239 HAAERIAFGKTLNAGQTCVAPDYVLVPRQRVDDFVDAYRSVVQRFypqVEGNP-----DYTSIINARQQQRLQGYLDDAR 313
Cdd:cd07148 248 AMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKL---VVGDPtdpdtEVGPLIRPREVDRVEEWVNEAV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 314 AKGAEVIALTAEATDRRMPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVL 393
Cdd:cd07148 325 AAGARLLCGGKRLSDTTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAV 404
|
410 420 430
....*....|....*....|....*....|....*
gi 2068619660 394 HHSHSGGVCLNDtllHVA--QDDMPFGGIGASGMG 426
Cdd:cd07148 405 RRLDATAVMVND---HTAfrVDWMPFAGRRQSGYG 436
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
8-374 |
2.30e-34 |
|
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: 134.18 E-value: 2.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 8 VEQAIAELQQRFQAQREAfmanPMPSadqRIAWLDSLKAALLADQDALVRCISEDFGNRSADEtlLAEMLPTVQGIRYA- 86
Cdd:cd07085 40 VDAAVAAAKAAFPAWSAT----PVLK---RQQVMFKFRQLLEENLDELARLITLEHGKTLADA--RGDVLRGLEVVEFAc 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 87 ---RKRLRRWMKPSRRHVglafmpaSARVIYQPLGVVGIIVPWNYPLF--LAIAPLvgALAAGNRVMLKLSEATPQTSQH 161
Cdd:cd07085 111 sipHLLKGEYLENVARGI-------DTYSYRQPLGVVAGITPFNFPAMipLWMFPM--AIACGNTFVLKPSERVPGAAMR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 162 LKELLASI-FPEELVSVVLGEAEIGmafarlpfDHLL---------FTGATSIGRHVMRAAADNLTPVTLELGGKSPAII 231
Cdd:cd07085 182 LAELLQEAgLPDGVLNVVHGGKEAV--------NALLdhpdikavsFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 232 SADVPLEHAAERI---AFGktlNAGQTCVAPDYVLVPRQRVDDFVDAYRSVVQ--RFYPQVEGNPDYTSIINARQQQRLQ 306
Cdd:cd07085 254 MPDADLEQTANALvgaAFG---AAGQRCMALSVAVAVGDEADEWIPKLVERAKklKVGAGDDPGADMGPVISPAAKERIE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 307 GYLDDARAKGAEVIaltaeaTDRRMPQ------------TLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARP 374
Cdd:cd07085 331 GLIESGVEEGAKLV------LDGRGVKvpgyengnfvgpTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANP 404
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
8-424 |
1.34e-31 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 126.61 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 8 VEQAIaelqqrfQAQREAFMANPMPSADQRIAWLDSLKAALLADQDALVRCISEDFGN---RSADEtlLAEMLPTVqGIR 84
Cdd:PRK09457 39 VDAAV-------RAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKplwEAATE--VTAMINKI-AIS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 85 YARKRLRRWMKPSRrhvglafMPASARVI-YQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSqhlk 163
Cdd:PRK09457 109 IQAYHERTGEKRSE-------MADGAAVLrHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVA---- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 164 ELLASIF-----PEELVSVVLGEAEIGMAFARLP-FDHLLFTGATSIGRHVMRAAADNltP---VTLELGGKSPAIISAD 234
Cdd:PRK09457 178 ELTVKLWqqaglPAGVLNLVQGGRETGKALAAHPdIDGLLFTGSANTGYLLHRQFAGQ--PekiLALEMGGNNPLVIDEV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 235 VPLEHAAERI---AFgktLNAGQTCVAPDYVLVPR-QRVDDFVDAYRSVVQRF---YPQVEGNPDYTSIINARQQQRLQG 307
Cdd:PRK09457 256 ADIDAAVHLIiqsAF---ISAGQRCTCARRLLVPQgAQGDAFLARLVAVAKRLtvgRWDAEPQPFMGAVISEQAAQGLVA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 308 YLDDARAKGAEVIaltAEATdRRMPQTLLL--------NVDDsmlVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLAL 379
Cdd:PRK09457 333 AQAQLLALGGKSL---LEMT-QLQAGTGLLtpgiidvtGVAE---LPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSA 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2068619660 380 YYFGYDRREQQHVLHHSHSGGVCLNDTLLHvAQDDMPFGGIGASG 424
Cdd:PRK09457 406 GLLSDDREDYDQFLLEIRAGIVNWNKPLTG-ASSAAPFGGVGASG 449
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
2-436 |
3.01e-27 |
|
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: 114.21 E-value: 3.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 2 VTPFGPVEQAI-------AELQQRFQAQREAFMANPMPSADQRIAWLDSLKAALLADQDALVRCISEDFGNRSADEtlLA 74
Cdd:cd07083 37 VSPFAPSEVVGttakadkAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEA--ID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 75 EMLPTVQGIRYARKRLRRWMKPSRRHVGlaFMPASARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEA 154
Cdd:cd07083 115 DVAEAIDFIRYYARAALRLRYPAVEVVP--YPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAED 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 155 TPQTSQHLKELLASI-FPEELVSVVLGE-AEIGMAFA---RLPFdhLLFTGATSIGRHVMRAAADNLT------PVTLEL 223
Cdd:cd07083 193 AVVVGYKVFEIFHEAgFPPGVVQFLPGVgEEVGAYLTeheRIRG--INFTGSLETGKKIYEAAARLAPgqtwfkRLYVET 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 224 GGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQRVDDFVDAYRSVVQRFY--PQVEGNPDYTSIINARQ 301
Cdd:cd07083 271 GGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSvgPPEENGTDLGPVIDAEQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 302 QQRLQGYLDDARAKGAEVIALTAEATDRR-MPQTLLLNVDDSMLVMQDEIFGPLLPV--VPYDCLDDALAYITARPRPLA 378
Cdd:cd07083 351 EAKVLSYIEHGKNEGQLVLGGKRLEGEGYfVAPTVVEEVPPKARIAQEEIFGPVLSVirYKDDDFAEALEVANSTPYGLT 430
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2068619660 379 LyyfGYDRREQQHVLHHS---HSGGVCLNDTLLHVAQDDMPFGGIGASGMGHYHGHEGFLT 436
Cdd:cd07083 431 G---GVYSRKREHLEEARrefHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHYLR 488
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
114-369 |
3.12e-27 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 113.84 E-value: 3.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 114 YQPLGVVGIIVPWNYPLF-----LAIAplvgaLAAGNRVMLKLSEATPQTSQHLKELLASIF-----PEELVSVVLGEAE 183
Cdd:cd07130 130 WNPLGVVGVITAFNFPVAvwgwnAAIA-----LVCGNVVVWKPSPTTPLTAIAVTKIVARVLeknglPGAIASLVCGGAD 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 184 IGMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYV 262
Cdd:cd07130 205 VGEALVKDPrVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 263 LVPRQRVDDFVDAyrsvVQRFYPQVE-GNPD-----YTSIINARQQQRLQGYLDDARAKGAEVIAlTAEATDRR----MP 332
Cdd:cd07130 285 IVHESIYDEVLER----LKKAYKQVRiGDPLddgtlVGPLHTKAAVDNYLAAIEEAKSQGGTVLF-GGKVIDGPgnyvEP 359
|
250 260 270
....*....|....*....|....*....|....*..
gi 2068619660 333 QTLLLNVDDSmlVMQDEIFGPLLPVVPYDCLDDALAY 369
Cdd:cd07130 360 TIVEGLSDAP--IVKEETFAPILYVLKFDTLEEAIAW 394
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
111-367 |
9.67e-27 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 112.72 E-value: 9.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 111 RVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASI-FPEELVSVVLGE-AEIGMAF 188
Cdd:PRK03137 166 RYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAgLPAGVVNFVPGSgSEVGDYL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 189 ARLPFDHLL-FTGATSIGRHVMRAAADN------LTPVTLELGGKSPAIISADVPLEHAAERI---AFGktlNAGQTCVA 258
Cdd:PRK03137 246 VDHPKTRFItFTGSREVGLRIYERAAKVqpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIvasAFG---FSGQKCSA 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 259 PDYVLVPRQRVDDFVDAyrsVVQRFYPQVEGNP----DYTSIINARQQQRLQGYLDDARAKGAEViaLTAEATDRR---M 331
Cdd:PRK03137 323 CSRAIVHEDVYDEVLEK---VVELTKELTVGNPednaYMGPVINQASFDKIMSYIEIGKEEGRLV--LGGEGDDSKgyfI 397
|
250 260 270
....*....|....*....|....*....|....*.
gi 2068619660 332 PQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDAL 367
Cdd:PRK03137 398 QPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHAL 433
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
116-426 |
1.71e-25 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 109.08 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 116 PLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKE-LLASIFPEELVSVVLGE-AEIGMAFARLP- 192
Cdd:PLN00412 158 PLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHcFHLAGFPKGLISCVTGKgSEIGDFLTMHPg 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 193 FDHLLFTGATSiGRHVMRAAAdnLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQRVDDF 272
Cdd:PLN00412 238 VNCISFTGGDT-GIAISKKAG--MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADAL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 273 VDAYRSVVQRF-YPQVEGNPDYTSIINARQQQRLQGYLDDARAKGAevialTAEATDRR----MPQTLLLNVDDSMLVMQ 347
Cdd:PLN00412 315 VEKVNAKVAKLtVGPPEDDCDITPVVSESSANFIEGLVMDAKEKGA-----TFCQEWKRegnlIWPLLLDNVRPDMRIAW 389
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068619660 348 DEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDTLLHvAQDDMPFGGIGASGMG 426
Cdd:PLN00412 390 EEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPAR-GPDHFPFQGLKDSGIG 467
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
98-426 |
3.30e-25 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 108.44 E-value: 3.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 98 RRHVGLAFMPASA----RVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELL--ASIfP 171
Cdd:cd07125 145 RELFSDPELPGPTgelnGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLheAGV-P 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 172 EELVSVVLGE-AEIGMAFARLP-FDHLLFTGATSIGRHVMRAAADN---LTPVTLELGGKSPAIISADVPLEHAAERI-- 244
Cdd:cd07125 224 RDVLQLVPGDgEEIGEALVAHPrIDGVIFTGSTETAKLINRALAERdgpILPLIAETGGKNAMIVDSTALPEQAVKDVvq 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 245 -AFGktlNAGQTCVAPDYVLVPRQRVDDF----VDAYRSVVqrfypqVeGNP-----DYTSIINARQQQRLQGYLDDARA 314
Cdd:cd07125 304 sAFG---SAGQRCSALRLLYLQEEIAERFiemlKGAMASLK------V-GDPwdlstDVGPLIDKPAGKLLRAHTELMRG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 315 KGAEVIALTAEATDRR-MPQTLLLNVDDSMLvmQDEIFGPLLPVVPYDC--LDDALAYITARprplalyyfGY------- 384
Cdd:cd07125 374 EAWLIAPAPLDDGNGYfVAPGIIEIVGIFDL--TTEVFGPILHVIRFKAedLDEAIEDINAT---------GYgltlgih 442
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2068619660 385 --DRREQQHVLHHSHSGGVCLNdtllhvaqDDM--------PFGGIGASGMG 426
Cdd:cd07125 443 srDEREIEYWRERVEAGNLYIN--------RNItgaivgrqPFGGWGLSGTG 486
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
115-426 |
1.67e-22 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 99.98 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 115 QPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASI-FPEELVSVVLGE-AEIGMAFARLP 192
Cdd:TIGR01238 159 ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAgFPAGTIQLLPGRgADVGAALTSDP 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 193 -FDHLLFTGATSIGRHVMRAAA---DNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQR 268
Cdd:TIGR01238 239 rIAGVAFTGSTEVAQLINQTLAqreDAPVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDV 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 269 VDDFVDAYRSVVQRFypqVEGNP-----DYTSIINARQQQRLQGYLDDARAKGAEVIALTAEATDRRMPQTLL---LNVD 340
Cdd:TIGR01238 319 ADRVLTMIQGAMQEL---KVGVPhllttDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDSRACQHGTFVaptLFEL 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 341 DSMLVMQDEIFGPLLPVVPY--DCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDTLLHVAQDDMPFG 418
Cdd:TIGR01238 396 DDIAELSEEVFGPVLHVVRYkaRELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFG 475
|
....*...
gi 2068619660 419 GIGASGMG 426
Cdd:TIGR01238 476 GQGLSGTG 483
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
15-378 |
5.04e-21 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 95.38 E-value: 5.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 15 LQQRFQAQREAFMANPMPSADQRiawldslkAALLADQDALVRCISEDFGNRSADETLLAEMLPTVQGIRYARKRLRRWM 94
Cdd:cd07084 1 PERALLAADISTKAARRLALPKR--------ADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 95 KPSRR-------HVGLAFMPASARVIYqPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELL- 166
Cdd:cd07084 73 IYSYRiphepgnHLGQGLKQQSHGYRW-PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLh 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 167 -ASIFPEELVSVVLGEAEIGMAFARLP-FDHLLFTGATSIGRHVMRAAADnlTPVTLELGGKSPAIISADVP-LEHAAER 243
Cdd:cd07084 152 yAGLLPPEDVTLINGDGKTMQALLLHPnPKMVLFTGSSRVAEKLALDAKQ--ARIYLELAGFNWKVLGPDAQaVDYVAWQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 244 IAFGKTLNAGQTCVAPDYVLVPRQrvddfvDAYRSVVQRFYPQVEGNPDYTSIINARQQQRLQGYLDDARAKGAEVIAL- 322
Cdd:cd07084 230 CVQDMTACSGQKCTAQSMLFVPEN------WSKTPLVEKLKALLARRKLEDLLLGPVQTFTTLAMIAHMENLLGSVLLFs 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068619660 323 TAEATDRRMPQTLLLNVDDSMLVMQD-----------EIFGPLLPVVPYDclDDALAYITARPRPLA 378
Cdd:cd07084 304 GKELKNHSIPSIYGACVASALFVPIDeilktyelvteEIFGPFAIVVEYK--KDQLALVLELLERMH 368
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
8-382 |
6.53e-18 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 86.04 E-value: 6.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 8 VEQAIAELQQRFQAQREA---FMANPMPSADQRIAWL-DSLKAALladqDALVRCISEDFGNrsadetLLAEMLPTVQGI 83
Cdd:PLN02315 51 VEASLEDYEEGLRACEEAakiWMQVPAPKRGEIVRQIgDALRAKL----DYLGRLVSLEMGK------ILAEGIGEVQEI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 84 ----RYA---RKRLRRWMKPSRR--HVGLAfmpasarvIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEA 154
Cdd:PLN02315 121 idmcDFAvglSRQLNGSIIPSERpnHMMME--------VWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 155 TPQTSQHLKELLASIF-----PEELVSVVLGEAEIGMAFA---RLPFdhLLFTGATSIGRHVMRAAADNLTPVTLELGGK 226
Cdd:PLN02315 193 TPLITIAMTKLVAEVLeknnlPGAIFTSFCGGAEIGEAIAkdtRIPL--VSFTGSSKVGLMVQQTVNARFGKCLLELSGN 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 227 SPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPRQRVDDFVDAYRSVvqrfYPQVE-GNP-DYTSIIN-----A 299
Cdd:PLN02315 271 NAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTV----YKQVKiGDPlEKGTLLGplhtpE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 300 RQQQRLQGyLDDARAKGAEVI-ALTAEATDRRMPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLA 378
Cdd:PLN02315 347 SKKNFEKG-IEIIKSQGGKILtGGSAIESEGNFVQPTIVEISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLS 425
|
....
gi 2068619660 379 LYYF 382
Cdd:PLN02315 426 SSIF 429
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
114-449 |
1.34e-16 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 83.10 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 114 YQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTS-QHLKELLASIFPEELVSVVLGEAE-IGmafARL 191
Cdd:PRK11809 766 HRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAaQAVRILLEAGVPAGVVQLLPGRGEtVG---AAL 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 192 PFDH----LLFTGATSIGRHVMRAAADNL------TPVTLELGGKSPAII--SAdvplehAAERI-------AFGktlNA 252
Cdd:PRK11809 843 VADArvrgVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVdsSA------LTEQVvadvlasAFD---SA 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 253 GQTCVAPDyVLVPRQRVDDFV-----DAYRSVVQrfypqveGNPDYTS-----IINARQQQRLQGYLDDARAKGAEVI-A 321
Cdd:PRK11809 914 GQRCSALR-VLCLQDDVADRTlkmlrGAMAECRM-------GNPDRLStdigpVIDAEAKANIERHIQAMRAKGRPVFqA 985
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 322 LTAEATDRR----MPQTL--LLNVDDsmlvMQDEIFGPLLPVVPY--DCLDDALAYITARPRPLALyyfGYDRR--EQ-Q 390
Cdd:PRK11809 986 ARENSEDWQsgtfVPPTLieLDSFDE----LKREVFGPVLHVVRYnrNQLDELIEQINASGYGLTL---GVHTRidETiA 1058
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2068619660 391 HVLHHSHSGGVCLNDTLLHVAQDDMPFGGIGASGMGhyhghegfltfSKAKGVLIKQRL 449
Cdd:PRK11809 1059 QVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTG-----------PKAGGPLYLYRL 1106
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
8-368 |
4.57e-16 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 80.28 E-value: 4.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 8 VEQAIAELQQRFQAQREAfmanpmpSADQRIAWLDSLKAALLADQDALVrcisedfgNRSADETLLAEML------PTVQ 81
Cdd:cd07129 1 VDAAAAAAAAAFESYRAL-------SPARRAAFLEAIADEIEALGDELV--------ARAHAETGLPEARlqgelgRTTG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 82 GIRYARKRLRR--WMKPSRRHVGLAFMPASA---RVIYQPLGVVGIIVPWNYPLFLAIAplvG-----ALAAGNRVMLKL 151
Cdd:cd07129 66 QLRLFADLVREgsWLDARIDPADPDRQPLPRpdlRRMLVPLGPVAVFGASNFPLAFSVA---GgdtasALAAGCPVVVKA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 152 SEATPQTSqhlkELLASI---------FPEELVSVVLG-EAEIGMAFARlpfdHLL-----FTGATSIGRHVMRAAADNL 216
Cdd:cd07129 143 HPAHPGTS----ELVARAiraalratgLPAGVFSLLQGgGREVGVALVK----HPAikavgFTGSRRGGRALFDAAAARP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 217 T--PVTLELGGKSPAIISADVpLEHAAERIAFGK----TLNAGQTCVAPDYVLVPR-QRVDDFVDAYRSVVQRFYPQVEG 289
Cdd:cd07129 215 EpiPFYAELGSVNPVFILPGA-LAERGEAIAQGFvgslTLGAGQFCTNPGLVLVPAgPAGDAFIAALAEALAAAPAQTML 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 290 NPdytSIINARQQ--QRLQGylddarAKGAEVIALTAEATDRRMPQTLLLNVDDSML----VMQDEIFGPLLPVVPYDCL 363
Cdd:cd07129 294 TP---GIAEAYRQgvEALAA------APGVRVLAGGAAAEGGNQAAPTLFKVDAAAFladpALQEEVFGPASLVVRYDDA 364
|
....*
gi 2068619660 364 DDALA 368
Cdd:cd07129 365 AELLA 369
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
110-449 |
5.17e-16 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 79.91 E-value: 5.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 110 ARVIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELLASI-FPE----------ELVSVV 178
Cdd:PRK13968 120 AVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDAgIPQgvygwlnadnDGVSQM 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 179 LGEAEIGMafarlpfdhLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVA 258
Cdd:PRK13968 200 INDSRIAA---------VTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAA 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 259 PDYVLVPRQRVDDFVDAYRSVVQRFY---PQVEGN---PDYTSIINARQQQRLQGYLDD-AR-AKGAEVIAltaeATDRR 330
Cdd:PRK13968 271 AKRFIIEEGIASAFTERFVAAAAALKmgdPRDEENalgPMARFDLRDELHHQVEATLAEgARlLLGGEKIA----GAGNY 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 331 MPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAYITARPRPLALYYFGYDRREQQHVLHHSHSGGVCLNDtllHV 410
Cdd:PRK13968 347 YAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFING---YC 423
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2068619660 411 AQD-DMPFGGIGASGMGHYHGHEGFLTFSKAKGVLiKQRL 449
Cdd:PRK13968 424 ASDaRVAFGGVKKSGFGRELSHFGLHEFCNIQTVW-KDRI 462
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
111-455 |
1.42e-15 |
|
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: 78.78 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 111 RVIYQPL-GVVGIIVPWNyplFLAIAP-LVGALA-AGNRVMLKLSEaTPQTSQHL--KELLASIFPEELVSVVLGEAE-I 184
Cdd:cd07123 164 RLEYRPLeGFVYAVSPFN---FTAIGGnLAGAPAlMGNVVLWKPSD-TAVLSNYLvyKILEEAGLPPGVINFVPGDGPvV 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 185 G-MAFARLPFDHLLFTGATSIGRHVMRAAADNLT-----P-VTLELGGKSPAII--SADV-PLEHAAERIAFGKtlnAGQ 254
Cdd:cd07123 240 GdTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDryrtyPrIVGETGGKNFHLVhpSADVdSLVTATVRGAFEY---QGQ 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 255 TCVAPDYVLVPRQRVDDFvdayRSVVQRFYPQVE-GNP-DYTSIINA----RQQQRLQGYLDDARA-KGAEVIAlTAEAT 327
Cdd:cd07123 317 KCSAASRAYVPESLWPEV----KERLLEELKEIKmGDPdDFSNFMGAvideKAFDRIKGYIDHAKSdPEAEIIA-GGKCD 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 328 DRR---MPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDclDDALAYI-----TARPRPLALYYFGYDR---REQQHVLHHS 396
Cdd:cd07123 392 DSVgyfVEPTVIETTDPKHKLMTEEIFGPVLTVYVYP--DSDFEETlelvdTTSPYALTGAIFAQDRkaiREATDALRNA 469
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2068619660 397 hSGGVCLND--TLLHVAQDdmPFGGIGASGmghyhghegflTFSKAKGVLIKQRLNLARLI 455
Cdd:cd07123 470 -AGNFYINDkpTGAVVGQQ--PFGGARASG-----------TNDKAGSPLNLLRWVSPRTI 516
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
8-449 |
2.76e-13 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 72.59 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 8 VEQAIAelqqrfqAQREAFMANPMPSADQRIAWLDSLKAALLADQDALVRCISedfgnRSADETL---LAEMLPTVQGIR 84
Cdd:PRK11905 592 VERALA-------AAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAV-----REAGKTLanaIAEVREAVDFLR 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 85 YARKRLRRWMKPSRRhvglafmpasarviyQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKE 164
Cdd:PRK11905 660 YYAAQARRLLNGPGH---------------KPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVR 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 165 LL--ASIfPEELVSVVLGE-AEIGMAFARLP-FDHLLFTGATSIGRHVMRAAADNLTPvtlelggkspaiisaDVPLeha 240
Cdd:PRK11905 725 LLheAGV-PKDALQLLPGDgRTVGAALVADPrIAGVMFTGSTEVARLIQRTLAKRSGP---------------PVPL--- 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 241 aerIAfgKTlnAGQTCVAPDYVLVPRQRVDDFV-DAYRSVVQR------FYPQ------------------VEGNPDYTS 295
Cdd:PRK11905 786 ---IA--ET--GGQNAMIVDSSALPEQVVADVIaSAFDSAGQRcsalrvLCLQedvadrvltmlkgamdelRIGDPWRLS 858
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 296 -----IINARQQQRLQGYLDDARAKGAEVIALTAEATDRR----MPQTLLLnvdDSMLVMQDEIFGPLLPVVPY--DCLD 364
Cdd:PRK11905 859 tdvgpVIDAEAQANIEAHIEAMRAAGRLVHQLPLPAETEKgtfvAPTLIEI---DSISDLEREVFGPVLHVVRFkaDELD 935
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 365 DALAYITARprplalyyfGY----------DRReQQHVLHHSHSGGVCLNDTLLHVAQDDMPFGGIGASGMGhyhghegf 434
Cdd:PRK11905 936 RVIDDINAT---------GYgltfglhsriDET-IAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTG-------- 997
|
490
....*....|....*
gi 2068619660 435 ltfSKAKGVLIKQRL 449
Cdd:PRK11905 998 ---PKAGGPLYLGRL 1009
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
113-370 |
2.24e-12 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 69.00 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 113 IYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKEL-LASIFPEELVSVVLGEAEIGMAFA-R 190
Cdd:PLN02419 246 IREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELaMEAGLPDGVLNIVHGTNDTVNAICdD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 191 LPFDHLLFTGATSIGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLV---PRQ 267
Cdd:PLN02419 326 EDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFvgdAKS 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 268 RVDDFVDayRSVVQRFYPQVEGNPDYTSIINARQQQR----LQGYLDDARA---KGAEVIALTAEATDRRMPqTLLLNVD 340
Cdd:PLN02419 406 WEDKLVE--RAKALKVTCGSEPDADLGPVISKQAKERicrlIQSGVDDGAKlllDGRDIVVPGYEKGNFIGP-TILSGVT 482
|
250 260 270
....*....|....*....|....*....|
gi 2068619660 341 DSMLVMQDEIFGPLLPVVPYDCLDDALAYI 370
Cdd:PLN02419 483 PDMECYKEEIFGPVLVCMQANSFDEAISII 512
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
109-368 |
3.46e-11 |
|
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: 65.37 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 109 SARVIYQPLGVVGI-IVPWNYP---LFLAIAPlvgALAAGNRVMLKLSEATPQTSQHL-KELLAS-IFPEELVSVVLGEA 182
Cdd:cd07128 136 VGQHILTPRRGVAVhINAFNFPvwgMLEKFAP---ALLAGVPVIVKPATATAYLTEAVvKDIVESgLLPEGALQLICGSV 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 183 eiGMAFARL-PFDHLLFTGATSIGRHVMR--AAADNLTPVTLELGGKSPAIISADVPlEHAAERIAFGK------TLNAG 253
Cdd:cd07128 213 --GDLLDHLgEQDVVAFTGSAATAAKLRAhpNIVARSIRFNAEADSLNAAILGPDAT-PGTPEFDLFVKevaremTVKAG 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 254 QTCVAPDYVLVPRQRVDDFVDAYRSvvqRFYPQVEGNP-----DYTSIINARQQQRLQGYLDDARAkGAEVIA-----LT 323
Cdd:cd07128 290 QKCTAIRRAFVPEARVDAVIEALKA---RLAKVVVGDPrlegvRMGPLVSREQREDVRAAVATLLA-EAEVVFggpdrFE 365
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2068619660 324 AEATDRR----MPQTLLL--NVDDSMLVMQDEIFGPLLPVVPYDCLDDALA 368
Cdd:cd07128 366 VVGADAEkgafFPPTLLLcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIE 416
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
109-361 |
1.59e-10 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 63.80 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 109 SARVIYQPLGVVGIIVPWNYPlfLAI--APLVGALAAGNRVMLKLSEATPQTSQHLKELL--ASIfPEELVSVVLGE-AE 183
Cdd:COG4230 673 AAPTVLRGRGVFVCISPWNFP--LAIftGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLheAGV-PADVLQLLPGDgET 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 184 IGmafARLPFDHL----LFTGATSIGRHVMRA-AADNLTPVTL--ELGGKSPAIISADVPLEHAAERI---AFGktlNAG 253
Cdd:COG4230 750 VG---AALVADPRiagvAFTGSTETARLINRTlAARDGPIVPLiaETGGQNAMIVDSSALPEQVVDDVlasAFD---SAG 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 254 QTCVAPDYVLVPRQRVDDFVDAYRSVVQRFypqVEGNPDYTS-----IINARQQQRLQGYLDDARAKGAEVIALTAEATD 328
Cdd:COG4230 824 QRCSALRVLCVQEDIADRVLEMLKGAMAEL---RVGDPADLStdvgpVIDAEARANLEAHIERMRAEGRLVHQLPLPEEC 900
|
250 260 270
....*....|....*....|....*....|....*...
gi 2068619660 329 RR---MPQTL--LLNVDDsmlvMQDEIFGPLLPVVPYD 361
Cdd:COG4230 901 ANgtfVAPTLieIDSISD----LEREVFGPVLHVVRYK 934
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
92-367 |
7.48e-10 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 60.96 E-value: 7.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 92 RWMKPSRRHVGLAfMPASARVIyqPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEAT----PQTSQHLKELLA 167
Cdd:cd07127 172 EWEKPQGKHDPLA-MEKTFTVV--PRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAAilplAITVQVAREVLA 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 168 SI-FPEELVSVVLG--EAEIGMAFARLPFDHLL-FTGATSIGRHVMRAAADNLtpVTLELGGKSPAIISADVPLEHAAER 243
Cdd:cd07127 249 EAgFDPNLVTLAADtpEEPIAQTLATRPEVRIIdFTGSNAFGDWLEANARQAQ--VYTEKAGVNTVVVDSTDDLKAMLRN 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 244 IAFGKTLNAGQTCVAPDYVLVPRQ--RVDDFVDAYRSVVQRFYPQVE---GNPDY-TSIINARQQQRLQGYLDDARAKGA 317
Cdd:cd07127 327 LAFSLSLYSGQMCTTPQNIYVPRDgiQTDDGRKSFDEVAADLAAAIDgllADPARaAALLGAIQSPDTLARIAEARQLGE 406
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2068619660 318 EVIALTAEA----TDRRMPQTLLLNVD--DSMLVMQdEIFGPLLPVVPYDCLDDAL 367
Cdd:cd07127 407 VLLASEAVAhpefPDARVRTPLLLKLDasDEAAYAE-ERFGPIAFVVATDSTDHSI 461
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
118-368 |
4.32e-09 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 58.56 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 118 GVVGIIVPWNYP---LFLAIAPlvgALAAGNRVMLKLSEATPQTSQHLKELL--ASIFPEELVSVVLGEAEiGMAFARLP 192
Cdd:PRK11903 150 GVALFINAFNFPawgLWEKAAP---ALLAGVPVIVKPATATAWLTQRMVKDVvaAGILPAGALSVVCGSSA-GLLDHLQP 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 193 FDHLLFTGATSIGRhVMR---AAADNLTPVTLELGGKSPAIISADVPLEHAA-----ERIAFGKTLNAGQTCVAPDYVLV 264
Cdd:PRK11903 226 FDVVSFTGSAETAA-VLRshpAVVQRSVRVNVEADSLNSALLGPDAAPGSEAfdlfvKEVVREMTVKSGQKCTAIRRIFV 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 265 PRQRVDDFVDAyrsVVQRFYPQVEGNPDYTSI-----INARQQQRLQGYLDDARAK------GAEVIALTAEATDRRMPQ 333
Cdd:PRK11903 305 PEALYDAVAEA---LAARLAKTTVGNPRNDGVrmgplVSRAQLAAVRAGLAALRAQaevlfdGGGFALVDADPAVAACVG 381
|
250 260 270
....*....|....*....|....*....|....*...
gi 2068619660 334 TLLLNVDD---SMLVMQDEIFGPLLPVVPYDCLDDALA 368
Cdd:PRK11903 382 PTLLGASDpdaATAVHDVEVFGPVATLLPYRDAAHALA 419
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
114-428 |
4.83e-09 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 58.67 E-value: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 114 YQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELL--ASIfPEELVSVVLGE-AEIGMAFAR 190
Cdd:PRK11904 682 LHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLheAGI-PKDVLQLLPGDgATVGAALTA 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 191 LP-FDHLLFTGATSIGRHVMRA-AADNLTPVTL--ELGGKSPAIISADVPLEHAAERI---AFGktlNAGQTCVAPDYVL 263
Cdd:PRK11904 761 DPrIAGVAFTGSTETARIINRTlAARDGPIVPLiaETGGQNAMIVDSTALPEQVVDDVvtsAFR---SAGQRCSALRVLF 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 264 VPRQRVDDFVDAYRSVVQRfypQVEGNP-----DYTSIINARQQQRLQGYLDDARaKGAEVIALTAEATDRRM-----PQ 333
Cdd:PRK11904 838 VQEDIADRVIEMLKGAMAE---LKVGDPrllstDVGPVIDAEAKANLDAHIERMK-REARLLAQLPLPAGTENghfvaPT 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 334 TLLLnvdDSMLVMQDEIFGPLLPVVPYDC--LDDALAYITARPRPLALyyfGYDRREQQHVLH---HSHSGGVCLNdtll 408
Cdd:PRK11904 914 AFEI---DSISQLEREVFGPILHVIRYKAsdLDKVIDAINATGYGLTL---GIHSRIEETADRiadRVRVGNVYVN---- 983
|
330 340 350
....*....|....*....|....*....|....
gi 2068619660 409 hvaqDDM--------PFGGIGASGMG------HY 428
Cdd:PRK11904 984 ----RNQigavvgvqPFGGQGLSGTGpkaggpHY 1013
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
112-368 |
1.39e-07 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 53.81 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 112 VIYQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQH-----LKELLASIFPEELVsVVLGEAEIGM 186
Cdd:cd07081 91 IIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRaatllLQAAVAAGAPENLI-GWIDNPSIEL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 187 AFARLPFDHLLFTGATSiGRHVMRAAADNLTPVTLELGGKSPAIISADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVpr 266
Cdd:cd07081 170 AQRLMKFPGIGLLLATG-GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIV-- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 267 qrVDDFVDAyrsVVQRFypqvEGNPDYtsIINARQQQRLQGYLDDARAKGAEVIALT----AEATDRRMPQTLLLNVDDS 342
Cdd:cd07081 247 --VDSVYDE---VMRLF----EGQGAY--KLTAEELQQVQPVILKNGDVNRDIVGQDaykiAAAAGLKVPQETRILIGEV 315
|
250 260 270
....*....|....*....|....*....|.
gi 2068619660 343 MLVMQDEIFG-----PLLPVVPYDCLDDALA 368
Cdd:cd07081 316 TSLAEHEPFAheklsPVLAMYRAANFADADA 346
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
114-440 |
1.16e-04 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 44.51 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 114 YQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELL-ASIF----PEELVSVV----LGEAEI 184
Cdd:PRK15398 127 YAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLnEAIVaaggPENLVVTVaeptIETAQR 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 185 GMAFARLPFdhLLFTGATSIGRHVMR-------AAADNltPvtlelggksPAIISADVPLEHAAERIAFGKTLNAGQTCV 257
Cdd:PRK15398 207 LMKHPGIAL--LVVTGGPAVVKAAMKsgkkaigAGAGN--P---------PVVVDETADIEKAARDIVKGASFDNNLPCI 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 258 APDYVLVprqrvddfVDayrSVVQRFYPQVEGNPDYtsIINARQQQRLQG--YLDDARA------KGAEVIALTAEATDR 329
Cdd:PRK15398 274 AEKEVIV--------VD---SVADELMRLMEKNGAV--LLTAEQAEKLQKvvLKNGGTVnkkwvgKDAAKILEAAGINVP 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 330 RMPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAyitarprpLALyyfgydrrEQQHVLHHS---HSGGVC-LN- 404
Cdd:PRK15398 341 KDTRLLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIA--------LAV--------KLEHGNRHTaimHSRNVDnLNk 404
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2068619660 405 -----DTLLHVaQDDMPFGGIGASGmghyhghEGFLTFSKA 440
Cdd:PRK15398 405 maraiQTSIFV-KNGPSYAGLGLGG-------EGFTTFTIA 437
|
|
| ALDH_Acyl-CoA-Red_LuxC |
cd07080 |
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase ... |
10-373 |
2.54e-04 |
|
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase enzyme responsible for synthesis of the aldehyde substrate for the luminescent reaction catalyzed by luciferase. The fatty acid reductase, a luminescence-specific, multienzyme complex (LuxCDE), reduces myristic acid to generate the long chain fatty aldehyde required for the luciferase-catalyzed reaction resulting in the emission of blue-green light. Mutational studies of conserved cysteines of LuxC revealed that the cysteine which aligns with the catalytic cysteine conserved throughout the ALDH superfamily is the LuxC acylation site. This CD is composed of mainly bacterial sequences but also includes a few archaeal sequences similar to the Methanospirillum hungateiacyl acyl-CoA reductase RfbN.
Pssm-ID: 143399 Cd Length: 422 Bit Score: 43.42 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 10 QAIAELQQRFQAQREAfmANPMPSaDQRIAWLDSLKAALLADQDALVRcisedfgnrsadetLLAEMLPTVQG-----IR 84
Cdd:cd07080 5 PDLDALIEELRLNRRA--LAALPV-EEIVDFLDRAGKRLLDPDYPLRQ--------------QAERLLPTVTGyseemLR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 85 YARKRLRRWMKPS------RRHVGLAFM-------PASARVIYQPLGVVGIIVPWNYPLfLAIAPLVGALAAGNRVMLKL 151
Cdd:cd07080 68 EGLKRLMALFRREnlerilERELGSPGIldewvppGRGGYIRAQPRGLVVHIIAGNVPL-LPVWSIVRGLLVKNVNLLKM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 152 SEATPQTSQHLKELLASIFPEELVSvvlgeaeigMAFARLPFDHllftGATSIGRHVMRAA--------------ADNLT 217
Cdd:cd07080 147 SSSDPLTATALLRSLADVDPNHPLT---------DSISVVYWPG----GDAELEERILASAdavvawggeeavkaIRSLL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 218 PVTLEL---GGK-SPAIIS----ADVPLEHAAERIAFGKTLNAGQTCVAPDYVLVPR---QRVDDF---VDAYRSVVQRF 283
Cdd:cd07080 214 PPGCRLidfGPKySFAVIDrealESEKLAEVADALAEDICRYDQQACSSPQVVFVEKdddEELREFaeaLAAALERLPRR 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 284 YPQVEGNPDYTS-IINARQQQRLqgylddarakgAEVIALTAEATDRRMpqtlllnvddsmlVMQDEI---FGPL---LP 356
Cdd:cd07080 294 YPALSLSAAESAkIARARLEAEF-----------YELKGGVSRDLGWTV-------------IISDEIgleASPLnrtVN 349
|
410
....*....|....*..
gi 2068619660 357 VVPYDCLDDALAYITAR 373
Cdd:cd07080 350 VKPVASLDDVLRPVTPY 366
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
116-235 |
4.04e-04 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 42.87 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 116 PLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELL--ASIFPEELVSVVLGEAEIGMAFARLPF 193
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLhlCGMPATDVDLIHSDGPTMNKILLEANP 221
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2068619660 194 DHLLFTGATSIGRHVMRAAADNltpVTLELGGKSPAIISADV 235
Cdd:cd07126 222 RMTLFTGSSKVAERLALELHGK---VKLEDAGFDWKILGPDV 260
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
114-440 |
1.02e-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: 41.45 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 114 YQPLGVVGIIVPWNYPLFLAIAPLVGALAAGNRVMLKLSEATPQTSQHLKELL-ASIF----PEELVSVV----LGEAEI 184
Cdd:cd07121 95 YAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELInKAIAeaggPDNLVVTVeeptIETTNE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 185 GMAFARLPFdhLLFTGATSIGRHVMR-------AAADNltPvtlelggksPAIISADVPLEHAAERIAFGKTLNAGQTCV 257
Cdd:cd07121 175 LMAHPDINL--LVVTGGPAVVKAALSsgkkaigAGAGN--P---------PVVVDETADIEKAARDIVQGASFDNNLPCI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 258 APDYVLVprqrVDdfvdayrSVVQRFYPQVEGNPDYtsIINARQ--QQRLQGYLDDARA--------KGAEVIALTAEAT 327
Cdd:cd07121 242 AEKEVIA----VD-------SVADYLIAAMQRNGAY--VLNDEQaeQLLEVVLLTNKGAtpnkkwvgKDASKILKAAGIE 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068619660 328 DRRMPQTLLLNVDDSMLVMQDEIFGPLLPVVPYDCLDDALAyitarprpLALyyfgydrrEQQHVLHHS---HSGGV-CL 403
Cdd:cd07121 309 VPADIRLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIE--------LAV--------ELEHGNRHTaiiHSKNVeNL 372
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2068619660 404 N------DTLLHVaQDDMPFGGIGASGmghyhghEGFLTFSKA 440
Cdd:cd07121 373 TkmaramQTTIFV-KNGPSYAGLGVGG-------EGYTTFTIA 407
|
|
| |
