|
Name |
Accession |
Description |
Interval |
E-value |
| fadJ |
PRK11154 |
fatty acid oxidation complex subunit alpha FadJ; |
2-609 |
2.16e-120 |
|
fatty acid oxidation complex subunit alpha FadJ;
Pssm-ID: 236864 [Multi-domain] Cd Length: 708 Bit Score: 373.46 E-value: 2.16e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIA--HAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNS 79
Cdd:PRK11154 112 CLGGGLELALACHYRVCtdDPKTVLGLPEVQLGLLPGSGGTQRLPRLIGVSTALDMILTGKQLRAKQALKLGLVDDVVPH 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 80 D-----PVEEAIRFAQRVSDQPLESRRLCNKPI-QSLpnmdsIFSEALLKMRRQHPGCL-AQEACVRAVQAAVQYPYEVG 152
Cdd:PRK11154 192 SillevAVELAKKGKPARRPLPVRERLLEGNPLgRAL-----LFKQARKKTLAKTQGNYpAPERILDVVRTGLEKGMSSG 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 153 IKKEEELFLYLLQSGQARALQYAFFAERKANKwstPSGASwktASARPVSSVGVVGLGTMGRGIV-ISFARARIPVIAVD 231
Cdd:PRK11154 267 YEAEARAFGELAMTPESAALRSIFFATTEMKK---DTGSD---AKPRPVNKVGVLGGGLMGGGIAyVTATKAGLPVRIKD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 232 SDKNQLATANKMITSVLEKE-------ASKMQQsghpwsgpKPRLTSSVKELGG---VDLVIEAVFEEMSLKKQVFAELS 301
Cdd:PRK11154 341 INPQGINHALKYSWDLLDKKvkrrhlkPSERDK--------QMALISGTTDYRGfkhADVVIEAVFEDLALKQQMVAEVE 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 302 AVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYSSPTTIATVMNLSKKIKKIGVVVGNCF 381
Cdd:PRK11154 413 QNCAPHTIFASNTSSLPIGQIAAAAARPEQVIGLHYFSPVEKMPLVEVIPHAKTSAETIATTVALAKKQGKTPIVVRDGA 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 382 GFVGNRMLNPYYNQAYFLLEEGSKPEEVDQVLEEFGFKMGPFRVSDLAGLDVGWKsrkgqglTGPTLLPGTPARKRGnrr 461
Cdd:PRK11154 493 GFYVNRILAPYINEAARLLLEGEPIEHIDAALVKFGFPVGPITLLDEVGIDVGTK-------IIPILEAALGERFSA--- 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 462 ycpiPDVLCEL---GRFGQKTGKGWYQYDKPLGRIHK-PDPWLSKFLSryrkthhIEPRT-ISQDEILERCLYSLINEAF 536
Cdd:PRK11154 563 ----PAAFDKLlndDRKGRKNGRGFYLYGQKGKKSKKqVDESVYPLLG-------ITPQSrLSANEIAERCVMLMLNEAV 631
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261878539 537 RILGEGIAASPEHIDVVYLHGYGWPRHKGGPMFYASTVGLPTVLEKLQKYYRQNPDipQLEPSDYLKKLASQG 609
Cdd:PRK11154 632 RCLDEGIIRSARDGDIGAVFGIGFPPFLGGPFRYMDSLGAGEVVAILERLAAQYGD--RFTPCERLVEMAERG 702
|
|
| fadB |
PRK11730 |
fatty acid oxidation complex subunit alpha FadB; |
1-609 |
2.41e-113 |
|
fatty acid oxidation complex subunit alpha FadB;
Pssm-ID: 183293 [Multi-domain] Cd Length: 715 Bit Score: 355.32 E-value: 2.41e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 1 MAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSD 80
Cdd:PRK11730 112 YALGGGCECVLATDYRVASPDARIGLPETKLGIMPGFGGTVRLPRLIGADNALEWIAAGKDVRAEDALKVGAVDAVVAPE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 81 PVEE-AIRFAQRVSDQPLE--SRRlcnKPIQS---LPNMDSIFSEALLKMR------RQHPgclAQEACVRAVQAAVQYP 148
Cdd:PRK11730 192 KLQEaALALLKQAIAGKLDwkARR---QPKLEplkLSKIEAMMSFTTAKGMvaqkagKHYP---APMTAVKTIEAAAGLG 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 149 YEVGIKKEEELFLYLLQSGQARALQYAFFAE----RKANKWStpsgaswktASARPVSSVGVVGLGTMGRGIVISFARAR 224
Cdd:PRK11730 266 RDEALELEAKGFVKLAKTNVARALVGIFLNDqyvkGKAKKLA---------KDAKPVKQAAVLGAGIMGGGIAYQSASKG 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 225 IPVIAVDSDKNQL----ATANKMITSVLEK---EASKMQQ---SGHPwsgpkprlTSSVKELGGVDLVIEAVFEEMSLKK 294
Cdd:PRK11730 337 VPVIMKDINQKALdlgmTEAAKLLNKQVERgkiDGAKMAGvlsSIRP--------TLDYAGFERVDVVVEAVVENPKVKA 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 295 QVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYSSPTTIATVMNLSKKIKKIG 374
Cdd:PRK11730 409 AVLAEVEQKVREDTILASNTSTISISLLAKALKRPENFCGMHFFNPVHRMPLVEVIRGEKTSDETIATVVAYASKMGKTP 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 375 VVVGNCFGFVGNRMLNPYYNQAYFLLEEGSKPEEVDQVLE-EFGFKMGPFRVSDLAGLDVGwksRKGQGLtgptLLPGTP 453
Cdd:PRK11730 489 IVVNDCPGFFVNRVLFPYFAGFSQLLRDGADFRQIDKVMEkQFGWPMGPAYLLDVVGIDTA---HHAQAV----MAEGFP 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 454 ARKRGNRRycPIPDVLCELGRFGQKTGKGWYQY--DKPlGRIHK-PDPWLSKFLsryrKTHHIEPRTISQDEILERCLYS 530
Cdd:PRK11730 562 DRMKKDYR--DAIDVLFEAKRFGQKNGKGFYRYeeDKK-GKPKKeVDPAVYELL----APVVQPKREFSDEEIIARMMIP 634
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261878539 531 LINEAFRILGEGIAASPEHIDVVYLHGYGWPRHKGGPMFYASTVGLPTVLEKLQKYYRQNpdiPQLEPSDYLKKLASQG 609
Cdd:PRK11730 635 MINEVVRCLEEGIVASPAEADMALVYGLGFPPFRGGAFRYLDTLGVANYVALADKYAHLG---PLYQVPEGLREMAANG 710
|
|
| FadB |
COG1250 |
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ... |
200-486 |
1.23e-103 |
|
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA dehydrogenase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440862 [Multi-domain] Cd Length: 281 Bit Score: 315.51 E-value: 1.23e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 200 PVSSVGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEKEASKmqqsgHPWSGPKP-------RLTSS 272
Cdd:COG1250 1 EIKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKK-----GKLTEEEAdaalariTPTTD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 273 VKELGGVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPS 352
Cdd:COG1250 76 LAALADADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIRG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 353 QYSSPTTIATVMNLSKKIKKIGVVVGNCFGFVGNRMLNPYYNQAYFLLEEGS-KPEEVDQVLEE-FGFKMGPFRVSDLAG 430
Cdd:COG1250 156 PATSDETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVaSPEDIDAAMRLgFGFPMGPFELADLVG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 261878539 431 LDVGWKSRKgqgltgpTLLPGTPARKrgnRRYCPIPDVLCELGRFGQKTGKGWYQY 486
Cdd:COG1250 236 LDTALAVLE-------VLYEALGDPR---YRPPPLLKKLVEAGRLGRKTGRGFYDY 281
|
|
| fa_ox_alpha_mit |
TIGR02441 |
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ... |
4-610 |
2.26e-97 |
|
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of mitochondrial multifunctional fatty acid degradation enzyme complex. Subunit activities include: enoyl-CoA hydratase (EC 4.2.1.17) _ 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35). Some characterization in human (SP:P40939), pig (SP:Q29554), and rat (SP:Q64428). The beta subunit has activity: acetyl-CoA C-acyltransferase (EC 2.3.1.16).
Pssm-ID: 131494 [Multi-domain] Cd Length: 737 Bit Score: 314.08 E-value: 2.26e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 4 GGGLELALGCHYRIAHAEAQ--VGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNS-- 79
Cdd:TIGR02441 121 GGGLELALACHYRIATKDRKtlLGLPEVMLGLLPGAGGTQRLPKLTGVPAALDMMLTGKKIRADRAKKMGIVDQLVDPlg 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 80 ---DPVEE---------AIRFAQRVSDQPLESRR---LCNKPIQSLPNM----DSIFSEALLKMRRQHPGCL-AQEACVR 139
Cdd:TIGR02441 201 pglKPAEEntieyleevAVKFAQGLANGKLSINRdkgLVHKITQYVMTNpfvrQQVYKTAEDKVMKQTKGLYpAPLKILD 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 140 AVQAAVQYPYEVGIKKEEELFLYLLQSGQARALQYAFFA--ERKANKWSTPSgaswktasaRPVSSVGVVGLGTMGRGIV 217
Cdd:TIGR02441 281 VVRTGYDQGPDAGYEAESKAFGELSMTFESKALIGLFHGqtDCKKNKFGKPQ---------RPVKTLAVLGAGLMGAGIA 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 218 ISFARARIPVIAVDSDKNQLATANKMITSVLEKEASKMQQSGHPWSGPKPRLTSSV--KELGGVDLVIEAVFEEMSLKKQ 295
Cdd:TIGR02441 352 QVSVDKGLKTVLKDATPAGLDRGQQQVFKGLNKKVKRKKITSLERDSILSNLTPTLdySGFKNADMVIEAVFEDLSLKHK 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 296 VFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYSSPTTIATVMNLSKKIKKIGV 375
Cdd:TIGR02441 432 VIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIITHDGTSKDTLASAVAVGLKQGKVVI 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 376 VVGNCFGFVGNRMLNPYYNQAYFLLEEGSKPEEVDQVLEEFGFKMGPFRVSDLAGLDVGwkSRKGQGLtgptllpgtpAR 455
Cdd:TIGR02441 512 VVKDGPGFYTTRCLGPMLAEVIRLLQEGVDPKKLDKLTTKFGFPVGAATLADEVGVDVA--EHVAEDL----------GK 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 456 KRGNRRYCPIPDVLCEL---GRFGQKTGKGWYQYDKPLGRIHKPDPWLSKFLSRYRKThhIEPRTISQDEILERCLYSLI 532
Cdd:TIGR02441 580 AFGERFGGGSAELLSELvkaGFLGRKSGKGIFIYQEGKKGSKKVNSDADEILAQYKLP--PKAEVSSPEDIQIRLVSRFV 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 533 NEAFRILGEGIAASPEHIDVVYLHGYGWPRHKGGPMFYASTVGLPTVLEKLQKY---YRQnpdipQLEPSDYLKKLASQG 609
Cdd:TIGR02441 658 NEAVLCLEEGILASPSEGDIGAVFGLGFPPFLGGPFRFVDLYGADKLVDKMEKYaaaYGV-----QFTPCQLLLDHAKSP 732
|
.
gi 261878539 610 N 610
Cdd:TIGR02441 733 G 733
|
|
| 3HCDH_N |
pfam02737 |
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ... |
203-380 |
1.54e-66 |
|
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin.
Pssm-ID: 397037 [Multi-domain] Cd Length: 180 Bit Score: 215.48 E-value: 1.54e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 203 SVGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEKEASKMQQSGHPWSGPKPRL--TSSVKELGGVD 280
Cdd:pfam02737 1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKGRITEEEVDAALARIsfTTDLAAAVDAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 281 LVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYSSPTTI 360
Cdd:pfam02737 81 LVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEKTSPETV 160
|
170 180
....*....|....*....|
gi 261878539 361 ATVMNLSKKIKKIGVVVGNC 380
Cdd:pfam02737 161 ATTVELAKKIGKTPVVVKDT 180
|
|
| PLN02545 |
PLN02545 |
3-hydroxybutyryl-CoA dehydrogenase |
198-491 |
1.42e-62 |
|
3-hydroxybutyryl-CoA dehydrogenase
Pssm-ID: 215300 [Multi-domain] Cd Length: 295 Bit Score: 209.20 E-value: 1.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 198 ARPVSSVGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEKEASKMQQSGHPWSGP--KPRLTSSVKE 275
Cdd:PLN02545 1 MAEIKKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLARLVKKGKMSQEEADATlgRIRCTTNLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 276 LGGVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYS 355
Cdd:PLN02545 81 LRDADFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGMHFMNPPPIMKLVEIIRGADT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 356 SPTTIATVMNLSKKIKKIGVVVGNCFGFVGNRMLNPYYNQAYFLLEEG-SKPEEVDQVLE-EFGFKMGPFRVSDLAGLDV 433
Cdd:PLN02545 161 SDEVFDATKALAERFGKTVVCSQDYPGFIVNRILMPMINEAFYALYTGvASKEDIDTGMKlGTNHPMGPLHLADFIGLDT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261878539 434 ------GWKSrkgqGLTGPTLLPgtparkrgnrryCPIPDVLCELGRFGQKTGKGWYQYDKPLG 491
Cdd:PLN02545 241 clsimkVLHE----GLGDSKYRP------------CPLLVQYVDAGRLGRKSGRGVYHYDGKKR 288
|
|
| PRK05808 |
PRK05808 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
201-486 |
5.17e-61 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 180269 [Multi-domain] Cd Length: 282 Bit Score: 204.43 E-value: 5.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 201 VSSVGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEKEASKMQQSGHPWSGPKPRLTSSV--KELGG 278
Cdd:PRK05808 3 IQKIGVIGAGTMGNGIAQVCAVAGYDVVMVDISDAAVDRGLATITKSLDRLVKKGKMTEADKEAALARITGTTdlDDLKD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 279 VDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYSSPT 358
Cdd:PRK05808 83 ADLVIEAATENMDLKKKIFAQLDEIAKPEAILATNTSSLSITELAAATKRPDKVIGMHFFNPVPVMKLVEIIRGLATSDA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 359 TIATVMNLSKKIKKIGVVVGNCFGFVGNRMLNPYYNQAYFLLEEG-SKPEEVDQVLEeFGFK--MGPFRVSDLAGLDVGW 435
Cdd:PRK05808 163 THEAVEALAKKIGKTPVEVKNAPGFVVNRILIPMINEAIFVLAEGvATAEDIDEGMK-LGCNhpIGPLALADLIGLDTCL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 261878539 436 KSRKgqgltgpTLLPGTparkrGNRRYCPIPdVLCEL---GRFGQKTGKGWYQY 486
Cdd:PRK05808 242 AIME-------VLYEGF-----GDSKYRPCP-LLRKMvaaGWLGRKTGRGFYDY 282
|
|
| PRK09260 |
PRK09260 |
3-hydroxyacyl-CoA dehydrogenase; |
201-487 |
3.67e-54 |
|
3-hydroxyacyl-CoA dehydrogenase;
Pssm-ID: 236434 [Multi-domain] Cd Length: 288 Bit Score: 186.53 E-value: 3.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 201 VSSVGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEKEAS--KMQQSGHPWSGPKPRLTSSVKE-LG 277
Cdd:PRK09260 1 IEKLVVVGAGVMGRGIAYVFAVSGFQTTLVDIKQEQLESAQQEIASIFEQGVArgKLTEAARQAALARLSYSLDLKAaVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 278 GVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYSSP 357
Cdd:PRK09260 81 DADLVIEAVPEKLELKKAVFETADAHAPAECYIATNTSTMSPTEIASFTKRPERVIAMHFFNPVHKMKLVELIRGLETSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 358 TTIATVMNLSKKIKKIGVVVGNCFGFVGNRMLNPYYNQAYFLLEEG-SKPEEVDQVLE-EFGFKMGPFRVSDLagldVGW 435
Cdd:PRK09260 161 ETVQVAKEVAEQMGKETVVVNEFPGFVTSRISALVGNEAFYMLQEGvATAEDIDKAIRlGLNFPMGPLELGDL----VGL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 261878539 436 KSRkgqgLTGPTLLPGTPARKrgnRRYCPIPDVLCELGRFGQKTGKGWYQYD 487
Cdd:PRK09260 237 DTR----LNNLKYLHETLGEK---YRPAPLLEKYVKAGRLGRKTGRGVYDYT 281
|
|
| PRK06130 |
PRK06130 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
200-486 |
4.34e-48 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 235707 [Multi-domain] Cd Length: 311 Bit Score: 170.72 E-value: 4.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 200 PVSSVGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEKEASKmqqSGHPWSGPKPRLTSSVKE-LGG 278
Cdd:PRK06130 3 PIQNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALERARGVIERALGVYAPL---GIASAGMGRIRMEAGLAAaVSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 279 VDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYSSPT 358
Cdd:PRK06130 80 ADLVIEAVPEKLELKRDVFARLDGLCDPDTIFATNTSGLPITAIAQAVTRPERFVGTHFFTPADVIPLVEVVRGDKTSPQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 359 TIATVMNLSKKIKKIGVVVG-NCFGFVGNRMLNPYYNQAYFLLEEG-SKPEEVDQVLE-EFGFKM---GPFRVSDLAGLD 432
Cdd:PRK06130 160 TVATTMALLRSIGKRPVLVKkDIPGFIANRIQHALAREAISLLEKGvASAEDIDEVVKwSLGIRLaltGPLEQRDMNGLD 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 261878539 433 V--GWKSRKGQGLTGPTLLPGTPARKRgnrrycpipdvlcELGRFGQKTGKGWYQY 486
Cdd:PRK06130 240 VhlAVASYLYQDLENRTTPSPLLEEKV-------------EAGELGAKSGQGFYAW 282
|
|
| PRK06035 |
PRK06035 |
3-hydroxyacyl-CoA dehydrogenase; Validated |
201-432 |
1.12e-47 |
|
3-hydroxyacyl-CoA dehydrogenase; Validated
Pssm-ID: 180361 [Multi-domain] Cd Length: 291 Bit Score: 168.90 E-value: 1.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 201 VSSVGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITS-------VLEKeaSKMQQSGHPWSGPKPRLTSSV 273
Cdd:PRK06035 3 IKVIGVVGSGVMGQGIAQVFARTGYDVTIVDVSEEILKNAMELIESgpyglrnLVEK--GKMSEDEAKAIMARIRTSTSY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 274 KELGGVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQ 353
Cdd:PRK06035 81 ESLSDADFIVEAVPEKLDLKRKVFAELERNVSPETIIASNTSGIMIAEIATALERKDRFIGMHWFNPAPVMKLIEVVRAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 354 YSSPTTIATVMNLSKKIKKIGVVVGNCFGFVGNRMLNPYYNQAYFLLEEG-SKPEEVDQVLE-EFGFKMGPFRVSDLAGL 431
Cdd:PRK06035 161 LTSEETFNTTVELSKKIGKIPIEVADVPGFFTTRFIEGWLLEAIRSFEIGiATIKDIDEMCKlAFGFPMGPFELMDIIGI 240
|
.
gi 261878539 432 D 432
Cdd:PRK06035 241 D 241
|
|
| PRK07819 |
PRK07819 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
197-486 |
1.45e-46 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 181133 [Multi-domain] Cd Length: 286 Bit Score: 165.93 E-value: 1.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 197 SARPVSSVGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEK--EASKMQQSGHPWSGPKPRLTSSVK 274
Cdd:PRK07819 1 MSDAIQRVGVVGAGQMGAGIAEVCARAGVDVLVFETTEELATAGRNRIEKSLERavSRGKLTERERDAALARLRFTTDLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 275 ELGGVDLVIEAVFEEMSLKKQVFAELSA-VCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQ 353
Cdd:PRK07819 81 DFADRQLVIEAVVEDEAVKTEIFAELDKvVTDPDAVLASNTSSIPIMKLAAATKRPGRVLGLHFFNPVPVLPLVELVPTL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 354 YSSPTTIATVMNL-SKKIKKIGVVVGNCFGFVGNRMLNPYYNQAYFLLEEG-SKPEEVDQVLEE-FGFKMGPFRVSDLAG 430
Cdd:PRK07819 161 VTSEATVARAEEFaSDVLGKQVVRAQDRSGFVVNALLVPYLLSAIRMVESGfATAEDIDKAMVLgCAHPMGPLRLSDLVG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261878539 431 LD-------VGWKSRKGQGLTGPTLLpgtparkrgnRRycpipdvLCELGRFGQKTGKGWYQY 486
Cdd:PRK07819 241 LDtvkaiadSMYEEFKEPLYAPPPLL----------LR-------MVEAGLLGKKSGRGFYTY 286
|
|
| PRK08268 |
PRK08268 |
3-hydroxy-acyl-CoA dehydrogenase; Validated |
199-486 |
4.54e-46 |
|
3-hydroxy-acyl-CoA dehydrogenase; Validated
Pssm-ID: 236211 [Multi-domain] Cd Length: 507 Bit Score: 170.41 E-value: 4.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 199 RPVSSVGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEKEASKMQQSGHPWSGPKPRLT--SSVKEL 276
Cdd:PRK08268 5 PSIATVAVIGAGAMGAGIAQVAAQAGHTVLLYDARAGAAAAARDGIAARLAKLVEKGKLTAEQADAALARLRpvEALADL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 277 GGVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYSS 356
Cdd:PRK08268 85 ADCDLVVEAIVERLDVKQALFAQLEAIVSPDCILATNTSSLSITAIAAALKHPERVAGLHFFNPVPLMKLVEVVSGLATD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 357 PTTIATVMNLSKKIKKIGVVVGNCFGFVGNRMLNPYYNQAYFLLEEG-SKPEEVDQVL-EEFGFKMGPFRVSDLAGLDVG 434
Cdd:PRK08268 165 PAVADALYALARAWGKTPVRAKDTPGFIVNRAARPYYTEALRVLEEGvADPATIDAILrEAAGFRMGPFELMDLIGLDVN 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 261878539 435 wksrkgqgltgptlLPGTPARKR---GNRRYCP--IPDVLCELGRFGQKTGKGWYQY 486
Cdd:PRK08268 245 --------------HAVMESVYRqfyQEPRFRPslIQQELVAAGRLGRKSGQGFYRY 287
|
|
| PRK07530 |
PRK07530 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
198-489 |
5.47e-42 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 181018 [Multi-domain] Cd Length: 292 Bit Score: 153.62 E-value: 5.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 198 ARPVSSVGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEKEAS--KMQQSGHPWSGPKPRLTSSVKE 275
Cdd:PRK07530 1 MMAIKKVGVIGAGQMGNGIAHVCALAGYDVLLNDVSADRLEAGLATINGNLARQVAkgKISEEARAAALARISTATDLED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 276 LGGVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYS 355
Cdd:PRK07530 81 LADCDLVIEAATEDETVKRKIFAQLCPVLKPEAILATNTSSISITRLASATDRPERFIGIHFMNPVPVMKLVELIRGIAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 356 SPTTIATVMNLSKKIKKIGVVVGNCFGFVGNRMLNPYYNQAYFLLEEG-SKPEEVDQVLeEFG--FKMGPFRVSDLAGLD 432
Cdd:PRK07530 161 DEATFEAAKEFVTKLGKTITVAEDFPAFIVNRILLPMINEAIYTLYEGvGSVEAIDTAM-KLGanHPMGPLELADFIGLD 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261878539 433 vgwksrkgqgltgpTLLP-------GTPARKrgnRRYCPIPDVLCELGRFGQKTGKGWYQY--DKP 489
Cdd:PRK07530 240 --------------TCLSimqvlhdGLADSK---YRPCPLLVKYVEAGWLGRKTGRGFYDYrgEVP 288
|
|
| CaiD |
COG1024 |
Enoyl-CoA hydratase/carnithine racemase [Lipid transport and metabolism]; Enoyl-CoA hydratase ... |
1-181 |
5.06e-34 |
|
Enoyl-CoA hydratase/carnithine racemase [Lipid transport and metabolism]; Enoyl-CoA hydratase/carnithine racemase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440647 [Multi-domain] Cd Length: 249 Bit Score: 129.90 E-value: 5.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 1 MAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSD 80
Cdd:COG1024 102 AALGGGLELALACDLRIAAEDARFGLPEVRLGLIPGGGGTQRLPRLVGLARAKELLLTGRRIDAEEALELGLVNRVVPDD 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 81 PV-EEAIRFAQRVSDQPLesrrlcnkpiqslpnmdsifseallkmrrqhpgcLAQEACVRAVQAAVQYPYEVGIKKEEEL 159
Cdd:COG1024 182 ELlAAALALAARLAAGPP----------------------------------LALAATKRALNAALEAPLDEALELEAEA 227
|
170 180
....*....|....*....|..
gi 261878539 160 FLYLLQSGQARALQYAFFAERK 181
Cdd:COG1024 228 FAELFASEDAREGIAAFLEKRK 249
|
|
| crotonase-like |
cd06558 |
Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse ... |
1-92 |
5.53e-30 |
|
Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse set of enzymes including enoyl-CoA hydratase, napthoate synthase, methylmalonyl-CoA decarboxylase, 3-hydoxybutyryl-CoA dehydratase, and dienoyl-CoA isomerase. Many of these play important roles in fatty acid metabolism. In addition to a conserved structural core and the formation of trimers (or dimers of trimers), a common feature in this superfamily is the stabilization of an enolate anion intermediate derived from an acyl-CoA substrate. This is accomplished by two conserved backbone NH groups in active sites that form an oxyanion hole.
Pssm-ID: 119339 [Multi-domain] Cd Length: 195 Bit Score: 116.89 E-value: 5.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 1 MAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSD 80
Cdd:cd06558 103 AALGGGLELALACDIRIAAEDAKFGLPEVKLGLVPGGGGTQRLPRLVGPARARELLLTGRRISAEEALELGLVDEVVPDE 182
|
90
....*....|...
gi 261878539 81 -PVEEAIRFAQRV 92
Cdd:cd06558 183 eLLAAALELARRL 195
|
|
| 3HCDH |
pfam00725 |
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda ... |
382-486 |
5.65e-30 |
|
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda crystallin. Some proteins include two copies of this domain.
Pssm-ID: 395588 [Multi-domain] Cd Length: 97 Bit Score: 113.47 E-value: 5.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 382 GFVGNRMLNPYYNQAYFLLEEG-SKPEEVDQVLEE-FGFKMGPFRVSDLAGLDVGWKSRKGQGLTGPTllpgtparkrGN 459
Cdd:pfam00725 1 GFVVNRLLAPYLNEAIRLVEEGvATPEDIDAAMRLgLGLPMGPFELSDLVGLDVGYHILEVLAEEFGD----------RA 70
|
90 100
....*....|....*....|....*..
gi 261878539 460 RRYCPIPDVLCELGRFGQKTGKGWYQY 486
Cdd:pfam00725 71 YRPPPLLEKLVEAGRLGRKTGKGFYKY 97
|
|
| PRK07657 |
PRK07657 |
enoyl-CoA hydratase; Provisional |
2-114 |
3.08e-27 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 181069 [Multi-domain] Cd Length: 260 Bit Score: 110.98 E-value: 3.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDP 81
Cdd:PRK07657 108 ALGGGLELALACDFRIAAESASLGLTETTLAIIPGAGGTQRLPRLIGVGRAKELIYTGRRISAQEAKEIGLVEFVVPAHL 187
|
90 100 110
....*....|....*....|....*....|....
gi 261878539 82 VEE-AIRFAQRVSDQPLESRRLCNKPIQSLPNMD 114
Cdd:PRK07657 188 LEEkAIEIAEKIASNGPIAVRQAKEAISNGIQVD 221
|
|
| PRK08293 |
PRK08293 |
3-hydroxyacyl-CoA dehydrogenase; |
204-486 |
6.17e-27 |
|
3-hydroxyacyl-CoA dehydrogenase;
Pssm-ID: 181359 [Multi-domain] Cd Length: 287 Bit Score: 110.80 E-value: 6.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 204 VGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMItsvlEKEASKMQQSGH-----PWSGPKPRL--TSSVKE- 275
Cdd:PRK08293 6 VTVAGAGVLGSQIAFQTAFHGFDVTIYDISDEALEKAKERI----AKLADRYVRDLEatkeaPAEAALNRItlTTDLAEa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 276 LGGVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYS 355
Cdd:PRK08293 82 VKDADLVIEAVPEDPEIKGDFYEELAKVAPEKTIFATNSSTLLPSQFAEATGRPEKFLALHFANEIWKNNTAEIMGHPGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 356 SPTTIATVMNLSKKIKKIGVVV-GNCFGFVGNRMLNPYYNQAYFLLEEG-SKPEEVDQV-LEEFGFKMGPFRVSDLAGLD 432
Cdd:PRK08293 162 DPEVFDTVVAFAKAIGMVPIVLkKEQPGYILNSLLVPFLSAALALWAKGvADPETIDKTwMIATGAPMGPFGILDIVGLD 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 261878539 433 VGWKSRKGQgltgptllpgtpARKRGNRRYCPIPDVLCEL---GRFGQKTGKGWYQY 486
Cdd:PRK08293 242 TAYNITSNW------------AEATDDENAKKAAALLKEYidkGKLGVATGEGFYNY 286
|
|
| PRK06129 |
PRK06129 |
3-hydroxyacyl-CoA dehydrogenase; Validated |
200-428 |
8.04e-26 |
|
3-hydroxyacyl-CoA dehydrogenase; Validated
Pssm-ID: 235706 [Multi-domain] Cd Length: 308 Bit Score: 108.21 E-value: 8.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 200 PVSSVGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEKEASKMQQSGHP--WSGPKPRLTSSVKE-L 276
Cdd:PRK06129 1 PMGSVAIIGAGLIGRAWAIVFARAGHEVRLWDADPAAAAAAPAYIAGRLEDLAAFDLLDGEApdAVLARIRVTDSLADaV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 277 GGVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYSS 356
Cdd:PRK06129 81 ADADYVQESAPENLELKRALFAELDALAPPHAILASSTSALLASAFTEHLAGRERCLVAHPINPPYLIPVVEVVPAPWTA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261878539 357 PTTIATVMNLSKKIKKIGVVVGNCF-GFVGNRMLNPYYNQAYFLLEEG-SKPEEVDQVLEE-FGFK---MGPFRVSDL 428
Cdd:PRK06129 161 PATLARAEALYRAAGQSPVRLRREIdGFVLNRLQGALLREAFRLVADGvASVDDIDAVIRDgLGLRwsfMGPFETIDL 238
|
|
| PRK07658 |
PRK07658 |
enoyl-CoA hydratase; Provisional |
2-183 |
1.43e-25 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 181070 [Multi-domain] Cd Length: 257 Bit Score: 106.26 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVnsdP 81
Cdd:PRK07658 105 ALGGGLELAMSCHIRFATESAKLGLPELNLGLIPGFAGTQRLPRYVGKAKALEMMLTSEPITGAEALKWGLVNGVF---P 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 82 VEEAIRFAQRVsdqpleSRRLCNKPIQSLpnmdsifsEALLKMrrqhpgclaqeacvraVQAAVQYPYEVGIKKEEELFL 161
Cdd:PRK07658 182 EETLLDDAKKL------AKKIAGKSPATT--------RAVLEL----------------LQTTKSSSYYEGVKREAKIFG 231
|
170 180
....*....|....*....|..
gi 261878539 162 YLLQSGQARALQYAFFAERKAN 183
Cdd:PRK07658 232 EVFTSEDAKEGVQAFLEKRKPS 253
|
|
| PRK09076 |
PRK09076 |
enoyl-CoA hydratase; Provisional |
2-187 |
2.91e-24 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 236373 [Multi-domain] Cd Length: 258 Bit Score: 102.30 E-value: 2.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNS-D 80
Cdd:PRK09076 106 AMGGGLECALACDIRIAEEQAQMALPEASVGLLPCAGGTQNLPWLVGEGWAKRMILCGERVDAATALRIGLVEEVVEKgE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 81 PVEEAIRFAQRVSdqplesrrlcnkpiqslpnmdsifseallkmrRQHPGCLAqeACVRAVQAAVQYPYEVGIKKEEELF 160
Cdd:PRK09076 186 AREAALALAQKVA--------------------------------NQSPSAVA--ACKTLIQAARNGPRAAALALERELF 231
|
170 180
....*....|....*....|....*..
gi 261878539 161 LYLLQSGQARALQYAFFAERKANkWST 187
Cdd:PRK09076 232 VDLFDTEDQREGVNAFLEKRAPQ-WKN 257
|
|
| PRK08269 |
PRK08269 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
212-487 |
1.24e-23 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 181340 [Multi-domain] Cd Length: 314 Bit Score: 102.06 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 212 MGRGIVISFARARIPVIAVDSDKNQ-------LATANKMITSVLEKEAS--KMQQSGHPWSGPKPRLTS---SVKELGGV 279
Cdd:PRK08269 1 MGQGIALAFAFAGHDVTLIDFKPRDaagwralDAEARAEIERTLAALVAlgRIDAAQADAVLARIAVVArdgAADALADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 280 DLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYSSPTT 359
Cdd:PRK08269 81 DLVFEAVPEVLDAKREALRWLGRHVDADAIIASTTSTFLVTDLQRHVAHPERFLNAHWLNPAYLMPLVEVSPSDATDPAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 360 IATVMNLSKKIKKIGVVVGNCFGFVGNRMLNPYYNQAYFLLEEG-SKPEEVDQVLEE-FGFK---MGPFRVSDLAGLDV- 433
Cdd:PRK08269 161 VDRLAALLERIGKVPVVCGPSPGYIVPRIQALAMNEAARMVEEGvASAEDIDKAIRTgFGLRfavLGLLEFIDWGGCDIl 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 261878539 434 GWKSRKGQGLTGPTllpgtparkrgnrRYCPiPDVL---CELGRFGQKTGKGWYQYD 487
Cdd:PRK08269 241 YYASRYLAGEIGPD-------------RFAP-PAIVvrnMEEGRDGLRTGAGFYDYA 283
|
|
| PRK05809 |
PRK05809 |
short-chain-enoyl-CoA hydratase; |
2-107 |
4.22e-22 |
|
short-chain-enoyl-CoA hydratase;
Pssm-ID: 180270 [Multi-domain] Cd Length: 260 Bit Score: 96.35 E-value: 4.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVN-SD 80
Cdd:PRK05809 108 ALGGGCELSMACDIRIASEKAKFGQPEVGLGITPGFGGTQRLARIVGPGKAKELIYTGDMINAEEALRIGLVNKVVEpEK 187
|
90 100
....*....|....*....|....*..
gi 261878539 81 PVEEAIRFAQRVSDQPLESRRLCNKPI 107
Cdd:PRK05809 188 LMEEAKALANKIAANAPIAVKLCKDAI 214
|
|
| PRK06688 |
PRK06688 |
enoyl-CoA hydratase; Provisional |
2-183 |
3.26e-21 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 235852 [Multi-domain] Cd Length: 259 Bit Score: 93.39 E-value: 3.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVnsdP 81
Cdd:PRK06688 107 AVGVGVSLALACDLVYASESAKFSLPFAKLGLCPDAGGSALLPRLIGRARAAEMLLLGEPLSAEEALRIGLVNRVV---P 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 82 VEEAIRFAQRVsdqpleSRRLCNKPiqslpnmdsifSEALLKMRrqhpgclaqeacvRAVQAAVQYPYEVGIKKEEELFL 161
Cdd:PRK06688 184 AAELDAEADAQ------AAKLAAGP-----------ASALRYTK-------------RAINAATLTELEEALAREAAGFG 233
|
170 180
....*....|....*....|..
gi 261878539 162 YLLQSGQARALQYAFFAERKAN 183
Cdd:PRK06688 234 RLLRTPDFREGATAFIEKRKPD 255
|
|
| PLN02600 |
PLN02600 |
enoyl-CoA hydratase |
2-100 |
4.02e-21 |
|
enoyl-CoA hydratase
Pssm-ID: 178210 [Multi-domain] Cd Length: 251 Bit Score: 92.94 E-value: 4.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNS-D 80
Cdd:PLN02600 99 ALGGGLELALSCDLRICGEEAVFGLPETGLAIIPGAGGTQRLPRLVGRSRAKELIFTGRRIGAREAASMGLVNYCVPAgE 178
|
90 100
....*....|....*....|.
gi 261878539 81 PVEEAIRFAQRVSDQ-PLESR 100
Cdd:PLN02600 179 AYEKALELAQEINQKgPLAIK 199
|
|
| PRK05862 |
PRK05862 |
enoyl-CoA hydratase; Provisional |
2-126 |
1.29e-19 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 180295 [Multi-domain] Cd Length: 257 Bit Score: 88.95 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDP 81
Cdd:PRK05862 105 ALGGGCELAMMCDIIIAADTAKFGQPEIKLGVLPGMGGSQRLTRAVGKAKAMDLCLTGRMMDAAEAERAGLVSRVVPADK 184
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 261878539 82 -VEEAIRFAQRVSDQPLESRRLCNKPIQSlpNMDSIFSEALLKMRR 126
Cdd:PRK05862 185 lLDEALAAATTIASFSLPAVMMAKEAVNR--AYETTLAEGLLFERR 228
|
|
| ECH_1 |
pfam00378 |
Enoyl-CoA hydratase/isomerase; This family contains a diverse set of enzymes including: ... |
2-96 |
4.46e-18 |
|
Enoyl-CoA hydratase/isomerase; This family contains a diverse set of enzymes including: enoyl-CoA hydratase, napthoate synthase, carnitate racemase, 3-hydroxybutyryl-CoA dehydratase and dodecanoyl-CoA delta-isomerase.
Pssm-ID: 395302 [Multi-domain] Cd Length: 251 Bit Score: 84.33 E-value: 4.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDP 81
Cdd:pfam00378 99 AIGGGCELALACDIIIAADNASFGLNETKLGIIPGAGGTDRLPRIIGHSKAMEMLLLGRRISAQEALKWGLVDKVVPEDQ 178
|
90
....*....|....*.
gi 261878539 82 V-EEAIRFAQRVSDQP 96
Cdd:pfam00378 179 LlDEARELAEKLAEKS 194
|
|
| PRK09674 |
PRK09674 |
enoyl-CoA hydratase-isomerase; Provisional |
2-100 |
3.54e-17 |
|
enoyl-CoA hydratase-isomerase; Provisional
Pssm-ID: 182026 [Multi-domain] Cd Length: 255 Bit Score: 81.74 E-value: 3.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSD- 80
Cdd:PRK09674 103 ALGAGCELALLCDIVIAGENARFGLPEITLGIMPGAGGTQRLIRSVGKSLASQMVLTGESITAQQAQQAGLVSEVFPPEl 182
|
90 100
....*....|....*....|.
gi 261878539 81 PVEEAIRFAQRVSDQ-PLESR 100
Cdd:PRK09674 183 TLERALQLASKIARHsPLALR 203
|
|
| PRK06494 |
PRK06494 |
enoyl-CoA hydratase; Provisional |
2-99 |
4.33e-17 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 180591 [Multi-domain] Cd Length: 259 Bit Score: 81.63 E-value: 4.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVnsdP 81
Cdd:PRK06494 105 AMGGGFELALACDLIVAAENATFALPEPRVGLAALAGGLHRLPRQIGLKRAMGMILTGRRVTAREGLELGFVNEVV---P 181
|
90
....*....|....*...
gi 261878539 82 VEEAIRFAQRVSDQPLES 99
Cdd:PRK06494 182 AGELLAAAERWADDILAC 199
|
|
| PRK08138 |
PRK08138 |
enoyl-CoA hydratase; Provisional |
2-96 |
2.54e-16 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 236162 [Multi-domain] Cd Length: 261 Bit Score: 79.33 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVV-NSD 80
Cdd:PRK08138 109 ALGGGCELAMHADIIVAGESASFGQPEIKVGLMPGAGGTQRLVRAVGKFKAMRMALTGCMVPAPEALAIGLVSEVVeDEQ 188
|
90
....*....|....*.
gi 261878539 81 PVEEAIRFAQRVSDQP 96
Cdd:PRK08138 189 TLPRALELAREIARMP 204
|
|
| PRK03580 |
PRK03580 |
crotonobetainyl-CoA hydratase; |
1-96 |
3.03e-15 |
|
crotonobetainyl-CoA hydratase;
Pssm-ID: 179599 [Multi-domain] Cd Length: 261 Bit Score: 75.89 E-value: 3.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 1 MAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSD 80
Cdd:PRK03580 104 YAFGGGFELALAADFIVCADNASFALPEAKLGIVPDSGGVLRLPKRLPPAIANEMVMTGRRMDAEEALRWGIVNRVVPQA 183
|
90
....*....|....*..
gi 261878539 81 PVEEAIR-FAQRVSDQP 96
Cdd:PRK03580 184 ELMDRAReLAQQLVNSA 200
|
|
| PRK07509 |
PRK07509 |
crotonase/enoyl-CoA hydratase family protein; |
2-105 |
1.10e-14 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 181008 [Multi-domain] Cd Length: 262 Bit Score: 74.53 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVnSDP 81
Cdd:PRK07509 113 CFGGGLQIALGADIRIAAPDTKLSIMEAKWGLVPDMAGTVSLRGLVRKDVARELTYTARVFSAEEALELGLVTHVS-DDP 191
|
90 100
....*....|....*....|....*...
gi 261878539 82 VEEAIRFAQRVS----DQPLESRRLCNK 105
Cdd:PRK07509 192 LAAALALAREIAqrspDAIAAAKRLINR 219
|
|
| PRK05869 |
PRK05869 |
enoyl-CoA hydratase; Validated |
2-98 |
7.91e-14 |
|
enoyl-CoA hydratase; Validated
Pssm-ID: 235632 [Multi-domain] Cd Length: 222 Bit Score: 71.02 E-value: 7.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDP 81
Cdd:PRK05869 110 ALGAGLTLALAADWRVSGDNVKFGATEILAGLAPSGDGMARLTRAAGPSRAKELVFSGRFFDAEEALALGLIDEMVAPDD 189
|
90
....*....|....*...
gi 261878539 82 V-EEAIRFAQRVSDQPLE 98
Cdd:PRK05869 190 VyDAAAAWARRFLDGPPH 207
|
|
| PRK06127 |
PRK06127 |
enoyl-CoA hydratase; Provisional |
3-87 |
1.06e-13 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 235705 Cd Length: 269 Bit Score: 71.66 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 3 FGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDPV 82
Cdd:PRK06127 118 IGGGMGIALACDIRIAAEDSRFGIPAARLGLGYGYDGVKNLVDLVGPSAAKDLFYTARRFDAAEALRIGLVHRVTAADDL 197
|
....*
gi 261878539 83 EEAIR 87
Cdd:PRK06127 198 ETALA 202
|
|
| PRK05980 |
PRK05980 |
crotonase/enoyl-CoA hydratase family protein; |
1-92 |
1.80e-13 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 180335 [Multi-domain] Cd Length: 260 Bit Score: 70.94 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 1 MAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVV-NS 79
Cdd:PRK05980 110 LAFGGGCEITEAVHLAIASERALFAKPEIRLGMPPTFGGTQRLPRLAGRKRALELLLTGDAFSAERALEIGLVNAVVpHE 189
|
90
....*....|...
gi 261878539 80 DPVEEAIRFAQRV 92
Cdd:PRK05980 190 ELLPAARALARRI 202
|
|
| PRK08252 |
PRK08252 |
crotonase/enoyl-CoA hydratase family protein; |
2-185 |
2.75e-13 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 181325 [Multi-domain] Cd Length: 254 Bit Score: 70.02 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNS-D 80
Cdd:PRK08252 102 ALAGGFELALACDLIVAARDAKFGLPEVKRGLVAAGGGLLRLPRRIPYHIAMELALTGDMLTAERAHELGLVNRLTEPgQ 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 81 PVEEAIRFAQRVSDqplesrrlcNKPiqslpnmdsifseallkmrrqhpgcLAQEACVRAVQAAVQYPYEVGIKKEEELF 160
Cdd:PRK08252 182 ALDAALELAERIAA---------NGP-------------------------LAVAASKRIVVESGDWSEDEMFARQRELI 227
|
170 180
....*....|....*....|....*
gi 261878539 161 LYLLQSGQARALQYAfFAERKANKW 185
Cdd:PRK08252 228 APVFTSADAKEGATA-FAEKRAPVW 251
|
|
| PRK08150 |
PRK08150 |
crotonase/enoyl-CoA hydratase family protein; |
4-121 |
2.79e-13 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 181254 Cd Length: 255 Bit Score: 70.05 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 4 GGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVV-NSDPV 82
Cdd:PRK08150 105 GGGLELASAAHIRVADESTYFALPEGQRGIFVGGGGSVRVPRLIGVARMTDMMLTGRVYDAQEGERLGLAQYLVpAGEAL 184
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 261878539 83 EEAIRFAQRV-SDQPLESRRLCNK-P-IQSLPNMDSIFSEAL 121
Cdd:PRK08150 185 DKAMELARRIaQNAPLTNFAVLNAlPrIADMSADDGLFVESL 226
|
|
| PRK06143 |
PRK06143 |
enoyl-CoA hydratase; Provisional |
4-87 |
9.88e-13 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 180423 Cd Length: 256 Bit Score: 68.52 E-value: 9.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 4 GGGLELALGCHYRIAHAEAQVGLPEVTLGlLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDPVE 83
Cdd:PRK06143 113 GGGLELAAACDLRIAAHDAQFGMPEVRVG-IPSVIHAALLPRLIGWARTRWLLLTGETIDAAQALAWGLVDRVVPLAELD 191
|
....
gi 261878539 84 EAIR 87
Cdd:PRK06143 192 AAVE 195
|
|
| PRK09245 |
PRK09245 |
crotonase/enoyl-CoA hydratase family protein; |
2-105 |
3.74e-12 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 181723 Cd Length: 266 Bit Score: 66.92 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDP 81
Cdd:PRK09245 114 AIGAGCDLACMCDIRIASETARFAESFVKLGLIPGDGGAWLLPRIIGMARAAEMAFTGDAIDAATALEWGLVSRVVPADQ 193
|
90 100
....*....|....*....|....*
gi 261878539 82 -VEEAIRFAQRVSDQPLESRRLCNK 105
Cdd:PRK09245 194 lLPAARALAERIAANPPHALRLTKR 218
|
|
| PRK08259 |
PRK08259 |
crotonase/enoyl-CoA hydratase family protein; |
2-96 |
1.23e-11 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 236205 Cd Length: 254 Bit Score: 65.30 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEA-------QVGLPevtlgLLPGarGTQLLPRLTGVPAALDLITSGRRILADEALKLGILD 74
Cdd:PRK08259 104 AVAGGLELALWCDLRVAEEDAvfgvfcrRWGVP-----LIDG--GTVRLPRLIGHSRAMDLILTGRPVDADEALAIGLAN 176
|
90 100
....*....|....*....|...
gi 261878539 75 KVVNS-DPVEEAIRFAQRVSDQP 96
Cdd:PRK08259 177 RVVPKgQARAAAEELAAELAAFP 199
|
|
| PRK07066 |
PRK07066 |
L-carnitine dehydrogenase; |
201-452 |
2.53e-11 |
|
L-carnitine dehydrogenase;
Pssm-ID: 168796 [Multi-domain] Cd Length: 321 Bit Score: 65.24 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 201 VSSVGVVGLGTMGRGIVisfARAR---IPVIAVDSDKNqlatANKMITSVLEKEASKMQQSG-HPWSGP-KPRLTSSVKE 275
Cdd:PRK07066 7 IKTFAAIGSGVIGSGWV---ARALahgLDVVAWDPAPG----AEAALRANVANAWPALERQGlAPGASPaRLRFVATIEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 276 -LGGVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQY 354
Cdd:PRK07066 80 cVADADFIQESAPEREALKLELHERISRAAKPDAIIASSTSGLLPTDFYARATHPERCVVGHPFNPVYLLPLVEVLGGER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 355 SSPTTIATVMNLskkIKKIGV----VVGNCFGFVGNRMLNPYYNQAYFLLEEG-SKPEEVDQVLeEFGFK-----MGPFR 424
Cdd:PRK07066 160 TAPEAVDAAMGI---YRALGMrplhVRKEVPGFIADRLLEALWREALHLVNEGvATTGEIDDAI-RFGAGirwsfMGTFL 235
|
250 260
....*....|....*....|....*....
gi 261878539 425 VSDLAGLDVGWKSRKGQglTGPTL-LPGT 452
Cdd:PRK07066 236 TYTLAGGDAGMRHFMQQ--FGPALeLPWT 262
|
|
| PRK07659 |
PRK07659 |
enoyl-CoA hydratase; Provisional |
2-128 |
2.61e-11 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 236073 [Multi-domain] Cd Length: 260 Bit Score: 64.28 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDP 81
Cdd:PRK07659 109 AAGLGLSIALTADYVIADISAKLAMNFIGIGLIPDGGGHFFLQKRVGENKAKQIIWEGKKLSATEALDLGLIDEVIGGDF 188
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 261878539 82 VEEAIRFAQRVSDQPLES-----RRLCNKPIQSLPNMDSIFSEALLKMRRQH 128
Cdd:PRK07659 189 QTAAKQKISEWLQKPLKAmietkQIYCELNRSQLEQVLQLEKRAQYAMRQTA 240
|
|
| PRK08788 |
PRK08788 |
enoyl-CoA hydratase; Validated |
2-87 |
4.12e-11 |
|
enoyl-CoA hydratase; Validated
Pssm-ID: 236338 Cd Length: 287 Bit Score: 64.16 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDP 81
Cdd:PRK08788 132 ALGGGFEAALSHHTIIAERGAKMGFPEILFNLFPGMGAYSFLARRVGPKLAEELILSGKLYTAEELHDMGLVDVLVEDGQ 211
|
....*.
gi 261878539 82 VEEAIR 87
Cdd:PRK08788 212 GEAAVR 217
|
|
| PRK06190 |
PRK06190 |
enoyl-CoA hydratase; Provisional |
2-101 |
5.03e-11 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 235733 Cd Length: 258 Bit Score: 63.45 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVV-NSD 80
Cdd:PRK06190 105 AVTGGLELALACDILIASERARFADTHARVGILPGWGLSVRLPQKVGIGRARRMSLTGDFLDAADALRAGLVTEVVpHDE 184
|
90 100
....*....|....*....|.
gi 261878539 81 PVEEAIRFAQRVSDQPLESRR 101
Cdd:PRK06190 185 LLPRARRLAASIAGNNPAAVR 205
|
|
| PRK06210 |
PRK06210 |
enoyl-CoA hydratase; Provisional |
4-95 |
5.95e-11 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 180472 Cd Length: 272 Bit Score: 63.57 E-value: 5.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 4 GGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDPV- 82
Cdd:PRK06210 121 GIGLTHALMCDVRFAADGAKFTTAFARRGLIAEHGISWILPRLVGHANALDLLLSARTFYAEEALRLGLVNRVVPPDELm 200
|
90
....*....|...
gi 261878539 83 EEAIRFAQRVSDQ 95
Cdd:PRK06210 201 ERTLAYAEDLARN 213
|
|
| PRK07468 |
PRK07468 |
crotonase/enoyl-CoA hydratase family protein; |
2-86 |
9.26e-11 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 180987 [Multi-domain] Cd Length: 262 Bit Score: 62.77 E-value: 9.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRlTGVPAALDLITSGRRILADEALKLGILDKVVNSDP 81
Cdd:PRK07468 111 AFGGGVGLISVCDVAIAVSGARFGLTETRLGLIPATISPYVVAR-MGEANARRVFMSARLFDAEEAVRLGLLSRVVPAER 189
|
....*
gi 261878539 82 VEEAI 86
Cdd:PRK07468 190 LDAAV 194
|
|
| PRK06023 |
PRK06023 |
crotonase/enoyl-CoA hydratase family protein; |
1-176 |
1.54e-08 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 168351 Cd Length: 251 Bit Score: 55.95 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 1 MAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSD 80
Cdd:PRK06023 107 LAIGIGTTIHLHCDLTFASPRSLFRTPFVDLALVPEAGSSLLAPRLMGHQRAFALLALGEGFSAEAAQEAGLIWKIVDEE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 81 PVE-EAIRFAQRVSDQPLESRRLcnkpiqslpnmdsifSEALLKMRRQHpgCLAQeacvravqaavqypyevgIKKEEEL 159
Cdd:PRK06023 187 AVEaETLKAAEELAAKPPQALQI---------------ARDLMRGPRED--ILAR------------------IDEEAKH 231
|
170
....*....|....*..
gi 261878539 160 FLYLLQSGQARALQYAF 176
Cdd:PRK06023 232 FAARLKSAEARAAFEAF 248
|
|
| PRK08260 |
PRK08260 |
enoyl-CoA hydratase; Provisional |
2-95 |
1.70e-08 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 236206 [Multi-domain] Cd Length: 296 Bit Score: 56.17 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDP 81
Cdd:PRK08260 124 AVGVGATMTLAMDIRLASTAARFGFVFGRRGIVPEAASSWFLPRLVGLQTALEWVYSGRVFDAQEALDGGLVRSVHPPDE 203
|
90
....*....|....*
gi 261878539 82 -VEEAIRFAQRVSDQ 95
Cdd:PRK08260 204 lLPAARALAREIADN 218
|
|
| PRK05870 |
PRK05870 |
enoyl-CoA hydratase; Provisional |
2-98 |
1.88e-08 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 180298 Cd Length: 249 Bit Score: 55.50 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNsDP 81
Cdd:PRK05870 106 AVGAGLNLALAADVRIAGPKALFDARFQKLGLHPGGGATWMLQRAVGPQVARAALLFGMRFDAEAAVRHGLALMVAD-DP 184
|
90
....*....|....*..
gi 261878539 82 VEEAIRFAQRVSDQPLE 98
Cdd:PRK05870 185 VAAALELAAGPAAAPRE 201
|
|
| 3HCDH |
pfam00725 |
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda ... |
523-614 |
2.91e-08 |
|
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda crystallin. Some proteins include two copies of this domain.
Pssm-ID: 395588 [Multi-domain] Cd Length: 97 Bit Score: 51.83 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 523 ILERCLYSLINEAFRILGEGIaASPEHIDVVYLHGYGWPRhkgGPMFYASTVGLPTVLEKLQKYYRQNPDiPQLEPSDYL 602
Cdd:pfam00725 3 VVNRLLAPYLNEAIRLVEEGV-ATPEDIDAAMRLGLGLPM---GPFELSDLVGLDVGYHILEVLAEEFGD-RAYRPPPLL 77
|
90
....*....|..
gi 261878539 603 KKLASQGNPPLK 614
Cdd:pfam00725 78 EKLVEAGRLGRK 89
|
|
| PRK07799 |
PRK07799 |
crotonase/enoyl-CoA hydratase family protein; |
2-93 |
4.37e-08 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 181122 [Multi-domain] Cd Length: 263 Bit Score: 54.72 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVV-NSD 80
Cdd:PRK07799 111 AIAGGTEILQGTDIRVAGESAKFGISEAKWSLFPMGGSAVRLVRQIPYTVACDLLLTGRHITAAEAKEIGLIGHVVpDGQ 190
|
90
....*....|...
gi 261878539 81 PVEEAIRFAQRVS 93
Cdd:PRK07799 191 ALDKALELAELIN 203
|
|
| PLN03214 |
PLN03214 |
probable enoyl-CoA hydratase/isomerase; Provisional |
5-100 |
1.03e-07 |
|
probable enoyl-CoA hydratase/isomerase; Provisional
Pssm-ID: 215635 Cd Length: 278 Bit Score: 53.73 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 5 GGLELALGCHYRIAHAEAQVGLPEVTLGL-LPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDP-V 82
Cdd:PLN03214 121 GGCAVSLCCDYRLQTTEGTMGLNEVALGIpVPKFWARLFMGRVIDRKVAESLLLRGRLVRPAEAKQLGLIDEVVPAAAlM 200
|
90
....*....|....*...
gi 261878539 83 EEAIRFAQRVSDQPLESR 100
Cdd:PLN03214 201 EAAASAMERALKLPSAAR 218
|
|
| PRK05995 |
PRK05995 |
enoyl-CoA hydratase; Provisional |
2-122 |
1.27e-07 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 235664 [Multi-domain] Cd Length: 262 Bit Score: 53.39 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPgargTQLLP---RLTGVPAALDLITSGRRILADEALKLGILDKVVN 78
Cdd:PRK05995 110 AYAGGMGLVAACDIAVAADHAVFCLSEVRLGLIP----ATISPyviRAMGERAARRYFLTAERFDAAEALRLGLVHEVVP 185
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 261878539 79 SDPVEEAI-RFAQRVSDQPLESRRLCNKPIQSLPNMDsiFSEALL 122
Cdd:PRK05995 186 AEALDAKVdELLAALVANSPQAVRAGKRLVRDVAGRP--IDAALI 228
|
|
| PRK06072 |
PRK06072 |
enoyl-CoA hydratase; Provisional |
4-105 |
1.40e-07 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 168377 [Multi-domain] Cd Length: 248 Bit Score: 52.86 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 4 GGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVpAALDLITSGRRILADEALKLGILDkvVNSDPVE 83
Cdd:PRK06072 102 GACIGIALSTDFKFASRDVKFVTAFQRLGLASDTGVAYFLLKLTGQ-RFYEILVLGGEFTAEEAERWGLLK--ISEDPLS 178
|
90 100
....*....|....*....|....*.
gi 261878539 84 EAIRFAQRVSDQPLES----RRLCNK 105
Cdd:PRK06072 179 DAEEMANRISNGPFQSyiaaKRMINL 204
|
|
| PRK05864 |
PRK05864 |
enoyl-CoA hydratase; Provisional |
2-93 |
2.15e-07 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 168278 [Multi-domain] Cd Length: 276 Bit Score: 52.91 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQV-------GLPEVTLGLlpgargTQLLPRLTGVPAALDLITSGRRILADEALKLGILD 74
Cdd:PRK05864 120 AIGGGLCLALAADIRVASSSAYFraaginnGLTASELGL------SYLLPRAIGSSRAFEIMLTGRDVDAEEAERIGLVS 193
|
90 100
....*....|....*....|
gi 261878539 75 -KVVNSDPVEEAIRFAQRVS 93
Cdd:PRK05864 194 rQVPDEQLLDTCYAIAARMA 213
|
|
| PRK06495 |
PRK06495 |
enoyl-CoA hydratase/isomerase family protein; |
2-101 |
2.82e-07 |
|
enoyl-CoA hydratase/isomerase family protein;
Pssm-ID: 168580 [Multi-domain] Cd Length: 257 Bit Score: 52.00 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQllpRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDP 81
Cdd:PRK06495 108 ALGAGLGLVASCDIIVASENAVFGLPEIDVGLAGGGKHAM---RLFGHSLTRRMMLTGYRVPAAELYRRGVIEACLPPEE 184
|
90 100
....*....|....*....|..
gi 261878539 82 -VEEAIRFAQRV-SDQPLESRR 101
Cdd:PRK06495 185 lMPEAMEIAREIaSKSPLATRL 206
|
|
| PRK06144 |
PRK06144 |
enoyl-CoA hydratase; Provisional |
2-93 |
3.01e-07 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 180424 [Multi-domain] Cd Length: 262 Bit Score: 52.30 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEV-TLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSD 80
Cdd:PRK06144 113 CVGGGAAIAAACDLRIATPSARFGFPIArTLGNCLSMSNLARLVALLGAARVKDMLFTARLLEAEEALAAGLVNEVVEDA 192
|
90
....*....|....
gi 261878539 81 PVE-EAIRFAQRVS 93
Cdd:PRK06144 193 ALDaRADALAELLA 206
|
|
| ECH_2 |
pfam16113 |
Enoyl-CoA hydratase/isomerase; This family contains a diverse set of enzymes including: ... |
4-136 |
3.69e-06 |
|
Enoyl-CoA hydratase/isomerase; This family contains a diverse set of enzymes including: enoyl-CoA hydratase, napthoate synthase, carnitate racemase, 3-hydroxybutyryl-CoA dehydratase and dodecanoyl-CoA delta-isomerase. This family differs from pfam00378 in the structure of it's C-terminus.
Pssm-ID: 465024 [Multi-domain] Cd Length: 331 Bit Score: 49.39 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 4 GGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRL---TGVPAALdlitSGRRILADEALKLGILDKVVNSD 80
Cdd:pfam16113 101 GGGVGLSVHGSFRVVTERTRFAMPETAIGLFPDVGGSYFLSRLpgeLGLYLAL----TGARLNGADALAAGLATHYVPSA 176
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 261878539 81 PVEEairfaqrvsdqpLESrRLCNKPIQSLPNMDSIFsEALLKMRRQHPGCLAQEA 136
Cdd:pfam16113 177 RLPA------------LEE-ALAALDWSDPADVDAVL-AEFAEESDPPPSPLAAHR 218
|
|
| PRK08140 |
PRK08140 |
enoyl-CoA hydratase; Provisional |
2-96 |
6.39e-06 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 236163 Cd Length: 262 Bit Score: 47.99 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDP 81
Cdd:PRK08140 110 AAGAGANLALACDIVLAARSASFIQAFVKIGLVPDSGGTWFLPRLVGMARALGLALLGEKLSAEQAEQWGLIWRVVDDAA 189
|
90
....*....|....*.
gi 261878539 82 V-EEAIRFAQRVSDQP 96
Cdd:PRK08140 190 LaDEAQQLAAHLATQP 205
|
|
| PRK08258 |
PRK08258 |
enoyl-CoA hydratase family protein; |
1-96 |
9.57e-06 |
|
enoyl-CoA hydratase family protein;
Pssm-ID: 181329 Cd Length: 277 Bit Score: 47.65 E-value: 9.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 1 MAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGT-QLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNS 79
Cdd:PRK08258 123 VCAGAGAILAMASDLRLGTPSAKTAFLFTRVGLAGADMGAcALLPRIIGQGRASELLYTGRSMSAEEGERWGFFNRLVEP 202
|
90
....*....|....*...
gi 261878539 80 DPV-EEAIRFAQRVSDQP 96
Cdd:PRK08258 203 EELlAEAQALARRLAAGP 220
|
|
| PLN02664 |
PLN02664 |
enoyl-CoA hydratase/delta3,5-delta2,4-dienoyl-CoA isomerase |
4-87 |
1.69e-05 |
|
enoyl-CoA hydratase/delta3,5-delta2,4-dienoyl-CoA isomerase
Pssm-ID: 178269 [Multi-domain] Cd Length: 275 Bit Score: 46.82 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 4 GGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNS-DPV 82
Cdd:PLN02664 124 GGGVDIVTACDIRYCSEDAFFSVKEVDLAITADLGTLQRLPSIVGYGNAMELALTGRRFSGSEAKELGLVSRVFGSkEDL 203
|
....*
gi 261878539 83 EEAIR 87
Cdd:PLN02664 204 DEGVR 208
|
|
| PRK05981 |
PRK05981 |
enoyl-CoA hydratase/isomerase; |
2-96 |
1.98e-05 |
|
enoyl-CoA hydratase/isomerase;
Pssm-ID: 235661 Cd Length: 266 Bit Score: 46.65 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDP 81
Cdd:PRK05981 114 AAGVGMSFALMGDLILCARSAYFLQAFRRIGLVPDGGSTWLLPRLVGKARAMELSLLGEKLPAETALQWGLVNRVVDDAE 193
|
90
....*....|....*.
gi 261878539 82 V-EEAIRFAQRVSDQP 96
Cdd:PRK05981 194 LmAEAMKLAHELANGP 209
|
|
| PRK09120 |
PRK09120 |
p-hydroxycinnamoyl CoA hydratase/lyase; Validated |
2-87 |
2.34e-05 |
|
p-hydroxycinnamoyl CoA hydratase/lyase; Validated
Pssm-ID: 236383 Cd Length: 275 Bit Score: 46.54 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDP 81
Cdd:PRK09120 115 CFGGGFSPLVACDLAIAADEAQFGLSEINWGIPPGGGVSKAMADTVGHRDALYYIMTGETFTGRKAAEMGLVNESVPLAQ 194
|
....*.
gi 261878539 82 VEEAIR 87
Cdd:PRK09120 195 LRARTR 200
|
|
| PRK06563 |
PRK06563 |
crotonase/enoyl-CoA hydratase family protein; |
6-97 |
5.61e-05 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 180625 [Multi-domain] Cd Length: 255 Bit Score: 45.34 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 6 GLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNS-DPVEE 84
Cdd:PRK06563 107 GIELMLAADIVVAADNTRFAQLEVQRGILPFGGATLRFPQAAGWGNAMRYLLTGDEFDAQEALRLGLVQEVVPPgEQLER 186
|
90
....*....|....
gi 261878539 85 AIRFAQRVSDQ-PL 97
Cdd:PRK06563 187 AIELAERIARAaPL 200
|
|
| PLN02740 |
PLN02740 |
Alcohol dehydrogenase-like |
186-403 |
1.52e-04 |
|
Alcohol dehydrogenase-like
Pssm-ID: 178341 [Multi-domain] Cd Length: 381 Bit Score: 44.40 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 186 STPSGASWKTASARPVSSVGVVGLGTMGRGiVISFARAR--IPVIAVDSDKNQLATANKM-ITSVLEKEASKmqqsghpw 262
Cdd:PLN02740 184 STGVGAAWNTANVQAGSSVAIFGLGAVGLA-VAEGARARgaSKIIGVDINPEKFEKGKEMgITDFINPKDSD-------- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 263 sgpKPrLTSSVKEL--GGVDLVIEAVFEEMSLKkqvfaelsavckpEAFLCTNtsaldvDEIASStdrphLVIGTHF--- 337
Cdd:PLN02740 255 ---KP-VHERIREMtgGGVDYSFECAGNVEVLR-------------EAFLSTH------DGWGLT-----VLLGIHPtpk 306
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261878539 338 FSPAHVMKLLE---VIPSQYSSPTTIATVMNLSKKIKKiGVVvgNCFGFVGNRMLNPYYNQAYFLLEEG 403
Cdd:PLN02740 307 MLPLHPMELFDgrsITGSVFGDFKGKSQLPNLAKQCMQ-GVV--NLDGFITHELPFEKINEAFQLLEDG 372
|
|
| liver_ADH_like1 |
cd08281 |
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ... |
187-286 |
1.79e-04 |
|
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. This group contains members identified as zinc dependent alcohol dehydrogenases (ADH), and class III ADG (aka formaldehyde dehydrogenase, FDH). Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. Class III ADH are also know as glutathione-dependent formaldehyde dehydrogenase (FDH), which convert aldehydes to the corresponding carboxylic acid and alcohol. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.
Pssm-ID: 176241 [Multi-domain] Cd Length: 371 Bit Score: 44.29 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 187 TPSGASWKTASARPVSSVGVVGLGTMG----RGIVISFARariPVIAVD--SDKNQLATANKMITSVLEKEASKMQQsgh 260
Cdd:cd08281 178 TGVGAVVNTAGVRPGQSVAVVGLGGVGlsalLGAVAAGAS---QVVAVDlnEDKLALARELGATATVNAGDPNAVEQ--- 251
|
90 100
....*....|....*....|....*...
gi 261878539 261 pwsgpkprltssVKEL--GGVDLVIEAV 286
Cdd:cd08281 252 ------------VRELtgGGVDYAFEMA 267
|
|
| PRK05617 |
PRK05617 |
3-hydroxyisobutyryl-CoA hydrolase; Provisional |
4-100 |
2.61e-04 |
|
3-hydroxyisobutyryl-CoA hydrolase; Provisional
Pssm-ID: 235533 [Multi-domain] Cd Length: 342 Bit Score: 43.66 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 4 GGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRL---TGVPAALdlitSGRRILADEALKLGILDKVVNSD 80
Cdd:PRK05617 113 GGGVGISAHGSHRIVTERTKMAMPETGIGFFPDVGGTYFLSRApgaLGTYLAL----TGARISAADALYAGLADHFVPSA 188
|
90 100
....*....|....*....|
gi 261878539 81 PVEEairFAQRVSDQPLESR 100
Cdd:PRK05617 189 DLPA---LLDALISLRWDSG 205
|
|
| PRK11423 |
PRK11423 |
methylmalonyl-CoA decarboxylase; Provisional |
2-127 |
3.59e-04 |
|
methylmalonyl-CoA decarboxylase; Provisional
Pssm-ID: 236908 [Multi-domain] Cd Length: 261 Bit Score: 42.71 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDP 81
Cdd:PRK11423 107 VWGGAFELIMSCDLIIAASTSTFAMTPANLGVPYNLSGILNFTNDAGFHIVKEMFFTASPITAQRALAVGILNHVVEVEE 186
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 261878539 82 VEEAIR-FAQRVSDQ-PL------ESRRLcnkpIQSLPNMDSIFSEALLKMRRQ 127
Cdd:PRK11423 187 LEDFTLqMAHHISEKaPLaiavikEQLRV----LGEAHPMNPDEFERIQGLRRA 236
|
|
| PRK08290 |
PRK08290 |
enoyl-CoA hydratase; Provisional |
5-96 |
5.98e-04 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 236220 [Multi-domain] Cd Length: 288 Bit Score: 42.26 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 5 GGLELALGCHYRIAHAEAQVGLPEVTLGLlPG----ARGTQLLPRltgvpAALDLITSGRRILADEALKLGILDKVVNSD 80
Cdd:PRK08290 132 GGLMLAWVCDLIVASDDAFFSDPVVRMGI-PGveyfAHPWELGPR-----KAKELLFTGDRLTADEAHRLGMVNRVVPRD 205
|
90
....*....|....*..
gi 261878539 81 PVE-EAIRFAQRVSDQP 96
Cdd:PRK08290 206 ELEaETLELARRIAAMP 222
|
|
| liver_alcohol_DH_like |
cd08277 |
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ... |
186-284 |
1.34e-03 |
|
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48) , then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.
Pssm-ID: 176238 [Multi-domain] Cd Length: 365 Bit Score: 41.56 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 186 STPSGASWKTASARPVSSVGVVGLGTMGRGiVISFAR----ARIPVIAVDSDKNQLATANKMITSVLEKEASKMQQsghp 261
Cdd:cd08277 170 STGYGAAWNTAKVEPGSTVAVFGLGAVGLS-AIMGAKiagaSRIIGVDINEDKFEKAKEFGATDFINPKDSDKPVS---- 244
|
90 100
....*....|....*....|....*
gi 261878539 262 wsgpkprltSSVKEL--GGVDLVIE 284
Cdd:cd08277 245 ---------EVIREMtgGGVDYSFE 260
|
|
| FDH_like_ADH2 |
cd08286 |
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ... |
199-286 |
2.68e-03 |
|
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase (FDH), which is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. This family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Another member is identified as a dihydroxyacetone reductase. Like the zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. Unlike ADH, where NAD(P)(H) acts as a cofactor, NADH in FDH is a tightly bound redox cofactor (similar to nicotinamide proteins). The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.
Pssm-ID: 176246 [Multi-domain] Cd Length: 345 Bit Score: 40.31 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 199 RPVSSVGVVGLGTMGRGIVISfARARIP--VIAVDSDKNQLATANKMITSvlekeaskmqqsgHPWSGPKPRLTSSVKEL 276
Cdd:cd08286 165 KPGDTVAIVGAGPVGLAALLT-AQLYSPskIIMVDLDDNRLEVAKKLGAT-------------HTVNSAKGDAIEQVLEL 230
|
90
....*....|...
gi 261878539 277 ---GGVDLVIEAV 286
Cdd:cd08286 231 tdgRGVDVVIEAV 243
|
|
| PLN02267 |
PLN02267 |
enoyl-CoA hydratase/isomerase family protein |
2-93 |
3.51e-03 |
|
enoyl-CoA hydratase/isomerase family protein
Pssm-ID: 215151 Cd Length: 239 Bit Score: 39.70 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQV-GLPEVTLGLLPGARGTQLLPRLTGVPAAL-DLITSGRRILADEALKLGILDKVVNS 79
Cdd:PLN02267 105 ASAAGFILALSHDYVLMRKDRGVlYMSEVDIGLPLPDYFMALLRAKIGSPAARrDVLLRAAKLTAEEAVEMGIVDSAHDS 184
|
90
....*....|....*.
gi 261878539 80 --DPVEEAIRFAQRVS 93
Cdd:PLN02267 185 aeETVEAAVRLGEELA 200
|
|
| PRK07827 |
PRK07827 |
enoyl-CoA hydratase family protein; |
4-107 |
4.65e-03 |
|
enoyl-CoA hydratase family protein;
Pssm-ID: 236109 [Multi-domain] Cd Length: 260 Bit Score: 39.28 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 4 GGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITsGRRILADEALKLGILdkVVNSDPVE 83
Cdd:PRK07827 114 AGGFGLVGACDIVVAGPESTFALTEARIGVAPAIISLTLLPRLSPRAAARYYLT-GEKFGAAEAARIGLV--TAAADDVD 190
|
90 100
....*....|....*....|....*....
gi 261878539 84 EAI-RFA---QRVSDQPL-ESRRLCNKPI 107
Cdd:PRK07827 191 AAVaALLadlRRGSPQGLaESKALTTAAV 219
|
|
| alcohol_DH_plants |
cd08301 |
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ... |
186-243 |
5.29e-03 |
|
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48) , then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.
Pssm-ID: 176261 [Multi-domain] Cd Length: 369 Bit Score: 39.59 E-value: 5.29e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 186 STPSGASWKTASARPVSSVGVVGLGTMGRGiVISFARAR--IPVIAVDSDKNQLATANKM 243
Cdd:cd08301 173 STGLGAAWNVAKVKKGSTVAIFGLGAVGLA-VAEGARIRgaSRIIGVDLNPSKFEQAKKF 231
|
|
| alcohol_DH_class_III |
cd08300 |
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ... |
186-243 |
5.34e-03 |
|
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde dehydrogenase(FDH), a member of the zinc dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes or ketones. Like many zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these FDHs form dimers, with 4 zinc ions per dimer. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.
Pssm-ID: 176260 [Multi-domain] Cd Length: 368 Bit Score: 39.52 E-value: 5.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261878539 186 STPSGASWKTASARPVSSVGVVGLGTMGRGiVISFARA----RIpvIAVDSDKNQLATANKM 243
Cdd:cd08300 172 TTGYGAVLNTAKVEPGSTVAVFGLGAVGLA-VIQGAKAagasRI--IGIDINPDKFELAKKF 230
|
|
| PLN02888 |
PLN02888 |
enoyl-CoA hydratase |
2-95 |
8.22e-03 |
|
enoyl-CoA hydratase
Pssm-ID: 215480 Cd Length: 265 Bit Score: 38.58 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 2 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVnsDP 81
Cdd:PLN02888 110 AITAGFEIALACDILVASRGAKFIDTHAKFGIFPSWGLSQKLSRIIGANRAREVSLTAMPLTAETAERWGLVNHVV--EE 187
|
90
....*....|....
gi 261878539 82 vEEAIRFAQRVSDQ 95
Cdd:PLN02888 188 -SELLKKAREVAEA 200
|
|
| Zn_ADH10 |
cd08263 |
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ... |
187-286 |
9.54e-03 |
|
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.
Pssm-ID: 176224 [Multi-domain] Cd Length: 367 Bit Score: 38.51 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261878539 187 TPSGASWKTASARPVSSVGVVGLGTMGRGIV-ISFARARIPVIAVDSDKNQLATANKMITSvlekeaskmqqsgHPWSGP 265
Cdd:cd08263 174 TAYGALKHAADVRPGETVAVIGVGGVGSSAIqLAKAFGASPIIAVDVRDEKLAKAKELGAT-------------HTVNAA 240
|
90 100
....*....|....*....|....
gi 261878539 266 KPRLTSSVKEL---GGVDLVIEAV 286
Cdd:cd08263 241 KEDAVAAIREItggRGVDVVVEAL 264
|
|
| |
