|
Name |
Accession |
Description |
Interval |
E-value |
| fadJ |
PRK11154 |
fatty acid oxidation complex subunit alpha FadJ; |
20-705 |
1.46e-132 |
|
fatty acid oxidation complex subunit alpha FadJ;
Pssm-ID: 236864 [Multi-domain] Cd Length: 708 Bit Score: 408.13 E-value: 1.46e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 20 PVNAISTTLLRDIKEGLQKAVIDHTIKAIVIC-GAEGKFSAGADIRGFSAPRTFG--LTL---GHVV-DEIQRNEKPVVA 92
Cdd:PRK11154 27 KMNTLKAEFAEQVRAILKQLREDKELKGVVFIsGKPDNFIAGADINMLAACKTAQeaEALarqGQQLfAEIEALPIPVVA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 93 AIQGMAFGGGLELALGCHYRIA--HAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILD 170
Cdd:PRK11154 107 AIHGACLGGGLELALACHYRVCtdDPKTVLGLPEVQLGLLPGSGGTQRLPRLIGVSTALDMILTGKQLRAKQALKLGLVD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 171 KVVNSD-----PVEEAIRFAQRVSDQPLESRRLCNKPI-QSLpnmdsIFSEALLKMRRQHPGCL-AQEACVRAVQAAVQY 243
Cdd:PRK11154 187 DVVPHSillevAVELAKKGKPARRPLPVRERLLEGNPLgRAL-----LFKQARKKTLAKTQGNYpAPERILDVVRTGLEK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 244 PYEVGIKKEEELFLYLLQSGQARALQYAFFAERKANKwstPSGASwktASARPVSSVGVVGLGTMGRGIV-ISFARARIP 322
Cdd:PRK11154 262 GMSSGYEAEARAFGELAMTPESAALRSIFFATTEMKK---DTGSD---AKPRPVNKVGVLGGGLMGGGIAyVTATKAGLP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 323 VIAVDSDKNQLATANKMITSVLEKE-------ASKMQQsghpwsgpKPRLTSSVKELGG---VDLVIEAVFEEMSLKKQV 392
Cdd:PRK11154 336 VRIKDINPQGINHALKYSWDLLDKKvkrrhlkPSERDK--------QMALISGTTDYRGfkhADVVIEAVFEDLALKQQM 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 393 FAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYSSPTTIATVMNLSKKIKKIGVV 472
Cdd:PRK11154 408 VAEVEQNCAPHTIFASNTSSLPIGQIAAAAARPEQVIGLHYFSPVEKMPLVEVIPHAKTSAETIATTVALAKKQGKTPIV 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 473 VGNCFGFVGNRMLNPYYNQAYFLLEEGSKPEEVDQVLEEFGFKMGPFRVSDLAGLDVGWKsrkgqglTGPTLLpgtpaRK 552
Cdd:PRK11154 488 VRDGAGFYVNRILAPYINEAARLLLEGEPIEHIDAALVKFGFPVGPITLLDEVGIDVGTK-------IIPILE-----AA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 553 RGNRRYCP-IPDVLCELGRFGQKTGKGWYQYDKPLGRIHK-PDPWLSKFLSryrkthhIEPRT-ISQDEILERCLYSLIN 629
Cdd:PRK11154 556 LGERFSAPaAFDKLLNDDRKGRKNGRGFYLYGQKGKKSKKqVDESVYPLLG-------ITPQSrLSANEIAERCVMLMLN 628
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68989263 630 EAFRILGEGIAASPEHIDVVYLHGYGWPRHKGGPMFYASTVGLPTVLEKLQKYYRQNPDipQLEPSDYLKKLASQG 705
Cdd:PRK11154 629 EAVRCLDEGIIRSARDGDIGAVFGIGFPPFLGGPFRYMDSLGAGEVVAILERLAAQYGD--RFTPCERLVEMAERG 702
|
|
| fadB |
PRK11730 |
fatty acid oxidation complex subunit alpha FadB; |
21-705 |
3.96e-120 |
|
fatty acid oxidation complex subunit alpha FadB;
Pssm-ID: 183293 [Multi-domain] Cd Length: 715 Bit Score: 376.12 E-value: 3.96e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 21 VNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRGFSAprTFGLTLGHVVDEIQRNEK----------PV 90
Cdd:PRK11730 28 VNKLDRATLASLGEALDALEAQSDLKGLLLTSAKDAFIVGADITEFLS--LFAAPEEELSQWLHFANSifnrledlpvPT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 91 VAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILD 170
Cdd:PRK11730 106 VAAINGYALGGGCECVLATDYRVASPDARIGLPETKLGIMPGFGGTVRLPRLIGADNALEWIAAGKDVRAEDALKVGAVD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 171 KVVNSDPVEE-AIRFAQRVSDQPLE--SRRlcnKPIQS---LPNMDSIFSEALLKMR------RQHPgclAQEACVRAVQ 238
Cdd:PRK11730 186 AVVAPEKLQEaALALLKQAIAGKLDwkARR---QPKLEplkLSKIEAMMSFTTAKGMvaqkagKHYP---APMTAVKTIE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 239 AAVQYPYEVGIKKEEELFLYLLQSGQARALQYAFFAE----RKANKWStpsgaswktASARPVSSVGVVGLGTMGRGIVI 314
Cdd:PRK11730 260 AAAGLGRDEALELEAKGFVKLAKTNVARALVGIFLNDqyvkGKAKKLA---------KDAKPVKQAAVLGAGIMGGGIAY 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 315 SFARARIPVIAVDSDKNQL----ATANKMITSVLEK---EASKMQQ---SGHPwsgpkprlTSSVKELGGVDLVIEAVFE 384
Cdd:PRK11730 331 QSASKGVPVIMKDINQKALdlgmTEAAKLLNKQVERgkiDGAKMAGvlsSIRP--------TLDYAGFERVDVVVEAVVE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 385 EMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYSSPTTIATVMNLSK 464
Cdd:PRK11730 403 NPKVKAAVLAEVEQKVREDTILASNTSTISISLLAKALKRPENFCGMHFFNPVHRMPLVEVIRGEKTSDETIATVVAYAS 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 465 KIKKIGVVVGNCFGFVGNRMLNPYYNQAYFLLEEGSKPEEVDQVLE-EFGFKMGPFRVSDLAGLDVGwksRKGQGLtgpt 543
Cdd:PRK11730 483 KMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDGADFRQIDKVMEkQFGWPMGPAYLLDVVGIDTA---HHAQAV---- 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 544 LLPGTPARKRGNRRycPIPDVLCELGRFGQKTGKGWYQY--DKPlGRIHK-PDPWLSKFLsryrKTHHIEPRTISQDEIL 620
Cdd:PRK11730 556 MAEGFPDRMKKDYR--DAIDVLFEAKRFGQKNGKGFYRYeeDKK-GKPKKeVDPAVYELL----APVVQPKREFSDEEII 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 621 ERCLYSLINEAFRILGEGIAASPEHIDVVYLHGYGWPRHKGGPMFYASTVGLPTVLEKLQKYYRQNpdiPQLEPSDYLKK 700
Cdd:PRK11730 629 ARMMIPMINEVVRCLEEGIVASPAEADMALVYGLGFPPFRGGAFRYLDTLGVANYVALADKYAHLG---PLYQVPEGLRE 705
|
....*
gi 68989263 701 LASQG 705
Cdd:PRK11730 706 MAANG 710
|
|
| fa_ox_alpha_mit |
TIGR02441 |
fatty acid oxidation complex, alpha subunit, mitochondrial; Members represent alpha subunit of ... |
5-682 |
3.03e-113 |
|
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: 358.77 E-value: 3.03e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 5 TRLHNALALIRLRNP--PVNAISTTLLRDIKEGLQKAVIDHTIK-AIVICGAEGKFSAGADIRGFSAPRTF--GLTLGH- 78
Cdd:TIGR02441 17 YEVKGDVAVVKIDSPnsKVNTLSKELFAEFKEVMNELWTNEAIKsAVLISGKPGSFVAGADIQMIAACKTAqeVTQLSQe 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 79 ---VVDEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQ--VGLPEVTLGLLPGARGTQLLPRLTGVPAALDLIT 153
Cdd:TIGR02441 97 gqeMFERIEKSQKPIVAAISGSCLGGGLELALACHYRIATKDRKtlLGLPEVMLGLLPGAGGTQRLPKLTGVPAALDMML 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 154 SGRRILADEALKLGILDKVVNS-----DPVEE---------AIRFAQRVSDQPLESRR---LCNKPIQSLPNM----DSI 212
Cdd:TIGR02441 177 TGKKIRADRAKKMGIVDQLVDPlgpglKPAEEntieyleevAVKFAQGLANGKLSINRdkgLVHKITQYVMTNpfvrQQV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 213 FSEALLKMRRQHPGCL-AQEACVRAVQAAVQYPYEVGIKKEEELFLYLLQSGQARALQYAFFA--ERKANKWSTPSgasw 289
Cdd:TIGR02441 257 YKTAEDKVMKQTKGLYpAPLKILDVVRTGYDQGPDAGYEAESKAFGELSMTFESKALIGLFHGqtDCKKNKFGKPQ---- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 290 ktasaRPVSSVGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEKEASKMQQSGHPWSGPKPRLTSSV 369
Cdd:TIGR02441 333 -----RPVKTLAVLGAGLMGAGIAQVSVDKGLKTVLKDATPAGLDRGQQQVFKGLNKKVKRKKITSLERDSILSNLTPTL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 370 --KELGGVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIP 447
Cdd:TIGR02441 408 dySGFKNADMVIEAVFEDLSLKHKVIKEVEAVVPPHCIIASNTSALPIKDIAAVSSRPEKVIGMHYFSPVDKMQLLEIIT 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 448 SQYSSPTTIATVMNLSKKIKKIGVVVGNCFGFVGNRMLNPYYNQAYFLLEEGSKPEEVDQVLEEFGFKMGPFRVSDLAGL 527
Cdd:TIGR02441 488 HDGTSKDTLASAVAVGLKQGKVVIVVKDGPGFYTTRCLGPMLAEVIRLLQEGVDPKKLDKLTTKFGFPVGAATLADEVGV 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 528 DVGwkSRKGQGLtgptllpgtpARKRGNRRYCPIPDVLCEL---GRFGQKTGKGWYQYDKPLGRIHKPDPWLSKFLSRYR 604
Cdd:TIGR02441 568 DVA--EHVAEDL----------GKAFGERFGGGSAELLSELvkaGFLGRKSGKGIFIYQEGKKGSKKVNSDADEILAQYK 635
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68989263 605 KThhIEPRTISQDEILERCLYSLINEAFRILGEGIAASPEHIDVVYLHGYGWPRHKGGPMFYASTVGLPTVLEKLQKY 682
Cdd:TIGR02441 636 LP--PKAEVSSPEDIQIRLVSRFVNEAVLCLEEGILASPSEGDIGAVFGLGFPPFLGGPFRFVDLYGADKLVDKMEKY 711
|
|
| FadB |
COG1250 |
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ... |
296-582 |
2.12e-101 |
|
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: 312.43 E-value: 2.12e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 296 PVSSVGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEKEASKmqqsgHPWSGPKP-------RLTSS 368
Cdd:COG1250 1 EIKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKK-----GKLTEEEAdaalariTPTTD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 369 VKELGGVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPS 448
Cdd:COG1250 76 LAALADADLVIEAVPEDLDLKQEVFAELDAVAPPDAILASNTSSLSITELAAATKRPERFIGLHFFNPVPLMPLVEVIRG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 449 QYSSPTTIATVMNLSKKIKKIGVVVGNCFGFVGNRMLNPYYNQAYFLLEEGS-KPEEVDQVLEE-FGFKMGPFRVSDLAG 526
Cdd:COG1250 156 PATSDETVATAVAFARRLGKTPVVVKDTPGFIVNRILVPYLNEAIRLLEEGVaSPEDIDAAMRLgFGFPMGPFELADLVG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 68989263 527 LDVGWKSRKgqgltgpTLLPGTPARKrgnRRYCPIPDVLCELGRFGQKTGKGWYQY 582
Cdd:COG1250 236 LDTALAVLE-------VLYEALGDPR---YRPPPLLKKLVEAGRLGRKTGRGFYDY 281
|
|
| 3HCDH_N |
pfam02737 |
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ... |
299-476 |
4.20e-65 |
|
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin.
Pssm-ID: 397037 [Multi-domain] Cd Length: 180 Bit Score: 213.55 E-value: 4.20e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 299 SVGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEKEASKMQQSGHPWSGPKPRL--TSSVKELGGVD 376
Cdd:pfam02737 1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALERIESSLERLVEKGRITEEEVDAALARIsfTTDLAAAVDAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 377 LVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYSSPTTI 456
Cdd:pfam02737 81 LVIEAVPENLELKRKLFAELDAIAPPDAILATNTSSLSITELAAATKRPERFIGLHFFNPPPLMPLVEVVRGEKTSPETV 160
|
170 180
....*....|....*....|
gi 68989263 457 ATVMNLSKKIKKIGVVVGNC 476
Cdd:pfam02737 161 ATTVELAKKIGKTPVVVKDT 180
|
|
| PLN02545 |
PLN02545 |
3-hydroxybutyryl-CoA dehydrogenase |
294-587 |
7.14e-62 |
|
3-hydroxybutyryl-CoA dehydrogenase
Pssm-ID: 215300 [Multi-domain] Cd Length: 295 Bit Score: 209.20 E-value: 7.14e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 294 ARPVSSVGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEKEASKMQQSGHPWSGP--KPRLTSSVKE 371
Cdd:PLN02545 1 MAEIKKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLDSISSSLARLVKKGKMSQEEADATlgRIRCTTNLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 372 LGGVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYS 451
Cdd:PLN02545 81 LRDADFIIEAIVESEDLKKKLFSELDRICKPSAILASNTSSISITRLASATQRPQQVIGMHFMNPPPIMKLVEIIRGADT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 452 SPTTIATVMNLSKKIKKIGVVVGNCFGFVGNRMLNPYYNQAYFLLEEG-SKPEEVDQVLE-EFGFKMGPFRVSDLAGLDV 529
Cdd:PLN02545 161 SDEVFDATKALAERFGKTVVCSQDYPGFIVNRILMPMINEAFYALYTGvASKEDIDTGMKlGTNHPMGPLHLADFIGLDT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68989263 530 ------GWKSrkgqGLTGPTLLPgtparkrgnrryCPIPDVLCELGRFGQKTGKGWYQYDKPLG 587
Cdd:PLN02545 241 clsimkVLHE----GLGDSKYRP------------CPLLVQYVDAGRLGRKSGRGVYHYDGKKR 288
|
|
| CaiD |
COG1024 |
Enoyl-CoA hydratase/carnithine racemase [Lipid transport and metabolism]; Enoyl-CoA hydratase ... |
5-277 |
2.59e-60 |
|
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: 203.09 E-value: 2.59e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 5 TRLHNALALIRLRNP-PVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRGFSAP------RTFGLTLG 77
Cdd:COG1024 3 VEREGGVATITLNRPeKLNALSLEMLAELAAALDEAEADPDVRVVVLTGAGKAFCAGADLKELAAAadpeeaRAFARGLQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 78 HVVDEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRR 157
Cdd:COG1024 83 RLFRALRRLPKPVIAAVNGAALGGGLELALACDLRIAAEDARFGLPEVRLGLIPGGGGTQRLPRLVGLARAKELLLTGRR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 158 ILADEALKLGILDKVVNSDPV-EEAIRFAQRVSDQPLesrrlcnkpiqslpnmdsifseallkmrrqhpgcLAQEACVRA 236
Cdd:COG1024 163 IDAEEALELGLVNRVVPDDELlAAALALAARLAAGPP----------------------------------LALAATKRA 208
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 68989263 237 VQAAVQYPYEVGIKKEEELFLYLLQSGQARALQYAFFAERK 277
Cdd:COG1024 209 LNAALEAPLDEALELEAEAFAELFASEDAREGIAAFLEKRK 249
|
|
| PRK05808 |
PRK05808 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
297-582 |
7.05e-60 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 180269 [Multi-domain] Cd Length: 282 Bit Score: 203.27 E-value: 7.05e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 297 VSSVGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEKEASKMQQSGHPWSGPKPRLTSSV--KELGG 374
Cdd:PRK05808 3 IQKIGVIGAGTMGNGIAQVCAVAGYDVVMVDISDAAVDRGLATITKSLDRLVKKGKMTEADKEAALARITGTTdlDDLKD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 375 VDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYSSPT 454
Cdd:PRK05808 83 ADLVIEAATENMDLKKKIFAQLDEIAKPEAILATNTSSLSITELAAATKRPDKVIGMHFFNPVPVMKLVEIIRGLATSDA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 455 TIATVMNLSKKIKKIGVVVGNCFGFVGNRMLNPYYNQAYFLLEEG-SKPEEVDQVLEeFGFK--MGPFRVSDLAGLDVGW 531
Cdd:PRK05808 163 THEAVEALAKKIGKTPVEVKNAPGFVVNRILIPMINEAIFVLAEGvATAEDIDEGMK-LGCNhpIGPLALADLIGLDTCL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 68989263 532 KSRKgqgltgpTLLPGTparkrGNRRYCPIPdVLCEL---GRFGQKTGKGWYQY 582
Cdd:PRK05808 242 AIME-------VLYEGF-----GDSKYRPCP-LLRKMvaaGWLGRKTGRGFYDY 282
|
|
| crotonase-like |
cd06558 |
Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse ... |
8-188 |
1.13e-57 |
|
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: 194.32 E-value: 1.13e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 8 HNALALIRLRNPP-VNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRGFSAP-------RTFGLTLGHV 79
Cdd:cd06558 6 DGGVATITLNRPEkRNALSLEMLDELAAALDEAEADPDVRVVVLTGAGKAFCAGADLKELAALsdageeaRAFIRELQEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 80 VDEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRIL 159
Cdd:cd06558 86 LRALLRLPKPVIAAVNGAALGGGLELALACDIRIAAEDAKFGLPEVKLGLVPGGGGTQRLPRLVGPARARELLLTGRRIS 165
|
170 180 190
....*....|....*....|....*....|
gi 68989263 160 ADEALKLGILDKVVNSD-PVEEAIRFAQRV 188
Cdd:cd06558 166 AEEALELGLVDEVVPDEeLLAAALELARRL 195
|
|
| PRK09260 |
PRK09260 |
3-hydroxyacyl-CoA dehydrogenase; |
297-583 |
2.83e-53 |
|
3-hydroxyacyl-CoA dehydrogenase;
Pssm-ID: 236434 [Multi-domain] Cd Length: 288 Bit Score: 185.76 E-value: 2.83e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 297 VSSVGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEKEAS--KMQQSGHPWSGPKPRLTSSVKE-LG 373
Cdd:PRK09260 1 IEKLVVVGAGVMGRGIAYVFAVSGFQTTLVDIKQEQLESAQQEIASIFEQGVArgKLTEAARQAALARLSYSLDLKAaVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 374 GVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYSSP 453
Cdd:PRK09260 81 DADLVIEAVPEKLELKKAVFETADAHAPAECYIATNTSTMSPTEIASFTKRPERVIAMHFFNPVHKMKLVELIRGLETSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 454 TTIATVMNLSKKIKKIGVVVGNCFGFVGNRMLNPYYNQAYFLLEEG-SKPEEVDQVLE-EFGFKMGPFRVSDLagldVGW 531
Cdd:PRK09260 161 ETVQVAKEVAEQMGKETVVVNEFPGFVTSRISALVGNEAFYMLQEGvATAEDIDKAIRlGLNFPMGPLELGDL----VGL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 68989263 532 KSRkgqgLTGPTLLPGTPARKrgnRRYCPIPDVLCELGRFGQKTGKGWYQYD 583
Cdd:PRK09260 237 DTR----LNNLKYLHETLGEK---YRPAPLLEKYVKAGRLGRKTGRGVYDYT 281
|
|
| PRK06130 |
PRK06130 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
296-582 |
4.56e-47 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 235707 [Multi-domain] Cd Length: 311 Bit Score: 169.18 E-value: 4.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 296 PVSSVGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEKEASKmqqSGHPWSGPKPRLTSSVKE-LGG 374
Cdd:PRK06130 3 PIQNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALERARGVIERALGVYAPL---GIASAGMGRIRMEAGLAAaVSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 375 VDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYSSPT 454
Cdd:PRK06130 80 ADLVIEAVPEKLELKRDVFARLDGLCDPDTIFATNTSGLPITAIAQAVTRPERFVGTHFFTPADVIPLVEVVRGDKTSPQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 455 TIATVMNLSKKIKKIGVVVG-NCFGFVGNRMLNPYYNQAYFLLEEG-SKPEEVDQVLE-EFGFKM---GPFRVSDLAGLD 528
Cdd:PRK06130 160 TVATTMALLRSIGKRPVLVKkDIPGFIANRIQHALAREAISLLEKGvASAEDIDEVVKwSLGIRLaltGPLEQRDMNGLD 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 68989263 529 V--GWKSRKGQGLTGPTLLPGTPARKRgnrrycpipdvlcELGRFGQKTGKGWYQY 582
Cdd:PRK06130 240 VhlAVASYLYQDLENRTTPSPLLEEKV-------------EAGELGAKSGQGFYAW 282
|
|
| PRK06035 |
PRK06035 |
3-hydroxyacyl-CoA dehydrogenase; Validated |
297-528 |
5.01e-47 |
|
3-hydroxyacyl-CoA dehydrogenase; Validated
Pssm-ID: 180361 [Multi-domain] Cd Length: 291 Bit Score: 168.51 E-value: 5.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 297 VSSVGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITS-------VLEKeaSKMQQSGHPWSGPKPRLTSSV 369
Cdd:PRK06035 3 IKVIGVVGSGVMGQGIAQVFARTGYDVTIVDVSEEILKNAMELIESgpyglrnLVEK--GKMSEDEAKAIMARIRTSTSY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 370 KELGGVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQ 449
Cdd:PRK06035 81 ESLSDADFIVEAVPEKLDLKRKVFAELERNVSPETIIASNTSGIMIAEIATALERKDRFIGMHWFNPAPVMKLIEVVRAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 450 YSSPTTIATVMNLSKKIKKIGVVVGNCFGFVGNRMLNPYYNQAYFLLEEG-SKPEEVDQVLE-EFGFKMGPFRVSDLAGL 527
Cdd:PRK06035 161 LTSEETFNTTVELSKKIGKIPIEVADVPGFFTTRFIEGWLLEAIRSFEIGiATIKDIDEMCKlAFGFPMGPFELMDIIGI 240
|
.
gi 68989263 528 D 528
Cdd:PRK06035 241 D 241
|
|
| PRK07658 |
PRK07658 |
enoyl-CoA hydratase; Provisional |
12-279 |
4.43e-46 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 181070 [Multi-domain] Cd Length: 257 Bit Score: 164.81 E-value: 4.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 12 ALIRLRNPPVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGaEGKF-SAGADIRGF----SAPRTFGLT-LGHVV-DEIQ 84
Cdd:PRK07658 13 AVITLNHPPANALSSQVLHELSELLDQVEKDDNVRVVVIHG-EGRFfSAGADIKEFtsvtEAEQATELAqLGQVTfERVE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 85 RNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEAL 164
Cdd:PRK07658 92 KFSKPVIAAIHGAALGGGLELAMSCHIRFATESAKLGLPELNLGLIPGFAGTQRLPRYVGKAKALEMMLTSEPITGAEAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 165 KLGILDKVVnsdPVEEAIRFAQRVsdqpleSRRLCNKPIQSLpnmdsifsEALLKMrrqhpgclaqeacvraVQAAVQYP 244
Cdd:PRK07658 172 KWGLVNGVF---PEETLLDDAKKL------AKKIAGKSPATT--------RAVLEL----------------LQTTKSSS 218
|
250 260 270
....*....|....*....|....*....|....*
gi 68989263 245 YEVGIKKEEELFLYLLQSGQARALQYAFFAERKAN 279
Cdd:PRK07658 219 YYEGVKREAKIFGEVFTSEDAKEGVQAFLEKRKPS 253
|
|
| PRK07819 |
PRK07819 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
293-582 |
9.42e-46 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 181133 [Multi-domain] Cd Length: 286 Bit Score: 164.77 E-value: 9.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 293 SARPVSSVGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEK--EASKMQQSGHPWSGPKPRLTSSVK 370
Cdd:PRK07819 1 MSDAIQRVGVVGAGQMGAGIAEVCARAGVDVLVFETTEELATAGRNRIEKSLERavSRGKLTERERDAALARLRFTTDLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 371 ELGGVDLVIEAVFEEMSLKKQVFAELSA-VCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQ 449
Cdd:PRK07819 81 DFADRQLVIEAVVEDEAVKTEIFAELDKvVTDPDAVLASNTSSIPIMKLAAATKRPGRVLGLHFFNPVPVLPLVELVPTL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 450 YSSPTTIATVMNL-SKKIKKIGVVVGNCFGFVGNRMLNPYYNQAYFLLEEG-SKPEEVDQVLEE-FGFKMGPFRVSDLAG 526
Cdd:PRK07819 161 VTSEATVARAEEFaSDVLGKQVVRAQDRSGFVVNALLVPYLLSAIRMVESGfATAEDIDKAMVLgCAHPMGPLRLSDLVG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 68989263 527 LD-------VGWKSRKGQGLTGPTLLpgtparkrgnRRycpipdvLCELGRFGQKTGKGWYQY 582
Cdd:PRK07819 241 LDtvkaiadSMYEEFKEPLYAPPPLL----------LR-------MVEAGLLGKKSGRGFYTY 286
|
|
| PRK08268 |
PRK08268 |
3-hydroxy-acyl-CoA dehydrogenase; Validated |
295-582 |
4.48e-45 |
|
3-hydroxy-acyl-CoA dehydrogenase; Validated
Pssm-ID: 236211 [Multi-domain] Cd Length: 507 Bit Score: 168.87 E-value: 4.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 295 RPVSSVGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEKEASKMQQSGHPWSGPKPRLT--SSVKEL 372
Cdd:PRK08268 5 PSIATVAVIGAGAMGAGIAQVAAQAGHTVLLYDARAGAAAAARDGIAARLAKLVEKGKLTAEQADAALARLRpvEALADL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 373 GGVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYSS 452
Cdd:PRK08268 85 ADCDLVVEAIVERLDVKQALFAQLEAIVSPDCILATNTSSLSITAIAAALKHPERVAGLHFFNPVPLMKLVEVVSGLATD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 453 PTTIATVMNLSKKIKKIGVVVGNCFGFVGNRMLNPYYNQAYFLLEEG-SKPEEVDQVL-EEFGFKMGPFRVSDLAGLDVG 530
Cdd:PRK08268 165 PAVADALYALARAWGKTPVRAKDTPGFIVNRAARPYYTEALRVLEEGvADPATIDAILrEAAGFRMGPFELMDLIGLDVN 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 68989263 531 wksrkgqgltgptlLPGTPARKR---GNRRYCP--IPDVLCELGRFGQKTGKGWYQY 582
Cdd:PRK08268 245 --------------HAVMESVYRqfyQEPRFRPslIQQELVAAGRLGRKSGQGFYRY 287
|
|
| PRK07530 |
PRK07530 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
294-585 |
1.24e-41 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 181018 [Multi-domain] Cd Length: 292 Bit Score: 153.62 E-value: 1.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 294 ARPVSSVGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEKEAS--KMQQSGHPWSGPKPRLTSSVKE 371
Cdd:PRK07530 1 MMAIKKVGVIGAGQMGNGIAHVCALAGYDVLLNDVSADRLEAGLATINGNLARQVAkgKISEEARAAALARISTATDLED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 372 LGGVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYS 451
Cdd:PRK07530 81 LADCDLVIEAATEDETVKRKIFAQLCPVLKPEAILATNTSSISITRLASATDRPERFIGIHFMNPVPVMKLVELIRGIAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 452 SPTTIATVMNLSKKIKKIGVVVGNCFGFVGNRMLNPYYNQAYFLLEEG-SKPEEVDQVLeEFG--FKMGPFRVSDLAGLD 528
Cdd:PRK07530 161 DEATFEAAKEFVTKLGKTITVAEDFPAFIVNRILLPMINEAIYTLYEGvGSVEAIDTAM-KLGanHPMGPLELADFIGLD 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68989263 529 vgwksrkgqgltgpTLLP-------GTPARKrgnRRYCPIPDVLCELGRFGQKTGKGWYQY--DKP 585
Cdd:PRK07530 240 --------------TCLSimqvlhdGLADSK---YRPCPLLVKYVEAGWLGRKTGRGFYDYrgEVP 288
|
|
| PRK07657 |
PRK07657 |
enoyl-CoA hydratase; Provisional |
4-210 |
6.49e-40 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 181069 [Multi-domain] Cd Length: 260 Bit Score: 147.57 E-value: 6.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 4 YTRLHNALALIRLRNP-PVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGA-EGKFSAGADIR---GFS---APRTFGLt 75
Cdd:PRK07657 7 VDYVTPHVVKITLNRPrAANALSLALLEELQNILTQINEEANVRVVILTGAgEKAFCAGADLKeraGMNeeqVRHAVSL- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 76 LGHVVDEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSG 155
Cdd:PRK07657 86 IRTTMEMVEQLPQPVIAAINGIALGGGLELALACDFRIAAESASLGLTETTLAIIPGAGGTQRLPRLIGVGRAKELIYTG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 68989263 156 RRILADEALKLGILDKVVNSDPVEE-AIRFAQRVSDQPLESRRLCNKPIQSLPNMD 210
Cdd:PRK07657 166 RRISAQEAKEIGLVEFVVPAHLLEEkAIEIAEKIASNGPIAVRQAKEAISNGIQVD 221
|
|
| PRK09076 |
PRK09076 |
enoyl-CoA hydratase; Provisional |
6-283 |
2.88e-39 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 236373 [Multi-domain] Cd Length: 258 Bit Score: 145.83 E-value: 2.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 6 RLHNALALIRLRNPPVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKF-SAGADIRGFS-----APRTFGLTLGHV 79
Cdd:PRK09076 8 EIDGHVAILTLNNPPANTWTADSLQALKQLVLELNADKDVYALVITGDGEKFfSAGADLNLFAdgdkaVAREMARRFGEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 80 VDEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRIL 159
Cdd:PRK09076 88 FEALSAFRGVSIAAINGYAMGGGLECALACDIRIAEEQAQMALPEASVGLLPCAGGTQNLPWLVGEGWAKRMILCGERVD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 160 ADEALKLGILDKVVNS-DPVEEAIRFAQRVSdqplesrrlcnkpiqslpnmdsifseallkmrRQHPGCLAqeACVRAVQ 238
Cdd:PRK09076 168 AATALRIGLVEEVVEKgEAREAALALAQKVA--------------------------------NQSPSAVA--ACKTLIQ 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 68989263 239 AAVQYPYEVGIKKEEELFLYLLQSGQARALQYAFFAERKANkWST 283
Cdd:PRK09076 214 AARNGPRAAALALERELFVDLFDTEDQREGVNAFLEKRAPQ-WKN 257
|
|
| PRK06688 |
PRK06688 |
enoyl-CoA hydratase; Provisional |
5-279 |
5.22e-39 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 235852 [Multi-domain] Cd Length: 259 Bit Score: 145.01 E-value: 5.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 5 TRLHNALALIRLRNP-PVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRGFSAPRTFGLT----LGHV 79
Cdd:PRK06688 9 VELEDGVLTITINRPdKKNALTAAMYQALADALEAAATDPAVRVVVLTGAGRAFSAGGDIKDFPKAPPKPPDelapVNRF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 80 VDEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRIL 159
Cdd:PRK06688 89 LRAIAALPKPVVAAVNGPAVGVGVSLALACDLVYASESAKFSLPFAKLGLCPDAGGSALLPRLIGRARAAEMLLLGEPLS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 160 ADEALKLGILDKVVnsdPVEEAIRFAQRVsdqpleSRRLCNKPiqslpnmdsifSEALLKMRrqhpgclaqeacvRAVQA 239
Cdd:PRK06688 169 AEEALRIGLVNRVV---PAAELDAEADAQ------AAKLAAGP-----------ASALRYTK-------------RAINA 215
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 68989263 240 AVQYPYEVGIKKEEELFLYLLQSGQARALQYAFFAERKAN 279
Cdd:PRK06688 216 ATLTELEEALAREAAGFGRLLRTPDFREGATAFIEKRKPD 255
|
|
| ECH_1 |
pfam00378 |
Enoyl-CoA hydratase/isomerase; This family contains a diverse set of enzymes including: ... |
9-192 |
1.13e-37 |
|
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: 140.96 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 9 NALALIRLRNP-PVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADI----RGFSAPRT-FGLTLGHVVDE 82
Cdd:pfam00378 4 AGVAVITLNRPeAVNALSAELITELIQALEKLRTDPSVRAVVLTGGDKAFCAGADLkemyGEGPAHQAlYRENVLDLWTL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 83 IQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADE 162
Cdd:pfam00378 84 LYTCPKPVIAAVNGYAIGGGCELALACDIIIAADNASFGLNETKLGIIPGAGGTDRLPRIIGHSKAMEMLLLGRRISAQE 163
|
170 180 190
....*....|....*....|....*....|.
gi 68989263 163 ALKLGILDKVVNSDPV-EEAIRFAQRVSDQP 192
Cdd:pfam00378 164 ALKWGLVDKVVPEDQLlDEARELAEKLAEKS 194
|
|
| PRK05809 |
PRK05809 |
short-chain-enoyl-CoA hydratase; |
11-203 |
2.65e-37 |
|
short-chain-enoyl-CoA hydratase;
Pssm-ID: 180270 [Multi-domain] Cd Length: 260 Bit Score: 140.27 E-value: 2.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 11 LALIRLRNP-PVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGA-EGKFSAGADIRGFS-----APRTFGLTLGHVVDEI 83
Cdd:PRK05809 14 IAVVTINRPkALNALNSETLKELDTVLDDIENDDNVYAVILTGAgEKAFVAGADISEMKdlneeEGRKFGLLGNKVFRKL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 84 QRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEA 163
Cdd:PRK05809 94 ENLDKPVIAAINGFALGGGCELSMACDIRIASEKAKFGQPEVGLGITPGFGGTQRLARIVGPGKAKELIYTGDMINAEEA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 68989263 164 LKLGILDKVVN-SDPVEEAIRFAQRVSDQPLESRRLCNKPI 203
Cdd:PRK05809 174 LRIGLVNKVVEpEKLMEEAKALANKIAANAPIAVKLCKDAI 214
|
|
| PRK05862 |
PRK05862 |
enoyl-CoA hydratase; Provisional |
12-222 |
6.40e-36 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 180295 [Multi-domain] Cd Length: 257 Bit Score: 136.33 E-value: 6.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 12 ALIRLRNP-PVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIrGFSAPRTFG-LTLGHVV---DEIQRN 86
Cdd:PRK05862 15 GLITLNRPkALNALNDALMDELGAALAAFDADEGIGAIVITGSEKAFAAGADI-KEMADLSFMdVYKGDYItnwEKVARI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 87 EKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKL 166
Cdd:PRK05862 94 RKPVIAAVAGYALGGGCELAMMCDIIIAADTAKFGQPEIKLGVLPGMGGSQRLTRAVGKAKAMDLCLTGRMMDAAEAERA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 68989263 167 GILDKVVNSDP-VEEAIRFAQRVSDQPLESRRLCNKPIQSlpNMDSIFSEALLKMRR 222
Cdd:PRK05862 174 GLVSRVVPADKlLDEALAAATTIASFSLPAVMMAKEAVNR--AYETTLAEGLLFERR 228
|
|
| PRK08138 |
PRK08138 |
enoyl-CoA hydratase; Provisional |
5-192 |
1.31e-34 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 236162 [Multi-domain] Cd Length: 261 Bit Score: 132.48 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 5 TRLHNALALIRLRNPPV-NAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRGFSAPRTFGLTLGHVV--- 80
Cdd:PRK08138 12 ERPADGVALLRLNRPEArNALNMEVRQQLAEHFTELSEDPDIRAIVLTGGEKVFAAGADIKEFATAGAIEMYLRHTEryw 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 81 DEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILA 160
Cdd:PRK08138 92 EAIAQCPKPVIAAVNGYALGGGCELAMHADIIVAGESASFGQPEIKVGLMPGAGGTQRLVRAVGKFKAMRMALTGCMVPA 171
|
170 180 190
....*....|....*....|....*....|...
gi 68989263 161 DEALKLGILDKVV-NSDPVEEAIRFAQRVSDQP 192
Cdd:PRK08138 172 PEALAIGLVSEVVeDEQTLPRALELAREIARMP 204
|
|
| PRK09674 |
PRK09674 |
enoyl-CoA hydratase-isomerase; Provisional |
8-196 |
2.39e-33 |
|
enoyl-CoA hydratase-isomerase; Provisional
Pssm-ID: 182026 [Multi-domain] Cd Length: 255 Bit Score: 128.73 E-value: 2.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 8 HNALALIRLRNPPV-NAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRGFsAPRTFGLTLG----HVVDE 82
Cdd:PRK09674 9 QQRVLLLTLNRPEArNALNNALLTQLVNELEAAATDTSIGVCVITGNARFFAAGADLNEM-AEKDLAATLNdprpQLWQR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 83 IQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADE 162
Cdd:PRK09674 88 LQAFNKPLIAAVNGYALGAGCELALLCDIVIAGENARFGLPEITLGIMPGAGGTQRLIRSVGKSLASQMVLTGESITAQQ 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 68989263 163 ALKLGILDKVVNSD-PVEEAIRFAQRVSDQ-PLESR 196
Cdd:PRK09674 168 AQQAGLVSEVFPPElTLERALQLASKIARHsPLALR 203
|
|
| PLN02600 |
PLN02600 |
enoyl-CoA hydratase |
11-196 |
9.56e-32 |
|
enoyl-CoA hydratase
Pssm-ID: 178210 [Multi-domain] Cd Length: 251 Bit Score: 124.15 E-value: 9.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 11 LALIRLRNPPV-NAISTTLLRDIKEGLQKAVIDHTIKAIVICGA-EGKFSAGADIR-----GFSAPRTFGLTLGHVVDEI 83
Cdd:PLN02600 5 IVELRLDRPEAkNAIGKEMLRGLRSAFEKIQADASARVVMLRSSvPGVFCAGADLKerrkmSPSEVQKFVNSLRSTFSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 84 QRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEA 163
Cdd:PLN02600 85 EALSIPTIAVVEGAALGGGLELALSCDLRICGEEAVFGLPETGLAIIPGAGGTQRLPRLVGRSRAKELIFTGRRIGAREA 164
|
170 180 190
....*....|....*....|....*....|....*
gi 68989263 164 LKLGILDKVVNS-DPVEEAIRFAQRVSDQ-PLESR 196
Cdd:PLN02600 165 ASMGLVNYCVPAgEAYEKALELAQEINQKgPLAIK 199
|
|
| 3HCDH |
pfam00725 |
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda ... |
478-582 |
8.68e-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: 113.08 E-value: 8.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 478 GFVGNRMLNPYYNQAYFLLEEG-SKPEEVDQVLEE-FGFKMGPFRVSDLAGLDVGWKSRKGQGLTGPTllpgtparkrGN 555
Cdd:pfam00725 1 GFVVNRLLAPYLNEAIRLVEEGvATPEDIDAAMRLgLGLPMGPFELSDLVGLDVGYHILEVLAEEFGD----------RA 70
|
90 100
....*....|....*....|....*..
gi 68989263 556 RRYCPIPDVLCELGRFGQKTGKGWYQY 582
Cdd:pfam00725 71 YRPPPLLEKLVEAGRLGRKTGKGFYKY 97
|
|
| PRK08293 |
PRK08293 |
3-hydroxyacyl-CoA dehydrogenase; |
300-582 |
8.07e-27 |
|
3-hydroxyacyl-CoA dehydrogenase;
Pssm-ID: 181359 [Multi-domain] Cd Length: 287 Bit Score: 110.80 E-value: 8.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 300 VGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMItsvlEKEASKMQQSGH-----PWSGPKPRL--TSSVKE- 371
Cdd:PRK08293 6 VTVAGAGVLGSQIAFQTAFHGFDVTIYDISDEALEKAKERI----AKLADRYVRDLEatkeaPAEAALNRItlTTDLAEa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 372 LGGVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYS 451
Cdd:PRK08293 82 VKDADLVIEAVPEDPEIKGDFYEELAKVAPEKTIFATNSSTLLPSQFAEATGRPEKFLALHFANEIWKNNTAEIMGHPGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 452 SPTTIATVMNLSKKIKKIGVVV-GNCFGFVGNRMLNPYYNQAYFLLEEG-SKPEEVDQV-LEEFGFKMGPFRVSDLAGLD 528
Cdd:PRK08293 162 DPEVFDTVVAFAKAIGMVPIVLkKEQPGYILNSLLVPFLSAALALWAKGvADPETIDKTwMIATGAPMGPFGILDIVGLD 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 68989263 529 VGWKSRKGQgltgptllpgtpARKRGNRRYCPIPDVLCEL---GRFGQKTGKGWYQY 582
Cdd:PRK08293 242 TAYNITSNW------------AEATDDENAKKAAALLKEYidkGKLGVATGEGFYNY 286
|
|
| PRK05980 |
PRK05980 |
crotonase/enoyl-CoA hydratase family protein; |
11-188 |
9.28e-27 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 180335 [Multi-domain] Cd Length: 260 Bit Score: 109.85 E-value: 9.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 11 LALIRLRNPP-VNAISTTLLRDIKEGLQKAVIDHTIKAIVICGA-EGKFSAGADIRGFS---------APRTF---GLTL 76
Cdd:PRK05980 13 IALLTLNRPEkLNALNYALIDRLLARLDAIEVDESVRAVILTGAgDRAFSAGADIHEFSasvaagadvALRDFvrrGQAM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 77 GHVVDEIQrneKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGR 156
Cdd:PRK05980 93 TARLEAFP---KPVIAAVNGLAFGGGCEITEAVHLAIASERALFAKPEIRLGMPPTFGGTQRLPRLAGRKRALELLLTGD 169
|
170 180 190
....*....|....*....|....*....|...
gi 68989263 157 RILADEALKLGILDKVV-NSDPVEEAIRFAQRV 188
Cdd:PRK05980 170 AFSAERALEIGLVNAVVpHEELLPAARALARRI 202
|
|
| PRK06129 |
PRK06129 |
3-hydroxyacyl-CoA dehydrogenase; Validated |
296-524 |
1.72e-25 |
|
3-hydroxyacyl-CoA dehydrogenase; Validated
Pssm-ID: 235706 [Multi-domain] Cd Length: 308 Bit Score: 107.44 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 296 PVSSVGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEKEASKMQQSGHP--WSGPKPRLTSSVKE-L 372
Cdd:PRK06129 1 PMGSVAIIGAGLIGRAWAIVFARAGHEVRLWDADPAAAAAAPAYIAGRLEDLAAFDLLDGEApdAVLARIRVTDSLADaV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 373 GGVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYSS 452
Cdd:PRK06129 81 ADADYVQESAPENLELKRALFAELDALAPPHAILASSTSALLASAFTEHLAGRERCLVAHPINPPYLIPVVEVVPAPWTA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68989263 453 PTTIATVMNLSKKIKKIGVVVGNCF-GFVGNRMLNPYYNQAYFLLEEG-SKPEEVDQVLEE-FGFK---MGPFRVSDL 524
Cdd:PRK06129 161 PATLARAEALYRAAGQSPVRLRREIdGFVLNRLQGALLREAFRLVADGvASVDDIDAVIRDgLGLRwsfMGPFETIDL 238
|
|
| PRK05869 |
PRK05869 |
enoyl-CoA hydratase; Validated |
11-194 |
1.88e-25 |
|
enoyl-CoA hydratase; Validated
Pssm-ID: 235632 [Multi-domain] Cd Length: 222 Bit Score: 104.92 E-value: 1.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 11 LALIRLRNPPVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADI---RGFSAPRTfgLTLGHV----VDEI 83
Cdd:PRK05869 18 LATLLLSRPPTNALTRQVYREIVAAANELGRRDDVAAVILYGGHEIFSAGDDMpelRTLSAQEA--DTAARVrqqaVDAV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 84 QRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEA 163
Cdd:PRK05869 96 AAIPKPTVAAITGYALGAGLTLALAADWRVSGDNVKFGATEILAGLAPSGDGMARLTRAAGPSRAKELVFSGRFFDAEEA 175
|
170 180 190
....*....|....*....|....*....|..
gi 68989263 164 LKLGILDKVVNSDPV-EEAIRFAQRVSDQPLE 194
Cdd:PRK05869 176 LALGLIDEMVAPDDVyDAAAAWARRFLDGPPH 207
|
|
| PRK07509 |
PRK07509 |
crotonase/enoyl-CoA hydratase family protein; |
8-201 |
5.87e-25 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 181008 [Multi-domain] Cd Length: 262 Bit Score: 104.96 E-value: 5.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 8 HNALALIRLRNP-PVNAISTTL---LRDIKEGLQKaviDHTIKAIVICGAEGKFSAGADIRGFSAP------RTFGLTLG 77
Cdd:PRK07509 10 EDGIADVRLNRPdKMNALDFAMfeeLIATIKRLKK---DRGIRAVILSGEGGAFCAGLDVKSVASSpgnavkLLFKRLPG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 78 ------HVVDEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDL 151
Cdd:PRK07509 87 nanlaqRVSLGWRRLPVPVIAALEGVCFGGGLQIALGADIRIAAPDTKLSIMEAKWGLVPDMAGTVSLRGLVRKDVAREL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 68989263 152 ITSGRRILADEALKLGILDKVVnSDPVEEAIRFAQRVS----DQPLESRRLCNK 201
Cdd:PRK07509 167 TYTARVFSAEEALELGLVTHVS-DDPLAAALALAREIAqrspDAIAAAKRLINR 219
|
|
| PRK06127 |
PRK06127 |
enoyl-CoA hydratase; Provisional |
5-183 |
6.18e-25 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 235705 Cd Length: 269 Bit Score: 104.79 E-value: 6.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 5 TRLHNALALIRLRNPP-VNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGK-FSAGADIRGFSAPRTF--GLTLGHVV 80
Cdd:PRK06127 15 AEKTGGLGRITFNNPArHNAMSLDMWEALPQALAAAEDDDAIRVVVLTGAGEKaFVSGADISQFEESRSDaeAVAAYEQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 81 DEIQRN-----EKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSG 155
Cdd:PRK06127 95 VEAAQAaladyAKPTIACIRGYCIGGGMGIALACDIRIAAEDSRFGIPAARLGLGYGYDGVKNLVDLVGPSAAKDLFYTA 174
|
170 180
....*....|....*....|....*...
gi 68989263 156 RRILADEALKLGILDKVVNSDPVEEAIR 183
Cdd:PRK06127 175 RRFDAAEALRIGLVHRVTAADDLETALA 202
|
|
| PRK08150 |
PRK08150 |
crotonase/enoyl-CoA hydratase family protein; |
5-217 |
8.35e-25 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 181254 Cd Length: 255 Bit Score: 104.33 E-value: 8.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 5 TRLHNALALIRLRNPPV-NAISTTLLRDIKEGLQKAviDHTIKAIVICGAEGKFSAGADIRGFSApRTFGLTLGH----- 78
Cdd:PRK08150 6 YELDGGVATIGLNRPAKrNALNDGLIAALRAAFARL--PEGVRAVVLHGEGDHFCAGLDLSELRE-RDAGEGMHHsrrwh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 79 -VVDEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRR 157
Cdd:PRK08150 83 rVFDKIQYGRVPVIAALHGAVVGGGLELASAAHIRVADESTYFALPEGQRGIFVGGGGSVRVPRLIGVARMTDMMLTGRV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68989263 158 ILADEALKLGILDKVV-NSDPVEEAIRFAQRV-SDQPLESRRLCN--KPIQSLPNMDSIFSEAL 217
Cdd:PRK08150 163 YDAQEGERLGLAQYLVpAGEALDKAMELARRIaQNAPLTNFAVLNalPRIADMSADDGLFVESL 226
|
|
| PRK06494 |
PRK06494 |
enoyl-CoA hydratase; Provisional |
11-195 |
1.33e-24 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 180591 [Multi-domain] Cd Length: 259 Bit Score: 103.58 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 11 LALIRLRNPPV-NAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGK-FSAGADIRGFSA-------PRTF-GLTLGHVV 80
Cdd:PRK06494 14 VTIVTLNRPEVmNALHLDAHFELEEVFDDFAADPEQWVAIVTGAGDKaFSAGNDLKEQAAggkrgwpESGFgGLTSRFDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 81 DeiqrneKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILA 160
Cdd:PRK06494 94 D------KPIIAAVNGVAMGGGFELALACDLIVAAENATFALPEPRVGLAALAGGLHRLPRQIGLKRAMGMILTGRRVTA 167
|
170 180 190
....*....|....*....|....*....|....*
gi 68989263 161 DEALKLGILDKVVnsdPVEEAIRFAQRVSDQPLES 195
Cdd:PRK06494 168 REGLELGFVNEVV---PAGELLAAAERWADDILAC 199
|
|
| PRK03580 |
PRK03580 |
crotonobetainyl-CoA hydratase; |
5-192 |
3.80e-24 |
|
crotonobetainyl-CoA hydratase;
Pssm-ID: 179599 [Multi-domain] Cd Length: 261 Bit Score: 102.47 E-value: 3.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 5 TRLHNALALIRLRNPPVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGK-FSAGADIR---------------GFSa 68
Cdd:PRK03580 7 TTRNGSILEITLDRPKANAIDAKTSFAMGEVFLNFRDDPELRVAIITGAGEKfFSAGWDLKaaaegeapdadfgpgGFA- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 69 prtfGLTlghvvdEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAA 148
Cdd:PRK03580 86 ----GLT------EIFDLDKPVIAAVNGYAFGGGFELALAADFIVCADNASFALPEAKLGIVPDSGGVLRLPKRLPPAIA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 68989263 149 LDLITSGRRILADEALKLGILDKVVNSDPVEEAIR-FAQRVSDQP 192
Cdd:PRK03580 156 NEMVMTGRRMDAEEALRWGIVNRVVPQAELMDRAReLAQQLVNSA 200
|
|
| PRK06023 |
PRK06023 |
crotonase/enoyl-CoA hydratase family protein; |
8-272 |
4.12e-24 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 168351 Cd Length: 251 Bit Score: 102.18 E-value: 4.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 8 HNALALIRLRNP-PVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRGFSAPRTFGLTLGHVVDE---- 82
Cdd:PRK06023 13 HPGVQVIRFNRPeKKNAITRAMYATMAKALKAADADDAIRAHVFLGTEGCFSAGNDMQDFLAAAMGGTSFGSEILDflia 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 83 IQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADE 162
Cdd:PRK06023 93 LAEAEKPIVSGVDGLAIGIGTTIHLHCDLTFASPRSLFRTPFVDLALVPEAGSSLLAPRLMGHQRAFALLALGEGFSAEA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 163 ALKLGILDKVVNSDPVE-EAIRFAQRVSDQPLESRRLcnkpiqslpnmdsifSEALLKMRRQHpgCLAQeacvravqaav 241
Cdd:PRK06023 173 AQEAGLIWKIVDEEAVEaETLKAAEELAAKPPQALQI---------------ARDLMRGPRED--ILAR----------- 224
|
250 260 270
....*....|....*....|....*....|.
gi 68989263 242 qypyevgIKKEEELFLYLLQSGQARALQYAF 272
Cdd:PRK06023 225 -------IDEEAKHFAARLKSAEARAAFEAF 248
|
|
| PRK08252 |
PRK08252 |
crotonase/enoyl-CoA hydratase family protein; |
22-281 |
1.00e-23 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 181325 [Multi-domain] Cd Length: 254 Bit Score: 100.83 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 22 NAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRGFSA---PRTFGLTLGHVVDeiQRNEKPVVAAIQGMA 98
Cdd:PRK08252 25 NAVNAAVAQGLAAALDELDADPDLSVGILTGAGGTFCAGMDLKAFARgerPSIPGRGFGGLTE--RPPRKPLIAAVEGYA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 99 FGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNS-DP 177
Cdd:PRK08252 103 LAGGFELALACDLIVAARDAKFGLPEVKRGLVAAGGGLLRLPRRIPYHIAMELALTGDMLTAERAHELGLVNRLTEPgQA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 178 VEEAIRFAQRVSDqplesrrlcNKPiqslpnmdsifseallkmrrqhpgcLAQEACVRAVQAAVQYPYEVGIKKEEELFL 257
Cdd:PRK08252 183 LDAALELAERIAA---------NGP-------------------------LAVAASKRIVVESGDWSEDEMFARQRELIA 228
|
250 260
....*....|....*....|....
gi 68989263 258 YLLQSGQARALQYAfFAERKANKW 281
Cdd:PRK08252 229 PVFTSADAKEGATA-FAEKRAPVW 251
|
|
| PRK06190 |
PRK06190 |
enoyl-CoA hydratase; Provisional |
8-197 |
3.39e-23 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 235733 Cd Length: 258 Bit Score: 99.66 E-value: 3.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 8 HNALALIRLRNPPV-NAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIR--GFSAPRTFGLTLGH-VVDEI 83
Cdd:PRK06190 11 HDRVRTLTLNRPEArNALSAALRRALFAALAEADADDDVDVVVLTGADPAFCAGLDLKelGGDGSAYGAQDALPnPSPAW 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 84 QRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEA 163
Cdd:PRK06190 91 PAMRKPVIGAINGAAVTGGLELALACDILIASERARFADTHARVGILPGWGLSVRLPQKVGIGRARRMSLTGDFLDAADA 170
|
170 180 190
....*....|....*....|....*....|....*
gi 68989263 164 LKLGILDKVV-NSDPVEEAIRFAQRVSDQPLESRR 197
Cdd:PRK06190 171 LRAGLVTEVVpHDELLPRARRLAASIAGNNPAAVR 205
|
|
| PRK08269 |
PRK08269 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
308-583 |
3.86e-23 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 181340 [Multi-domain] Cd Length: 314 Bit Score: 100.90 E-value: 3.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 308 MGRGIVISFARARIPVIAVDSDKNQ-------LATANKMITSVLEKEAS--KMQQSGHPWSGPKPRLTS---SVKELGGV 375
Cdd:PRK08269 1 MGQGIALAFAFAGHDVTLIDFKPRDaagwralDAEARAEIERTLAALVAlgRIDAAQADAVLARIAVVArdgAADALADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 376 DLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYSSPTT 455
Cdd:PRK08269 81 DLVFEAVPEVLDAKREALRWLGRHVDADAIIASTTSTFLVTDLQRHVAHPERFLNAHWLNPAYLMPLVEVSPSDATDPAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 456 IATVMNLSKKIKKIGVVVGNCFGFVGNRMLNPYYNQAYFLLEEG-SKPEEVDQVLEE-FGFK---MGPFRVSDLAGLDV- 529
Cdd:PRK08269 161 VDRLAALLERIGKVPVVCGPSPGYIVPRIQALAMNEAARMVEEGvASAEDIDKAIRTgFGLRfavLGLLEFIDWGGCDIl 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 68989263 530 GWKSRKGQGLTGPTllpgtparkrgnrRYCPiPDVL---CELGRFGQKTGKGWYQYD 583
Cdd:PRK08269 241 YYASRYLAGEIGPD-------------RFAP-PAIVvrnMEEGRDGLRTGAGFYDYA 283
|
|
| PRK06495 |
PRK06495 |
enoyl-CoA hydratase/isomerase family protein; |
11-197 |
4.27e-23 |
|
enoyl-CoA hydratase/isomerase family protein;
Pssm-ID: 168580 [Multi-domain] Cd Length: 257 Bit Score: 99.38 E-value: 4.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 11 LALIRLRNPPVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRGFSAPRTF-GLTLGH------VVDEI 83
Cdd:PRK06495 14 VAVVTLDNPPVNALSRELRDELIAVFDEISERPDVRVVVLTGAGKVFCAGADLKGRPDVIKGpGDLRAHnrrtreCFHAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 84 QRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQllpRLTGVPAALDLITSGRRILADEA 163
Cdd:PRK06495 94 RECAKPVIAAVNGPALGAGLGLVASCDIIVASENAVFGLPEIDVGLAGGGKHAM---RLFGHSLTRRMMLTGYRVPAAEL 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 68989263 164 LKLGILDKVVNSDP-VEEAIRFAQRV-SDQPLESRR 197
Cdd:PRK06495 171 YRRGVIEACLPPEElMPEAMEIAREIaSKSPLATRL 206
|
|
| PRK06143 |
PRK06143 |
enoyl-CoA hydratase; Provisional |
12-183 |
5.17e-23 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 180423 Cd Length: 256 Bit Score: 98.95 E-value: 5.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 12 ALIRLRNP-PVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGK-FSAGADIRGFSA-----PRTFGLTLGHVVDEIQ 84
Cdd:PRK06143 18 ATLTIRNAgSLNILGTPVILALTQALRWLAADPDVRVLVLRGAGEKaFIGGADIKEMATldqasAEAFISRLRDLCDAVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 85 RNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGlLPGARGTQLLPRLTGVPAALDLITSGRRILADEAL 164
Cdd:PRK06143 98 HFPVPVIARIPGWCLGGGLELAAACDLRIAAHDAQFGMPEVRVG-IPSVIHAALLPRLIGWARTRWLLLTGETIDAAQAL 176
|
170
....*....|....*....
gi 68989263 165 KLGILDKVVNSDPVEEAIR 183
Cdd:PRK06143 177 AWGLVDRVVPLAELDAAVE 195
|
|
| PRK05864 |
PRK05864 |
enoyl-CoA hydratase; Provisional |
11-189 |
1.38e-22 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 168278 [Multi-domain] Cd Length: 276 Bit Score: 98.37 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 11 LALIRLRNPP-VNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGAD---------IRGFSAPrTFGLTLGHVV 80
Cdd:PRK05864 20 IALITLNRPErMNSMAFDVMVPLKEALAEVSYDNSVRVVVLTGAGRGFSSGADhksagvvphVEGLTRP-TYALRSMELL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 81 DEI----QRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQV-------GLPEVTLGLlpgargTQLLPRLTGVPAAL 149
Cdd:PRK05864 99 DDVilalRRLHQPVIAAVNGPAIGGGLCLALAADIRVASSSAYFraaginnGLTASELGL------SYLLPRAIGSSRAF 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 68989263 150 DLITSGRRILADEALKLGILD-KVVNSDPVEEAIRFAQRVS 189
Cdd:PRK05864 173 EIMLTGRDVDAEEAERIGLVSrQVPDEQLLDTCYAIAARMA 213
|
|
| PRK05995 |
PRK05995 |
enoyl-CoA hydratase; Provisional |
10-218 |
2.17e-22 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 235664 [Multi-domain] Cd Length: 262 Bit Score: 97.30 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 10 ALALIRLRNPPV-NAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIR--------GFSAPRTFGLTLGHVV 80
Cdd:PRK05995 13 QVATVTLNRPDVrNAFNETVIAELTAAFRALDADDSVRAVVLAGAGKAFCAGADLNwmkkmagySDDENRADARRLADML 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 81 DEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPgargTQLLP---RLTGVPAALDLITSGRR 157
Cdd:PRK05995 93 RAIYRCPKPVIARVHGDAYAGGMGLVAACDIAVAADHAVFCLSEVRLGLIP----ATISPyviRAMGERAARRYFLTAER 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68989263 158 ILADEALKLGILDKVVNSDPVEEAI-RFAQRVSDQPLESRRLCNKPIQSLPNMDsiFSEALL 218
Cdd:PRK05995 169 FDAAEALRLGLVHEVVPAEALDAKVdELLAALVANSPQAVRAGKRLVRDVAGRP--IDAALI 228
|
|
| PRK09245 |
PRK09245 |
crotonase/enoyl-CoA hydratase family protein; |
42-201 |
4.11e-22 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 181723 Cd Length: 266 Bit Score: 96.58 E-value: 4.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 42 DHTIKAIVICGAEGKFSAGADIRGFSAPR-TFGLTLGHVVDE----IQR-------NEKPVVAAIQGMAFGGGLELALGC 109
Cdd:PRK09245 46 DRSVRAVILTGAGTAFSSGGNVKDMRARVgAFGGSPADIRQGyrhgIQRiplalynLEVPVIAAVNGPAIGAGCDLACMC 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 110 HYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDP-VEEAIRFAQRV 188
Cdd:PRK09245 126 DIRIASETARFAESFVKLGLIPGDGGAWLLPRIIGMARAAEMAFTGDAIDAATALEWGLVSRVVPADQlLPAARALAERI 205
|
170
....*....|...
gi 68989263 189 SDQPLESRRLCNK 201
Cdd:PRK09245 206 AANPPHALRLTKR 218
|
|
| PRK08259 |
PRK08259 |
crotonase/enoyl-CoA hydratase family protein; |
42-192 |
5.00e-22 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 236205 Cd Length: 254 Bit Score: 96.12 E-value: 5.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 42 DHTIKAIVICGAEGKFSAGADIRGFSAPRtfgltlGHVVDEIQ---------RNEKPVVAAIQGMAFGGGLELALGCHYR 112
Cdd:PRK08259 45 DDAASVAVLWGAGGTFCAGADLKAVGTGR------GNRLHPSGdgpmgpsrmRLSKPVIAAVSGYAVAGGLELALWCDLR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 113 IAHAEA-------QVGLPevtlgLLPGarGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNS-DPVEEAIRF 184
Cdd:PRK08259 119 VAEEDAvfgvfcrRWGVP-----LIDG--GTVRLPRLIGHSRAMDLILTGRPVDADEALAIGLANRVVPKgQARAAAEEL 191
|
....*...
gi 68989263 185 AQRVSDQP 192
Cdd:PRK08259 192 AAELAAFP 199
|
|
| PRK07799 |
PRK07799 |
crotonase/enoyl-CoA hydratase family protein; |
22-189 |
6.60e-22 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 181122 [Multi-domain] Cd Length: 263 Bit Score: 95.94 E-value: 6.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 22 NAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADI--------------RGFSAPRTFGLTLGHvvdeiqRNE 87
Cdd:PRK07799 27 NALSTEMLRIMVDAWDRVDNDPDIRSCILTGAGGAFCAGMDLkaatkkppgdsfkdGSYDPSRIDALLKGR------RLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 88 KPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLG 167
Cdd:PRK07799 101 KPLIAAVEGPAIAGGTEILQGTDIRVAGESAKFGISEAKWSLFPMGGSAVRLVRQIPYTVACDLLLTGRHITAAEAKEIG 180
|
170 180
....*....|....*....|...
gi 68989263 168 ILDKVV-NSDPVEEAIRFAQRVS 189
Cdd:PRK07799 181 LIGHVVpDGQALDKALELAELIN 203
|
|
| PRK08260 |
PRK08260 |
enoyl-CoA hydratase; Provisional |
6-191 |
1.20e-21 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 236206 [Multi-domain] Cd Length: 296 Bit Score: 95.84 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 6 RLHNALALIRLRNPP-VNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRGFSAprTFGL---------- 74
Cdd:PRK08260 9 DVADGIATITLNRPDkLNAFTVTMARELIEAFDAADADDAVRAVIVTGAGRAFCAGADLSAGGN--TFDLdaprtpvead 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 75 --------------TLGHVVDEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLP 140
Cdd:PRK08260 87 eedradpsddgvrdGGGRVTLRIFDSLKPVIAAVNGPAVGVGATMTLAMDIRLASTAARFGFVFGRRGIVPEAASSWFLP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 68989263 141 RLTGVPAALDLITSGRRILADEALKLGILDKVVNSDP-VEEAIRFAQRVSDQ 191
Cdd:PRK08260 167 RLVGLQTALEWVYSGRVFDAQEALDGGLVRSVHPPDElLPAARALAREIADN 218
|
|
| PRK06210 |
PRK06210 |
enoyl-CoA hydratase; Provisional |
8-191 |
3.45e-21 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 180472 Cd Length: 272 Bit Score: 94.00 E-value: 3.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 8 HNALALIRLRNPP-VNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADI-----------------RGFSAP 69
Cdd:PRK06210 13 DSGVAVITLNRPDrLNAWTPVMEAEVYAAMDRAEADPAVRVIVLTGAGRGFCAGADMgelqtidpsdgrrdtdvRPFVGN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 70 R-TFGLTLGHVVDEIQrneKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAA 148
Cdd:PRK06210 93 RrPDYQTRYHFLTALR---KPVIAAINGACAGIGLTHALMCDVRFAADGAKFTTAFARRGLIAEHGISWILPRLVGHANA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 68989263 149 LDLITSGRRILADEALKLGILDKVVNSDPV-EEAIRFAQRVSDQ 191
Cdd:PRK06210 170 LDLLLSARTFYAEEALRLGLVNRVVPPDELmERTLAYAEDLARN 213
|
|
| PRK07659 |
PRK07659 |
enoyl-CoA hydratase; Provisional |
7-224 |
3.34e-20 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 236073 [Multi-domain] Cd Length: 260 Bit Score: 90.86 E-value: 3.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 7 LHNALALIRLRNPPV-NAISTTLLRDIKEGLqKAVIDHTIKAIVICGaEGK-FSAGADIRGFSAPrTFGLTLGHVVDEIQ 84
Cdd:PRK07659 12 YEGRVATIMLNRPEAlNALDEPMLKELLQAL-KEVAESSAHIVVLRG-NGRgFSAGGDIKMMLSS-NDESKFDGVMNTIS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 85 R-------NEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRR 157
Cdd:PRK07659 89 EivvtlytMPKLTISAIHGPAAGLGLSIALTADYVIADISAKLAMNFIGIGLIPDGGGHFFLQKRVGENKAKQIIWEGKK 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68989263 158 ILADEALKLGILDKVVNSDPVEEAIRFAQRVSDQPLES-----RRLCNKPIQSLPNMDSIFSEALLKMRRQH 224
Cdd:PRK07659 169 LSATEALDLGLIDEVIGGDFQTAAKQKISEWLQKPLKAmietkQIYCELNRSQLEQVLQLEKRAQYAMRQTA 240
|
|
| PRK06144 |
PRK06144 |
enoyl-CoA hydratase; Provisional |
3-189 |
3.37e-20 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 180424 [Multi-domain] Cd Length: 262 Bit Score: 90.82 E-value: 3.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 3 EYTRLHNALALIRLRNPPVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGK-FSAGADIRGFSAPRT------FGLT 75
Cdd:PRK06144 11 LLEVRGGIARITFNRPAARNAMTWAMYEGLAEICEAIAADPSIRAVVLRGAGDKaFVAGTDIAQFRAFSTaedavaYERR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 76 LGHVVDEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEV-TLGLLPGARGTQLLPRLTGVPAALDLITS 154
Cdd:PRK06144 91 IDRVLGALEQLRVPTIAAIAGACVGGGAAIAAACDLRIATPSARFGFPIArTLGNCLSMSNLARLVALLGAARVKDMLFT 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 68989263 155 GRRILADEALKLGILDKVVNSDPVE-EAIRFAQRVS 189
Cdd:PRK06144 171 ARLLEAEEALAAGLVNEVVEDAALDaRADALAELLA 206
|
|
| PRK05870 |
PRK05870 |
enoyl-CoA hydratase; Provisional |
1-194 |
8.82e-20 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 180298 Cd Length: 249 Bit Score: 89.40 E-value: 8.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 1 MAEYTRLHNA--LALIRLRNPP-VNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRG-FSAP-RTFGLT 75
Cdd:PRK05870 1 MMDPVLLDVDdgVALITVNDPDrRNAVTAEMSAQLRAAVAAAEADPDVHALVVTGAGKAFCAGADLTAlGAAPgRPAEDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 76 LGHVVD---EIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLI 152
Cdd:PRK05870 81 LRRIYDgflAVASCPLPTIAAVNGAAVGAGLNLALAADVRIAGPKALFDARFQKLGLHPGGGATWMLQRAVGPQVARAAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 68989263 153 TSGRRILADEALKLGILDKVVNsDPVEEAIRFAQRVSDQPLE 194
Cdd:PRK05870 161 LFGMRFDAEAAVRHGLALMVAD-DPVAAALELAAGPAAAPRE 201
|
|
| ECH_2 |
pfam16113 |
Enoyl-CoA hydratase/isomerase; This family contains a diverse set of enzymes including: ... |
11-232 |
8.91e-20 |
|
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: 90.99 E-value: 8.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 11 LALIRLRNPPV-NAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGK-FSAGADIRGF---------SAPRTFgltlghV 79
Cdd:pfam16113 1 VGVITLNRPKAlNALNLEMVRALLAALKAWEDDPAVKLVVLKGAGERaFCAGGDVRALyeaakagggEAGRDF------F 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 80 VDE------IQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRL---TGVPAALd 150
Cdd:pfam16113 75 REEyrlnylIATYPKPYVALMDGIVMGGGVGLSVHGSFRVVTERTRFAMPETAIGLFPDVGGSYFLSRLpgeLGLYLAL- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 151 litSGRRILADEALKLGILDKVVNSDPVEEairfaqrvsdqpLESrRLCNKPIQSLPNMDSIFsEALLKMRRQHPGCLAQ 230
Cdd:pfam16113 154 ---TGARLNGADALAAGLATHYVPSARLPA------------LEE-ALAALDWSDPADVDAVL-AEFAEESDPPPSPLAA 216
|
..
gi 68989263 231 EA 232
Cdd:pfam16113 217 HR 218
|
|
| PRK07468 |
PRK07468 |
crotonase/enoyl-CoA hydratase family protein; |
22-182 |
1.09e-19 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 180987 [Multi-domain] Cd Length: 262 Bit Score: 89.35 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 22 NAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIR----GFSAPRTF----GLTLGHVVDEIQRNEKPVVAA 93
Cdd:PRK07468 27 NALSARMIAELTTAARRLAADAAVRVVVLTGAGKSFCAGGDLGwmraQMTADRATrieeARRLAMMLKALNDLPKPLIGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 94 IQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRlTGVPAALDLITSGRRILADEALKLGILDKVV 173
Cdd:PRK07468 107 IQGQAFGGGVGLISVCDVAIAVSGARFGLTETRLGLIPATISPYVVAR-MGEANARRVFMSARLFDAEEAVRLGLLSRVV 185
|
....*....
gi 68989263 174 NSDPVEEAI 182
Cdd:PRK07468 186 PAERLDAAV 194
|
|
| PRK06072 |
PRK06072 |
enoyl-CoA hydratase; Provisional |
8-201 |
2.34e-19 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 168377 [Multi-domain] Cd Length: 248 Bit Score: 88.30 E-value: 2.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 8 HNALALIRLRNP-PVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGaEGK-FSAGADIRGFSAPRTFGL--TLGHVVDEI 83
Cdd:PRK06072 7 REGYAIVTMSRPdKLNALNLEMRNEFISKLKQINADPKIRVVIVTG-EGRaFCVGADLSEFAPDFAIDLreTFYPIIREI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 84 QRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVpAALDLITSGRRILADEA 163
Cdd:PRK06072 86 RFSDKIYISAINGVTAGACIGIALSTDFKFASRDVKFVTAFQRLGLASDTGVAYFLLKLTGQ-RFYEILVLGGEFTAEEA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 68989263 164 LKLGILDkvVNSDPVEEAIRFAQRVSDQPLES----RRLCNK 201
Cdd:PRK06072 165 ERWGLLK--ISEDPLSDAEEMANRISNGPFQSyiaaKRMINL 204
|
|
| PRK07511 |
PRK07511 |
enoyl-CoA hydratase; Provisional |
5-224 |
4.70e-19 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 181009 [Multi-domain] Cd Length: 260 Bit Score: 87.36 E-value: 4.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 5 TRLHNALALIRLRNPPV-NAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRGFSAPRTFGLT-------- 75
Cdd:PRK07511 7 SRREGSTLVLTLSNPGArNALHPDMYAAGIEALNTAERDPSIRAVVLTGAGGFFCAGGNLNRLLENRAKPPSvqaasidg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 76 LGHVVDEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSG 155
Cdd:PRK07511 87 LHDWIRAIRAFPKPVIAAVEGAAAGAGFSLALACDLLVAARDAKFVMAYVKVGLTPDGGGSWFLARALPRQLATELLLEG 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68989263 156 RRILADEALKLGILDKVVN-SDPVEEAIRFAQRVSDQPLES----RRLCNK-PIQSLpnmdsifsEALLKMRRQH 224
Cdd:PRK07511 167 KPISAERLHALGVVNRLAEpGQALAEALALADQLAAGSPNAlariKSLIADaPEATL--------AAQLEAERDH 233
|
|
| PLN03214 |
PLN03214 |
probable enoyl-CoA hydratase/isomerase; Provisional |
10-196 |
5.87e-18 |
|
probable enoyl-CoA hydratase/isomerase; Provisional
Pssm-ID: 215635 Cd Length: 278 Bit Score: 84.55 E-value: 5.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 10 ALALIRLRNPPVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGK--FSAGADIRGFSAPRT-------FGLTLGHVV 80
Cdd:PLN03214 21 GIAVVWLAKEPVNSMTLAMWRSLDDALTALENDPTVRGVVFASGLRRdvFTAGNDIAELYAPKTsaaryaeFWLTQTTFL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 81 DEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGL-LPGARGTQLLPRLTGVPAALDLITSGRRIL 159
Cdd:PLN03214 101 VRLLRSRLATVCAIRGACPAGGCAVSLCCDYRLQTTEGTMGLNEVALGIpVPKFWARLFMGRVIDRKVAESLLLRGRLVR 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 68989263 160 ADEALKLGILDKVVNSDP-VEEAIRFAQRVSDQPLESR 196
Cdd:PLN03214 181 PAEAKQLGLIDEVVPAAAlMEAAASAMERALKLPSAAR 218
|
|
| PRK08258 |
PRK08258 |
enoyl-CoA hydratase family protein; |
29-192 |
7.58e-18 |
|
enoyl-CoA hydratase family protein;
Pssm-ID: 181329 Cd Length: 277 Bit Score: 84.25 E-value: 7.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 29 LRDIKEGLQKAvidHTIKAIVICGAEGKFSAGADIRGFSAPRT---------FGLTLGHVVDEIQRNEKPVVAAIQGMAF 99
Cdd:PRK08258 49 LRDLFRELVYA---DDVKAVVLTGAGGNFCSGGDVHEIIGPLTkmdmpellaFTRMTGDLVKAMRACPQPIIAAVDGVCA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 100 GGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGT-QLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDPV 178
Cdd:PRK08258 126 GAGAILAMASDLRLGTPSAKTAFLFTRVGLAGADMGAcALLPRIIGQGRASELLYTGRSMSAEEGERWGFFNRLVEPEEL 205
|
170
....*....|....*
gi 68989263 179 -EEAIRFAQRVSDQP 192
Cdd:PRK08258 206 lAEAQALARRLAAGP 220
|
|
| PRK08290 |
PRK08290 |
enoyl-CoA hydratase; Provisional |
1-192 |
9.10e-18 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 236220 [Multi-domain] Cd Length: 288 Bit Score: 84.24 E-value: 9.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 1 MAEYTR--LHNALALIRLRNPPV-NAISTTLLRDIKEGLQKAVIDHTIKAIVIcGAEGK-FSAGADIRGFSAPRTFG--- 73
Cdd:PRK08290 2 EYEYVRyeVAGRIARITLNRPEArNAQNRQMLYELDAAFRRAEADDAVRVIVL-AGAGKhFSAGHDLGSGTPGRDRDpgp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 74 -----LTLGHV----VDEIQRNE---------------KPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGl 129
Cdd:PRK08290 81 dqhptLWWDGAtkpgVEQRYAREwevylgmcrrwrdlpKPTIAQVQGACIAGGLMLAWVCDLIVASDDAFFSDPVVRMG- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 68989263 130 LPG----ARGTQLLPRltgvpAALDLITSGRRILADEALKLGILDKVVNSDPVE-EAIRFAQRVSDQP 192
Cdd:PRK08290 160 IPGveyfAHPWELGPR-----KAKELLFTGDRLTADEAHRLGMVNRVVPRDELEaETLELARRIAAMP 222
|
|
| PRK07827 |
PRK07827 |
enoyl-CoA hydratase family protein; |
22-203 |
1.14e-17 |
|
enoyl-CoA hydratase family protein;
Pssm-ID: 236109 [Multi-domain] Cd Length: 260 Bit Score: 83.58 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 22 NAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRgfSAPRTFGLTLGHVVDE----------IQRNEKPVV 91
Cdd:PRK07827 28 NALSARLVAQLHDGLRAAAADPAVRAVVLTHTGGTFCAGADLS--EAGGGGGDPYDAAVARaremtallraIVELPKPVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 92 AAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITsGRRILADEALKLGILdk 171
Cdd:PRK07827 106 AAIDGHVRAGGFGLVGACDIVVAGPESTFALTEARIGVAPAIISLTLLPRLSPRAAARYYLT-GEKFGAAEAARIGLV-- 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 68989263 172 VVNSDPVEEAI-RFA---QRVSDQPL-ESRRLCNKPI 203
Cdd:PRK07827 183 TAAADDVDAAVaALLadlRRGSPQGLaESKALTTAAV 219
|
|
| PRK07854 |
PRK07854 |
enoyl-CoA hydratase; Provisional |
10-193 |
2.95e-17 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 236115 [Multi-domain] Cd Length: 243 Bit Score: 81.99 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 10 ALALIRLRNPPV-NAISTTLLRDIKEGLQKAViDHTIKAIVICGAEGKFSAGADIRGFSAPRTFGLTLGHVVDEIQRNEK 88
Cdd:PRK07854 9 QVLTIELQRPERrNALNAELCEELREAVRKAV-DESARAIVLTGQGTVFCAGADLSGDVYADDFPDALIEMLHAIDAAPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 89 PVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGI 168
Cdd:PRK07854 88 PVIAAINGPAIGAGLQLAMACDLRVVAPEAYFQFPVAKYGIALDNWTIRRLSSLVGGGRARAMLLGAEKLTAEQALATGM 167
|
170 180
....*....|....*....|....*.
gi 68989263 169 LDKVVNSDpveEAIRFAQRVSDQ-PL 193
Cdd:PRK07854 168 ANRIGTLA---DAQAWAAEIAGLaPL 190
|
|
| PRK05617 |
PRK05617 |
3-hydroxyisobutyryl-CoA hydrolase; Provisional |
5-196 |
1.82e-16 |
|
3-hydroxyisobutyryl-CoA hydrolase; Provisional
Pssm-ID: 235533 [Multi-domain] Cd Length: 342 Bit Score: 81.40 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 5 TRLHNALALIRLrNPP--VNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGK-FSAGADIRGFSAPRTFGLTLGHVV- 80
Cdd:PRK05617 7 AEVEGGVGVITL-NRPkaLNALSLEMIRAIDAALDAWEDDDAVAAVVIEGAGERgFCAGGDIRALYEAARAGDPLAADRf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 81 --DE------IQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRL---TGVPAAL 149
Cdd:PRK05617 86 frEEyrlnalIARYPKPYIALMDGIVMGGGVGISAHGSHRIVTERTKMAMPETGIGFFPDVGGTYFLSRApgaLGTYLAL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 68989263 150 dlitSGRRILADEALKLGILDKVVNSDPVEEairFAQRVSDQPLESR 196
Cdd:PRK05617 166 ----TGARISAADALYAGLADHFVPSADLPA---LLDALISLRWDSG 205
|
|
| PRK08140 |
PRK08140 |
enoyl-CoA hydratase; Provisional |
7-192 |
4.49e-16 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 236163 Cd Length: 262 Bit Score: 78.80 E-value: 4.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 7 LHNALALIRLRNPP-VNAISTTLLRDIKEGLqKAVIDHTIKAIVICGAEGKFSAGADI--RGFsAPRTFGLTLGHVVDE- 82
Cdd:PRK08140 10 IEAGVATLTLNRPDkLNSFTREMHRELREAL-DQVEDDGARALLLTGAGRGFCAGQDLadRDV-TPGGAMPDLGESIETf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 83 -------IQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSG 155
Cdd:PRK08140 88 ynplvrrLRALPLPVIAAVNGVAAGAGANLALACDIVLAARSASFIQAFVKIGLVPDSGGTWFLPRLVGMARALGLALLG 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 68989263 156 RRILADEALKLGILDKVVNSDPV-EEAIRFAQRVSDQP 192
Cdd:PRK08140 168 EKLSAEQAEQWGLIWRVVDDAALaDEAQQLAAHLATQP 205
|
|
| PRK08139 |
PRK08139 |
enoyl-CoA hydratase; Validated |
6-188 |
6.22e-16 |
|
enoyl-CoA hydratase; Validated
Pssm-ID: 181249 Cd Length: 266 Bit Score: 78.45 E-value: 6.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 6 RLHNALALIRLRNPP-VNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRGFSAPR-------TFGLTlG 77
Cdd:PRK08139 16 EDRDGVATLTLNRPQaFNALSEAMLAALQAALDAIAADPSVRVVVLAAAGKAFCAGHDLKEMRAARglayfraLFARC-S 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 78 HVVDEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLL---PGARGTQLLPRltgvPAALDLITS 154
Cdd:PRK08139 95 RVMQAIVALPQPVIARVHGIATAAGCQLVASCDLAVAADTARFAVPGVNIGLFcstPMVALSRNVPR----KQAMEMLLT 170
|
170 180 190
....*....|....*....|....*....|....*
gi 68989263 155 GRRILADEALKLGILDKVVNSDPVEEAI-RFAQRV 188
Cdd:PRK08139 171 GEFIDAATAREWGLVNRVVPADALDAAVaRLAAVI 205
|
|
| PRK06213 |
PRK06213 |
crotonase/enoyl-CoA hydratase family protein; |
1-181 |
1.71e-15 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 235744 Cd Length: 229 Bit Score: 76.17 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 1 MAEYTrLHNALALIRLRNPPVNAISTTLLRDIKEGLQKAVIDHtiKAIVICGAEGKFSAGADIRGF-SAPR------TFG 73
Cdd:PRK06213 4 LVSYT-LEDGVATITLDDGKVNALSPAMIDALNAALDQAEDDR--AVVVITGQPGIFSGGFDLKVMtSGAQaaiallTAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 74 LTLGHvvdEIQRNEKPVVAAIQGMAFGGGLELALGCHYRI-AHAEAQVGLPEVTLGLLPGARGTQLLP-RLTgvPAALDL 151
Cdd:PRK06213 81 STLAR---RLLSHPKPVIVACTGHAIAKGAFLLLSADYRIgVHGPFKIGLNEVAIGMTMPHAAIELARdRLT--PSAFQR 155
|
170 180 190
....*....|....*....|....*....|.
gi 68989263 152 ITSGRRILA-DEALKLGILDKVVNSDPVEEA 181
Cdd:PRK06213 156 AVINAEMFDpEEAVAAGFLDEVVPPEQLLAR 186
|
|
| PRK11423 |
PRK11423 |
methylmalonyl-CoA decarboxylase; Provisional |
5-223 |
2.15e-15 |
|
methylmalonyl-CoA decarboxylase; Provisional
Pssm-ID: 236908 [Multi-domain] Cd Length: 261 Bit Score: 76.60 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 5 TRLHNALALIRLRNPP-VNAISTTLLRDIKEGLQkAVIDHTIKAIVICGAEGK--FSAGADIRGFSA----PRTFGLTLG 77
Cdd:PRK11423 8 VVTINKIATITFNNPAkRNALSKVLIDDLMQALS-DLNRPEIRVVILRAPSGSkvWSAGHDIHELPSggrdPLSYDDPLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 78 HVVDEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRR 157
Cdd:PRK11423 87 QILRMIQKFPKPVIAMVEGSVWGGAFELIMSCDLIIAASTSTFAMTPANLGVPYNLSGILNFTNDAGFHIVKEMFFTASP 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 68989263 158 ILADEALKLGILDKVVNSDPVEEAIR-FAQRVSDQ-PL------ESRRLcnkpIQSLPNMDSIFSEALLKMRRQ 223
Cdd:PRK11423 167 ITAQRALAVGILNHVVEVEELEDFTLqMAHHISEKaPLaiavikEQLRV----LGEAHPMNPDEFERIQGLRRA 236
|
|
| PRK06142 |
PRK06142 |
crotonase/enoyl-CoA hydratase family protein; |
1-172 |
2.48e-15 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 235714 Cd Length: 272 Bit Score: 76.94 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 1 MAEYT----RLHNALALIRLRNP-PVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRGFSA------- 68
Cdd:PRK06142 2 MTTYEsftvELADHVAQVTLNRPgKGNAMNPAFWSELPEIFRWLDADPEVRAVVLSGSGKHFSYGIDLPAMAGvfgqlgk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 69 -----PRTFG----LTLGHVVDEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLL 139
Cdd:PRK06142 82 dglarPRTDLrreiLRLQAAINAVADCRKPVIAAVQGWCIGGGVDLISACDMRYASADAKFSVREVDLGMVADVGSLQRL 161
|
170 180 190
....*....|....*....|....*....|...
gi 68989263 140 PRLTGVPAALDLITSGRRILADEALKLGILDKV 172
Cdd:PRK06142 162 PRIIGDGHLRELALTGRDIDAAEAEKIGLVNRV 194
|
|
| PRK05981 |
PRK05981 |
enoyl-CoA hydratase/isomerase; |
8-192 |
3.42e-14 |
|
enoyl-CoA hydratase/isomerase;
Pssm-ID: 235661 Cd Length: 266 Bit Score: 73.23 E-value: 3.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 8 HNALALIRLRNPPV-NAISTTLLRDIKEGLQKAVIDHT-IKAIVICGAEGKFSAGADIRGF-SAPRTF------GLTLGH 78
Cdd:PRK05981 11 DGGVAILTLDHPEVmNAVSIDMLGGLAEALDAIEDGKAeVRCLVLTGAGRGFCTGANLQGRgSGGRESdsggdaGAALET 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 79 V----VDEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITS 154
Cdd:PRK05981 91 AyhpfLRRLRNLPCPIVTAVNGPAAGVGMSFALMGDLILCARSAYFLQAFRRIGLVPDGGSTWLLPRLVGKARAMELSLL 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 68989263 155 GRRILADEALKLGILDKVVNSDPV-EEAIRFAQRVSDQP 192
Cdd:PRK05981 171 GEKLPAETALQWGLVNRVVDDAELmAEAMKLAHELANGP 209
|
|
| PRK09120 |
PRK09120 |
p-hydroxycinnamoyl CoA hydratase/lyase; Validated |
22-183 |
4.24e-14 |
|
p-hydroxycinnamoyl CoA hydratase/lyase; Validated
Pssm-ID: 236383 Cd Length: 275 Bit Score: 73.12 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 22 NAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRGFSApRTFGLTLGhVVDEIQRN-----------EKPV 90
Cdd:PRK09120 30 NAMSPTLNREMIDVLDALEFDDDAGVLVLTGAGDAWSAGMDLKEYFR-ETDAQPEI-LQERIRREaygwwrrlrwyQKPT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 91 VAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILD 170
Cdd:PRK09120 108 IAMVNGWCFGGGFSPLVACDLAIAADEAQFGLSEINWGIPPGGGVSKAMADTVGHRDALYYIMTGETFTGRKAAEMGLVN 187
|
170
....*....|...
gi 68989263 171 KVVNSDPVEEAIR 183
Cdd:PRK09120 188 ESVPLAQLRARTR 200
|
|
| PRK07260 |
PRK07260 |
enoyl-CoA hydratase; Provisional |
9-219 |
6.09e-14 |
|
enoyl-CoA hydratase; Provisional
Pssm-ID: 180910 [Multi-domain] Cd Length: 255 Bit Score: 72.46 E-value: 6.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 9 NALALIRLRNPPV-NAISTTLLRDIKEGLQKAVIDHTIKAIVIcGAEGK-FSAGADI----RGFSAPRTFGLT-LGHVVD 81
Cdd:PRK07260 10 DDLATLTLNRPEVsNGFNIPMCQEILEALRLAEEDPSVRFLLI-NANGKvFSVGGDLvemkRAVDEDDVQSLVkIAELVN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 82 EI----QRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRR 157
Cdd:PRK07260 89 EIsfaiKQLPKPVIMCVDGAVAGAAANMAVAADFCIASTKTKFIQAFVGVGLAPDAGGLFLLTRAIGLNRATHLAMTGEA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68989263 158 ILADEALKLGILDKVVNSDPVEeairfaqRVSDQPLEsrRLCNKPIQSLPNMDSIFSEALLK 219
Cdd:PRK07260 169 LTAEKALEYGFVYRVAESEKLE-------KTCEQLLK--KLRRGSSNSYAAIKSLVWESFFK 221
|
|
| PRK07938 |
PRK07938 |
enoyl-CoA hydratase family protein; |
5-181 |
7.30e-14 |
|
enoyl-CoA hydratase family protein;
Pssm-ID: 181174 Cd Length: 249 Bit Score: 71.93 E-value: 7.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 5 TRLHNALALIRLRNPPVNAISTTLLRDIKEGLQKAVIDHTIKAIVICgAEGK-FSAGADIRGFSAPRTFGLTLG------ 77
Cdd:PRK07938 6 TTPEPGIAEVTVDYPPVNALPSAGWFALADAITAAGADPDTRVVVLR-AEGRgFNAGVDIKELQATPGFTALIDanrgcf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 78 HVVDEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGArgTQlLPRLTGVPAALDLITSGRR 157
Cdd:PRK07938 85 AAFRAVYECAVPVIAAVHGFCLGGGIGLVGNADVIVASDDATFGLPEVDRGALGAA--TH-LQRLVPQHLMRALFFTAAT 161
|
170 180
....*....|....*....|....
gi 68989263 158 ILADEALKLGILDKVVNSDPVEEA 181
Cdd:PRK07938 162 ITAAELHHFGSVEEVVPRDQLDEA 185
|
|
| PLN02664 |
PLN02664 |
enoyl-CoA hydratase/delta3,5-delta2,4-dienoyl-CoA isomerase |
22-183 |
1.05e-13 |
|
enoyl-CoA hydratase/delta3,5-delta2,4-dienoyl-CoA isomerase
Pssm-ID: 178269 [Multi-domain] Cd Length: 275 Bit Score: 71.86 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 22 NAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRGFSAPRTFGLT----------------LGHVVDEIQR 85
Cdd:PLN02664 30 NALSLDFFTEFPKALSSLDQNPNVSVIILSGAGDHFCSGIDLKTLNSISEQSSSgdrgrsgerlrrkikfLQDAITAIEQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 86 NEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALK 165
Cdd:PLN02664 110 CRKPVIAAIHGACIGGGVDIVTACDIRYCSEDAFFSVKEVDLAITADLGTLQRLPSIVGYGNAMELALTGRRFSGSEAKE 189
|
170
....*....|....*....
gi 68989263 166 LGILDKVVNS-DPVEEAIR 183
Cdd:PLN02664 190 LGLVSRVFGSkEDLDEGVR 208
|
|
| PLN02888 |
PLN02888 |
enoyl-CoA hydratase |
5-191 |
3.15e-13 |
|
enoyl-CoA hydratase
Pssm-ID: 215480 Cd Length: 265 Bit Score: 70.55 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 5 TRLHNALALIRLRNP-PVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRgfSAPRTFGltlGHVVDE- 82
Cdd:PLN02888 14 PKSRNGIATITINRPkALNALTRPMMVELAAAFKRLDEDDSVKVIILTGSGRAFCSGVDLT--AAEEVFK---GDVKDVe 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 83 ------IQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGR 156
Cdd:PLN02888 89 tdpvaqMERCRKPIIGAINGFAITAGFEIALACDILVASRGAKFIDTHAKFGIFPSWGLSQKLSRIIGANRAREVSLTAM 168
|
170 180 190
....*....|....*....|....*....|....*
gi 68989263 157 RILADEALKLGILDKVVNSDpveEAIRFAQRVSDQ 191
Cdd:PLN02888 169 PLTAETAERWGLVNHVVEES---ELLKKAREVAEA 200
|
|
| PRK08788 |
PRK08788 |
enoyl-CoA hydratase; Validated |
91-183 |
3.34e-13 |
|
enoyl-CoA hydratase; Validated
Pssm-ID: 236338 Cd Length: 287 Bit Score: 70.71 E-value: 3.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 91 VAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILD 170
Cdd:PRK08788 125 IALVQGDALGGGFEAALSHHTIIAERGAKMGFPEILFNLFPGMGAYSFLARRVGPKLAEELILSGKLYTAEELHDMGLVD 204
|
90
....*....|...
gi 68989263 171 KVVNSDPVEEAIR 183
Cdd:PRK08788 205 VLVEDGQGEAAVR 217
|
|
| PRK06563 |
PRK06563 |
crotonase/enoyl-CoA hydratase family protein; |
5-193 |
1.49e-12 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 180625 [Multi-domain] Cd Length: 255 Bit Score: 68.06 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 5 TRLHNALALIRLRNP-PVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRGFSAPRTFGLTLgHVVDEI 83
Cdd:PRK06563 3 RERRGHVLLIGLDRPaKRNAFDSAMLDDLALALGEYEADDELRVAVLFAHGEHFTAGLDLADVAPKLAAGGFP-FPEGGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 84 -------QRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGR 156
Cdd:PRK06563 82 dpwgtvgRRLSKPLVVAVQGYCLTLGIELMLAADIVVAADNTRFAQLEVQRGILPFGGATLRFPQAAGWGNAMRYLLTGD 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 68989263 157 RILADEALKLGILDKVVNS-DPVEEAIRFAQRVSDQ-PL 193
Cdd:PRK06563 162 EFDAQEALRLGLVQEVVPPgEQLERAIELAERIARAaPL 200
|
|
| PRK07066 |
PRK07066 |
L-carnitine dehydrogenase; |
297-548 |
3.46e-11 |
|
L-carnitine dehydrogenase;
Pssm-ID: 168796 [Multi-domain] Cd Length: 321 Bit Score: 65.24 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 297 VSSVGVVGLGTMGRGIVisfARAR---IPVIAVDSDKNqlatANKMITSVLEKEASKMQQSG-HPWSGP-KPRLTSSVKE 371
Cdd:PRK07066 7 IKTFAAIGSGVIGSGWV---ARALahgLDVVAWDPAPG----AEAALRANVANAWPALERQGlAPGASPaRLRFVATIEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 372 -LGGVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQY 450
Cdd:PRK07066 80 cVADADFIQESAPEREALKLELHERISRAAKPDAIIASSTSGLLPTDFYARATHPERCVVGHPFNPVYLLPLVEVLGGER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 451 SSPTTIATVMNLskkIKKIGV----VVGNCFGFVGNRMLNPYYNQAYFLLEEG-SKPEEVDQVLeEFGFK-----MGPFR 520
Cdd:PRK07066 160 TAPEAVDAAMGI---YRALGMrplhVRKEVPGFIADRLLEALWREALHLVNEGvATTGEIDDAI-RFGAGirwsfMGTFL 235
|
250 260
....*....|....*....|....*....
gi 68989263 521 VSDLAGLDVGWKSRKGQglTGPTL-LPGT 548
Cdd:PRK07066 236 TYTLAGGDAGMRHFMQQ--FGPALeLPWT 262
|
|
| PLN02267 |
PLN02267 |
enoyl-CoA hydratase/isomerase family protein |
27-189 |
2.07e-10 |
|
enoyl-CoA hydratase/isomerase family protein
Pssm-ID: 215151 Cd Length: 239 Bit Score: 61.65 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 27 TLLRDIKEGLQKAVIDHTIKAIVICGAEGKF-SAGADIRGFSAPRTFGLTLGHVVDEIQRNEK-------PVVAAIQGMA 98
Cdd:PLN02267 26 TLIDSIRSALRQVKSQATPGSVLITTAEGKFfSNGFDLAWAQAAGSAPSRLHLMVAKLRPLVAdlislpmPTIAAVTGHA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 99 FGGGLELALGCHYRIAHAEAQV-GLPEVTLGLLPGARGTQLLPRLTGVPAAL-DLITSGRRILADEALKLGILDKVVNS- 175
Cdd:PLN02267 106 SAAGFILALSHDYVLMRKDRGVlYMSEVDIGLPLPDYFMALLRAKIGSPAARrDVLLRAAKLTAEEAVEMGIVDSAHDSa 185
|
170
....*....|....*
gi 68989263 176 -DPVEEAIRFAQRVS 189
Cdd:PLN02267 186 eETVEAAVRLGEELA 200
|
|
| PRK07110 |
PRK07110 |
polyketide biosynthesis enoyl-CoA hydratase; Validated |
22-198 |
8.97e-10 |
|
polyketide biosynthesis enoyl-CoA hydratase; Validated
Pssm-ID: 235936 Cd Length: 249 Bit Score: 59.98 E-value: 8.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 22 NAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRG----FSAPRTFGLTLghVVDEIQRNEKPVVAAIQGM 97
Cdd:PRK07110 27 NAFSDELCDQLHEAFDTIAQDPRYKVVILTGYPNYFATGGTQEGllslQTGKGTFTEAN--LYSLALNCPIPVIAAMQGH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 98 AFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDP 177
Cdd:PRK07110 105 AIGGGLVLGLYADIVVLSRESVYTANFMKYGFTPGMGATAILPEKLGLALGQEMLLTARYYRGAELKKRGVPFPVLPRAE 184
|
170 180
....*....|....*....|..
gi 68989263 178 V-EEAIRFAQRVSDQPLESRRL 198
Cdd:PRK07110 185 VlEKALELARSLAEKPRHSLVL 206
|
|
| PLN02921 |
PLN02921 |
naphthoate synthase |
10-188 |
3.82e-09 |
|
naphthoate synthase
Pssm-ID: 178509 [Multi-domain] Cd Length: 327 Bit Score: 59.03 E-value: 3.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 10 ALALIRLRNPPV-NAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGK-FSAGAD--IR---GFSAPRTFGLTlgHVVD- 81
Cdd:PLN02921 76 GIAKITINRPERrNAFRPRTVKELQRAFNDARDDSSVGVIILTGKGTKaFCSGGDqaVRgkdGYVGPDDAGRL--NVLDl 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 82 --EIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEA---QVGlPEVtlGLLPGARGTQLLPRLTGVPAALDLITSGR 156
Cdd:PLN02921 154 qiQIRRLPKPVIAMVAGYAVGGGHILHMVCDLTIAADNAvfgQTG-PKV--GSFDAGYGSSIMARLVGQKKAREMWFLAR 230
|
170 180 190
....*....|....*....|....*....|...
gi 68989263 157 RILADEALKLGILDKVVNSDPVE-EAIRFAQRV 188
Cdd:PLN02921 231 FYTASEALKMGLVNTVVPLDELEgETVKWCREI 263
|
|
| PRK08272 |
PRK08272 |
crotonase/enoyl-CoA hydratase family protein; |
22-209 |
2.01e-08 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 236213 Cd Length: 302 Bit Score: 56.59 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 22 NAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRGF----------SAPRTFGLTLGHVVDEI-------- 83
Cdd:PRK08272 32 NAITADTPLELRAAVERADLDPGVHVILVSGAGKGFCAGYDLSAYaegsssggggGAYPGKRQAVNHLPDDPwdpmidyq 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 84 --QRN----------EKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEV------TLGL----LPGARGTQLLpr 141
Cdd:PRK08272 112 mmSRFvrgfmslwhaHKPTVAKVHGYCVAGGTDIALHCDQVIAADDAKIGYPPTrvwgvpATGMwayrLGPQRAKRLL-- 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 68989263 142 LTGvpaalDLITsGRriladEALKLGIldkVVNSDPVEE----AIRFAQRVSDQPLE----SRRLCNkpiQSLPNM 209
Cdd:PRK08272 190 FTG-----DCIT-GA-----QAAEWGL---AVEAVPPEElderTERLVERIAAVPVNqlamVKLAVN---SALLQQ 248
|
|
| PLN02874 |
PLN02874 |
3-hydroxyisobutyryl-CoA hydrolase-like protein |
8-180 |
3.20e-08 |
|
3-hydroxyisobutyryl-CoA hydrolase-like protein
Pssm-ID: 178462 [Multi-domain] Cd Length: 379 Bit Score: 56.35 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 8 HNALALIRLRNPPV-NAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRGFSAPRTFGLTLGHVV------ 80
Cdd:PLN02874 18 KGRVRVITLNRPRQlNVISLSVVSLLAEFLEQWEKDDSVELIIIKGAGRAFSAGGDLKMFYDGRESDDSCLEVVyrmywl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 81 -DEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALdLITSGRRIL 159
Cdd:PLN02874 98 cYHIHTYKKTQVALVHGLVMGGGAGLMVPMKFRVVTEKTVFATPEASVGFHTDCGFSYILSRLPGHLGEY-LALTGARLN 176
|
170 180
....*....|....*....|.
gi 68989263 160 ADEALKLGILDKVVNSDPVEE 180
Cdd:PLN02874 177 GKEMVACGLATHFVPSEKLPE 197
|
|
| 3HCDH |
pfam00725 |
3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; This family also includes lambda ... |
619-710 |
3.66e-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: 51.45 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 619 ILERCLYSLINEAFRILGEGIaASPEHIDVVYLHGYGWPRhkgGPMFYASTVGLPTVLEKLQKYYRQNPDiPQLEPSDYL 698
Cdd:pfam00725 3 VVNRLLAPYLNEAIRLVEEGV-ATPEDIDAAMRLGLGLPM---GPFELSDLVGLDVGYHILEVLAEEFGD-RAYRPPPLL 77
|
90
....*....|..
gi 68989263 699 KKLASQGNPPLK 710
Cdd:pfam00725 78 EKLVEAGRLGRK 89
|
|
| PRK05674 |
PRK05674 |
gamma-carboxygeranoyl-CoA hydratase; Validated |
22-131 |
6.21e-08 |
|
gamma-carboxygeranoyl-CoA hydratase; Validated
Pssm-ID: 168168 Cd Length: 265 Bit Score: 54.43 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 22 NAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIR--------GFSAPRTFGLTLGHVVDEIQRNEKPVVAA 93
Cdd:PRK05674 28 NAFNAQMIRELILALDQVQSDASLRFLLLRGRGRHFSAGADLAwmqqsadlDYNTNLDDARELAELMYNLYRLKIPTLAV 107
|
90 100 110
....*....|....*....|....*....|....*...
gi 68989263 94 IQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLP 131
Cdd:PRK05674 108 VQGAAFGGALGLISCCDMAIGADDAQFCLSEVRIGLAP 145
|
|
| PRK07396 |
PRK07396 |
dihydroxynaphthoic acid synthetase; Validated |
9-188 |
1.32e-07 |
|
dihydroxynaphthoic acid synthetase; Validated
Pssm-ID: 180958 [Multi-domain] Cd Length: 273 Bit Score: 53.74 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 9 NALALIRLRNPPV-NAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGK-FSAGAD--IRGFSA-------PRTfgltlg 77
Cdd:PRK07396 21 DGIAKITINRPEVrNAFRPKTVKEMIDAFADARDDDNIGVIILTGAGDKaFCSGGDqkVRGYGGyvdddgvPRL------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 78 HVVD---EIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEA---QVGlPEVtlGLLPGARGTQLLPRLTGVPAALDL 151
Cdd:PRK07396 95 NVLDlqrLIRTCPKPVIAMVAGYAIGGGHVLHLVCDLTIAADNAifgQTG-PKV--GSFDGGYGASYLARIVGQKKAREI 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 68989263 152 ITSGRRILADEALKLGILDKVVNSDPVE-EAIRFAQRV 188
Cdd:PRK07396 172 WFLCRQYDAQEALDMGLVNTVVPLADLEkETVRWCREM 209
|
|
| PRK07112 |
PRK07112 |
enoyl-CoA hydratase/isomerase; |
22-246 |
1.61e-06 |
|
enoyl-CoA hydratase/isomerase;
Pssm-ID: 235938 Cd Length: 255 Bit Score: 50.07 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 22 NAISTTLLRDIKEGLQKavIDHTIKAIVICGAEGKFSAGADIRG------------FSAPRTFGLTLghvvdEIQRNEKP 89
Cdd:PRK07112 26 NTINDRLIAECMDVLDR--CEHAATIVVLEGLPEVFCFGADFSAiaekpdagradlIDAEPLYDLWH-----RLATGPYV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 90 VVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGArgtqLLP---RLTGVPAA--LDLITsgRRILADEAL 164
Cdd:PRK07112 99 TIAHVRGKVNAGGIGFVAASDIVIADETAPFSLSELLFGLIPAC----VLPfliRRIGTQKAhyMTLMT--QPVTAQQAF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 165 KLGILDkVVNSDPVEEAIRFAQRVsdqplesRRLcNKPiqSLPNMDSIFSEALLKMRRQHPGCLA-----------QEAC 233
Cdd:PRK07112 173 SWGLVD-AYGANSDTLLRKHLLRL-------RCL-NKA--AVARYKSYASTLDDTVAAARPAALAaniemfadpenLRKI 241
|
250
....*....|...
gi 68989263 234 VRAVQAAvQYPYE 246
Cdd:PRK07112 242 ARYVETG-KFPWE 253
|
|
| PRK12478 |
PRK12478 |
crotonase/enoyl-CoA hydratase family protein; |
10-220 |
8.11e-06 |
|
crotonase/enoyl-CoA hydratase family protein;
Pssm-ID: 183548 Cd Length: 298 Bit Score: 48.41 E-value: 8.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 10 ALALIRLRNPP-VNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRG----------------------F 66
Cdd:PRK12478 14 PVATITLNRPEqLNTIVPPMPDEIEAAIGLAERDQDIKVIVLRGAGRAFSGGYDFGGgfqhwgeammtdgrwdpgkdfaM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 67 SAPRTFGLTLGHVvdEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGllpGARGTQL-LPRLTGV 145
Cdd:PRK12478 94 VTARETGPTQKFM--AIWRASKPVIAQVHGWCVGGASDYALCADIVIASDDAVIGTPYSRMW---GAYLTGMwLYRLSLA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68989263 146 PAALDLITsGRRILADEALKLGILDKVVnsdPVEeaiRFAQRVSDQPLESRRLcnkPIQSLPNMDSIFSEALLKM 220
Cdd:PRK12478 169 KVKWHSLT-GRPLTGVQAAEAELINEAV---PFE---RLEARVAEVATELARI---PLSQLQAQKLIVNQAYENM 233
|
|
| PLN02988 |
PLN02988 |
3-hydroxyisobutyryl-CoA hydrolase |
17-232 |
3.61e-05 |
|
3-hydroxyisobutyryl-CoA hydrolase
Pssm-ID: 178568 [Multi-domain] Cd Length: 381 Bit Score: 46.63 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 17 RNPPVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRGFSAPRTFG---LTLGHVVDEIQRN------E 87
Cdd:PLN02988 26 RPKQLNALSFHMISRLLQLFLAFEEDPSVKLVILKGHGRAFCAGGDVAAVVRDIEQGnwrLGANFFSDEYMLNyvmatyS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 88 KPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITsGRRILADEALKLG 167
Cdd:PLN02988 106 KAQVSILNGIVMGGGAGVSVHGRFRIATENTVFAMPETALGLFPDVGASYFLSRLPGFFGEYVGLT-GARLDGAEMLACG 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 68989263 168 IldkvvnsdpveeAIRFAQRVSDQPLESrRLCNkpiqsLPNMDSIFSEALLKMRRQHPGCLAQEA 232
Cdd:PLN02988 185 L------------ATHFVPSTRLTALEA-DLCR-----IGSNDPTFASTILDAYTQHPRLKPQSA 231
|
|
| PRK08321 |
PRK08321 |
1,4-dihydroxy-2-naphthoyl-CoA synthase; |
57-188 |
1.05e-04 |
|
1,4-dihydroxy-2-naphthoyl-CoA synthase;
Pssm-ID: 181386 Cd Length: 302 Bit Score: 45.01 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 57 FSAGAD--IRGFSAPRTFGLTLGHVVD----------EIQR----NEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQV 120
Cdd:PRK08321 89 FCSGGDqrIRGRDGYQYAEGDEADTVDparagrlhilEVQRlirfMPKVVIAVVPGWAAGGGHSLHVVCDLTLASREHAR 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68989263 121 GL---PEVtlGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDPVE-EAIRFAQRV 188
Cdd:PRK08321 169 FKqtdADV--GSFDGGYGSAYLARQVGQKFAREIFFLGRTYSAEEAHDMGAVNAVVPHAELEtEALEWAREI 238
|
|
| PRK07327 |
PRK07327 |
enoyl-CoA hydratase/isomerase family protein; |
3-190 |
1.39e-04 |
|
enoyl-CoA hydratase/isomerase family protein;
Pssm-ID: 235991 Cd Length: 268 Bit Score: 44.24 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 3 EYTRLHNALALIRLRNPPV-NAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGAD---IRGFSAPRTFGLTLGH 78
Cdd:PRK07327 14 RFDRPPPGVLEIVLNGPGAlNAADARMHRELADIWRDVDRDPDVRVVLIRGEGKAFSAGGDlalVEEMADDFEVRARVWR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 79 VVDEIQRN----EKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITS 154
Cdd:PRK07327 94 EARDLVYNvincDKPIVSAIHGPAVGAGLVAALLADISIAAKDARIIDGHTRLGVAAGDHAAIVWPLLCGMAKAKYYLLL 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 68989263 155 GRRILADEALKLGILDKVVNSDPVEE-AIRFAQRVSD 190
Cdd:PRK07327 174 CEPVSGEEAERIGLVSLAVDDDELLPkALEVAERLAA 210
|
|
| PLN02740 |
PLN02740 |
Alcohol dehydrogenase-like |
282-499 |
1.83e-04 |
|
Alcohol dehydrogenase-like
Pssm-ID: 178341 [Multi-domain] Cd Length: 381 Bit Score: 44.40 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 282 STPSGASWKTASARPVSSVGVVGLGTMGRGiVISFARAR--IPVIAVDSDKNQLATANKM-ITSVLEKEASKmqqsghpw 358
Cdd:PLN02740 184 STGVGAAWNTANVQAGSSVAIFGLGAVGLA-VAEGARARgaSKIIGVDINPEKFEKGKEMgITDFINPKDSD-------- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 359 sgpKPrLTSSVKEL--GGVDLVIEAVFEEMSLKkqvfaelsavckpEAFLCTNtsaldvDEIASStdrphLVIGTHF--- 433
Cdd:PLN02740 255 ---KP-VHERIREMtgGGVDYSFECAGNVEVLR-------------EAFLSTH------DGWGLT-----VLLGIHPtpk 306
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 68989263 434 FSPAHVMKLLE---VIPSQYSSPTTIATVMNLSKKIKKiGVVvgNCFGFVGNRMLNPYYNQAYFLLEEG 499
Cdd:PLN02740 307 MLPLHPMELFDgrsITGSVFGDFKGKSQLPNLAKQCMQ-GVV--NLDGFITHELPFEKINEAFQLLEDG 372
|
|
| PLN02157 |
PLN02157 |
3-hydroxyisobutyryl-CoA hydrolase-like protein |
17-192 |
2.19e-04 |
|
3-hydroxyisobutyryl-CoA hydrolase-like protein
Pssm-ID: 177817 [Multi-domain] Cd Length: 401 Bit Score: 44.29 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 17 RNPPVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADI--------RGF-SAPRTFGLTLGHVVDEIQRNE 87
Cdd:PLN02157 54 RPPALNALTTHMGYRLQKLYKNWEEDPNIGFVMMKGSGRAFCAGGDIvslyhlrkRGSpDAIREFFSSLYSFIYLLGTYL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 88 KPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALdLITSGRRILADEALKLG 167
Cdd:PLN02157 134 KPHVAILNGVTMGGGTGVSIPGTFRVATDRTIFATPETIIGFHPDAGASFNLSHLPGRLGEY-LGLTGLKLSGAEMLACG 212
|
170 180
....*....|....*....|....*..
gi 68989263 168 ILDKVVNSD--PVEEAiRFAQRVSDQP 192
Cdd:PLN02157 213 LATHYIRSEeiPVMEE-QLKKLLTDDP 238
|
|
| liver_ADH_like1 |
cd08281 |
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ... |
283-382 |
2.82e-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: 43.91 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 283 TPSGASWKTASARPVSSVGVVGLGTMG----RGIVISFARariPVIAVD--SDKNQLATANKMITSVLEKEASKMQQsgh 356
Cdd:cd08281 178 TGVGAVVNTAGVRPGQSVAVVGLGGVGlsalLGAVAAGAS---QVVAVDlnEDKLALARELGATATVNAGDPNAVEQ--- 251
|
90 100
....*....|....*....|....*...
gi 68989263 357 pwsgpkprltssVKEL--GGVDLVIEAV 382
Cdd:cd08281 252 ------------VRELtgGGVDYAFEMA 267
|
|
| PLN02851 |
PLN02851 |
3-hydroxyisobutyryl-CoA hydrolase-like protein |
16-144 |
1.75e-03 |
|
3-hydroxyisobutyryl-CoA hydrolase-like protein
Pssm-ID: 178443 [Multi-domain] Cd Length: 407 Bit Score: 41.50 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 16 LRNPP-VNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIrgfsaprtfgLTLGHVVDEIQRNE------- 87
Cdd:PLN02851 57 LNRPSsLNALTIPMVARLKRLYESWEENPDIGFVLMKGSGRAFCSGADV----------VSLYHLINEGNVEEcklffen 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 68989263 88 ------------KPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTG 144
Cdd:PLN02851 127 lykfvylqgtylKPNVAIMDGITMGCGAGISIPGMFRVVTDKTVFAHPEVQMGFHPDAGASYYLSRLPG 195
|
|
| liver_alcohol_DH_like |
cd08277 |
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ... |
282-380 |
1.90e-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: 41.17 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 282 STPSGASWKTASARPVSSVGVVGLGTMGRGiVISFAR----ARIPVIAVDSDKNQLATANKMITSVLEKEASKMQQsghp 357
Cdd:cd08277 170 STGYGAAWNTAKVEPGSTVAVFGLGAVGLS-AIMGAKiagaSRIIGVDINEDKFEKAKEFGATDFINPKDSDKPVS---- 244
|
90 100
....*....|....*....|....*
gi 68989263 358 wsgpkprltSSVKEL--GGVDLVIE 380
Cdd:cd08277 245 ---------EVIREMtgGGVDYSFE 260
|
|
| FDH_like_ADH2 |
cd08286 |
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ... |
295-382 |
3.86e-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: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 295 RPVSSVGVVGLGTMGRGIVISfARARIP--VIAVDSDKNQLATANKMITSvlekeaskmqqsgHPWSGPKPRLTSSVKEL 372
Cdd:cd08286 165 KPGDTVAIVGAGPVGLAALLT-AQLYSPskIIMVDLDDNRLEVAKKLGAT-------------HTVNSAKGDAIEQVLEL 230
|
90
....*....|...
gi 68989263 373 ---GGVDLVIEAV 382
Cdd:cd08286 231 tdgRGVDVVIEAV 243
|
|
| alcohol_DH_plants |
cd08301 |
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ... |
282-339 |
6.67e-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: 6.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 68989263 282 STPSGASWKTASARPVSSVGVVGLGTMGRGiVISFARAR--IPVIAVDSDKNQLATANKM 339
Cdd:cd08301 173 STGLGAAWNVAKVKKGSTVAIFGLGAVGLA-VAEGARIRgaSRIIGVDLNPSKFEQAKKF 231
|
|
| alcohol_DH_class_III |
cd08300 |
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ... |
282-339 |
6.79e-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: 6.79e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68989263 282 STPSGASWKTASARPVSSVGVVGLGTMGRGiVISFARA----RIpvIAVDSDKNQLATANKM 339
Cdd:cd08300 172 TTGYGAVLNTAKVEPGSTVAVFGLGAVGLA-VIQGAKAagasRI--IGIDINPDKFELAKKF 230
|
|
| |
