|
Name |
Accession |
Description |
Interval |
E-value |
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
50-821 |
0e+00 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 1260.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 50 GAPLWVWIPYGGLVAVFNIGPIRRQV-SAGVMGVMEalQFLPTISETEQTAIDAGTVWMEGELFSGKPDFEKTLDQLYPE 128
Cdd:PRK09463 1 LWSLWLLVPLAIILLPLNLPPLRRSLiSAPLLKWFR--KVLPPMSQTEREALEAGTVWWEGELFSGKPDWKKLLNYPKPT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 129 LSDDEQAFLDGPCEEVCAMVDDWQV-HQRGDLSTETWDYLKEKGFFGLIIPEAYGGKGFSVAARSAVVQKLGGHSVPLSI 207
Cdd:PRK09463 79 LTAEEQAFLDGPVEELCRMVNDWQItHELADLPPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 208 TVMVPNSLGPGELLLHYGTDEQQDHYLPRLARGEILPSFALTEPNAGSDAGAMESTGEVFEDE---DGELKLRLNWEKRY 284
Cdd:PRK09463 159 TVMVPNSLGPGELLLHYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGVVCKGEwqgEEVLGMRLTWNKRY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 285 ISLAAISGVLGLAFKLHDPENHLGKGEDLGITCALVPTDTPGVKLGRRHDPLGVAFFNCPTEGEDVVLPLDAIIGGKDGA 364
Cdd:PRK09463 239 ITLAPIATVLGLAFKLYDPDGLLGDKEDLGITCALIPTDTPGVEIGRRHFPLNVPFQNGPTRGKDVFIPLDYIIGGPKMA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 365 GEGWAMLMDALSAGRGIMLPAQAVGGGKMVTRVAGGHAAIREQFGLSIGKFEGIEEPLARIAGYTYIMDAARTYTNGAVD 444
Cdd:PRK09463 319 GQGWRMLMECLSVGRGISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNAYLMDAARTLTTAAVD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 445 QGEKPGVVSAIMKYNTTELQRDLVNDGMDVLAGNGISQGPNNLMGLAYQAQPISITVEGANILTRTMMIFGQGAIRCHPY 524
Cdd:PRK09463 399 LGEKPSVLSAIAKYHLTERGRQVINDAMDIHGGKGICLGPNNFLARAYQAAPIAITVEGANILTRSLMIFGQGAIRCHPY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 525 ALDEIEALMEGD---VDAFDDAFWSHIGHVVRNGFRALGLSLTRGRLASSPVRGPAAPYYRKMAWASASFAFFADLAMGS 601
Cdd:PRK09463 479 VLKEMEAAQNNDkqaLKAFDKALFGHIGFVVSNAVRSFWLGLTGGRLSAAPVDDATKRYYRQLNRLSANLALLADVSMLV 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 602 LGGMLKRKEKITGRFADILSWMYLGTAVLTRFEKEGRPEEQEAFLHWSMQHAFAQMQEAFDGLFENLKVPGGTWLLRGLV 681
Cdd:PRK09463 559 LGGSLKRRERLSARLGDILSQLYLASAVLKRYEDEGRPEADLPLVHWAVQDALYQAEQALDGLLRNFPNRVVAGLLRVLV 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 682 APWSRLNTigeRPGDDLGSTLARAIQEKAGAREWLTEDLYVPDDPDQPLGELERAFRLSREAYHVGQKIKAAIRAGDLPK 761
Cdd:PRK09463 639 FPLGRRYR---APSDKLDHQVAKLLQTPSATRDRLTRGQYLPPSENNPVGRLEEALLDVIAAEPIEKKICKALKKGKLPF 715
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 762 RRPHQLLEEAVEHGVITEEDRALVRRADAARERYIQVDAFDLEEYRQGRMLPGQPADRGA 821
Cdd:PRK09463 716 LRLDELADEALAAGVISEEEAALLREAEEARLRVINVDDFDPEELAAKPVKLPEKVQKVE 775
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
54-802 |
0e+00 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 979.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 54 WVWIPYGGLVAVFNIGPIRRQVSAgvmgvMEALQF----LPTISETEQTAIDAGTVWMEGELFSGKPDFEKTLDQLYPEL 129
Cdd:PRK13026 4 LIILLLIAIVLVFAVKPLRRQFIT-----RPVFKFfkkvLPPLSDTEREAMEAGDVWWEGELFSGKPDWQKLHSYPKPTL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 130 SDDEQAFLDGPCEEVCAMVDDWQ-VHQRGDLSTETWDYLKEKGFFGLIIPEAYGGKGFSVAARSAVVQKLGGHSVPLSIT 208
Cdd:PRK13026 79 TAEEQAFIDNEVETLLTMLDDWDiVQNRKDLPPEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 209 VMVPNSLGPGELLLHYGTDEQQDHYLPRLARGEILPSFALTEPNAGSDAGAMESTGEVFEDE-DGE--LKLRLNWEKRYI 285
Cdd:PRK13026 159 VMVPNSLGPGELLTHYGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTGIVCRGEfEGEevLGLRLTWDKRYI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 286 SLAAISGVLGLAFKLHDPENHLGKGEDLGITCALVPTDTPGVKLGRRHDPLGVAFFNCPTEGEDVVLPLDAIIGGKDGAG 365
Cdd:PRK13026 239 TLAPVATVLGLAFKLRDPDGLLGDKKELGITCALIPTDHPGVEIGRRHNPLGMAFMNGTTRGKDVFIPLDWIIGGPDYAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 366 EGWAMLMDALSAGRGIMLPAQAVGGGKMVTRVAGGHAAIREQFGLSIGKFEGIEEPLARIAGYTYIMDAARTYTNGAVDQ 445
Cdd:PRK13026 319 RGWRMLVECLSAGRGISLPALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGNTYLLEAARRLTTTGLDL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 446 GEKPGVVSAIMKYNTTELQRDLVNDGMDVLAGNGISQGPNNLMGLAYQAQPISITVEGANILTRTMMIFGQGAIRCHPYA 525
Cdd:PRK13026 399 GVKPSVVTAIAKYHMTELARDVVNDAMDIHAGKGIQLGPKNYLGHAYMAVPIAITVEGANILTRNLMIFGQGATRCHPYV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 526 LDEIEALMEGD----VDAFDDAFWSHIGHVVRNGFRALGLSLTRGRLASSPVRGPAAPYYRKMAWASASFAFFADLAMGS 601
Cdd:PRK13026 479 LAEMEAAAMEDehegLEAFDSLLFKHIGYAARNAFRALFSALTGSRFISAPVSGETAQYYKDMSRLSAALALLADLSMLI 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 602 LGGMLKRKEKITGRFADILSWMYLGTAVLTRFEKEGRPEEQEAFLHWSMQHAFAQMQEAFDGLFENLKVPGGTWLLRGLV 681
Cdd:PRK13026 559 LGGDLKRKEMLSARLGDVLSQLYLASATLKRFEDNGRQQDDLPAVHYAMQDCLHLAAKALDEFLRNFPNRPVAWLLRALI 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 682 APWSRLNtigERPGDDLGSTLARAIQEKAGAREWLTEDLYVPDDPDQPLGELERAFRLSREAYHVGQKIKAAIRAGDLPK 761
Cdd:PRK13026 639 FPLGNHF---RAPSDKLARQLAELMMTPGPARDRLTALCYIFEGDKDGVARVEQAFLAQYAVKPLYKKLKKAQREGKLPR 715
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 2255954741 762 RRP-HQLLEEAVEHGVITEEDRALVRRADAARERYIQVDAFD 802
Cdd:PRK13026 716 KVPlLELFAKALEKGVITADEAEKLLAADKLRLDAIQVDDFT 757
|
|
| FadE_coli |
NF038187 |
acyl-CoA dehydrogenase FadE; This HMM describes a narrow clade of medium-chain and long-chain ... |
20-805 |
0e+00 |
|
acyl-CoA dehydrogenase FadE; This HMM describes a narrow clade of medium-chain and long-chain acyl-CoA dehydrogenases that includes YafH from Escherichia coli K-12 and Salmonella enterica LT2 (also called FadF), now called FadE.
Pssm-ID: 439499 [Multi-domain] Cd Length: 816 Bit Score: 919.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 20 GMLLVLAVLGYTGAPLWAWALAGAVGLYGGGA----PLWVWIPYGGLVAVFNIGPIRRQ-VSAGVM----GVMealqflP 90
Cdd:NF038187 6 AMLVLLGALAYHRVSLLTSSLILAAVMAAGTAaglwSLWLWLPFLIIALPLNVPSIRQSlISAPALkafrKVM------P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 91 TISETEQTAIDAGTVWMEGELFSGKPDFEKTLDQLYPELSDDEQAFLDGPCEEVCAMVDDWQV-HQRGDLSTETWDYLKE 169
Cdd:NF038187 80 EMSSTEKEAIDAGTTWWEADLFRGNPDWKKLHNYPKPRLTAEEQAFLDGPVEEVCRMVNDFQItHELADLPPEVWQYLKD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 170 KGFFGLIIPEAYGGKGFSVAARSAVVQKLGGHSVPLSITVMVPNSLGPGELLLHYGTDEQQDHYLPRLARGEILPSFALT 249
Cdd:NF038187 160 HRFFAMIIKKEYGGLEFSAYAQSRVLQKLAGVSSILASTVGVPNSLGPGELLQHYGTEEQKDHYLPRLARGEEIPCFALT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 250 EPNAGSDAGAMESTGEVFEDE-DGE--LKLRLNWEKRYISLAAISGVLGLAFKLHDPENHLGKGEDLGITCALVPTDTPG 326
Cdd:NF038187 240 SPEAGSDAGSIPDFGVVCKGEwQGEevLGMRLTWNKRYITLAPVATVLGLAFKLRDPDHLLGDKEELGITCALIPTDTPG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 327 VKLGRRHDPLGVAFFNCPTEGEDVVLPLDAIIGGKDGAGEGWAMLMDALSAGRGIMLPAQAVGGGKMVTRVAGGHAAIRE 406
Cdd:NF038187 320 VEIGRRHFPLNVPFQNGPTRGKDIFVPLDFIIGGPKMAGQGWRMLVECLSVGRGITLPSNSTGGLKSAALATGAYARIRR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 407 QFGLSIGKFEGIEEPLARIAGYTYIMDAARTYTNGAVDQGEKPGVVSAIMKYNTTELQRDLVNDGMDVLAGNGISQGPNN 486
Cdd:NF038187 400 QFKLPIGKMEGIEEPLARIAGNAYLMDAAATLTTTGIDLGEKPSVISAIVKYHCTHRGQRSIIDAMDIHGGKGICLGPNN 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 487 LMGLAYQAQPISITVEGANILTRTMMIFGQGAIRCHPYALDEIEALMEGD----VDAFDDAFWSHIGHVVRNGFRALGLS 562
Cdd:NF038187 480 FLARGYQGAPIAITVEGANILTRSMIIYGQGAIRCHPYVLAEMEAAQDNDseqaLNDFDKALFGHIGFVGSNLVRSFWLG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 563 LTRGRLASSPVRGPAAPYYRKMAWASASFAFFADLAMGSLGGMLKRKEKITGRFADILSWMYLGTAVLTRFEKEGRPEEQ 642
Cdd:NF038187 560 LTNGRFSSAPYKDATRRYYQQLNRLSANLALLSDVSMAVLGGSLKRRERISARLGDILSQLYLASATLKRYEDEGRQKED 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 643 EAFLHWSMQHAFAQMQEAFDGLFENL--KVPGGtwLLRGLVAPWSRLNTigeRPGDDLGSTLARAIQEKAGAREWLTEDL 720
Cdd:NF038187 640 LPLVHWAVQDSLYQAEQALDDLLRNFpnRLVAG--LLRVIIFPFGRPLK---APSDKLDHKVAKILQTPSATRSRLGRGQ 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 721 YVPDDPDQPLGELERAFR--LSREAYHvgQKI-KAAIRagDLPKRRPHQLLEEAVEHGVITEEDRALVRRADAARERYIQ 797
Cdd:NF038187 715 YLTPSEHNPVGLLEQALKdiLAAEPIH--DRVcKAAGK--RLPFMRLDKLAEEGLALGVITEEEAALLERAEASRLRSIN 790
|
....*...
gi 2255954741 798 VDAFDLEE 805
Cdd:NF038187 791 VDDFDPDE 798
|
|
| ACDH_C |
pfam09317 |
Acyl-CoA dehydrogenase, C-terminal, bacterial type; This C-terminal domain is functionally ... |
519-801 |
2.76e-140 |
|
Acyl-CoA dehydrogenase, C-terminal, bacterial type; This C-terminal domain is functionally uncharacterized and is predominantly found in various prokaryotic acyl-coenzyme A dehydrogenases and seems to be essential for its function.
Pssm-ID: 430522 [Multi-domain] Cd Length: 284 Bit Score: 417.66 E-value: 2.76e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 519 IRCHPYALDEIEALMEGD----VDAFDDAFWSHIGHVVRNGFRALGLSLTRGRLASSPVRGPAAPYYRKMAWASASFAFF 594
Cdd:pfam09317 1 IRCHPYVLKEMEAAQNEDkeqaLKAFDRALFGHIGFALSNAARSLVLGLTGGRFASAPVAGETARYYRQLNRLSAAFALL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 595 ADLAMGSLGGMLKRKEKITGRFADILSWMYLGTAVLTRFEKEGRPEEQEAFLHWSMQHAFAQMQEAFDGLFENLKVPGGT 674
Cdd:pfam09317 81 ADLAMLVLGGSLKRRERLSARLGDVLSQLYLASAVLKRFEDEGRPEADLPLVHWAMQDALYQAQQALDGVLRNFPNRPVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 675 WLLRGLVAPWSRLNtigERPGDDLGSTLARAIQEKAGAREWLTEDLYVPDDPDQPLGELERAFRLSREAYHVGQKIKAAI 754
Cdd:pfam09317 161 WLLRVLVFPLGRRY---RKPSDKLGHEVAQLLQEPGEARDRLTAGVYLPDDPDDPVGRLEAAFQAVLAAEPLEKKLKKAI 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2255954741 755 RAGDLPKRRPHQLLEEAVEHGVITEEDRALVRRADAARERYIQVDAF 801
Cdd:pfam09317 238 KAGKLPKLTLEELIEEALEKGVITEEEAELLREAEALRLDVIQVDDF 284
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
128-513 |
5.57e-89 |
|
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism]; Acyl-CoA dehydrogenase related to the alkylation response protein AidB is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 441563 [Multi-domain] Cd Length: 381 Bit Score: 287.51 E-value: 5.57e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 128 ELSDDEQAFLDGP---CEEVCA-MVDDWqvHQRGDLSTETWDYLKEKGFFGLIIPEAYGGKGFSVAARSAVVQKLGGHSV 203
Cdd:COG1960 4 ELTEEQRALRDEVrefAEEEIApEAREW--DREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 204 PLSITVMVPNslGPGELLLHYGTDEQQDHYLPRLARGEILPSFALTEPNAGSDAGAMESTGEvfEDEDGelkLRLNWEKR 283
Cdd:COG1960 82 SLALPVGVHN--GAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAV--RDGDG---YVLNGQKT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 284 YISLAAISGVLGLAFKLHDPENHlgkgedLGITCALVPTDTPGVKLGRRHDPLGVAFF-NCPTEGEDVVLPLDAIIGgkd 362
Cdd:COG1960 155 FITNAPVADVILVLARTDPAAGH------RGISLFLVPKDTPGVTVGRIEDKMGLRGSdTGELFFDDVRVPAENLLG--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 363 GAGEGWAMLMDALSAGRgIMLPAQAVGGGKMVTRVAGGHAAIREQFGLSIGKFEGIEEPLARIAGYTYIMDAARTYTNGA 442
Cdd:COG1960 226 EEGKGFKIAMSTLNAGR-LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWL 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2255954741 443 VDQGEKPGVVSAIMKYNTTELQRDLVNDGMDVLAGNGISQgpNNLMGLAYQAQPISITVEGANILTRTMMI 513
Cdd:COG1960 305 LDAGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTR--EYPLERLYRDARILTIYEGTNEIQRLIIA 373
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
162-482 |
6.05e-45 |
|
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases; Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.
Pssm-ID: 173847 [Multi-domain] Cd Length: 373 Bit Score: 166.29 E-value: 6.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 162 ETWDYLKEKGFFGLIIPEAYGGKGFSVAARSAVVQKLGGHSVPLSITVMVPNSLgPGELLLHYGTDEQQDHYLPRLARGE 241
Cdd:cd01158 34 EVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVIVSVHNSL-GANPIIKFGTEEQKKKYLPPLATGE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 242 ILPSFALTEPNAGSDAGAMESTGEvfEDEDGelkLRLNWEKRYISLAAISGVLgLAFKLHDPEnhlgKGEDlGITCALVP 321
Cdd:cd01158 113 KIGAFALSEPGAGSDAAALKTTAK--KDGDD---YVLNGSKMWITNGGEADFY-IVFAVTDPS----KGYR-GITAFIVE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 322 TDTPGVKLGRRHDPLGV-AFFNCPTEGEDVVLPLDAIIGGKdgaGEGWAMLMDALSAGRgIMLPAQAVGGGKMVTRVAGG 400
Cdd:cd01158 182 RDTPGLSVGKKEDKLGIrGSSTTELIFEDVRVPKENILGEE---GEGFKIAMQTLDGGR-IGIAAQALGIAQAALDAAVD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 401 HAAIREQFGLSIGKFEGIEEPLARIAgyTYImDAARTYTNGAV---DQGEKPGVVSAIMKYNTTELQRDLVNDGMDVLAG 477
Cdd:cd01158 258 YAKERKQFGKPIADFQGIQFKLADMA--TEI-EAARLLTYKAArlkDNGEPFIKEAAMAKLFASEVAMRVTTDAVQIFGG 334
|
....*
gi 2255954741 478 NGISQ 482
Cdd:cd01158 335 YGYTK 339
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
215-481 |
6.62e-43 |
|
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. In contrast, AXO catalyzes a different oxidative half-reaction, in which the reduced FAD is reoxidized by molecular oxygen. The ACAD family includes the eukaryotic beta-oxidation enzymes, short (SCAD), medium (MCAD), long (LCAD) and very-long (VLCAD) chain acyl-CoA dehydrogenases. These enzymes all share high sequence similarity, but differ in their substrate specificities. The ACAD family also includes amino acid catabolism enzymes such as Isovaleryl-CoA dehydrogenase (IVD), short/branched chain acyl-CoA dehydrogenases(SBCAD), Isobutyryl-CoA dehydrogenase (IBDH), glutaryl-CoA deydrogenase (GCD) and Crotonobetainyl-CoA dehydrogenase. The mitochondrial ACAD's are generally homotetramers, except for VLCAD, which is a homodimer. Related enzymes include the SOS adaptive reponse proten aidB, Naphthocyclinone hydroxylase (NcnH), and and Dibenzothiophene (DBT) desulfurization enzyme C (DszC)
Pssm-ID: 173838 [Multi-domain] Cd Length: 327 Bit Score: 158.99 E-value: 6.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 215 LGPGELLLHYGTDEQQDHYLPRLARGEILPSFALTEPNAGSDAGAMESTGEVFEDEdgelkLRLNWEKRYISLAAISGVL 294
Cdd:cd00567 42 LLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDG-----YVLNGRKIFISNGGDADLF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 295 GLAFKLHDPENHLGkgedlGITCALVPTDTPGVKLGRRHDPLGV-AFFNCPTEGEDVVLPLDAIIGgkdGAGEGWAMLMD 373
Cdd:cd00567 117 IVLARTDEEGPGHR-----GISAFLVPADTPGVTVGRIWDKMGMrGSGTGELVFDDVRVPEDNLLG---EEGGGFELAMK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 374 ALSAGRgIMLPAQAVGGGKMVTRVAGGHAAIREQFGLSIGKFEGIEEPLARIAGYTYIMDAARTYTNGAVDQGE-KPGVV 452
Cdd:cd00567 189 GLNVGR-LLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPdEARLE 267
|
250 260
....*....|....*....|....*....
gi 2255954741 453 SAIMKYNTTELQRDLVNDGMDVLAGNGIS 481
Cdd:cd00567 268 AAMAKLFATEAAREVADLAMQIHGGRGYS 296
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
110-479 |
5.59e-42 |
|
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is found in the mitochondria of eukaryotes and in some bacteria. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. VLCAD acts as a homodimer.
Pssm-ID: 173850 [Multi-domain] Cd Length: 409 Bit Score: 158.79 E-value: 5.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 110 ELFSGKpdfeKTLDQLYPE---LSDDEQAFLD---GPCEE-VCAMVDDWQVHQRGDLSTETWDYLKEKGFFGLIIPEAYG 182
Cdd:cd01161 5 NMFLGD----IVTKQVFPYpsvLTEEQTEELNmlvGPVEKfFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 183 GKGFSVAARSAVVQKLGgHSVPLSITVMVPNSLGPGELLLhYGTDEQQDHYLPRLARGEILPSFALTEPNAGSDAGAMES 262
Cdd:cd01161 81 GLGLNNTQYARLAEIVG-MDLGFSVTLGAHQSIGFKGILL-FGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 263 TGEVfeDEDGELKLrLNWEKRYISLAAISGVLgLAFKLHDPENHLGKGEDlGITCALVPTDTPGVKLGRRHDPLGVAFFN 342
Cdd:cd01161 159 TAVL--SEDGKHYV-LNGSKIWITNGGIADIF-TVFAKTEVKDATGSVKD-KITAFIVERSFGGVTNGPPEKKMGIKGSN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 343 -CPTEGEDVVLPLDAIIGgkdGAGEGWAMLMDALSAGRgIMLPAQAVGGGKMVTRVAGGHAAIREQFGLSIGKFEGIEEP 421
Cdd:cd01161 234 tAEVYFEDVKIPVENVLG---EVGDGFKVAMNILNNGR-FGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEK 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 422 LARIAGYTYIMDAARTYTNGAVDQGEKP--GVVSAIMKYNTTELQRDLVNDGMDVLAGNG 479
Cdd:cd01161 310 LANMAILQYATESMAYMTSGNMDRGLKAeyQIEAAISKVFASEAAWLVVDEAIQIHGGMG 369
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
162-479 |
4.70e-27 |
|
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA dehydrogenase, which catalyzes the third step in leucine catabolism, the conversion of isovaleryl-CoA (3-methylbutyryl-CoA) into 3-methylcrotonyl-CoA. IVD is a homotetramer and has the greatest affinity for small branched chain substrates.
Pssm-ID: 173845 [Multi-domain] Cd Length: 376 Bit Score: 114.05 E-value: 4.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 162 ETWDYLKEKGFFGLIIPEAYGGKGFSVAARSAVVQKL-----------GGHSvPLSITVMVPNslgpgelllhyGTDEQQ 230
Cdd:cd01156 37 DLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEIsrasgsvalsyGAHS-NLCINQIYRN-----------GSAAQK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 231 DHYLPRLARGEILPSFALTEPNAGSDAGAMESTGEVFEDEdgelkLRLNWEKRYISLAAISGVLgLAFKLHDPENHLGkg 310
Cdd:cd01156 105 EKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDR-----YVLNGSKMWITNGPDADTL-VVYAKTDPSAGAH-- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 311 edlGITCALVPTDTPGV-------KLGRRHDPLGVAFFncptegEDVVLPLDAIIGGKdgaGEGWAMLMDALSAGRgIML 383
Cdd:cd01156 177 ---GITAFIVEKGMPGFsraqkldKLGMRGSNTCELVF------EDCEVPEENILGGE---NKGVYVLMSGLDYER-LVL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 384 PAQAVGGGKMVTRVAGGHAAIREQFGLSIGKFEGIEEPLARIagYT-------YIMDAARTYTNGAVDQGEKPGVvsaIM 456
Cdd:cd01156 244 AGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADM--YTrlnasrsYLYTVAKACDRGNMDPKDAAGV---IL 318
|
330 340
....*....|....*....|...
gi 2255954741 457 kYnTTELQRDLVNDGMDVLAGNG 479
Cdd:cd01156 319 -Y-AAEKATQVALDAIQILGGNG 339
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
129-479 |
2.83e-25 |
|
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- dehydrogenation of short branched chain acyl-CoA intermediates in valine catabolism. It is predicted to be a homotetramer.
Pssm-ID: 173851 [Multi-domain] Cd Length: 375 Bit Score: 108.68 E-value: 2.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 129 LSDDEQAF----LDGPCEEVCAMVDDWQvhQRGDLSTETWDYLKEKGFFGLIIPEAYGGKGFSVAARSAVVQKLGGHSVP 204
Cdd:cd01162 1 LNEEQRAIqevaRAFAAKEMAPHAADWD--QKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 205 ----LSITVMVpnslgpGELLLHYGTDEQQDHYLPRLARGEILPSFALTEPNAGSDAGAMESTGEvfedEDGELKLrLNW 280
Cdd:cd01162 79 taayISIHNMC------AWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAV----REGDHYV-LNG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 281 EKRYISLAAISGVLGLAFKlhdpenhlgKGED--LGITCALVPTDTPGVKLGRRHDPLGvaFFNCPTEG---EDVVLPLD 355
Cdd:cd01162 148 SKAFISGAGDSDVYVVMAR---------TGGEgpKGISCFVVEKGTPGLSFGANEKKMG--WNAQPTRAvifEDCRVPVE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 356 AIIGGKdgaGEGWAMLMDALSAGRgIMLPAQAVGGGKMVTRVAGGHAAIREQFGLSIGKFEGIEEPLARIAGYTYimdAA 435
Cdd:cd01162 217 NRLGGE---GQGFGIAMAGLNGGR-LNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELV---AS 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2255954741 436 RTYTNGA---VDQGEKPGV-VSAIMKYNTTELQRDLVNDGMDVLAGNG 479
Cdd:cd01162 290 RLMVRRAasaLDRGDPDAVkLCAMAKRFATDECFDVANQALQLHGGYG 337
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
129-481 |
3.47e-25 |
|
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans.
Pssm-ID: 173840 [Multi-domain] Cd Length: 386 Bit Score: 108.60 E-value: 3.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 129 LSDDEQAFLDGP---C-EEVCAMVDDWqvHQRGDLSTETWDYLKEKGFFGlIIPEAYGGKGFSVAARSAVVQKLGGHSVP 204
Cdd:cd01151 13 LTEEERAIRDTArefCqEELAPRVLEA--YREEKFDRKIIEEMGELGLLG-ATIKGYGCAGLSSVAYGLIAREVERVDSG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 205 LSITVMVPNSLGPGELLLhYGTDEQQDHYLPRLARGEILPSFALTEPNAGSDAGAMESTGEvfEDEDGelkLRLNWEKRY 284
Cdd:cd01151 90 YRSFMSVQSSLVMLPIYD-FGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRAR--KDGGG---YKLNGSKTW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 285 ISLAAISGVLgLAFKLHDPENhlgkgedlGITCALVPTDTPGV-------KLGRRHDPLGVAFFncptegEDVVLPLDAI 357
Cdd:cd01151 164 ITNSPIADVF-VVWARNDETG--------KIRGFILERGMKGLsapkiqgKFSLRASITGEIVM------DNVFVPEENL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 358 IGGKDGAGEGWAMLMDAlsagRgIMLPAQAVGGGKMVTRVAGGHAAIREQFGLSIGKFEGIEEPLARIAGYTYIMDAART 437
Cdd:cd01151 229 LPGAEGLRGPFKCLNNA----R-YGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACL 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2255954741 438 YTNGAVDQGE-KPGVVSaIMKYNTTELQRDLVNDGMDVLAGNGIS 481
Cdd:cd01151 304 RVGRLKDQGKaTPEQIS-LLKRNNCGKALEIARTAREMLGGNGIS 347
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
142-479 |
4.93e-25 |
|
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found in the mitochondria of eukaryotes and in some prokaryotes. It catalyzes the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of LCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. LCAD acts as a homodimer.
Pssm-ID: 173849 [Multi-domain] Cd Length: 372 Bit Score: 107.97 E-value: 4.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 142 EEVCAMVDDWQvhQRGDLSTETWDYLKEKGFFGLIIPEAYGGKGFSVAARSAVVQKLGgHSVPLSITVMVPNSLGpGELL 221
Cdd:cd01160 16 KEVAPFHHEWE--KAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELA-RAGGSGPGLSLHTDIV-SPYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 222 LHYGTDEQQDHYLPRLARGEILPSFALTEPNAGSDAGAMESTGEvfedEDGELKLrLNWEKRYISLAAISGVLGLAFKLH 301
Cdd:cd01160 92 TRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTAR----KDGDHYV-LNGSKTFITNGMLADVVIVVARTG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 302 DPENHLGkgedlGITCALVPTDTPGVKLGRRHDPLGVA-------FFncptegEDVVLPLDAIIGGKdgaGEGWAMLMDA 374
Cdd:cd01160 167 GEARGAG-----GISLFLVERGTPGFSRGRKLKKMGWKaqdtaelFF------DDCRVPAENLLGEE---NKGFYYLMQN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 375 LSAGRgIMLPAQAVGGGKMVTRVAGGHAAIREQFGLSIGKFEGIEEPLARIAGYtyiMDAARTYTNGAV---DQGEKPGV 451
Cdd:cd01160 233 LPQER-LLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATK---VAVTRAFLDNCAwrhEQGRLDVA 308
|
330 340
....*....|....*....|....*...
gi 2255954741 452 VSAIMKYNTTELQRDLVNDGMDVLAGNG 479
Cdd:cd01160 309 EASMAKYWATELQNRVAYECVQLHGGWG 336
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
167-486 |
3.73e-21 |
|
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 96.65 E-value: 3.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 167 LKEKGFFGLIIPEAYGGKGFSVAARSAVVQKLGGHSVPLSITVMVPNSLGPgeLLLHYGTDEQQDHYLPRLARGEILPSF 246
Cdd:cd01152 44 LAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIGIDLAGP--TILAYGTDEQKRRFLPPILSGEEIWCQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 247 ALTEPNAGSDAGAMESTGEvfedEDGElKLRLNWEKRYISLAAISGVLGLAFKLhDPENHLGKgedlGITCALVPTDTPG 326
Cdd:cd01152 122 GFSEPGAGSDLAGLRTRAV----RDGD-DWVVNGQKIWTSGAHYADWAWLLVRT-DPEAPKHR----GISILLVDMDSPG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 327 VKLGRRHDPLGVAFFnCPTEGEDVVLPLDAIIGgkdGAGEGWAMLMDALSAGRGIMLPAQAVGGGKMVTRVaggHAAIRE 406
Cdd:cd01152 192 VTVRPIRSINGGEFF-NEVFLDDVRVPDANRVG---EVNDGWKVAMTTLNFERVSIGGSAATFFELLLARL---LLLTRD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 407 QFGLSigKFEGIEEPLARIAGYTYIMDAARTYTNGAVDQGEKPGVVSAIMKYNTTELQRDLVNDGMDVLAGNGISQGPNN 486
Cdd:cd01152 265 GRPLI--DDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFGSELAQELAELALELLGTAALLRDPAP 342
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
130-241 |
6.19e-21 |
|
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain.
Pssm-ID: 460686 [Multi-domain] Cd Length: 113 Bit Score: 88.67 E-value: 6.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 130 SDDEQAFLDGP---CEEVCA-MVDDWqvHQRGDLSTETWDYLKEKGFFGLIIPEAYGGKGFSVAARSAVVQKLGGHSVPL 205
Cdd:pfam02771 1 TEEQEALRDTVrefAEEEIApHAAEW--DEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASV 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 2255954741 206 SITVMVPNSLGpGELLLHYGTDEQQDHYLPRLARGE 241
Cdd:pfam02771 79 ALALSVHSSLG-APPILRFGTEEQKERYLPKLASGE 113
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
129-479 |
1.65e-19 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 91.71 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 129 LSDDEQAFLDGPCE---EVCAMVDDWQVHQRGDLSTETWDYLKEKGFFGLIIPEAYGGKGFSVAARSAVVQKLGGHSVPl 205
Cdd:PRK12341 5 LTEEQELLLASIRElitRNFPEEYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCGAP- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 206 sitvmvPNSLGPGELL---LHYGTDEQQ----DHYLprlARGEILPSFALTEPNAGSDAGAMESTgevFEDEDGelKLRL 278
Cdd:PRK12341 84 ------AFLITNGQCIhsmRRFGSAEQLrktaESTL---ETGDPAYALALTEPGAGSDNNSATTT---YTRKNG--KVYL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 279 NWEKRYISLAAISG-VLGLAFKLHDPENHlgkgedLGITCALVPTDTPGVKLGRRHDPLGVAFFNCPTEGEDVVLPLDAI 357
Cdd:PRK12341 150 NGQKTFITGAKEYPyMLVLARDPQPKDPK------KAFTLWWVDSSKPGIKINPLHKIGWHMLSTCEVYLDNVEVEESDL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 358 IGGKdgaGEGWAMLMDALSAGRgIMLPAQAVGGGKMVTRVAGGHAAIREQFGLSIGKFEGIEEPLARIAGYTYIMDAART 437
Cdd:PRK12341 224 VGEE---GMGFLNVMYNFEMER-LINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVY 299
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2255954741 438 YTNGAVDQGEKPGVVSAIMKYNTTELQRDLVNDGMDVLAGNG 479
Cdd:PRK12341 300 KVAWQADNGQSLRTSAALAKLYCARTAMEVIDDAIQIMGGLG 341
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
245-338 |
2.46e-18 |
|
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a beta-barrel fold.
Pssm-ID: 460685 [Multi-domain] Cd Length: 95 Bit Score: 80.79 E-value: 2.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 245 SFALTEPNAGSDAGAMESTGevfEDEDGElKLRLNWEKRYISLAAISGVLGLAFKLHDPENHlgkgedLGITCALVPTDT 324
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTA---ADGDGG-GWVLNGTKWWITNAGIADLFLVLARTGGDDRH------GGISLFLVPKDA 70
|
90
....*....|....
gi 2255954741 325 PGVKLGRRHDPLGV 338
Cdd:pfam02770 71 PGVSVRRIETKLGV 84
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
129-481 |
9.85e-18 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 86.04 E-value: 9.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 129 LSDDEQAFLDGPCEEVCAmvDDWQVH----QRGDLSTETW-DYLKEKGFFGLIIPEAYGGKGFSVAARSAVVQKLGGHSV 203
Cdd:PRK03354 5 LNDEQELFVAGIRELMAS--ENWEAYfaecDRDSVYPERFvKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 204 PLSITVMVPNSLGPgelLLHYGTDEQQDHYLPRLARGEILPSFALTEPNAGSDAGAMESTgevFEDEDGelKLRLNWEKR 283
Cdd:PRK03354 83 PTYVLYQLPGGFNT---FLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTT---YTRRNG--KVYLNGSKC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 284 YISLAAisGVLGLAFKLHDpenhlGKGEDLGI-TCALVPTDTPGV------KLGRRHDPLG-VAFFNCPTEGEDVVlpld 355
Cdd:PRK03354 155 FITSSA--YTPYIVVMARD-----GASPDKPVyTEWFVDMSKPGIkvtkleKLGLRMDSCCeITFDDVELDEKDMF---- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 356 aiigGKDgaGEGWAMLMDALSAGRgIMLPAQAVGGGKMVTRVAGGHAAIREQFGLSIGKFEGIEEPLARIAGYTYIM--- 432
Cdd:PRK03354 224 ----GRE--GNGFNRVKEEFDHER-FLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMknm 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2255954741 433 --DAARTYTNGAVDQGEkpgvvSAIMKYNTTELQRDLVNDGMDVLAGNGIS 481
Cdd:PRK03354 297 lyEAAWKADNGTITSGD-----AAMCKYFCANAAFEVVDSAMQVLGGVGIA 342
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
164-479 |
2.49e-17 |
|
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which catalyze the alpha,beta dehydrogenation of the corresponding medium chain acyl-CoA by FAD, which becomes reduced. The reduced form of MCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. MCAD is a homotetramer.
Pssm-ID: 173846 [Multi-domain] Cd Length: 378 Bit Score: 84.94 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 164 WDYLKEKGFFGLI---IPEAYGGKGFSVAARSAVVQKLGGHSVPLSITVMVpNSLGPGELLLHyGTDEQQDHYLPRLARG 240
Cdd:cd01157 35 WPLIKRAWELGLMnthIPEDCGGLGLGTFDTCLITEELAYGCTGVQTAIEA-NSLGQMPVIIS-GNDEQKKKYLGRMTEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 241 EILPSFALTEPNAGSDAGAMESTGEVFEDEdgelkLRLNWEKRYISLAAISG-VLGLAFKLHDPENHLGKgedlGITCAL 319
Cdd:cd01157 113 PLMCAYCVTEPGAGSDVAGIKTKAEKKGDE-----YIINGQKMWITNGGKANwYFLLARSDPDPKCPASK----AFTGFI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 320 VPTDTPGVKLGRRH--------DPLGVAFfncptegEDVVLPLDAIIGGKdgaGEGWAMLMDALSAGRGImLPAQAVGGG 391
Cdd:cd01157 184 VEADTPGIQPGRKElnmgqrcsDTRGITF-------EDVRVPKENVLIGE---GAGFKIAMGAFDKTRPP-VAAGAVGLA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 392 KMVTRVAGGHAAIREQFGLSIGKFEGIEEPLARIAGYTYIMDAARTYTNGAVDQGEKPGVVSAIMKYNTTELQRDLVNDG 471
Cdd:cd01157 253 QRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAFAADIANQLATDA 332
|
....*...
gi 2255954741 472 MDVLAGNG 479
Cdd:cd01157 333 VQIFGGNG 340
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
164-452 |
3.18e-15 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 78.77 E-value: 3.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 164 WDYLKEKGFFGLIIPEAYGGKGFSVA-----------ARSAVVQKLGGHSvPLSITVMVPNslgpgelllhyGTDEQQDH 232
Cdd:PLN02519 65 WKLMGDFNLHGITAPEEYGGLGLGYLyhciameeisrASGSVGLSYGAHS-NLCINQLVRN-----------GTPAQKEK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 233 YLPRLARGEILPSFALTEPNAGSDAGAMESTGEvfEDEDGELklrLNWEKRYISLAAISGVLgLAFKLHDPENHlgkgeD 312
Cdd:PLN02519 133 YLPKLISGEHVGALAMSEPNSGSDVVSMKCKAE--RVDGGYV---LNGNKMWCTNGPVAQTL-VVYAKTDVAAG-----S 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 313 LGITCALVPTDTPGVKLGRRHDPLGVAFFN-CPTEGEDVVLPLDAIIGGKdgaGEGWAMLMDALSAGRgIMLPAQAVGGG 391
Cdd:PLN02519 202 KGITAFIIEKGMPGFSTAQKLDKLGMRGSDtCELVFENCFVPEENVLGQE---GKGVYVMMSGLDLER-LVLAAGPLGLM 277
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2255954741 392 KMVTRVAGGHAAIREQFGLSIGKFEGIEEPLARI-----AGYTYIMDAARTYTNGAVDQGEKPGVV 452
Cdd:PLN02519 278 QACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMytslqSSRSYVYSVARDCDNGKVDRKDCAGVI 343
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
146-483 |
2.55e-14 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 76.13 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 146 AMVDDWQVHQRGDLSTEtwdyLKEKGFFGLIIPEAYGGKGFSVAARSAVVQKLGGHSVPLSITVMVPNSLGPGELLlHYG 225
Cdd:PTZ00461 60 AREDDINMHFNRDLFKQ----LGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLAHSMLFVNNFY-YSA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 226 TDEQQDHYLPRLARGEILPSFALTEPNAGSDAGAMESTGEvfedEDGELKLRLNWEKRYISLAAISGVLGLAFKLHdpen 305
Cdd:PTZ00461 135 SPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAK----KDSNGNYVLNGSKIWITNGTVADVFLIYAKVD---- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 306 hlGKgedlgITCALVPTDTPGVKLGRRHDPLGV-AFFNCPTEGEDVVLPLDAIIGGKdgaGEGWAMLMDALSAGRgIMLP 384
Cdd:PTZ00461 207 --GK-----ITAFVVERGTKGFTQGPKIDKCGMrASHMCQLFFEDVVVPAENLLGEE---GKGMVGMMRNLELER-VTLA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 385 AQAVGGGKMVTRVAGGHAAIREQFGLSIGKFEGIEEPLARIAGYTYIMDAARTYTNGAVDQGEKPGVVSAIMKYNTTELQ 464
Cdd:PTZ00461 276 AMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKLFATPIA 355
|
330
....*....|....*....
gi 2255954741 465 RDLVNDGMDVLAGNGISQG 483
Cdd:PTZ00461 356 KKVADSAIQVMGGMGYSRD 374
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
162-458 |
3.15e-14 |
|
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173842 [Multi-domain] Cd Length: 407 Bit Score: 75.50 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 162 ETWDYLKEKGFFGLIIPEAYGGKGFSVAARSAVVQKLGGHSVPLsitvMVPNSLGPG-ELLLHYGTDEQQDHYLPRLARG 240
Cdd:cd01153 40 EALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPL----MYASGTQGAaATLLAHGTEAQREKWIPRLAEG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 241 EILPSFALTEPNAGSDAGAMESTGEvfEDEDGElkLRLNWEKRYIS--------------LA----AISGVLGLAFKLHD 302
Cdd:cd01153 116 EWTGTMCLTEPDAGSDLGALRTKAV--YQADGS--WRINGVKRFISagehdmsenivhlvLArsegAPPGVKGLSLFLVP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 303 peNHLGKGEDLGITCALVPTdtpgvKLGRRHDP-LGVAFFNCPTEgedvvlpldaIIGGKdgaGEGWAMLMDALSAGRgI 381
Cdd:cd01153 192 --KFLDDGERNGVTVARIEE-----KMGLHGSPtCELVFDNAKGE----------LIGEE---GMGLAQMFAMMNGAR-L 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 382 MLPAQAVGGGKMVTRVAGGHAAIREQFGLSIGKFEGIEEPLARIAGYTYIMDAART--------YTNGAVDQGEKPGVVS 453
Cdd:cd01153 251 GVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAPAVTIIHHPDVRRSLMTQKAYAegsraldlYTATVQDLAERKATEG 330
|
....*
gi 2255954741 454 AIMKY 458
Cdd:cd01153 331 EDRKA 335
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
171-480 |
1.87e-12 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 70.27 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 171 GFFGLIIpEAYGGKGFSVAARSAVVQKLGGHSVPLSITVMVPNSLGPGELLLhYGTDEQQDHYLPRLARGEILPSFALTE 250
Cdd:PLN02526 73 GIAGGTI-KGYGCPGLSITASAIATAEVARVDASCSTFILVHSSLAMLTIAL-CGSEAQKQKYLPSLAQLDTVACWALTE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 251 PNAGSDAGAMESTGEvfEDEDGELklrLNWEKRYISLAAISGVLgLAFKLHDPENHlgkgedlgITCALVPTDTPGVKLG 330
Cdd:PLN02526 151 PDYGSDASSLNTTAT--KVEGGWI---LNGQKRWIGNSTFADVL-VIFARNTTTNQ--------INGFIVKKGAPGLKAT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 331 RRHDPLGVAFF-NCPTEGEDVVLPLDAIIGGKDgageGWAMLMDALSAGRgIMLPAQAVGGGKMVTRVAGGHAAIREQFG 409
Cdd:PLN02526 217 KIENKIGLRMVqNGDIVLKDVFVPDEDRLPGVN----SFQDTNKVLAVSR-VMVAWQPIGISMGVYDMCHRYLKERKQFG 291
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2255954741 410 LSIGKFEGIEEPLARIAGYTYIM-----DAARTYTNGAVDQGEkpgvvSAIMKYNTTELQRDLVNDGMDVLAGNGI 480
Cdd:PLN02526 292 APLAAFQINQEKLVRMLGNIQAMflvgwRLCKLYESGKMTPGH-----ASLGKAWITKKARETVALGRELLGGNGI 362
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
155-286 |
2.10e-11 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 67.59 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 155 QRGDLST-----ETWDYLKEKGFFGLIIPEAYGGKGFSVAARSAVVQKLGGHSVPLSitvMVPN-SLGPGELLLHYGTDE 228
Cdd:PTZ00456 91 KDGNVTTpkgfkEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFS---MYPGlSIGAANTLMAWGSEE 167
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2255954741 229 QQDHYLPRLARGEILPSFALTEPNAGSDAGAMESTGEvfEDEDGELKlrLNWEKRYIS 286
Cdd:PTZ00456 168 QKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAE--PSADGSYK--ITGTKIFIS 221
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
365-481 |
6.86e-11 |
|
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.
Pssm-ID: 395354 [Multi-domain] Cd Length: 149 Bit Score: 61.12 E-value: 6.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 365 GEGWAMLMDALSAGRgIMLPAQAVGGGKMVTRVAGGHAAIREQFGLSIGKFEGIEEPLARIAGYTyimDAARTYTNGAV- 443
Cdd:pfam00441 1 GRGFRVAMETLNHER-LAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEI---EAARLLVYRAAe 76
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2255954741 444 --DQGEKPGVVSAIMKYNTTELQRDLVNDGMDVLAGNGIS 481
Cdd:pfam00441 77 alDAGGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYL 116
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
168-426 |
8.48e-11 |
|
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACAD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. ACAD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173844 [Multi-domain] Cd Length: 394 Bit Score: 64.72 E-value: 8.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 168 KEKGFFGLIIPEAYGGKGFSvAARSAVVQKLGGHSV--PLSITVMVPNSlGPGELLLHYGTDEQQDHYLPRLARGEILPS 245
Cdd:cd01155 51 KAEGLWNLFLPEVSGLSGLT-NLEYAYLAEETGRSFfaPEVFNCQAPDT-GNMEVLHRYGSEEQKKQWLEPLLDGKIRSA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 246 FALTEPN-AGSDAGAMESTGEVFEDEdgelkLRLNWEKRYISLAA-----ISGVLGLAfklhDPENHLGKGEDLGItcaL 319
Cdd:cd01155 129 FAMTEPDvASSDATNIECSIERDGDD-----YVINGRKWWSSGAGdprckIAIVMGRT----DPDGAPRHRQQSMI---L 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 320 VPTDTPGVKLGRrhdPLGVAFFNCPTEG------EDVVLPLDAIIGGKdgaGEGWAMLMDALSAGRgIMLPAQAVGGGKM 393
Cdd:cd01155 197 VPMDTPGVTIIR---PLSVFGYDDAPHGhaeitfDNVRVPASNLILGE---GRGFEIAQGRLGPGR-IHHCMRLIGAAER 269
|
250 260 270
....*....|....*....|....*....|....*
gi 2255954741 394 VTRVAGGHAAIREQFGLSIGKFEGIEEPLA--RIA 426
Cdd:cd01155 270 ALELMCQRAVSREAFGKKLAQHGVVAHWIAksRIE 304
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
155-334 |
4.85e-06 |
|
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, which catalyzes the first two steps of DBT desulfurization in mesophilic bacteria. DszC converts DBT to DBT-sulfoxide, which is then converted to DBT-sulfone. Bacteria with this enzyme are candidates for the removal of organic sulfur compounds from fossil fuels, which pollute the environment. An equivalent enzyme tdsC, is found in thermophilic bacteria. This alignment also contains a closely related uncharacterized subgroup.
Pssm-ID: 173852 [Multi-domain] Cd Length: 377 Bit Score: 49.63 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 155 QRGDLSTETWDYLKEKGFFGLIIPEAYGGKGFSVAARSAVVQKLGGhsVPLSITVMVPNSLGPGELLLHYGTDEQQDHYL 234
Cdd:cd01163 19 RQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAA--ADSNIAQALRAHFGFVEALLLAGPEQFRKRWF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 235 PRLARGEILPsfaltepNAGSDAGAMESTGEVFEDEDGELKLRLNWEKRYISLAAISgvlglafKLHDPENHLGKGEDLG 314
Cdd:cd01163 97 GRVLNGWIFG-------NAVSERGSVRPGTFLTATVRDGGGYVLNGKKFYSTGALFS-------DWVTVSALDEEGKLVF 162
|
170 180
....*....|....*....|
gi 2255954741 315 itcALVPTDTPGVklgRRHD 334
Cdd:cd01163 163 ---AAVPTDRPGI---TVVD 176
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
188-479 |
1.68e-04 |
|
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of several genes involved in the SOS adaptive response to DNA alkylation damage, whose expression is activated by the Ada protein. Its function has not been entirely elucidated; however, it is similar in sequence and function to acyl-CoA dehydrogenases. It has been proposed that aidB directly destroys DNA alkylating agents such as nitrosoguanidines (nitrosated amides) or their reaction intermediates.
Pssm-ID: 173843 [Multi-domain] Cd Length: 418 Bit Score: 45.05 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 188 VAARSAVVQKLGGHSVPLSIT-VMVPnslgpgeLLLHYGTDEQQdHYLPRLA----RGEILPSFALTEPNAGSDAGAMES 262
Cdd:cd01154 96 FAAGYLLSDAAAGLLCPLTMTdAAVY-------ALRKYGPEELK-QYLPGLLsdryKTGLLGGTWMTEKQGGSDLGANET 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 263 TGEVFEDEdgelKLRLNWEKRYISLAAISGVLGLAFKLHDPEnhlGKGedlGITCALVPTDTP-----GVKLGRRHDPLG 337
Cdd:cd01154 168 TAERSGGG----VYRLNGHKWFASAPLADAALVLARPEGAPA---GAR---GLSLFLVPRLLEdgtrnGYRIRRLKDKLG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 338 VAffNCPTeGEdvVLPLDAI---IGGKdgaGEGWAMLMDALSAGRgimlPAQAVGGGKMVTRV---AGGHAAIREQFGLS 411
Cdd:cd01154 238 TR--SVAT-GE--VEFDDAEaylIGDE---GKGIYYILEMLNISR----LDNAVAALGIMRRAlseAYHYARHRRAFGKP 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 412 IgkfegIEEPLAR---------IAGYTYI-MDAARTYTNGAVDQGEKPGVV---SAIMKYNTTELQRDLVNDGMDVLAGN 478
Cdd:cd01154 306 L-----IDHPLMRrdlaemevdVEAATALtFRAARAFDRAAADKPVEAHMArlaTPVAKLIACKRAAPVTSEAMEVFGGN 380
|
.
gi 2255954741 479 G 479
Cdd:cd01154 381 G 381
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
216-261 |
1.86e-04 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 45.17 E-value: 1.86e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2255954741 216 GPGELLLHYGTDEQQDHYLPRLARGEILPSFALTEPN-AGSDAGAME 261
Cdd:PLN02876 524 GNMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIE 570
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
203-410 |
1.42e-03 |
|
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in the peroxisomal fatty acid beta-oxidation, the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. In a second oxidative half-reaction, the reduced FAD is reoxidized by molecular oxygen. AXO is generally a homodimer, but it has been reported to form a different type of oligomer in yeast. There are several subtypes of AXO's, based on substrate specificity. Palmitoyl-CoA oxidase acts on straight-chain fatty acids and prostanoids; whereas, the closely related Trihydroxycoprostanoly-CoA oxidase has the greatest activity for 2-methyl branched side chains of bile precursors. Pristanoyl-CoA oxidase, acts on 2-methyl branched fatty acids. AXO has an additional domain, C-terminal to the region with similarity to acyl-CoA dehydrogenases, which is included in this alignment.
Pssm-ID: 173839 [Multi-domain] Cd Length: 610 Bit Score: 42.32 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 203 VPLSITVMVPNSLGPGELLLHY----------GTDEQQDHYLPRLARGEILPSFALTEPNAGSDAGAMESTGeVFEDEDG 272
Cdd:cd01150 85 LALTNSLGGYDLSLGAKLGLHLglfgnaiknlGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTA-TYDPLTQ 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 273 ELKLR---LNWEKRYISLAAISGVLGLAF-KLHDPenhlgkGEDLGITCALVP---TDT----PGV-------KLGRRHD 334
Cdd:cd01150 164 EFVINtpdFTATKWWPGNLGKTATHAVVFaQLITP------GKNHGLHAFIVPirdPKThqplPGVtvgdigpKMGLNGV 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255954741 335 PLGVAFFNcptegeDVVLPLDAIIG-----GKDG--------AGEGWAMLMDALSAGRGIMLPAQAVGGGKMVTrVAGGH 401
Cdd:cd01150 238 DNGFLQFR------NVRIPRENLLNrfgdvSPDGtyvspfkdPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAAT-IAIRY 310
|
....*....
gi 2255954741 402 AAIREQFGL 410
Cdd:cd01150 311 SAVRRQFGP 319
|
|
| |
