|
Name |
Accession |
Description |
Interval |
E-value |
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
42-815 |
0e+00 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 1414.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 42 HAPGWLLLIFWvliaIVAVPLLLPDLRRQYFTKPLFSWFQKVLPPMSETERDAIDAGTVWWDGELFSGRPDWDKLLAYPK 121
Cdd:PRK09463 1 LWSLWLLVPLA----IILLPLNLPPLRRSLISAPLLKWFRKVLPPMSQTEREALEAGTVWWEGELFSGKPDWKKLLNYPK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 122 VQLTEEEQAFIDGPTEELCAMVSDWEIGQAM-DLPPAAWEHIKTHGFFALIIPKEYGGKGFSAYAHSQVAMKLATRSGDL 200
Cdd:PRK09463 77 PTLTAEEQAFLDGPVEELCRMVNDWQITHELaDLPPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 201 ASTVMVPNSLGPAELLLHYGTDEQRNHYLPRLARGDDIPCFALTGPLAGSDAGAMPDTGVICKGEWEGKETLGLRLNWEK 280
Cdd:PRK09463 157 AVTVMVPNSLGPGELLLHYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGVVCKGEWQGEEVLGMRLTWNK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 281 RYITLGPVATLLGLAFKAHDPDHLLGEEEDLGISLALIPTDTPGVEIGRRHLPLGAAFMNGPNSGKDVFIPLEFLIGGQE 360
Cdd:PRK09463 237 RYITLAPIATVLGLAFKLYDPDGLLGDKEDLGITCALIPTDTPGVEIGRRHFPLNVPFQNGPTRGKDVFIPLDYIIGGPK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 361 MLGKGWMMLMNCLSVGRSISLPAVGTGAAKFTSLVTGQYAQVREQFNVPLSAFEGIQEALARIGGNAWLMDSARMLTANA 440
Cdd:PRK09463 317 MAGQGWRMLMECLSVGRGISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNAYLMDAARTLTTAA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 441 VDMGEKPSVLSAILKYHLTERGRECISHAMDVHGGKGIIMGPNNYLGRSWQGAPIFITVEGANILSRNLMIFGQGAIRCH 520
Cdd:PRK09463 397 VDLGEKPSVLSAIAKYHLTERGRQVINDAMDIHGGKGICLGPNNFLARAYQAAPIAITVEGANILTRSLMIFGQGAIRCH 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 521 PFVLKEMALAGREDHDqALKEFDGLLMQHIGFAVSNAASTLVLNLGIGHFEKAPGNRLSQGYFRALNRQAAAFALLADLS 600
Cdd:PRK09463 477 PYVLKEMEAAQNNDKQ-ALKAFDKALFGHIGFVVSNAVRSFWLGLTGGRLSAAPVDDATKRYYRQLNRLSANLALLADVS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 601 MMLLGGELKRRERLSARLGDVLSHMYLASAALKRYHDLDSPDHLEPLFAWAMEESLGQSERALDELLSNFPNKILGCLLR 680
Cdd:PRK09463 556 MLVLGGSLKRRERLSARLGDILSQLYLASAVLKRYEDEGRPEADLPLVHWAVQDALYQAEQALDGLLRNFPNRVVAGLLR 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 681 VIVFPFGRRHTGPSDALDAEVAAVIGRAkgDPTLEELLAGCYRPQSAQDPVGALQHAYDLLGASHPLQKKLHAALKSGQV 760
Cdd:PRK09463 636 VLVFPLGRRYRAPSDKLDHQVAKLLQTP--SATRDRLTRGQYLPPSENNPVGRLEEALLDVIAAEPIEKKICKALKKGKL 713
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1524473354 761 KPTAGEHAIDAALHAGVLQPAEAQTLRDAEAARRKVIDVDDFSKEELLQAEGKVR 815
Cdd:PRK09463 714 PFLRLDELADEALAAGVISEEEAALLREAEEARLRVINVDDFDPEELAAKPVKLP 768
|
|
| FadE_coli |
NF038187 |
acyl-CoA dehydrogenase FadE; This HMM describes a narrow clade of medium-chain and long-chain ... |
13-807 |
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: 1113.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 13 IAYLAHRRTAPLPALGAVAVYLLAMGAWSHAPGWLLLIFwvliAIVAVPLLLPDLRRQYFTKPLFSWFQKVLPPMSETER 92
Cdd:NF038187 11 LGALAYHRVSLLTSSLILAAVMAAGTAAGLWSLWLWLPF----LIIALPLNVPSIRQSLISAPALKAFRKVMPEMSSTEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 93 DAIDAGTVWWDGELFSGRPDWDKLLAYPKVQLTEEEQAFIDGPTEELCAMVSDWEIGQAM-DLPPAAWEHIKTHGFFALI 171
Cdd:NF038187 87 EAIDAGTTWWEADLFRGNPDWKKLHNYPKPRLTAEEQAFLDGPVEEVCRMVNDFQITHELaDLPPEVWQYLKDHRFFAMI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 172 IPKEYGGKGFSAYAHSQVAMKLATRSGDLASTVMVPNSLGPAELLLHYGTDEQRNHYLPRLARGDDIPCFALTGPLAGSD 251
Cdd:NF038187 167 IKKEYGGLEFSAYAQSRVLQKLAGVSSILASTVGVPNSLGPGELLQHYGTEEQKDHYLPRLARGEEIPCFALTSPEAGSD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 252 AGAMPDTGVICKGEWEGKETLGLRLNWEKRYITLGPVATLLGLAFKAHDPDHLLGEEEDLGISLALIPTDTPGVEIGRRH 331
Cdd:NF038187 247 AGSIPDFGVVCKGEWQGEEVLGMRLTWNKRYITLAPVATVLGLAFKLRDPDHLLGDKEELGITCALIPTDTPGVEIGRRH 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 332 LPLGAAFMNGPNSGKDVFIPLEFLIGGQEMLGKGWMMLMNCLSVGRSISLPAVGTGAAKFTSLVTGQYAQVREQFNVPLS 411
Cdd:NF038187 327 FPLNVPFQNGPTRGKDIFVPLDFIIGGPKMAGQGWRMLVECLSVGRGITLPSNSTGGLKSAALATGAYARIRRQFKLPIG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 412 AFEGIQEALARIGGNAWLMDSARMLTANAVDMGEKPSVLSAILKYHLTERGRECISHAMDVHGGKGIIMGPNNYLGRSWQ 491
Cdd:NF038187 407 KMEGIEEPLARIAGNAYLMDAAATLTTTGIDLGEKPSVISAIVKYHCTHRGQRSIIDAMDIHGGKGICLGPNNFLARGYQ 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 492 GAPIFITVEGANILSRNLMIFGQGAIRCHPFVLKEMALAGREDHDQALKEFDGLLMQHIGFAVSNAASTLVLNLGIGHFE 571
Cdd:NF038187 487 GAPIAITVEGANILTRSMIIYGQGAIRCHPYVLAEMEAAQDNDSEQALNDFDKALFGHIGFVGSNLVRSFWLGLTNGRFS 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 572 KAPGNRLSQGYFRALNRQAAAFALLADLSMMLLGGELKRRERLSARLGDVLSHMYLASAALKRYHDLDSPDHLEPLFAWA 651
Cdd:NF038187 567 SAPYKDATRRYYQQLNRLSANLALLSDVSMAVLGGSLKRRERISARLGDILSQLYLASATLKRYEDEGRQKEDLPLVHWA 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 652 MEESLGQSERALDELLSNFPNKILGCLLRVIVFPFGRRHTGPSDALDAEVAAVIgrAKGDPTLEELLAGCYRPQSAQDPV 731
Cdd:NF038187 647 VQDSLYQAEQALDDLLRNFPNRLVAGLLRVIIFPFGRPLKAPSDKLDHKVAKIL--QTPSATRSRLGRGQYLTPSEHNPV 724
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1524473354 732 GALQHAYDLLGASHPLQKKLHAAlkSGQVKPTAGEHAIDA-ALHAGVLQPAEAQTLRDAEAARRKVIDVDDFSKEEL 807
Cdd:NF038187 725 GLLEQALKDILAAEPIHDRVCKA--AGKRLPFMRLDKLAEeGLALGVITEEEAALLERAEASRLRSINVDDFDPDEL 799
|
|
| ACDH_C |
pfam09317 |
Acyl-CoA dehydrogenase, C-terminal, bacterial type; This C-terminal domain is functionally ... |
517-802 |
2.28e-125 |
|
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: 377.22 E-value: 2.28e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 517 IRCHPFVLKEMALAGREDHDQALKEFDGLLMQHIGFAVSNAASTLVLNLGIGHFEKAPGNRLSQGYFRALNRQAAAFALL 596
Cdd:pfam09317 1 IRCHPYVLKEMEAAQNEDKEQALKAFDRALFGHIGFALSNAARSLVLGLTGGRFASAPVAGETARYYRQLNRLSAAFALL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 597 ADLSMMLLGGELKRRERLSARLGDVLSHMYLASAALKRYHDLDSPDHLEPLFAWAMEESLGQSERALDELLSNFPNKILG 676
Cdd:pfam09317 81 ADLAMLVLGGSLKRRERLSARLGDVLSQLYLASAVLKRFEDEGRPEADLPLVHWAMQDALYQAQQALDGVLRNFPNRPVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 677 CLLRVIVFPFGRRHTGPSDALDAEVAAVIGraKGDPTLEELLAGCYRPQSAQDPVGALQHAYDLLGASHPLQKKLHAALK 756
Cdd:pfam09317 161 WLLRVLVFPLGRRYRKPSDKLGHEVAQLLQ--EPGEARDRLTAGVYLPDDPDDPVGRLEAAFQAVLAAEPLEKKLKKAIK 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1524473354 757 SGQVKPTAGEHAIDAALHAGVLQPAEAQTLRDAEAARRKVIDVDDF 802
Cdd:pfam09317 239 AGKLPKLTLEELIEEALEKGVITEEEAELLREAEALRLDVIQVDDF 284
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
123-511 |
1.13e-90 |
|
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: 290.59 E-value: 1.13e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 123 QLTEEEQAFIDgPTEELCAMVSDW---EIGQAMDLPPAAWEHIKTHGFFALIIPKEYGGKGFSAYAHSQVAMKLATRSGD 199
Cdd:COG1960 4 ELTEEQRALRD-EVREFAEEEIAPearEWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 200 LASTVMVPNslGPAELLLHYGTDEQRNHYLPRLARGDDIPCFALTGPLAGSDAGAMPDTGVICKGEWegketlglRLNWE 279
Cdd:COG1960 83 LALPVGVHN--GAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGY--------VLNGQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 280 KRYITLGPVATLLGLAFKAHDpdhllgEEEDLGISLALIPTDTPGVEIGRRHLPLG-AAFMNGPNSGKDVFIPLEFLIGG 358
Cdd:COG1960 153 KTFITNAPVADVILVLARTDP------AAGHRGISLFLVPKDTPGVTVGRIEDKMGlRGSDTGELFFDDVRVPAENLLGE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 359 qemLGKGWMMLMNCLSVGRsISLPAVGTGAAKFTSLVTGQYAQVREQFNVPLSAFEGIQEALARIGGNAWLMDSARMLTA 438
Cdd:COG1960 227 ---EGKGFKIAMSTLNAGR-LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAA 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1524473354 439 NAVDMGEKPSVLSAILKYHLTERGRECISHAMDVHGGKGIImgpNNY-LGRSWQGAPIFITVEGANILSRNLMI 511
Cdd:COG1960 303 WLLDAGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYT---REYpLERLYRDARILTIYEGTNEIQRLIIA 373
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
210-510 |
1.03e-47 |
|
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: 172.47 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 210 LGPAELLLHYGTDEQRNHYLPRLARGDDIPCFALTGPLAGSDAGAMPDTGVICKGEWegketlglRLNWEKRYITLGPVA 289
Cdd:cd00567 42 LLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGY--------VLNGRKIFISNGGDA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 290 TLLGLAFKAHDPDhllgeEEDLGISLALIPTDTPGVEIGRRHLPLGaafMNGPNSG----KDVFIPLEFLIGGQemlGKG 365
Cdd:cd00567 114 DLFIVLARTDEEG-----PGHRGISAFLVPADTPGVTVGRIWDKMG---MRGSGTGelvfDDVRVPEDNLLGEE---GGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 366 WMMLMNCLSVGRsISLPAVGTGAAKFTSLVTGQYAQVREQFNVPLSAFEGIQEALARIggnAWLMDSARMLTANAVDMG- 444
Cdd:cd00567 183 FELAMKGLNVGR-LLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADM---AAELEAARLLLYRAAWLLd 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1524473354 445 ---EKPSVLSAILKYHLTERGRECISHAMDVHGGKGIIMGpnNYLGRSWQGAPIFITVEGANILSRNLM 510
Cdd:cd00567 259 qgpDEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSRE--YPVERYLRDARAARIAEGTAEIQRLII 325
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
42-815 |
0e+00 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 1414.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 42 HAPGWLLLIFWvliaIVAVPLLLPDLRRQYFTKPLFSWFQKVLPPMSETERDAIDAGTVWWDGELFSGRPDWDKLLAYPK 121
Cdd:PRK09463 1 LWSLWLLVPLA----IILLPLNLPPLRRSLISAPLLKWFRKVLPPMSQTEREALEAGTVWWEGELFSGKPDWKKLLNYPK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 122 VQLTEEEQAFIDGPTEELCAMVSDWEIGQAM-DLPPAAWEHIKTHGFFALIIPKEYGGKGFSAYAHSQVAMKLATRSGDL 200
Cdd:PRK09463 77 PTLTAEEQAFLDGPVEELCRMVNDWQITHELaDLPPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 201 ASTVMVPNSLGPAELLLHYGTDEQRNHYLPRLARGDDIPCFALTGPLAGSDAGAMPDTGVICKGEWEGKETLGLRLNWEK 280
Cdd:PRK09463 157 AVTVMVPNSLGPGELLLHYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGVVCKGEWQGEEVLGMRLTWNK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 281 RYITLGPVATLLGLAFKAHDPDHLLGEEEDLGISLALIPTDTPGVEIGRRHLPLGAAFMNGPNSGKDVFIPLEFLIGGQE 360
Cdd:PRK09463 237 RYITLAPIATVLGLAFKLYDPDGLLGDKEDLGITCALIPTDTPGVEIGRRHFPLNVPFQNGPTRGKDVFIPLDYIIGGPK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 361 MLGKGWMMLMNCLSVGRSISLPAVGTGAAKFTSLVTGQYAQVREQFNVPLSAFEGIQEALARIGGNAWLMDSARMLTANA 440
Cdd:PRK09463 317 MAGQGWRMLMECLSVGRGISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNAYLMDAARTLTTAA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 441 VDMGEKPSVLSAILKYHLTERGRECISHAMDVHGGKGIIMGPNNYLGRSWQGAPIFITVEGANILSRNLMIFGQGAIRCH 520
Cdd:PRK09463 397 VDLGEKPSVLSAIAKYHLTERGRQVINDAMDIHGGKGICLGPNNFLARAYQAAPIAITVEGANILTRSLMIFGQGAIRCH 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 521 PFVLKEMALAGREDHDqALKEFDGLLMQHIGFAVSNAASTLVLNLGIGHFEKAPGNRLSQGYFRALNRQAAAFALLADLS 600
Cdd:PRK09463 477 PYVLKEMEAAQNNDKQ-ALKAFDKALFGHIGFVVSNAVRSFWLGLTGGRLSAAPVDDATKRYYRQLNRLSANLALLADVS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 601 MMLLGGELKRRERLSARLGDVLSHMYLASAALKRYHDLDSPDHLEPLFAWAMEESLGQSERALDELLSNFPNKILGCLLR 680
Cdd:PRK09463 556 MLVLGGSLKRRERLSARLGDILSQLYLASAVLKRYEDEGRPEADLPLVHWAVQDALYQAEQALDGLLRNFPNRVVAGLLR 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 681 VIVFPFGRRHTGPSDALDAEVAAVIGRAkgDPTLEELLAGCYRPQSAQDPVGALQHAYDLLGASHPLQKKLHAALKSGQV 760
Cdd:PRK09463 636 VLVFPLGRRYRAPSDKLDHQVAKLLQTP--SATRDRLTRGQYLPPSENNPVGRLEEALLDVIAAEPIEKKICKALKKGKL 713
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1524473354 761 KPTAGEHAIDAALHAGVLQPAEAQTLRDAEAARRKVIDVDDFSKEELLQAEGKVR 815
Cdd:PRK09463 714 PFLRLDELADEALAAGVISEEEAALLREAEEARLRVINVDDFDPEELAAKPVKLP 768
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
50-808 |
0e+00 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 1140.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 50 IFWVLIAIVAVPLLLPDLRRQYFTKPLFSWFQKVLPPMSETERDAIDAGTVWWDGELFSGRPDWDKLLAYPKVQLTEEEQ 129
Cdd:PRK13026 4 LIILLLIAIVLVFAVKPLRRQFITRPVFKFFKKVLPPLSDTEREAMEAGDVWWEGELFSGKPDWQKLHSYPKPTLTAEEQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 130 AFIDGPTEELCAMVSDWEIGQA-MDLPPAAWEHIKTHGFFALIIPKEYGGKGFSAYAHSQVAMKLATRSGDLASTVMVPN 208
Cdd:PRK13026 84 AFIDNEVETLLTMLDDWDIVQNrKDLPPEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 209 SLGPAELLLHYGTDEQRNHYLPRLARGDDIPCFALTGPLAGSDAGAMPDTGVICKGEWEGKETLGLRLNWEKRYITLGPV 288
Cdd:PRK13026 164 SLGPGELLTHYGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTGIVCRGEFEGEEVLGLRLTWDKRYITLAPV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 289 ATLLGLAFKAHDPDHLLGEEEDLGISLALIPTDTPGVEIGRRHLPLGAAFMNGPNSGKDVFIPLEFLIGGQEMLGKGWMM 368
Cdd:PRK13026 244 ATVLGLAFKLRDPDGLLGDKKELGITCALIPTDHPGVEIGRRHNPLGMAFMNGTTRGKDVFIPLDWIIGGPDYAGRGWRM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 369 LMNCLSVGRSISLPAVGTGAAKFTSLVTGQYAQVREQFNVPLSAFEGIQEALARIGGNAWLMDSARMLTANAVDMGEKPS 448
Cdd:PRK13026 324 LVECLSAGRGISLPALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGNTYLLEAARRLTTTGLDLGVKPS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 449 VLSAILKYHLTERGRECISHAMDVHGGKGIIMGPNNYLGRSWQGAPIFITVEGANILSRNLMIFGQGAIRCHPFVLKEMA 528
Cdd:PRK13026 404 VVTAIAKYHMTELARDVVNDAMDIHAGKGIQLGPKNYLGHAYMAVPIAITVEGANILTRNLMIFGQGATRCHPYVLAEME 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 529 LAGREDHDQALKEFDGLLMQHIGFAVSNAASTLVLNLGIGHFEKAPGNRLSQGYFRALNRQAAAFALLADLSMMLLGGEL 608
Cdd:PRK13026 484 AAAMEDEHEGLEAFDSLLFKHIGYAARNAFRALFSALTGSRFISAPVSGETAQYYKDMSRLSAALALLADLSMLILGGDL 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 609 KRRERLSARLGDVLSHMYLASAALKRYHDLDSPDHLEPLFAWAMEESLGQSERALDELLSNFPNKILGCLLRVIVFPFGR 688
Cdd:PRK13026 564 KRKEMLSARLGDVLSQLYLASATLKRFEDNGRQQDDLPAVHYAMQDCLHLAAKALDEFLRNFPNRPVAWLLRALIFPLGN 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 689 RHTGPSDALDAEVAAVIgrAKGDPTLEELLAGCYRPQSAQDPVGALQHAYDLLGASHPLQKKLHAALKSGQVKP-TAGEH 767
Cdd:PRK13026 644 HFRAPSDKLARQLAELM--MTPGPARDRLTALCYIFEGDKDGVARVEQAFLAQYAVKPLYKKLKKAQREGKLPRkVPLLE 721
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1524473354 768 AIDAALHAGVLQPAEAQTLRDAEAARRKVIDVDDFSKEELL 808
Cdd:PRK13026 722 LFAKALEKGVITADEAEKLLAADKLRLDAIQVDDFTPDFME 762
|
|
| FadE_coli |
NF038187 |
acyl-CoA dehydrogenase FadE; This HMM describes a narrow clade of medium-chain and long-chain ... |
13-807 |
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: 1113.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 13 IAYLAHRRTAPLPALGAVAVYLLAMGAWSHAPGWLLLIFwvliAIVAVPLLLPDLRRQYFTKPLFSWFQKVLPPMSETER 92
Cdd:NF038187 11 LGALAYHRVSLLTSSLILAAVMAAGTAAGLWSLWLWLPF----LIIALPLNVPSIRQSLISAPALKAFRKVMPEMSSTEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 93 DAIDAGTVWWDGELFSGRPDWDKLLAYPKVQLTEEEQAFIDGPTEELCAMVSDWEIGQAM-DLPPAAWEHIKTHGFFALI 171
Cdd:NF038187 87 EAIDAGTTWWEADLFRGNPDWKKLHNYPKPRLTAEEQAFLDGPVEEVCRMVNDFQITHELaDLPPEVWQYLKDHRFFAMI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 172 IPKEYGGKGFSAYAHSQVAMKLATRSGDLASTVMVPNSLGPAELLLHYGTDEQRNHYLPRLARGDDIPCFALTGPLAGSD 251
Cdd:NF038187 167 IKKEYGGLEFSAYAQSRVLQKLAGVSSILASTVGVPNSLGPGELLQHYGTEEQKDHYLPRLARGEEIPCFALTSPEAGSD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 252 AGAMPDTGVICKGEWEGKETLGLRLNWEKRYITLGPVATLLGLAFKAHDPDHLLGEEEDLGISLALIPTDTPGVEIGRRH 331
Cdd:NF038187 247 AGSIPDFGVVCKGEWQGEEVLGMRLTWNKRYITLAPVATVLGLAFKLRDPDHLLGDKEELGITCALIPTDTPGVEIGRRH 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 332 LPLGAAFMNGPNSGKDVFIPLEFLIGGQEMLGKGWMMLMNCLSVGRSISLPAVGTGAAKFTSLVTGQYAQVREQFNVPLS 411
Cdd:NF038187 327 FPLNVPFQNGPTRGKDIFVPLDFIIGGPKMAGQGWRMLVECLSVGRGITLPSNSTGGLKSAALATGAYARIRRQFKLPIG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 412 AFEGIQEALARIGGNAWLMDSARMLTANAVDMGEKPSVLSAILKYHLTERGRECISHAMDVHGGKGIIMGPNNYLGRSWQ 491
Cdd:NF038187 407 KMEGIEEPLARIAGNAYLMDAAATLTTTGIDLGEKPSVISAIVKYHCTHRGQRSIIDAMDIHGGKGICLGPNNFLARGYQ 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 492 GAPIFITVEGANILSRNLMIFGQGAIRCHPFVLKEMALAGREDHDQALKEFDGLLMQHIGFAVSNAASTLVLNLGIGHFE 571
Cdd:NF038187 487 GAPIAITVEGANILTRSMIIYGQGAIRCHPYVLAEMEAAQDNDSEQALNDFDKALFGHIGFVGSNLVRSFWLGLTNGRFS 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 572 KAPGNRLSQGYFRALNRQAAAFALLADLSMMLLGGELKRRERLSARLGDVLSHMYLASAALKRYHDLDSPDHLEPLFAWA 651
Cdd:NF038187 567 SAPYKDATRRYYQQLNRLSANLALLSDVSMAVLGGSLKRRERISARLGDILSQLYLASATLKRYEDEGRQKEDLPLVHWA 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 652 MEESLGQSERALDELLSNFPNKILGCLLRVIVFPFGRRHTGPSDALDAEVAAVIgrAKGDPTLEELLAGCYRPQSAQDPV 731
Cdd:NF038187 647 VQDSLYQAEQALDDLLRNFPNRLVAGLLRVIIFPFGRPLKAPSDKLDHKVAKIL--QTPSATRSRLGRGQYLTPSEHNPV 724
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1524473354 732 GALQHAYDLLGASHPLQKKLHAAlkSGQVKPTAGEHAIDA-ALHAGVLQPAEAQTLRDAEAARRKVIDVDDFSKEEL 807
Cdd:NF038187 725 GLLEQALKDILAAEPIHDRVCKA--AGKRLPFMRLDKLAEeGLALGVITEEEAALLERAEASRLRSINVDDFDPDEL 799
|
|
| ACDH_C |
pfam09317 |
Acyl-CoA dehydrogenase, C-terminal, bacterial type; This C-terminal domain is functionally ... |
517-802 |
2.28e-125 |
|
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: 377.22 E-value: 2.28e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 517 IRCHPFVLKEMALAGREDHDQALKEFDGLLMQHIGFAVSNAASTLVLNLGIGHFEKAPGNRLSQGYFRALNRQAAAFALL 596
Cdd:pfam09317 1 IRCHPYVLKEMEAAQNEDKEQALKAFDRALFGHIGFALSNAARSLVLGLTGGRFASAPVAGETARYYRQLNRLSAAFALL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 597 ADLSMMLLGGELKRRERLSARLGDVLSHMYLASAALKRYHDLDSPDHLEPLFAWAMEESLGQSERALDELLSNFPNKILG 676
Cdd:pfam09317 81 ADLAMLVLGGSLKRRERLSARLGDVLSQLYLASAVLKRFEDEGRPEADLPLVHWAMQDALYQAQQALDGVLRNFPNRPVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 677 CLLRVIVFPFGRRHTGPSDALDAEVAAVIGraKGDPTLEELLAGCYRPQSAQDPVGALQHAYDLLGASHPLQKKLHAALK 756
Cdd:pfam09317 161 WLLRVLVFPLGRRYRKPSDKLGHEVAQLLQ--EPGEARDRLTAGVYLPDDPDDPVGRLEAAFQAVLAAEPLEKKLKKAIK 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1524473354 757 SGQVKPTAGEHAIDAALHAGVLQPAEAQTLRDAEAARRKVIDVDDF 802
Cdd:pfam09317 239 AGKLPKLTLEELIEEALEKGVITEEEAELLREAEALRLDVIQVDDF 284
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
123-511 |
1.13e-90 |
|
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: 290.59 E-value: 1.13e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 123 QLTEEEQAFIDgPTEELCAMVSDW---EIGQAMDLPPAAWEHIKTHGFFALIIPKEYGGKGFSAYAHSQVAMKLATRSGD 199
Cdd:COG1960 4 ELTEEQRALRD-EVREFAEEEIAPearEWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 200 LASTVMVPNslGPAELLLHYGTDEQRNHYLPRLARGDDIPCFALTGPLAGSDAGAMPDTGVICKGEWegketlglRLNWE 279
Cdd:COG1960 83 LALPVGVHN--GAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGY--------VLNGQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 280 KRYITLGPVATLLGLAFKAHDpdhllgEEEDLGISLALIPTDTPGVEIGRRHLPLG-AAFMNGPNSGKDVFIPLEFLIGG 358
Cdd:COG1960 153 KTFITNAPVADVILVLARTDP------AAGHRGISLFLVPKDTPGVTVGRIEDKMGlRGSDTGELFFDDVRVPAENLLGE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 359 qemLGKGWMMLMNCLSVGRsISLPAVGTGAAKFTSLVTGQYAQVREQFNVPLSAFEGIQEALARIGGNAWLMDSARMLTA 438
Cdd:COG1960 227 ---EGKGFKIAMSTLNAGR-LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAA 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1524473354 439 NAVDMGEKPSVLSAILKYHLTERGRECISHAMDVHGGKGIImgpNNY-LGRSWQGAPIFITVEGANILSRNLMI 511
Cdd:COG1960 303 WLLDAGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYT---REYpLERLYRDARILTIYEGTNEIQRLIIA 373
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
210-510 |
1.03e-47 |
|
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: 172.47 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 210 LGPAELLLHYGTDEQRNHYLPRLARGDDIPCFALTGPLAGSDAGAMPDTGVICKGEWegketlglRLNWEKRYITLGPVA 289
Cdd:cd00567 42 LLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGY--------VLNGRKIFISNGGDA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 290 TLLGLAFKAHDPDhllgeEEDLGISLALIPTDTPGVEIGRRHLPLGaafMNGPNSG----KDVFIPLEFLIGGQemlGKG 365
Cdd:cd00567 114 DLFIVLARTDEEG-----PGHRGISAFLVPADTPGVTVGRIWDKMG---MRGSGTGelvfDDVRVPEDNLLGEE---GGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 366 WMMLMNCLSVGRsISLPAVGTGAAKFTSLVTGQYAQVREQFNVPLSAFEGIQEALARIggnAWLMDSARMLTANAVDMG- 444
Cdd:cd00567 183 FELAMKGLNVGR-LLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADM---AAELEAARLLLYRAAWLLd 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1524473354 445 ---EKPSVLSAILKYHLTERGRECISHAMDVHGGKGIIMGpnNYLGRSWQGAPIFITVEGANILSRNLM 510
Cdd:cd00567 259 qgpDEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSRE--YPVERYLRDARAARIAEGTAEIQRLII 325
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
147-477 |
2.28e-41 |
|
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: 155.89 E-value: 2.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 147 EIGQAMDLPPAAWEHIKTHGFFALIIPKEYGGKGFSAYAHSQVAMKLATRSGDLASTVMVPNSLgPAELLLHYGTDEQRN 226
Cdd:cd01158 24 EMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVIVSVHNSL-GANPIIKFGTEEQKK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 227 HYLPRLARGDDIPCFALTGPLAGSDAGAMPDTGVICKGEWegketlglRLNWEKRYITLGPVATLLgLAFKAHDPDhlLG 306
Cdd:cd01158 103 KYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDY--------VLNGSKMWITNGGEADFY-IVFAVTDPS--KG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 307 EEedlGISLALIPTDTPGVEIGRRHLPLGaafMNGPNSG----KDVFIPLEFLIgGQEmlGKGWMMLMNCLSVGR-SISL 381
Cdd:cd01158 172 YR---GITAFIVERDTPGLSVGKKEDKLG---IRGSSTTelifEDVRVPKENIL-GEE--GEGFKIAMQTLDGGRiGIAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 382 PAVGTGAAKFTSLVtgQYAQVREQFNVPLSAFEGIQEALARIggnAWLMDSARMLTANAVDM---GEKPSVLSAILKYHL 458
Cdd:cd01158 243 QALGIAQAALDAAV--DYAKERKQFGKPIADFQGIQFKLADM---ATEIEAARLLTYKAARLkdnGEPFIKEAAMAKLFA 317
|
330
....*....|....*....
gi 1524473354 459 TERGRECISHAMDVHGGKG 477
Cdd:cd01158 318 SEVAMRVTTDAVQIFGGYG 336
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
105-516 |
6.84e-40 |
|
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: 152.62 E-value: 6.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 105 ELFSGRPDWDKLLAYPKV---QLTEEEQAFIdGPTEELCAMVSD-WEIGQAMDLPPAAWEHIKTHGFFALIIPKEYGGKG 180
Cdd:cd01161 5 NMFLGDIVTKQVFPYPSVlteEQTEELNMLV-GPVEKFFEEVNDpAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 181 FSAYAHSQVAMKLAtRSGDLASTVMVPNSLGPAELLLhYGTDEQRNHYLPRLARGDDIPCFALTGPLAGSDAGAMPDTGV 260
Cdd:cd01161 84 LNNTQYARLAEIVG-MDLGFSVTLGAHQSIGFKGILL-FGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 261 ICKgewEGKETLglrLNWEKRYITLGPVATLLgLAFKAHDPDHLLGEEEDlGISLALIPTDTPGVEIGRRHLPLGaafMN 340
Cdd:cd01161 162 LSE---DGKHYV---LNGSKIWITNGGIADIF-TVFAKTEVKDATGSVKD-KITAFIVERSFGGVTNGPPEKKMG---IK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 341 GPNSG----KDVFIPLEFLIGgqeMLGKGWMMLMNCLSVGRsISLPAVGTGAAKFTSLVTGQYAQVREQFNVPLSAFEGI 416
Cdd:cd01161 231 GSNTAevyfEDVKIPVENVLG---EVGDGFKVAMNILNNGR-FGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 417 QEALARIGGNAWLMDSARMLTANAVDMGEKP--SVLSAILKYHLTERGRECISHAMDVHGGKGIIMGPNnyLGRSWQGAP 494
Cdd:cd01161 307 QEKLANMAILQYATESMAYMTSGNMDRGLKAeyQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYG--VERVLRDLR 384
|
410 420
....*....|....*....|..
gi 1524473354 495 IFITVEGANILSRnLMIFGQGA 516
Cdd:cd01161 385 IFRIFEGTNEILR-LFIALTGL 405
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
111-478 |
7.72e-35 |
|
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: 137.10 E-value: 7.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 111 PDWDKLLAYpKVQLTEEEQAFIDGpTEELCA------MVSDWEIGqamDLPPAAWEHIKTHGFFAlIIPKEYGGKGFSAY 184
Cdd:cd01151 1 FNWEDPLNL-DDLLTEEERAIRDT-AREFCQeelaprVLEAYREE---KFDRKIIEEMGELGLLG-ATIKGYGCAGLSSV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 185 AHSQVAMKLATRSGDLASTVMVPNSLGPAELLLhYGTDEQRNHYLPRLARGDDIPCFALTGPLAGSDAGAMPdtgviCKG 264
Cdd:cd01151 75 AYGLIAREVERVDSGYRSFMSVQSSLVMLPIYD-FGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGME-----TRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 265 EWEGKetlGLRLNWEKRYITLGPVATLLGLAFKahdpdhllgEEEDLGISLALIPTDTPGVEIGRRHLPLG-AAFMNGPN 343
Cdd:cd01151 149 RKDGG---GYKLNGSKTWITNSPIADVFVVWAR---------NDETGKIRGFILERGMKGLSAPKIQGKFSlRASITGEI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 344 SGKDVFIPLEFLIGGQEMLGKGwmmlMNCLSVGR-SISLPAVgtGAAKFTSLVTGQYAQVREQFNVPLSAFEGIQEALAR 422
Cdd:cd01151 217 VMDNVFVPEENLLPGAEGLRGP----FKCLNNARyGIAWGAL--GAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLAD 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1524473354 423 IGGNAWLMDSARMLTANAVDMGEKPSVLSAILKYHLTERGRECISHAMDVHGGKGI 478
Cdd:cd01151 291 MLTEIALGLLACLRVGRLKDQGKATPEQISLLKRNNCGKALEIARTAREMLGGNGI 346
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
137-477 |
1.09e-26 |
|
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: 112.59 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 137 EELCAMVSDWEIgqAMDLPPAAWEHIKTHGFFALIIPKEYGGKGFSAYAHSQVAMKLAtRSGDLASTVMVPNSLGpAELL 216
Cdd:cd01160 16 KEVAPFHHEWEK--AGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELA-RAGGSGPGLSLHTDIV-SPYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 217 LHYGTDEQRNHYLPRLARGDDIPCFALTGPLAGSDAGAMPDTGVICKGEWegketlglRLNWEKRYITLGPVATLLGLAF 296
Cdd:cd01160 92 TRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHY--------VLNGSKTFITNGMLADVVIVVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 297 KAHDPDHLLGeeedlGISLALIPTDTPGVEIGRRHLPLG-------AAFMNgpnsgkDVFIPLEFLIgGQEmlGKGWMML 369
Cdd:cd01160 164 RTGGEARGAG-----GISLFLVERGTPGFSRGRKLKKMGwkaqdtaELFFD------DCRVPAENLL-GEE--NKGFYYL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 370 MNCLSVGRsISLPAVGTGAAKFTSLVTGQYAQVREQFNVPLSAFEGIQEALARIGGNAWLMDSARMLTANAVDMGEKPSV 449
Cdd:cd01160 230 MQNLPQER-LLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVA 308
|
330 340
....*....|....*....|....*...
gi 1524473354 450 LSAILKYHLTERGRECISHAMDVHGGKG 477
Cdd:cd01160 309 EASMAKYWATELQNRVAYECVQLHGGWG 336
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
124-477 |
3.89e-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: 108.30 E-value: 3.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 124 LTEEEQAFI----DGPTEELCAMVSDWEigQAMDLPPAAWEHIKTHGFFALIIPKEYGGKGFSAYAHSQVAMKLATrsGD 199
Cdd:cd01162 1 LNEEQRAIQevarAFAAKEMAPHAADWD--QKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALST--GC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 200 LASTVMVPNSLGPAELLLHYGTDEQRNHYLPRLARGDDIPCFALTGPLAGSDAGAMPDTGVIckgewEGKETLglrLNWE 279
Cdd:cd01162 77 VSTAAYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVR-----EGDHYV---LNGS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 280 KRYITLGPVATLLGLAFKAhdpdhllGEEEDLGISLALIPTDTPGVEIGRRHLPLGaaFMNGPNSG---KDVFIPLEFLI 356
Cdd:cd01162 149 KAFISGAGDSDVYVVMART-------GGEGPKGISCFVVEKGTPGLSFGANEKKMG--WNAQPTRAvifEDCRVPVENRL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 357 GGQemlGKGWMMLMNCLSVGRsISLPAVGTGAAKFTSLVTGQYAQVREQFNVPLSAFEGIQEALARIggnAWLMDSARML 436
Cdd:cd01162 220 GGE---GQGFGIAMAGLNGGR-LNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADM---ATELVASRLM 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1524473354 437 ---TANAVDMGEKPSV-LSAILKYHLTERGRECISHAMDVHGGKG 477
Cdd:cd01162 293 vrrAASALDRGDPDAVkLCAMAKRFATDECFDVANQALQLHGGYG 337
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
147-493 |
2.01e-23 |
|
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: 103.26 E-value: 2.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 147 EIGQAMDLPPAAWEHIKTHGFFALIIPKEYGGKGFSAYAHSQVAMKLATRSGDLA------STVMVPNslgpaelLLHYG 220
Cdd:cd01156 27 KIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVAlsygahSNLCINQ-------IYRNG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 221 TDEQRNHYLPRLARGDDIPCFALTGPLAGSDAGAMPdtgviCKGEWEGKEtlgLRLNWEKRYITLGPVATLLgLAFKAHD 300
Cdd:cd01156 100 SAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMK-----LRAEKKGDR---YVLNGSKMWITNGPDADTL-VVYAKTD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 301 PDhllgeEEDLGISLALIPTDTPGVEIGRRHLPLGaafMNGPNSGK----DVFIPLEFLIGGqemLGKGWMMLMNCLSVG 376
Cdd:cd01156 171 PS-----AGAHGITAFIVEKGMPGFSRAQKLDKLG---MRGSNTCElvfeDCEVPEENILGG---ENKGVYVLMSGLDYE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 377 RSIsLPAVGTGAAKFTSLVTGQYAQVREQFNVPLSAFEGIQEALARIGGNawlMDSARML---TANAVDMGEKPSVLSAI 453
Cdd:cd01156 240 RLV-LAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTR---LNASRSYlytVAKACDRGNMDPKDAAG 315
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1524473354 454 LKYHLTERGRECISHAMDVHGGKGIImgpNNY-LGRSWQGA 493
Cdd:cd01156 316 VILYAAEKATQVALDAIQILGGNGYI---NDYpTGRLLRDA 353
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
125-236 |
3.26e-20 |
|
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: 86.75 E-value: 3.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 125 TEEEQAFIDGP----TEELCAMVSDWEigQAMDLPPAAWEHIKTHGFFALIIPKEYGGKGFSAYAHSQVAMKLATRSGDL 200
Cdd:pfam02771 1 TEEQEALRDTVrefaEEEIAPHAAEWD--EEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASV 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 1524473354 201 ASTVMVPNSLGpAELLLHYGTDEQRNHYLPRLARGD 236
Cdd:pfam02771 79 ALALSVHSSLG-APPILRFGTEEQKERYLPKLASGE 113
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
172-477 |
1.36e-19 |
|
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: 91.49 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 172 IPKEYGGKGFSAYAHSQVAMKLATRSGDLASTVMVpNSLGPAELLLHyGTDEQRNHYLPRLARGDDIPCFALTGPLAGSD 251
Cdd:cd01157 51 IPEDCGGLGLGTFDTCLITEELAYGCTGVQTAIEA-NSLGQMPVIIS-GNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSD 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 252 AgampdTGVICKGEWEGKETLglrLNWEKRYITLGPVAT-LLGLAFKAHDPDHLLGEeedlGISLALIPTDTPGVEIGRR 330
Cdd:cd01157 129 V-----AGIKTKAEKKGDEYI---INGQKMWITNGGKANwYFLLARSDPDPKCPASK----AFTGFIVEADTPGIQPGRK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 331 HLPLGAAFMNGPN-SGKDVFIPLEFLIGGQemlGKGWMMLMNCLSVGRsislPAVGTGAAKFTSLV---TGQYAQVREQF 406
Cdd:cd01157 197 ELNMGQRCSDTRGiTFEDVRVPKENVLIGE---GAGFKIAMGAFDKTR----PPVAAGAVGLAQRAldeATKYALERKTF 269
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524473354 407 NVPLSAFEGIQEALARIGGNAWLMDSARMLTANAVDMGEKPSVLSAILKYHLTERGRECISHAMDVHGGKG 477
Cdd:cd01157 270 GKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAFAADIANQLATDAVQIFGGNG 340
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
124-479 |
8.93e-18 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 86.45 E-value: 8.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 124 LTEEEQAF---IDGPTEELCA--MVSDWEIGQamdLPPAAWEHIKTHGFFALIIpKEYGGKGFSAYAHSQVAMKLATRSG 198
Cdd:PLN02526 29 LTPEEQALrkrVRECMEKEVApiMTEYWEKAE---FPFHIIPKLGSLGIAGGTI-KGYGCPGLSITASAIATAEVARVDA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 199 DLASTVMVPNSLGPAELLLhYGTDEQRNHYLPRLARGDDIPCFALTGPLAGSDAGAMPDTGVICKGEWegketlglRLNW 278
Cdd:PLN02526 105 SCSTFILVHSSLAMLTIAL-CGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGW--------ILNG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 279 EKRYITLGPVATLLGLAFKAHDPDHLLGeeedlgislALIPTDTPGVEIGRRHLPLGAAFM-NGPNSGKDVFIPLEFLIG 357
Cdd:PLN02526 176 QKRWIGNSTFADVLVIFARNTTTNQING---------FIVKKGAPGLKATKIENKIGLRMVqNGDIVLKDVFVPDEDRLP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 358 GQemlgKGWMMLMNCLSVGRsISLPAVGTGAAKFTSLVTGQYAQVREQFNVPLSAFEGIQEALARIGGN-------AW-- 428
Cdd:PLN02526 247 GV----NSFQDTNKVLAVSR-VMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNiqamflvGWrl 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1524473354 429 --LMDSARMLTANAvdmgekpsvlsAILKYHLTERGRECISHAMDVHGGKGII 479
Cdd:PLN02526 322 ckLYESGKMTPGHA-----------SLGKAWITKKARETVALGRELLGGNGIL 363
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
126-491 |
3.11e-16 |
|
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: 81.24 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 126 EEEQAFIDGPTEELCAMV-SDWEIGQAMDLPPAAWEHIKTH------GFFALIIPKEYGGKGFSAYAHSQVAMKLAtRSG 198
Cdd:cd01152 1 PSEEAFRAEVRAWLAAHLpPELREESALGYREGREDRRRWQralaaaGWAAPGWPKEYGGRGASLMEQLIFREEMA-AAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 199 DLASTVMV-PNSLGPAelLLHYGTDEQRNHYLPRLARGDDIPCFALTGPLAGSDAGAMPDTGVICKGEWegketlglRLN 277
Cdd:cd01152 80 APVPFNQIgIDLAGPT--ILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDW--------VVN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 278 WEKRYITLGPVATLLGLAFKAhDPDhllgEEEDLGISLALIPTDTPGVEIGRRHLPLGAAFMNgPNSGKDVFIPLEFLIG 357
Cdd:cd01152 150 GQKIWTSGAHYADWAWLLVRT-DPE----APKHRGISILLVDMDSPGVTVRPIRSINGGEFFN-EVFLDDVRVPDANRVG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 358 GQemlGKGWMMLMNCLSVGRSislpAVGTGAAKFTSLVTGQYAQVREQFNvPLSAFEGIQEALARIGGNAWLMDSARMLT 437
Cdd:cd01152 224 EV---NDGWKVAMTTLNFERV----SIGGSAATFFELLLARLLLLTRDGR-PLIDDPLVRQRLARLEAEAEALRLLVFRL 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1524473354 438 ANAVDMGEKPSVLSAILKYHLTERGRECISHAMDVHGGKGIIMGPNN--YLGRSWQ 491
Cdd:cd01152 296 ASALAAGKPPGAEASIAKLFGSELAQELAELALELLGTAALLRDPAPgaELAGRWE 351
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
159-514 |
5.29e-16 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 81.08 E-value: 5.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 159 WEHIKTHGFFALIIPKEYGGKGFsAYAHSQVAMKLATR-SGDLASTVMVPNSLGPAELLLHyGTDEQRNHYLPRLARGDD 237
Cdd:PLN02519 65 WKLMGDFNLHGITAPEEYGGLGL-GYLYHCIAMEEISRaSGSVGLSYGAHSNLCINQLVRN-GTPAQKEKYLPKLISGEH 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 238 IPCFALTGPLAGSDAGAMPdtgviCKGEwegKETLGLRLNWEKRYITLGPVATLLGLAFKAhdpDHLLGEEedlGISLAL 317
Cdd:PLN02519 143 VGALAMSEPNSGSDVVSMK-----CKAE---RVDGGYVLNGNKMWCTNGPVAQTLVVYAKT---DVAAGSK---GITAFI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 318 IPTDTPGVEIGRRHLPLGaafMNGPNSGKDVF----IPLEFLIGGQemlGKGWMMLMNCLSVGRSIsLPAVGTGAAKFTS 393
Cdd:PLN02519 209 IEKGMPGFSTAQKLDKLG---MRGSDTCELVFencfVPEENVLGQE---GKGVYVMMSGLDLERLV-LAAGPLGLMQACL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 394 LVTGQYAQVREQFNVPLSAFEGIQEALARI-----GGNAWLMDSARMLTANAVDMGEKPSVLsailkYHLTERGRECISH 468
Cdd:PLN02519 282 DVVLPYVRQREQFGRPIGEFQFIQGKLADMytslqSSRSYVYSVARDCDNGKVDRKDCAGVI-----LCAAERATQVALQ 356
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1524473354 469 AMDVHGGKGIImgpNNY-LGRSWQGAPIFITVEGANILSRnlMIFGQ 514
Cdd:PLN02519 357 AIQCLGGNGYI---NEYpTGRLLRDAKLYEIGAGTSEIRR--MLIGR 398
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
240-335 |
1.51e-14 |
|
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: 70.00 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 240 CFALTGPLAGSDAGAMPDTGVICKGEwegketlGLRLNWEKRYITLGPVATLLGLAFKAHDPDHllgeeeDLGISLALIP 319
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGG-------GWVLNGTKWWITNAGIADLFLVLARTGGDDR------HGGISLFLVP 67
|
90
....*....|....*.
gi 1524473354 320 TDTPGVEIGRRHLPLG 335
Cdd:pfam02770 68 KDAPGVSVRRIETKLG 83
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
155-477 |
2.70e-14 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 75.54 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 155 PPAAWEHIKTHGFFALIIPKEYGGKGFSAYAHSQVAMKLAtRSGdlASTVMVPNSLGPAELLlHYGTDEQ-RNHYLPRLA 233
Cdd:PRK12341 39 PREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVS-KCG--APAFLITNGQCIHSMR-RFGSAEQlRKTAESTLE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 234 RGDDIPCFALTGPLAGSDAGAMPDTGVickgEWEGKetlgLRLNWEKRYITLGPVAT-LLGLAFKAHDPDhllgeeEDLG 312
Cdd:PRK12341 115 TGDPAYALALTEPGAGSDNNSATTTYT----RKNGK----VYLNGQKTFITGAKEYPyMLVLARDPQPKD------PKKA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 313 ISLALIPTDTPGV------EIGRRHLPLGAAFMNgpnsgkDVFIPLEFLIGGQemlGKGWMMLMNCLSVGRsISLPAVGT 386
Cdd:PRK12341 181 FTLWWVDSSKPGIkinplhKIGWHMLSTCEVYLD------NVEVEESDLVGEE---GMGFLNVMYNFEMER-LINAARSL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 387 GAAKFTSLVTGQYAQVREQFNVPLSAFEGIQEALARIGGNAWLMDSARMLTANAVDMGEKPSVLSAILKYHLTERGRECI 466
Cdd:PRK12341 251 GFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAALAKLYCARTAMEVI 330
|
330
....*....|.
gi 1524473354 467 SHAMDVHGGKG 477
Cdd:PRK12341 331 DDAIQIMGGLG 341
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
166-477 |
7.99e-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: 74.35 E-value: 7.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 166 GFFALIIPKEYGGKGFSAYAHSQVA-MKLATrsgdlASTVMVPNSLGP-AELLLHYGTDEQRNHYLPRLARGDDIPCFAL 243
Cdd:cd01153 49 GWMALGVPEEYGGQGLPITVYSALAeIFSRG-----DAPLMYASGTQGaAATLLAHGTEAQREKWIPRLAEGEWTGTMCL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 244 TGPLAGSDAG-----AMPDTGvickGEWegketlglRLNWEKRYITLGpvatllglafkAHDPD----HLL------GEE 308
Cdd:cd01153 124 TEPDAGSDLGalrtkAVYQAD----GSW--------RINGVKRFISAG-----------EHDMSenivHLVlarsegAPP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 309 EDLGISLALIP-----TDTPGVEIGRRHLPLGaafMNGPNSGKDVFIPLEFLIGGQEMLGKGWMM-LMNCLSVGrsISLP 382
Cdd:cd01153 181 GVKGLSLFLVPkflddGERNGVTVARIEEKMG---LHGSPTCELVFDNAKGELIGEEGMGLAQMFaMMNGARLG--VGTQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 383 AVGTGAAKFtsLVTGQYAQVREQFNVPLSAFEGIQEALARIGGNAWLMDSAR--------MLTANAVDMGEKPSV----- 449
Cdd:cd01153 256 GTGLAEAAY--LNALAYAKERKQGGDLIKAAPAVTIIHHPDVRRSLMTQKAYaegsraldLYTATVQDLAERKATegedr 333
|
330 340 350
....*....|....*....|....*....|....*..
gi 1524473354 450 ---------LSAILKYHLTERGRECISHAMDVHGGKG 477
Cdd:cd01153 334 kalsaladlLTPVVKGFGSEAALEAVSDAIQVHGGSG 370
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
123-478 |
1.50e-11 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 67.16 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 123 QLTEEEQAFIDGPTEelcAMVSD-WE-----IGQAMDLPPAAWEHIKTHGFFALIIPKEYGGKGFSAYAHSQVAMKLAtR 196
Cdd:PRK03354 4 NLNDEQELFVAGIRE---LMASEnWEayfaeCDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELG-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 197 SGdlASTVMVPNSLGPAELLLHYGTDEQRNHYLPRLARGDDIPCFALTGPLAGSDAGAMPDTgvicKGEWEGKetlgLRL 276
Cdd:PRK03354 80 LG--APTYVLYQLPGGFNTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTT----YTRRNGK----VYL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 277 NWEKRYITLGP-VATLLGLAFKAHDPDHLLGEEEDLGISLaliptdtPGVEIGRRHlPLG--------AAFMNGPNSGKD 347
Cdd:PRK03354 150 NGSKCFITSSAyTPYIVVMARDGASPDKPVYTEWFVDMSK-------PGIKVTKLE-KLGlrmdscceITFDDVELDEKD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 348 VFiplefligGQEmlGKGWMMLMNCLSVGR-SISLPAVGTGAAKFTSlvTGQYAQVREQFNVPLSAFEGIQEALARIGGN 426
Cdd:PRK03354 222 MF--------GRE--GNGFNRVKEEFDHERfLVALTNYGTAMCAFED--AARYANQRVQFGEAIGRFQLIQEKFAHMAIK 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1524473354 427 AWLMDSARMLTANAVDMGEKPSVLSAILKYHLTERGRECISHAMDVHGGKGI 478
Cdd:PRK03354 290 LNSMKNMLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGI 341
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
363-503 |
3.80e-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: 61.89 E-value: 3.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 363 GKGWMMLMNCLSVGR-SISLPAVGTGAAKFtsLVTGQYAQVREQFNVPLSAFEGIQEALARIGGNAwlmDSARMLT---A 438
Cdd:pfam00441 1 GRGFRVAMETLNHERlAIAAMALGLARRAL--DEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEI---EAARLLVyraA 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1524473354 439 NAVDMGEKPSVLSAILKYHLTERGRECISHAMDVHGGKGIImgPNNYLGRSWQGAPIFITVEGAN 503
Cdd:pfam00441 76 EALDAGGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYL--REYPVERLYRDARVLRIGEGTS 138
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
166-477 |
3.96e-10 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 62.65 E-value: 3.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 166 GFFALIIPKEYGGKGFSAYAHSQVAMKLATRS-----GDLASTVMVPNSLgpaellLHYGTDEQRNHYLPRLARGDDIPC 240
Cdd:PTZ00461 81 GVMGVTVPEADGGAGMDAVAAVIIHHELSKYDpgfclAYLAHSMLFVNNF------YYSASPAQRARWLPKVLTGEHVGA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 241 FALTGPLAGSDAGAMPDTGvicKGEWEGKETlglrLNWEKRYITLGPVATLLglafkahdpdhLLGEEEDLGISLALIPT 320
Cdd:PTZ00461 155 MGMSEPGAGTDVLGMRTTA---KKDSNGNYV----LNGSKIWITNGTVADVF-----------LIYAKVDGKITAFVVER 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 321 DTPGVEIGRRHLPLGaafMNGPNSGK----DVFIPLEFLIGGQemlGKGWMMLMNCLSVGRsISLPAVGTGAAKFTSLVT 396
Cdd:PTZ00461 217 GTKGFTQGPKIDKCG---MRASHMCQlffeDVVVPAENLLGEE---GKGMVGMMRNLELER-VTLAAMAVGIAERSVELM 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 397 GQYAQVREQFNVPLSAFEGIQEALARIGGNAwlmDSARMLT---ANAVDMGEKPSVLSAILKYHLTERGRECISHAMDVH 473
Cdd:PTZ00461 290 TSYASERKAFGKPISNFGQIQRYIAEGYADT---EAAKALVysvSHNVHPGNKNRLGSDAAKLFATPIAKKVADSAIQVM 366
|
....
gi 1524473354 474 GGKG 477
Cdd:PTZ00461 367 GGMG 370
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
137-481 |
2.91e-09 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 60.65 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 137 EELCAMVSDWEIGQamdlPP---AAWEHIKTHGFFALIIPKEYGGKGFSAYAHSQVAMKLATRSGDLAstvMVPN-SLGP 212
Cdd:PTZ00456 84 SEGCVLLKDGNVTT----PKgfkEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFS---MYPGlSIGA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 213 AELLLHYGTDEQRNHYLPRLARGDDIPCFALTGPLAGSDAGAMPDTGVICK-GEWegketlglRLNWEKRYITLGP---V 288
Cdd:PTZ00456 157 ANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSAdGSY--------KITGTKIFISAGDhdlT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 289 ATLLGLAFkAHDPDHLLGEEedlGISLALIPTDTP----------GVEIGRRHLPLG-----AAFMNGPNSgkdvfipLE 353
Cdd:PTZ00456 229 ENIVHIVL-ARLPNSLPTTK---GLSLFLVPRHVVkpdgsletakNVKCIGLEKKMGikgssTCQLSFENS-------VG 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 354 FLIGGQEMLGKGWMMLMNCLSVGRSISlpavGTGAAKFTSLVTGQYAQVREQfnvpLSAFEGIQE--------------- 418
Cdd:PTZ00456 298 YLIGEPNAGMKQMFTFMNTARVGTALE----GVCHAELAFQNALRYARERRS----MRALSGTKEpekpadriichanvr 369
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1524473354 419 -------ALARiGGNAWLMDSARMLT--ANAVD------MGEKPSVLSAILKYHLTERGRECISHAMDVHGGKGIIMG 481
Cdd:PTZ00456 370 qnilfakAVAE-GGRALLLDVGRLLDihAAAKDaatreaLDHEIGFYTPIAKGCLTEWGVEAASRCLQVWGGHGYIKG 446
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
163-493 |
6.22e-09 |
|
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: 58.94 E-value: 6.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 163 KTHGFFALIIPKEYGGKGFS--AYAHsqvamkLATRSGD--LASTVM---VPNSlGPAELLLHYGTDEQRNHYLPRLARG 235
Cdd:cd01155 51 KAEGLWNLFLPEVSGLSGLTnlEYAY------LAEETGRsfFAPEVFncqAPDT-GNMEVLHRYGSEEQKKQWLEPLLDG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 236 DDIPCFALTGP-LAGSDAgampdTGVICKGEWEGKETLglrLNWEKRYIT--LGP---VATLLGLAfkahDPDhllGEEE 309
Cdd:cd01155 124 KIRSAFAMTEPdVASSDA-----TNIECSIERDGDDYV---INGRKWWSSgaGDPrckIAIVMGRT----DPD---GAPR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 310 DLGISLALIPTDTPGVEIGRrhlPLGA-AFMNGPN-----SGKDVFIPLEFLIGGQemlGKGWMMLMNCLSVGRsISLPA 383
Cdd:cd01155 189 HRQQSMILVPMDTPGVTIIR---PLSVfGYDDAPHghaeiTFDNVRVPASNLILGE---GRGFEIAQGRLGPGR-IHHCM 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 384 VGTGAAKFTSLVTGQYAQVREQFNVPLSAFEGIQEALA--RIGgnawlMDSARMLTANAVDM-------GEKPSVlsAIL 454
Cdd:cd01155 262 RLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAksRIE-----IEQARLLVLKAAHMidtvgnkAARKEI--AMI 334
|
330 340 350
....*....|....*....|....*....|....*....
gi 1524473354 455 KYHLTERGRECISHAMDVHGGKGIimGPNNYLGRSWQGA 493
Cdd:cd01155 335 KVAAPRMALKIIDRAIQVHGAAGV--SQDTPLANMYAWA 371
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
213-479 |
3.17e-03 |
|
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: 40.82 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 213 AELLLHYGTDEQRnHYLPRLA-RGDDIPCFA---LTGPLAGSDAGAMPDTGVI-CKGEWegketlglRLNWEKrYITLGP 287
Cdd:cd01154 120 VYALRKYGPEELK-QYLPGLLsDRYKTGLLGgtwMTEKQGGSDLGANETTAERsGGGVY--------RLNGHK-WFASAP 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 288 VATL-LGLAFKAHDPDhllGEEedlGISLALIPTDTP-----GVEIGRRHLPLGAAFMNgpnSGKDVFIPLE-FLIGGQe 360
Cdd:cd01154 190 LADAaLVLARPEGAPA---GAR---GLSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVA---TGEVEFDDAEaYLIGDE- 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 361 mlGKGWMMLMNCLSVGRsISLPAVGTGAAKFTSLVTGQYAQVREQFNVPLSAFEGIQEALARI-----GGNAWLMDSARM 435
Cdd:cd01154 260 --GKGIYYILEMLNISR-LDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMevdveAATALTFRAARA 336
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1524473354 436 LTANAVDMGEK---PSVLSAILKYHLTERGRECISHAMDVHGGKGII 479
Cdd:cd01154 337 FDRAAADKPVEahmARLATPVAKLIACKRAAPVTSEAMEVFGGNGYL 383
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
150-327 |
7.87e-03 |
|
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: 39.61 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 150 QAMDLPPAAWEHIKTHGFFALIIPKEYGGKGFSAYAHSQVAMKLATRSGDLAStvMVPNSLGPAELLLHYGTDEQRNHYL 229
Cdd:cd01163 19 RQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQ--ALRAHFGFVEALLLAGPEQFRKRWF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 230 PRLARGddipcfALTGPLAGSDAGAMPDTGVICKGEWEGketlGLRLNWEKRYITLGPVATLLGLAfkAHDPdhllgEEE 309
Cdd:cd01163 97 GRVLNG------WIFGNAVSERGSVRPGTFLTATVRDGG----GYVLNGKKFYSTGALFSDWVTVS--ALDE-----EGK 159
|
170
....*....|....*...
gi 1524473354 310 DLGislALIPTDTPGVEI 327
Cdd:cd01163 160 LVF---AAVPTDRPGITV 174
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
383-490 |
8.15e-03 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 37.33 E-value: 8.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524473354 383 AVGTGAAK-----FTSLVTGQyaqVREQFNVPLSAFEGIQEALARIggnAWLMDSARMLTANAVDMGEKPS--------- 448
Cdd:pfam08028 4 AAALGAARaalaeFTERARGR---VRAYFGVPLAEDPATQLALAEA---AARIDAARLLLERAAARIEAAAaagkpvtpa 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1524473354 449 --VLSAILKYHLTERGRECISHAMDVHGGKGIIMgpNNYLGRSW 490
Cdd:pfam08028 78 lrAEARRAAAFATELAVAAVDALFRAAGGSALFQ--DSPLQRIW 119
|
|
| |
