|
Name |
Accession |
Description |
Interval |
E-value |
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
2-545 |
1.05e-134 |
|
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: 405.56 E-value: 1.05e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 2 RALTVQRV--KFAMDLPLLKRAGQDLAEKTknfvsrsLVIGEVLSMADMATGVKCGIIYWLFGGAIRNLGSPEHVTKWFQ 79
Cdd:cd01150 55 REELYEELkrKAKTDVERMGELMADDPEKM-------LALTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 80 PLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVIDTPCENAEKMYIGN-AMYGNYAAVFAQLIIDGRSQGPHCF 158
Cdd:cd01150 128 GANNLEIIGCFAQTELGHGSNLQGLETTATYDPLTQEFVINTPDFTATKWWPGNlGKTATHAVVFAQLITPGKNHGLHAF 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 159 IVPVRDENG-SLYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSVAPDGQYHSPIRNKSARFNAMLAALTP 237
Cdd:cd01150 208 IVPIRDPKThQPLPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDPNKRYGAMLGTRSG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 238 SRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGPKTKE-EVKIIEHQTQTLRLMPHLATALALTFVSRY-------AGALLD 309
Cdd:cd01150 288 GRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPKPSDpEVQILDYQLQQYRLFPQLAAAYAFHFAAKSlvemyheIIKELL 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 310 EDVFQgkelvNSRSLQALVAGLKAYSTWENIRCLQDCRECTGG---MVVGR--ELLAQYTKQ--YEekplfG----LLQN 378
Cdd:cd01150 368 QGNSE-----LLAELHALSAGLKAVATWTAAQGIQECREACGGhgyLAMNRlpTLRDDNDPFctYE-----GdntvLLQQ 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 379 WAESVGDKLRTSFLafnmdtvddLAFLLKAVKFRERVLQRGLVARIYYKVKTKKEDfFHAWNSCLHHVASLSLAHTHRVT 458
Cdd:cd01150 438 TANYLLKKYAQAFS---------LADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGS-FEARNNSQVHLRCAAKAHTEYTV 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 459 LEQFSLAVKSCPDQEDQTLLMKFCLLYGTKLVFQERAWYLEHKYLTPMASTRIRNQLLDLCDSVKDDARRVISTFNIPHT 538
Cdd:cd01150 508 LQRFHESVEEIVDPSVRAVLKRLCDLYALWLLEEHIADFLEGGFLGGQDVKAVREALLALLPQLRPDAVALVDAFDLPDF 587
|
....*..
gi 218563752 539 YLHAPIA 545
Cdd:cd01150 588 VLNSPIG 594
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
34-545 |
6.72e-105 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 331.05 E-value: 6.72e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 34 SRSLVIGEVLSMADMATGVKCGIIYWLFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDLS 113
Cdd:PLN02636 121 AKYFAITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 114 AQEFVIDTPCENAEKMYIGNA-MYGNYAAVFAQLIIDG------RSQGPHCFIVPVRD-ENGSLYPGVTAIDMMYKEGLH 185
Cdd:PLN02636 201 TDEFVINTPNDGAIKWWIGNAaVHGKFATVFARLKLPThdskgvSDMGVHAFIVPIRDmKTHQVLPGVEIRDCGHKVGLN 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 186 GVDNGILIFDKVRIPRENLLDKFGSVAPDGQYHSPIRNKSARFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRR 265
Cdd:PLN02636 281 GVDNGALRFRSVRIPRDNLLNRFGDVSRDGKYTSSLPTINKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQ 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 266 QFGPKTKEEVKIIEHQTQTLRLMPHLATALALTFVSRYAGALLDE-DVFQGKELVNsrSLQALVAGLKAYSTWENIRCLQ 344
Cdd:PLN02636 361 QFGPPKQPEISILDYQSQQHKLMPMLASTYAFHFATEYLVERYSEmKKTHDDQLVA--DVHALSAGLKAYITSYTAKALS 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 345 DCRECTGG--------------------------MVVGRELLAQYTKQYEEKPLFGLLQNWAESVGDKLRTSFLAFN--- 395
Cdd:PLN02636 439 TCREACGGhgyaavnrfgslrndhdifqtfegdnTVLLQQVAADLLKQYKEKFQGGTLSVTWNYLRESMNTYLSQPNpvt 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 396 -----MDTVDDLAFLLKAVKFRERVLQRGLVARIyyKVKTKKEDFFHAWNSCLHHVASLSLAHTHRVTLEQFSLAVKSCP 470
Cdd:PLN02636 519 trwegEEHLRDPKFQLDAFRYRTSRLLQTAALRL--RKHSKTLGSFGAWNRCLNHLLTLAESHIESVILAKFIEAVERCP 596
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 218563752 471 DQEDQTLLMKFCLLYGTKLVFQERAWYLEHKYLTPMASTRIRNQLLDLCDSVKDDARRVISTFNIPHTYLHAPIA 545
Cdd:PLN02636 597 DRSTRAALKLVCDLYALDRIWKDIGTYRNVDYVAPNKAKAIHKLTEYLSFQVRNVAKELVDAFGLPDHVTRAPIA 671
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
2-545 |
1.12e-101 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 322.11 E-value: 1.12e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 2 RALTVQRVKFamdlpLLKRAGQD--LAEKTKNFVSRSLVIGEVLSMADMATGVKCGIIYWLFGGAIRNLGSPEHVTKWFQ 79
Cdd:PLN02312 104 REITMKRILY-----LLERGVFRgwLTETGPEAELRKLALLEVIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHDKWLK 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 80 PLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVIDTPCENAEKMYIGNA-MYGNYAAVFAQLIIDGRSQGPHCF 158
Cdd:PLN02312 179 DTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFVINTPCESAQKYWIGGAaNHATHTIVFSQLHINGKNEGVHAF 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 159 IVPVRDENGSLYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSVAPDGQYHSPIRNKSARFNAMLAALTPS 238
Cdd:PLN02312 259 IAQIRDQDGNICPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNSVADVSPDGKYVSAIKDPDQRFGAFLAPLTSG 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 239 RLAVAFQAMGAMKLGLTIAIRYSHSRRQF-----GPktkeEVKIIEHQTQTLRLMPHLATALALTFVSRYAgalldEDVF 313
Cdd:PLN02312 339 RVTIAVSAIYSSKVGLAIAIRYSLSRRAFsvtpnGP----EVLLLDYPSHQRRLLPLLAKTYAMSFAANDL-----KMIY 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 314 QGKELVNSRSLQALVAGLKAYSTWENIRCLQDCRECTGG------------------------------MVVGRELLAQY 363
Cdd:PLN02312 410 VKRTPESNKAIHVVSSGFKAVLTWHNMRTLQECREACGGqglktenrvgqlkaeydvqstfegdnnvlmQQVSKALLAEY 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 364 -TKQYEEKPLFGL----LQNWAESVGDKLRTSflafnmdTVDDLAFLLKAVKFRErvlqRGLVARIYYKVKT---KKEDF 435
Cdd:PLN02312 490 vSAKKRNKPFKGLglehMNGPRPVIPTQLTSS-------TLRDSQFQLNLFCLRE----RDLLERFASEVSElqsKGESR 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 436 FHAWNSCLHHVASLSLAHTHRVTLEQFSLAVKSCPDQEDQTLLMKFCLLYgTKLVFQERAWYLEHKYLTPMASTRIRNQL 515
Cdd:PLN02312 559 EFAFLLSYQLAEDLGRAFSERAILQTFLDAEANLPTGSLKDVLGLLRSLY-VLISLDEDPSFLRYGYLSPDNVALVRKEV 637
|
570 580 590
....*....|....*....|....*....|
gi 218563752 516 LDLCDSVKDDARRVISTFNIPHTYLhAPIA 545
Cdd:PLN02312 638 AKLCGELRPHALALVSSFGIPDAFL-SPIA 666
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
64-352 |
1.41e-52 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 190.06 E-value: 1.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 64 AIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVIDTPCENAEKMYIGN-AMYGNYAAV 142
Cdd:PTZ00460 105 AFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHTPSVEAVKFWPGElGFLCNFALV 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 143 FAQLIIDGRSQGPHCFIVPVRDENG-SLYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSVAPDGQYhspI 221
Cdd:PTZ00460 185 YAKLIVNGKNKGVHPFMVRIRDKEThKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLARYIKVSEDGQV---E 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 222 R--NKSARFNAMLAaltpSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGPKTKEEVKIIEHQTQTLRLMPHLATALALTF 299
Cdd:PTZ00460 262 RqgNPKVSYASMMY----MRNLIIDQYPRFAAQALTVAIRYSIYRQQFTNDNKQENSVLEYQTQQQKLLPLLAEFYACIF 337
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 218563752 300 VSRYAGALLDEDV--FQGKELVNSRSLQALVAGLKAYSTWENIRCLQDCRECTGG 352
Cdd:PTZ00460 338 GGLKIKELVDDNFnrVQKNDFSLLQLTHAILSAAKANYTYFVSNCAEWCRLSCGG 392
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
57-540 |
2.59e-49 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 181.57 E-value: 2.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 57 IYW-LFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVIDTPCENAEKMYIGN-A 134
Cdd:PLN02443 101 LHWgMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFVIHSPTLTSSKWWPGGlG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 135 MYGNYAAVFAQLIIDGRSQGPHCFIVPVRD-ENGSLYPGVTAIDMMYKEGLHG---VDNGILIFDKVRIPRENLLDKFGS 210
Cdd:PLN02443 181 KVSTHAVVYARLITNGKDHGIHGFIVQLRSlDDHSPLPGVTVGDIGMKFGNGAyntMDNGFLRFDHVRIPRDQMLMRLSK 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 211 VAPDGQYHSPIRNKSARFNAMLAAltpsRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGPKTKE-EVKIIEHQTQTLRLMP 289
Cdd:PLN02443 261 VTREGKYVQSDVPRQLVYGTMVYV----RQTIVADASTALSRAVCIATRYSAVRRQFGSQDGGpETQVIDYKTQQSRLFP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 290 HLATALALTFVSRYAGALLdEDVFQGKELVNSRSLQ---ALVAGLKAYSTWENIRCLQDCRECTGGMvvGR-------EL 359
Cdd:PLN02443 337 LLASAYAFRFVGEWLKWLY-TDVTQRLEANDFSTLPeahACTAGLKSLTTSATADGIEECRKLCGGH--GYlcssglpEL 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 360 LAQYTK--QYEEKPLFGLLQ------NWAESVGDKLRTSFLAFNMDTVDDL----------------AFLLKAvkFRERV 415
Cdd:PLN02443 414 FAVYVPacTYEGDNVVLLLQvarflmKTVSQLGSGKKPVGTTAYMGRVQHLlqcrcgvqtaedwlnpSVVLEA--FEARA 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 416 LQRGLVARIYYKVKTKKEDFFHAWNSCLHHVAslsLAHTHRVTLEQFSLAVKS-CPDQEDQTLLMKFCLLYGTKLVFQER 494
Cdd:PLN02443 492 ARMAVTCAQNLSKFENQEAGFQELSADLVEAA---VAHCQLIVVSKFIEKLQQdIPGKGVKKQLQNLCYIYALYLLHKHL 568
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 218563752 495 AWYLEHKYLTPMASTRIRNQLLDLCDSVKDDARRVISTFNIPHTYL 540
Cdd:PLN02443 569 GDFLSTGCITPKQASLANDQLRSLYSQVRPNAVALVDAFNYTDHYL 614
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
37-363 |
9.84e-47 |
|
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: 168.48 E-value: 9.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 37 LVIGEVLSMADMATGVKCGIiYWLFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDlsAQE 116
Cdd:COG1960 70 ALVLEELARADASLALPVGV-HNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRD--GDG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 117 FVIdtpceNAEKMYIGNAMYGNYAAVFAQLIIDGRSQGPHCFIVPvRDEngslyPGVTAIDMMYKEGLHGVDNGILIFDK 196
Cdd:COG1960 147 YVL-----NGQKTFITNAPVADVILVLARTDPAAGHRGISLFLVP-KDT-----PGVTVGRIEDKMGLRGSDTGELFFDD 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 197 VRIPRENLLDKFGsvapdgqyhspirnksARFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGpktkeeVK 276
Cdd:COG1960 216 VRVPAENLLGEEG----------------KGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFG------RP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 277 IIEHQTQTLRLMPHLATALALTFVSRYAGALLDEDvfqgkelvnsRSLQALVAGLKAYSTWENIRCLQDCRECTGGMVVG 356
Cdd:COG1960 274 IADFQAVQHRLADMAAELEAARALVYRAAWLLDAG----------EDAALEAAMAKLFATEAALEVADEALQIHGGYGYT 343
|
....*...
gi 218563752 357 REL-LAQY 363
Cdd:COG1960 344 REYpLERL 351
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
58-358 |
2.55e-37 |
|
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: 140.88 E-value: 2.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 58 YWLFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDlsAQEFVIdtpceNAEKMYIGNAMYG 137
Cdd:cd00567 41 LLLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKD--GDGYVL-----NGRKIFISNGGDA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 138 NYAAVFAQLIIDG-RSQGPHCFIVPvRDEngslyPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSVapdgq 216
Cdd:cd00567 114 DLFIVLARTDEEGpGHRGISAFLVP-ADT-----PGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGG----- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 217 yhspirnksarFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGpktkeeVKIIEHQTQTLRLMPHLATALA 296
Cdd:cd00567 183 -----------FELAMKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQFG------KPLAEFQAVQFKLADMAAELEA 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218563752 297 LTFVSRYAGALLDEDvfqgkelvnSRSLQALVAGLKAYSTWENIRCLQDCRECTGGMVVGRE 358
Cdd:cd00567 246 ARLLLYRAAWLLDQG---------PDEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSRE 298
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
31-268 |
4.75e-26 |
|
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: 110.05 E-value: 4.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 31 NFVSRSLVIGEvLSMADMATGVKCGIIYWLFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATF 110
Cdd:cd01158 59 DFLAYAIAIEE-LAKVDASVAVIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 111 DlsAQEFVIdtpceNAEKMYIGNAMYGNYAAVFAQLIIDGRSQGPHCFIVPvRDEngslyPGVTAIDMMYKEGLHGVDNG 190
Cdd:cd01158 138 D--GDDYVL-----NGSKMWITNGGEADFYIVFAVTDPSKGYRGITAFIVE-RDT-----PGLSVGKKEDKLGIRGSSTT 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 218563752 191 ILIFDKVRIPRENLLDKFGsvapDGqyhspirnksarFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFG 268
Cdd:cd01158 205 ELIFEDVRVPKENILGEEG----EG------------FKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFG 266
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
63-268 |
3.66e-20 |
|
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: 92.81 E-value: 3.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 63 GAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDlsAQEFVIdtpceNAEKMYIGNAMYGNYAAV 142
Cdd:cd01151 103 LPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKD--GGGYKL-----NGSKTWITNSPIADVFVV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 143 FAQLIIDGRSQGphcFIVPvRDengslYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLdkfgsvapdgqyhspir 222
Cdd:cd01151 176 WARNDETGKIRG---FILE-RG-----MKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL----------------- 229
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 218563752 223 NKSARFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFG 268
Cdd:cd01151 230 PGAEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFG 275
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
65-352 |
4.40e-20 |
|
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: 92.18 E-value: 4.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 65 IRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDlsAQEFVIdtpceNAEKMYIGNAMYGNYAAVFA 144
Cdd:cd01160 91 ITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKD--GDHYVL-----NGSKTFITNGMLADVVIVVA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 145 QLIIDGRSQ-GPHCFIVpvrdENGSlyPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLdkfgsvapdGQyhspiRN 223
Cdd:cd01160 164 RTGGEARGAgGISLFLV----ERGT--PGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLL---------GE-----EN 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 224 KSarFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGpKTKEEVKIIEHQtqtlrlMPHLATALAltfVSRy 303
Cdd:cd01160 224 KG--FYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFG-KTLAQLQVVRHK------IAELATKVA---VTR- 290
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 218563752 304 agALLDEDVfqgKELVNSRSLQALVAGLKAYSTWENIRCLQDCRECTGG 352
Cdd:cd01160 291 --AFLDNCA---WRHEQGRLDVAEASMAKYWATELQNRVAYECVQLHGG 334
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
66-273 |
6.76e-18 |
|
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: 85.54 E-value: 6.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 66 RNlGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDlsAQEFVIdtpceNAEKMYIGNAMYGNYAAVFAQ 145
Cdd:cd01156 97 RN-GSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKK--GDRYVL-----NGSKMWITNGPDADTLVVYAK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 146 LIIDGRSQGPHCFIVpvrdENGslYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSvapdGQYhspirnks 225
Cdd:cd01156 169 TDPSAGAHGITAFIV----EKG--MPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENK----GVY-------- 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 218563752 226 arfnAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGPKTKE 273
Cdd:cd01156 231 ----VLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGE 274
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
90-195 |
8.96e-16 |
|
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: 72.70 E-value: 8.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 90 FAMTERGHGSNARGIQTEAtFDLSAQEFVIdtpceNAEKMYIGNAMYGNYAAVFAQLIIDGRSQGPHCFIVPVRDengsl 169
Cdd:pfam02770 2 FALTEPGAGSDVASLKTTA-ADGDGGGWVL-----NGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDA----- 70
|
90 100
....*....|....*....|....*.
gi 218563752 170 yPGVTAIDMMYKEGLHGVDNGILIFD 195
Cdd:pfam02770 71 -PGVSVRRIETKLGVRGLPTGELVFD 95
|
|
| ACOX |
pfam01756 |
Acyl-CoA oxidase; This is a family of Acyl-CoA oxidases EC:1.3.3.6. Acyl-coA oxidase converts ... |
401-544 |
1.02e-15 |
|
Acyl-CoA oxidase; This is a family of Acyl-CoA oxidases EC:1.3.3.6. Acyl-coA oxidase converts acyl-CoA into trans-2- enoyl-CoA.
Pssm-ID: 460314 [Multi-domain] Cd Length: 180 Bit Score: 75.28 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 401 DLAFLLKAvkFRERVlqRGLVARIYYKVKTKKE---DFFHAWNSCLHHVASLSLAHTHRVTLEQFSLAVKSCPDQEDQTL 477
Cdd:pfam01756 1 DPEVLLKA--FEWRA--ARLLREAAEKLQALLKsgkSQFEAWNNQSVELVRAAKAHAEYFVLRTFVERLSTSLDPPLKPV 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 218563752 478 LMKFCLLYGTKLVFQERAWYLEHKYLTPMASTRIRNQLLDLCDSVKDDARRVISTFNIPHTYLHAPI 544
Cdd:pfam01756 77 LKKLCKLYALWTIEKHLGDFLQGGYLSPEQIDLIREAILELLAELRPNAVALVDAFDFPDFILNSAL 143
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
38-311 |
2.17e-12 |
|
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: 69.01 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 38 VIGEVLSMADMATGVKCGIiYWLFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATfdLSAQEF 117
Cdd:cd01162 67 IIFEALSTGCVSTAAYISI-HNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAV--REGDHY 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 118 VIdtpceNAEKMYIGNAMYGNYAAVFAQLIIDGrSQGPHCFIVpvrdENGSlyPGVTAIDMMYKEGLHGVDNGILIFDKV 197
Cdd:cd01162 144 VL-----NGSKAFISGAGDSDVYVVMARTGGEG-PKGISCFVV----EKGT--PGLSFGANEKKMGWNAQPTRAVIFEDC 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 198 RIPRENLLdkfgsvAPDGQyhspirnksaRFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGPKTKEEvki 277
Cdd:cd01162 212 RVPVENRL------GGEGQ----------GFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADF--- 272
|
250 260 270
....*....|....*....|....*....|....*..
gi 218563752 278 iehqtQTLRL-MPHLATAL--ALTFVSRYAGALLDED 311
Cdd:cd01162 273 -----QALQFkLADMATELvaSRLMVRRAASALDRGD 304
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
59-327 |
2.46e-12 |
|
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: 68.96 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 59 WLFGGAIRNL---GSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVidtpceNAEKMYIGN-- 133
Cdd:cd01153 87 SGTQGAAATLlahGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSWRI------NGVKRFISAge 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 134 -AMYGNyaavfAQLIIDGRSQGP-------HCFIVPVRDENGSlYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPrenLL 205
Cdd:cd01153 161 hDMSEN-----IVHLVLARSEGAppgvkglSLFLVPKFLDDGE-RNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LI 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 206 dkfgsvapdGQYHSPIRnksarfnAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGP--KTKEEVKIIEHQTQ 283
Cdd:cd01153 232 ---------GEEGMGLA-------QMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDliKAAPAVTIIHHPDV 295
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 218563752 284 TLRLMPHLATALALTFVSRYAGALLDEDVFQGKELVNSRSLQAL 327
Cdd:cd01153 296 RRSLMTQKAYAEGSRALDLYTATVQDLAERKATEGEDRKALSAL 339
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
65-268 |
1.41e-11 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 66.44 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 65 IRNlGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEAtfDLSAQEFVIdtpceNAEKMYIGNAMYGNYAAVFA 144
Cdd:PLN02519 122 VRN-GTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKA--ERVDGGYVL-----NGNKMWCTNGPVAQTLVVYA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 145 QLIIDGRSQGPHCFIVpvrdENGslYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSvapdGQYhspirnk 224
Cdd:PLN02519 194 KTDVAAGSKGITAFII----EKG--MPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGK----GVY------- 256
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 218563752 225 sarfnAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFG 268
Cdd:PLN02519 257 -----VMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFG 295
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
63-352 |
2.55e-11 |
|
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: 65.86 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 63 GAIRNLGsPEHVTKWFQPLQEQKY-TGMFA---MTERGHGSNARGIQTEATFDLSaqefviDTPCENAEKMYIGNAMyGN 138
Cdd:cd01154 121 YALRKYG-PEELKQYLPGLLSDRYkTGLLGgtwMTEKQGGSDLGANETTAERSGG------GVYRLNGHKWFASAPL-AD 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 139 YAAVFAQLI-IDGRSQGPHCFIVPVRDENGSLypgvtaidmmykeglhgvdNGILIfdkvriprENLLDKFG--SVAP-- 213
Cdd:cd01154 193 AALVLARPEgAPAGARGLSLFLVPRLLEDGTR-------------------NGYRI--------RRLKDKLGtrSVATge 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 214 ---DGQYHSPIRNKSARFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGpKTkeevkIIEH---QTQTLRL 287
Cdd:cd01154 246 vefDDAEAYLIGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFG-KP-----LIDHplmRRDLAEM 319
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 218563752 288 MPHLATALALTFvsRYAGALldeDVFQGKELVNSRSLQALVAGLKAYSTWENIRCLQDCRECTGG 352
Cdd:cd01154 320 EVDVEAATALTF--RAARAF---DRAAADKPVEAHMARLATPVAKLIACKRAAPVTSEAMEVFGG 379
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
65-268 |
2.89e-11 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 65.64 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 65 IRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATfdLSAQEFVIdtpceNAEKMYIGNAMYGNYAAVFA 144
Cdd:PLN02526 121 IALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTAT--KVEGGWIL-----NGQKRWIGNSTFADVLVIFA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 145 QLIIDGRSQGphcFIVpvrdENGSlyPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLdkfgsvapdgqyhsPIRNK 224
Cdd:PLN02526 194 RNTTTNQING---FIV----KKGA--PGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRL--------------PGVNS 250
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 218563752 225 SARFNAMLAAltpSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFG 268
Cdd:PLN02526 251 FQDTNKVLAV---SRVMVAWQPIGISMGVYDMCHRYLKERKQFG 291
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
69-306 |
4.60e-10 |
|
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: 61.83 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 69 GSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEAtfDLSAQEFVIdtpceNAEKMYIGNAMYGNYAAVFAQLII 148
Cdd:cd01157 97 GNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYII-----NGQKMWITNGGKANWYFLLARSDP 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 149 DGR---SQGPHCFIVPvRDENGsLYPGVTAIDMmykeGLHGVDNGILIFDKVRIPRENLLDKFGsvapdgqyhspirnks 225
Cdd:cd01157 170 DPKcpaSKAFTGFIVE-ADTPG-IQPGRKELNM----GQRCSDTRGITFEDVRVPKENVLIGEG---------------- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 226 ARFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGpktkeeVKIIEHQTQTLrLMPHLATALALTFVSRYAG 305
Cdd:cd01157 228 AGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFG------KLIAEHQAVSF-MLADMAMKVELARLAYQRA 300
|
.
gi 218563752 306 A 306
Cdd:cd01157 301 A 301
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
60-268 |
2.70e-07 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 53.02 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 60 LFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDlSAQEFVIdtpceNAEKMYIGNAMYGNY 139
Cdd:PTZ00461 125 LFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKD-SNGNYVL-----NGSKIWITNGTVADV 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 140 AAVFAQliIDGRSQGphcFIVpvrdENGSlyPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSvapdgqyhs 219
Cdd:PTZ00461 199 FLIYAK--VDGKITA---FVV----ERGT--KGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGK--------- 258
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 218563752 220 pirnksaRFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFG 268
Cdd:PTZ00461 259 -------GMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFG 300
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
228-362 |
4.82e-06 |
|
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: 46.48 E-value: 4.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563752 228 FNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGpktkeeVKIIEHqtQTLRLMphLATALALTFVSRY---- 303
Cdd:pfam00441 4 FRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFG------RPLIDF--QLVRHK--LAEMAAEIEAARLlvyr 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 218563752 304 AGALLDEDVFQGKElvnsrslqalVAGLKAYSTWENIRCLQDCRECTGGMVVGRELLAQ 362
Cdd:pfam00441 74 AAEALDAGGPDGAE----------ASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVE 122
|
|
| |
