|
Name |
Accession |
Description |
Interval |
E-value |
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
2-544 |
5.73e-143 |
|
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: 426.36 E-value: 5.73e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 2 RALTVQRV--KFAMDLPLLKRAGQDLAEKTknfvsrsLVIGEVLSMADMATGVKCGIIYWLFGGAIRNLGSPEHVTKWFQ 79
Cdd:cd01150 55 REELYEELkrKAKTDVERMGELMADDPEKM-------LALTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 80 PLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVIDTPCENAEKMYIGN-AMYGNYAAVFAQLIIDGRSQGPHCF 158
Cdd:cd01150 128 GANNLEIIGCFAQTELGHGSNLQGLETTATYDPLTQEFVINTPDFTATKWWPGNlGKTATHAVVFAQLITPGKNHGLHAF 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 159 IVPVRDENG-SLYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSVAPDGQYHSPIRNKSARFNAMLAALTP 237
Cdd:cd01150 208 IVPIRDPKThQPLPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDPNKRYGAMLGTRSG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 238 SRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGPKTKE-EVKIIEHQTQTLRLMPHLATALALTFVSRY-------AGALLD 309
Cdd:cd01150 288 GRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPKPSDpEVQILDYQLQQYRLFPQLAAAYAFHFAAKSlvemyheIIKELL 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 310 EDVFQgkelvNSRSLQALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQVVGREL 389
Cdd:cd01150 368 QGNSE-----LLAELHALSAGLKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYL 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 390 LAQYTKQYEekplfgllqnwaesvgdklrtsflafnmdtvddLAFLLKAVKFRERVLQRGLVARIYYKVKTKKEDfFHAW 469
Cdd:cd01150 443 LKKYAQAFS---------------------------------LADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGS-FEAR 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767918701 470 NSCLHHVASLSLAHTHRVTLEQFSLAVKSCPDQEDQTLLMKFCLLYGTKLVFQERAWYLEHKYLTPMASTRIRNQ 544
Cdd:cd01150 489 NNSQVHLRCAAKAHTEYTVLQRFHESVEEIVDPSVRAVLKRLCDLYALWLLEEHIADFLEGGFLGGQDVKAVREA 563
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
34-535 |
6.25e-119 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 366.88 E-value: 6.25e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 34 SRSLVIGEVLSMADMATGVKCGIIYWLFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDLS 113
Cdd:PLN02636 121 AKYFAITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 114 AQEFVIDTPCENAEKMYIGNA-MYGNYAAVFAQLIIDG------RSQGPHCFIVPVRD-ENGSLYPGVTAIDMMYKEGLH 185
Cdd:PLN02636 201 TDEFVINTPNDGAIKWWIGNAaVHGKFATVFARLKLPThdskgvSDMGVHAFIVPIRDmKTHQVLPGVEIRDCGHKVGLN 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 186 GVDNGILIFDKVRIPRENLLDKFGSVAPDGQYHSPIRNKSARFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRR 265
Cdd:PLN02636 281 GVDNGALRFRSVRIPRDNLLNRFGDVSRDGKYTSSLPTINKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQ 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 266 QFGPKTKEEVKIIEHQTQTLRLMPHLATALALTFVSRYAGALLDE-DVFQGKELVNsrSLQALVAGLKAYSTWENIRCLQ 344
Cdd:PLN02636 361 QFGPPKQPEISILDYQSQQHKLMPMLASTYAFHFATEYLVERYSEmKKTHDDQLVA--DVHALSAGLKAYITSYTAKALS 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 345 DCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQVVGRELLAQYTKQYEEKPLFGLLQNWAESVGDKL-RTSFLA 423
Cdd:PLN02636 439 TCREACGGHGYAAVNRFGSLRNDHDIFQTFEGDNTVLLQQVAADLLKQYKEKFQGGTLSVTWNYLRESMNTYLsQPNPVT 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 424 FNMDTVD---DLAFLLKAVKFR-ERVLQRglvARIYYKVKTKKEDFFHAWNSCLHHVASLSLAHTHRVTLEQFSLAVKSC 499
Cdd:PLN02636 519 TRWEGEEhlrDPKFQLDAFRYRtSRLLQT---AALRLRKHSKTLGSFGAWNRCLNHLLTLAESHIESVILAKFIEAVERC 595
|
490 500 510
....*....|....*....|....*....|....*.
gi 767918701 500 PDQEDQTLLMKFCLLYGTKLVFQERAWYLEHKYLTP 535
Cdd:PLN02636 596 PDRSTRAALKLVCDLYALDRIWKDIGTYRNVDYVAP 631
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
2-546 |
1.87e-113 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 352.54 E-value: 1.87e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 2 RALTVQRVKFamdlpLLKRAGQD--LAEKTKNFVSRSLVIGEVLSMADMATGVKCGIIYWLFGGAIRNLGSPEHVTKWFQ 79
Cdd:PLN02312 104 REITMKRILY-----LLERGVFRgwLTETGPEAELRKLALLEVIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHDKWLK 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 80 PLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVIDTPCENAEKMYIGNA-MYGNYAAVFAQLIIDGRSQGPHCF 158
Cdd:PLN02312 179 DTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFVINTPCESAQKYWIGGAaNHATHTIVFSQLHINGKNEGVHAF 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 159 IVPVRDENGSLYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSVAPDGQYHSPIRNKSARFNAMLAALTPS 238
Cdd:PLN02312 259 IAQIRDQDGNICPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNSVADVSPDGKYVSAIKDPDQRFGAFLAPLTSG 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 239 RLAVAFQAMGAMKLGLTIAIRYSHSRRQF-----GPktkeEVKIIEHQTQTLRLMPHLATALALTFVSRYAgalldEDVF 313
Cdd:PLN02312 339 RVTIAVSAIYSSKVGLAIAIRYSLSRRAFsvtpnGP----EVLLLDYPSHQRRLLPLLAKTYAMSFAANDL-----KMIY 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 314 QGKELVNSRSLQALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQVVGRELLAQY 393
Cdd:PLN02312 410 VKRTPESNKAIHVVSSGFKAVLTWHNMRTLQECREACGGQGLKTENRVGQLKAEYDVQSTFEGDNNVLMQQVSKALLAEY 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 394 -TKQYEEKPLFGL----LQNWAESVGDKLRTSflafnmdTVDDLAFLLKAVKFRErvlqRGLVARIYYKVKT---KKEDF 465
Cdd:PLN02312 490 vSAKKRNKPFKGLglehMNGPRPVIPTQLTSS-------TLRDSQFQLNLFCLRE----RDLLERFASEVSElqsKGESR 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 466 FHAWNSCLHHVASLSLAHTHRVTLEQFSLAVKSCPDQEDQTLLMKFCLLYgTKLVFQERAWYLEHKYLTPMASTRIRNQA 545
Cdd:PLN02312 559 EFAFLLSYQLAEDLGRAFSERAILQTFLDAEANLPTGSLKDVLGLLRSLY-VLISLDEDPSFLRYGYLSPDNVALVRKEV 637
|
.
gi 767918701 546 A 546
Cdd:PLN02312 638 A 638
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
64-437 |
1.74e-60 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 211.63 E-value: 1.74e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 64 AIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVIDTPCENAEKMYIGN-AMYGNYAAV 142
Cdd:PTZ00460 105 AFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHTPSVEAVKFWPGElGFLCNFALV 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 143 FAQLIIDGRSQGPHCFIVPVRDENG-SLYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSVAPDGQYhspI 221
Cdd:PTZ00460 185 YAKLIVNGKNKGVHPFMVRIRDKEThKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLARYIKVSEDGQV---E 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 222 R--NKSARFNAMLAaltpSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGPKTKEEVKIIEHQTQTLRLMPHLATALALTF 299
Cdd:PTZ00460 262 RqgNPKVSYASMMY----MRNLIIDQYPRFAAQALTVAIRYSIYRQQFTNDNKQENSVLEYQTQQQKLLPLLAEFYACIF 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 300 VSRYAGALLDEDV--FQGKELVNSRSLQALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGD 377
Cdd:PTZ00460 338 GGLKIKELVDDNFnrVQKNDFSLLQLTHAILSAAKANYTYFVSNCAEWCRLSCGGHGYAHYSGLPAIYFDMSPNITLEGE 417
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767918701 378 DVVMLQVVGRELLAQYtKQYEEKP-----LFGLLQNWAESVGDKlrtsflafnmDTVDDLAFLLK 437
Cdd:PTZ00460 418 NQIMYLQLARYLLKQL-QHAVQKPekvpeYFNFLSHITEKLADQ----------TTIESLGQLLG 471
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
37-393 |
8.65e-58 |
|
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: 197.76 E-value: 8.65e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 37 LVIGEVLSMADMATGVKCGIiYWLFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDlsAQE 116
Cdd:COG1960 70 ALVLEELARADASLALPVGV-HNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRD--GDG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 117 FVIdtpceNAEKMYIGNAMYGNYAAVFAQLIIDGRSQGPHCFIVPvRDEngslyPGVTAIDMMYKEGLHGVDNGILIFDK 196
Cdd:COG1960 147 YVL-----NGQKTFITNAPVADVILVLARTDPAAGHRGISLFLVP-KDT-----PGVTVGRIEDKMGLRGSDTGELFFDD 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 197 VRIPRENLLDKFGsvapdgqyhspirnksARFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGpktkeeVK 276
Cdd:COG1960 216 VRVPAENLLGEEG----------------KGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFG------RP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 277 IIEHQTQTLRLMPHLATALALTFVSRYAGALLDEDvfqgkelvnsRSLQALVAGLKAYSTWENIRCLQDCRECTGGMGYM 356
Cdd:COG1960 274 IADFQAVQHRLADMAAELEAARALVYRAAWLLDAG----------EDAALEAAMAKLFATEAALEVADEALQIHGGYGYT 343
|
330 340 350
....*....|....*....|....*....|....*..
gi 767918701 357 MENRISGLKCDTDVFATFEGDDVVMLQVVGRELLAQY 393
Cdd:COG1960 344 REYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRP 380
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
57-390 |
2.68e-56 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 200.45 E-value: 2.68e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 57 IYW-LFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVIDTPCENAEKMYIGN-A 134
Cdd:PLN02443 101 LHWgMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFVIHSPTLTSSKWWPGGlG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 135 MYGNYAAVFAQLIIDGRSQGPHCFIVPVRD-ENGSLYPGVTAIDMMYKEGLHG---VDNGILIFDKVRIPRENLLDKFGS 210
Cdd:PLN02443 181 KVSTHAVVYARLITNGKDHGIHGFIVQLRSlDDHSPLPGVTVGDIGMKFGNGAyntMDNGFLRFDHVRIPRDQMLMRLSK 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 211 VAPDGQYHSPIRNKSARFNAMLAAltpsRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGPKTKE-EVKIIEHQTQTLRLMP 289
Cdd:PLN02443 261 VTREGKYVQSDVPRQLVYGTMVYV----RQTIVADASTALSRAVCIATRYSAVRRQFGSQDGGpETQVIDYKTQQSRLFP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 290 HLATALALTFVSRYAGALLdEDVFQGKELVNSRSLQ---ALVAGLKAYSTWENIRCLQDCRECTGGMGYMMEnriSGLKc 366
Cdd:PLN02443 337 LLASAYAFRFVGEWLKWLY-TDVTQRLEANDFSTLPeahACTAGLKSLTTSATADGIEECRKLCGGHGYLCS---SGLP- 411
|
330 340 350
....*....|....*....|....*....|
gi 767918701 367 dtDVFA------TFEGDDVVMLQVVGRELL 390
Cdd:PLN02443 412 --ELFAvyvpacTYEGDNVVLLLQVARFLM 439
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
58-387 |
1.01e-43 |
|
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. In contrast, AXO catalyzes a different oxidative half-reaction, in which the reduced FAD is reoxidized by molecular oxygen. The ACAD family includes the eukaryotic beta-oxidation enzymes, short (SCAD), medium (MCAD), long (LCAD) and very-long (VLCAD) chain acyl-CoA dehydrogenases. These enzymes all share high sequence similarity, but differ in their substrate specificities. The ACAD family also includes amino acid catabolism enzymes such as Isovaleryl-CoA dehydrogenase (IVD), short/branched chain acyl-CoA dehydrogenases(SBCAD), Isobutyryl-CoA dehydrogenase (IBDH), glutaryl-CoA deydrogenase (GCD) and Crotonobetainyl-CoA dehydrogenase. The mitochondrial ACAD's are generally homotetramers, except for VLCAD, which is a homodimer. Related enzymes include the SOS adaptive reponse proten aidB, Naphthocyclinone hydroxylase (NcnH), and and Dibenzothiophene (DBT) desulfurization enzyme C (DszC)
Pssm-ID: 173838 [Multi-domain] Cd Length: 327 Bit Score: 158.22 E-value: 1.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 58 YWLFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDlsAQEFVIdtpceNAEKMYIGNAMYG 137
Cdd:cd00567 41 LLLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKD--GDGYVL-----NGRKIFISNGGDA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 138 NYAAVFAQLIIDG-RSQGPHCFIVPvRDEngslyPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSVapdgq 216
Cdd:cd00567 114 DLFIVLARTDEEGpGHRGISAFLVP-ADT-----PGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGG----- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 217 yhspirnksarFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGpktkeeVKIIEHQTQTLRLMPHLATALA 296
Cdd:cd00567 183 -----------FELAMKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQFG------KPLAEFQAVQFKLADMAAELEA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 297 LTFVSRYAGALLDEDvfqgkelvnSRSLQALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEG 376
Cdd:cd00567 246 ARLLLYRAAWLLDQG---------PDEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEG 316
|
330
....*....|.
gi 767918701 377 DDVVMLQVVGR 387
Cdd:cd00567 317 TAEIQRLIIAR 327
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
31-391 |
1.45e-29 |
|
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: 120.07 E-value: 1.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 31 NFVSRSLVIGEvLSMADMATGVKCGIIYWLFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATF 110
Cdd:cd01158 59 DFLAYAIAIEE-LAKVDASVAVIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 111 DlsAQEFVIdtpceNAEKMYIGNAMYGNYAAVFAQLIIDGRSQGPHCFIVPvRDEngslyPGVTAIDMMYKEGLHGVDNG 190
Cdd:cd01158 138 D--GDDYVL-----NGSKMWITNGGEADFYIVFAVTDPSKGYRGITAFIVE-RDT-----PGLSVGKKEDKLGIRGSSTT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 191 ILIFDKVRIPRENLLDKFGsvapDGqyhspirnksarFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGpK 270
Cdd:cd01158 205 ELIFEDVRVPKENILGEEG----EG------------FKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFG-K 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 271 TKEEVKIIEHQTQTLRLMphLATALALTFVsryAGALLDedvfQGKELVNSRSLQALVAGLKAystwenIRCLQDCRECT 350
Cdd:cd01158 268 PIADFQGIQFKLADMATE--IEAARLLTYK---AARLKD----NGEPFIKEAAMAKLFASEVA------MRVTTDAVQIF 332
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 767918701 351 GGMGYMMENRISGLKCDTDVFATFEGDDVVMLQVVGRELLA 391
Cdd:cd01158 333 GGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
65-390 |
2.79e-27 |
|
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: 113.36 E-value: 2.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 65 IRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDlsAQEFVIdtpceNAEKMYIGNAMYGNYAAVFA 144
Cdd:cd01160 91 ITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKD--GDHYVL-----NGSKTFITNGMLADVVIVVA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 145 QLIIDGRSQ-GPHCFIVpvrdENGSlyPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLdkfgsvapdGQyhspiRN 223
Cdd:cd01160 164 RTGGEARGAgGISLFLV----ERGT--PGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLL---------GE-----EN 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 224 KSarFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGpKTKEEVKIIEHQtqtlrlMPHLATALAltfVSRy 303
Cdd:cd01160 224 KG--FYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFG-KTLAQLQVVRHK------IAELATKVA---VTR- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 304 agALLDEDVfqgKELVNSRSLQALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQ 383
Cdd:cd01160 291 --AFLDNCA---WRHEQGRLDVAEASMAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKE 365
|
....*..
gi 767918701 384 VVGRELL 390
Cdd:cd01160 366 LISRQMV 372
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
63-388 |
1.52e-22 |
|
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: 99.74 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 63 GAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDlsAQEFVIdtpceNAEKMYIGNAMYGNYAAV 142
Cdd:cd01151 103 LPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKD--GGGYKL-----NGSKTWITNSPIADVFVV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 143 FAQLIIDGRSQGphcFIVPvRDengslYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLdkfgsvapdgqyhspir 222
Cdd:cd01151 176 WARNDETGKIRG---FILE-RG-----MKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL----------------- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 223 NKSARFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFG-PKTKEEV---KIIEHQTQTlrlmpHLATALALT 298
Cdd:cd01151 230 PGAEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGrPLAAFQLvqkKLADMLTEI-----ALGLLACLR 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 299 fVSRyagaLLDedvfQGKELVNSRSLqalvagLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDD 378
Cdd:cd01151 305 -VGR----LKD----QGKATPEQISL------LKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTH 369
|
330
....*....|
gi 767918701 379 VVMLQVVGRE 388
Cdd:cd01151 370 DIHALILGRA 379
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
25-376 |
2.34e-21 |
|
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: 96.38 E-value: 2.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 25 LAEKtknfVSRSLVIGEVLSmADMATGVKcGIIYWlfggairnlGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGI 104
Cdd:cd01161 92 LAEI----VGMDLGFSVTLG-AHQSIGFK-GILLF---------GTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 105 QTEATFDLSAQEFVIdtpceNAEKMYIGNAMYGNYAAVFAQliidgrsqgphcfiVPVRDENGSLYPGVTAidMMYKEGL 184
Cdd:cd01161 157 RTTAVLSEDGKHYVL-----NGSKIWITNGGIADIFTVFAK--------------TEVKDATGSVKDKITA--FIVERSF 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 185 HGVDNGI--------------LIFDKVRIPRENLLDKFGsvapDGqyhspirnksarFNAMLAALTPSRLAVAFQAMGAM 250
Cdd:cd01161 216 GGVTNGPpekkmgikgsntaeVYFEDVKIPVENVLGEVG----DG------------FKVAMNILNNGRFGMGAALIGTM 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 251 KLGLTIAIRYSHSRRQFGPKTKEEVKIIEHqtqtlrlmphLATALALTFVSR----YAGALLDedvfqgKELVNSRSLQA 326
Cdd:cd01161 280 KRCIEKAVDYANNRKQFGKKIHEFGLIQEK----------LANMAILQYATEsmayMTSGNMD------RGLKAEYQIEA 343
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 767918701 327 LVAglKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEG 376
Cdd:cd01161 344 AIS--KVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEG 391
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
66-391 |
1.40e-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: 87.85 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 66 RNlGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDlsAQEFVIdtpceNAEKMYIGNAMYGNYAAVFAQ 145
Cdd:cd01156 97 RN-GSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKK--GDRYVL-----NGSKMWITNGPDADTLVVYAK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 146 LIIDGRSQGPHCFIVpvrdENGslYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSvapdGQYhspirnks 225
Cdd:cd01156 169 TDPSAGAHGITAFIV----EKG--MPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENK----GVY-------- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 226 arfnAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGPKTKeEVKIIEHQtqtlrlMPHLATAL--ALTFVSRY 303
Cdd:cd01156 231 ----VLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIG-EFQLVQGK------LADMYTRLnaSRSYLYTV 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 304 AGAlLDEDVFQGKElvnsrslqalVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQ 383
Cdd:cd01156 300 AKA-CDRGNMDPKD----------AAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRM 368
|
....*...
gi 767918701 384 VVGRELLA 391
Cdd:cd01156 369 VIGRELFK 376
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
38-392 |
3.11e-17 |
|
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: 83.65 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 38 VIGEVLSMADMATGVKCGIiYWLFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATfdLSAQEF 117
Cdd:cd01162 67 IIFEALSTGCVSTAAYISI-HNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAV--REGDHY 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 118 VIdtpceNAEKMYIGNAMYGNYAAVFAQLIIDGrSQGPHCFIVpvrdENGSlyPGVTAIDMMYKEGLHGVDNGILIFDKV 197
Cdd:cd01162 144 VL-----NGSKAFISGAGDSDVYVVMARTGGEG-PKGISCFVV----EKGT--PGLSFGANEKKMGWNAQPTRAVIFEDC 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 198 RIPRENLLdkfgsvAPDGQyhspirnksaRFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGPKTKEEvki 277
Cdd:cd01162 212 RVPVENRL------GGEGQ----------GFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADF--- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 278 iehqtQTLRL-MPHLATAL--ALTFVSRYAGALLDEDvfqgKELVnsrslqALVAGLKAYSTwenIRCLQDCRECT---G 351
Cdd:cd01162 273 -----QALQFkLADMATELvaSRLMVRRAASALDRGD----PDAV------KLCAMAKRFAT---DECFDVANQALqlhG 334
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 767918701 352 GMGYMMENRISGLKCDTDVFATFEGDDVVMLQVVGRELLAQ 392
Cdd:cd01162 335 GYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
90-195 |
8.69e-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: 8.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 90 FAMTERGHGSNARGIQTEAtFDLSAQEFVIdtpceNAEKMYIGNAMYGNYAAVFAQLIIDGRSQGPHCFIVPVRDengsl 169
Cdd:pfam02770 2 FALTEPGAGSDVASLKTTA-ADGDGGGWVL-----NGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDA----- 70
|
90 100
....*....|....*....|....*.
gi 767918701 170 yPGVTAIDMMYKEGLHGVDNGILIFD 195
Cdd:pfam02770 71 -PGVSVRRIETKLGVRGLPTGELVFD 95
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
59-376 |
4.19e-15 |
|
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: 77.43 E-value: 4.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 59 WLFGGAIRNL---GSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVidtpceNAEKMYIGN-- 133
Cdd:cd01153 87 SGTQGAAATLlahGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSWRI------NGVKRFISAge 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 134 -AMYGNyaavfAQLIIDGRSQGP-------HCFIVPVRDENGSlYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPrenLL 205
Cdd:cd01153 161 hDMSEN-----IVHLVLARSEGAppgvkglSLFLVPKFLDDGE-RNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LI 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 206 dkfgsvapdGQYHSPIRnksarfnAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGP--KTKEEVKIIEHQTQ 283
Cdd:cd01153 232 ---------GEEGMGLA-------QMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDliKAAPAVTIIHHPDV 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 284 TLRLMPHLATALALTFVSRYAGALLDEDVFQGKELVNSRSLQALVAGL----KAYSTWENIRCLQDCRECTGGMGYMMEN 359
Cdd:cd01153 296 RRSLMTQKAYAEGSRALDLYTATVQDLAERKATEGEDRKALSALADLLtpvvKGFGSEAALEAVSDAIQVHGGSGYTREY 375
|
330
....*....|....*..
gi 767918701 360 RISGLKCDTDVFATFEG 376
Cdd:cd01153 376 PIEQYYRDARITTIYEG 392
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
63-387 |
1.00e-14 |
|
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: 76.26 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 63 GAIRNLGsPEHVTKWFQPLQEQKY-TGMFA---MTERGHGSNARGIQTEATFDLSaqefviDTPCENAEKMYIGNAMyGN 138
Cdd:cd01154 121 YALRKYG-PEELKQYLPGLLSDRYkTGLLGgtwMTEKQGGSDLGANETTAERSGG------GVYRLNGHKWFASAPL-AD 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 139 YAAVFAQLI-IDGRSQGPHCFIVPVRDENGSLypgvtaidmmykeglhgvdNGILIfdkvriprENLLDKFG--SVAP-- 213
Cdd:cd01154 193 AALVLARPEgAPAGARGLSLFLVPRLLEDGTR-------------------NGYRI--------RRLKDKLGtrSVATge 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 214 ---DGQYHSPIRNKSARFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGpKTkeevkIIEH---QTQTLRL 287
Cdd:cd01154 246 vefDDAEAYLIGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFG-KP-----LIDHplmRRDLAEM 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 288 MPHLATALALTFvsRYAGALldeDVFQGKELVNSRSLQALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCD 367
Cdd:cd01154 320 EVDVEAATALTF--RAARAF---DRAAADKPVEAHMARLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHRE 394
|
330 340
....*....|....*....|....
gi 767918701 368 TDVFATFEGDDVV----MLQVVGR 387
Cdd:cd01154 395 AQVTPIWEGTGNIqaldVLRVLVK 418
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
69-390 |
1.05e-13 |
|
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: 73.00 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 69 GSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEAtfDLSAQEFVIdtpceNAEKMYIGNAMYGNYAAVFAQLII 148
Cdd:cd01157 97 GNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYII-----NGQKMWITNGGKANWYFLLARSDP 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 149 DGR---SQGPHCFIVPvRDENGsLYPGVTAIDMmykeGLHGVDNGILIFDKVRIPRENLLDKFGsvapdgqyhspirnks 225
Cdd:cd01157 170 DPKcpaSKAFTGFIVE-ADTPG-IQPGRKELNM----GQRCSDTRGITFEDVRVPKENVLIGEG---------------- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 226 ARFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGpktkeeVKIIEHQTQTLrLMPHLATALALTFVSRYAG 305
Cdd:cd01157 228 AGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFG------KLIAEHQAVSF-MLADMAMKVELARLAYQRA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 306 AlldEDVFQGKElvnsRSLQALVAglKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQVV 385
Cdd:cd01157 301 A---WEVDSGRR----NTYYASIA--KAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLII 371
|
....*
gi 767918701 386 GRELL 390
Cdd:cd01157 372 SREHL 376
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
65-389 |
4.25e-13 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 71.42 E-value: 4.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 65 IRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATfdLSAQEFVIdtpceNAEKMYIGNAMYGNYAAVFA 144
Cdd:PLN02526 121 IALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTAT--KVEGGWIL-----NGQKRWIGNSTFADVLVIFA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 145 QLIIDGRSQGphcFIVpvrdENGSlyPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLdkfgsvapdgqyhsPIRNK 224
Cdd:PLN02526 194 RNTTTNQING---FIV----KKGA--PGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRL--------------PGVNS 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 225 SARFNAMLAAltpSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGpktkeeVKIIEHQTQTLRLMPHLATALALTFVSRYA 304
Cdd:PLN02526 251 FQDTNKVLAV---SRVMVAWQPIGISMGVYDMCHRYLKERKQFG------APLAAFQINQEKLVRMLGNIQAMFLVGWRL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 305 GALLDedvfQGKELVNSRSLQalvaglKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQV 384
Cdd:PLN02526 322 CKLYE----SGKMTPGHASLG------KAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALV 391
|
....*
gi 767918701 385 VGREL 389
Cdd:PLN02526 392 TGREI 396
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
228-389 |
7.53e-12 |
|
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: 63.43 E-value: 7.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 228 FNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGpktkeeVKIIEHqtQTLRLMphLATALALTFVSRY---- 303
Cdd:pfam00441 4 FRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFG------RPLIDF--QLVRHK--LAEMAAEIEAARLlvyr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 304 AGALLDEDVFQGKElvnsrslqalVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQ 383
Cdd:pfam00441 74 AAEALDAGGPDGAE----------ASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRN 143
|
....*.
gi 767918701 384 VVGREL 389
Cdd:pfam00441 144 IIARRL 149
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
65-392 |
9.10e-12 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 67.21 E-value: 9.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 65 IRNlGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEAtfDLSAQEFVIdtpceNAEKMYIGNAMYGNYAAVFA 144
Cdd:PLN02519 122 VRN-GTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKA--ERVDGGYVL-----NGNKMWCTNGPVAQTLVVYA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 145 QLIIDGRSQGPHCFIVpvrdENGslYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSvapdGQYhspirnk 224
Cdd:PLN02519 194 KTDVAAGSKGITAFII----EKG--MPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGK----GVY------- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 225 sarfnAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGpKTKEEVKIIehQTQTLRLMPHLATALALTF-VSRY 303
Cdd:PLN02519 257 -----VMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFG-RPIGEFQFI--QGKLADMYTSLQSSRSYVYsVARD 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 304 AgallDEDVFQGKElvnsrslqalVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQ 383
Cdd:PLN02519 329 C----DNGKVDRKD----------CAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRM 394
|
....*....
gi 767918701 384 VVGRELLAQ 392
Cdd:PLN02519 395 LIGRELFKE 403
|
|
| ACOX |
pfam01756 |
Acyl-CoA oxidase; This is a family of Acyl-CoA oxidases EC:1.3.3.6. Acyl-coA oxidase converts ... |
431-544 |
3.92e-09 |
|
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: 56.40 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 431 DLAFLLKAvkFRERVlqRGLVARIYYKVKTKKE---DFFHAWNSCLHHVASLSLAHTHRVTLEQFSLAVKSCPDQEDQTL 507
Cdd:pfam01756 1 DPEVLLKA--FEWRA--ARLLREAAEKLQALLKsgkSQFEAWNNQSVELVRAAKAHAEYFVLRTFVERLSTSLDPPLKPV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 767918701 508 LMKFCLLYGTKLVFQERAWYLEHKYLTPMASTRIRNQ 544
Cdd:pfam01756 77 LKKLCKLYALWTIEKHLGDFLQGGYLSPEQIDLIREA 113
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
53-393 |
4.83e-08 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 55.12 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 53 KCGIIYWLFGGA-----IRNLGSPEHVTKWFQplqEQKYTG----MFAMTERGHGSNARGIQTEATFDlSAQEFVidtpc 123
Cdd:PRK12341 79 KCGAPAFLITNGqcihsMRRFGSAEQLRKTAE---STLETGdpayALALTEPGAGSDNNSATTTYTRK-NGKVYL----- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 124 eNAEKMYIGNAMYGNYAAVFAQliiDGRSQGPH-CF---IVPVRDengslyPGVTaIDMMYKEGLHGVDNGILIFDKVRI 199
Cdd:PRK12341 150 -NGQKTFITGAKEYPYMLVLAR---DPQPKDPKkAFtlwWVDSSK------PGIK-INPLHKIGWHMLSTCEVYLDNVEV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 200 PRENLLDKFGsvapDGqyhspirnksarFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGPKTKEEVKIIE 279
Cdd:PRK12341 219 EESDLVGEEG----MG------------FLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQE 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 280 HQT------QTLRLMphlatalaltfvsRYAGALldedvfqgkELVNSRSLQALVAGLKAYSTWENIRCLQDCRECTGGM 353
Cdd:PRK12341 283 KLTlmaikiENMRNM-------------VYKVAW---------QADNGQSLRTSAALAKLYCARTAMEVIDDAIQIMGGL 340
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 767918701 354 GYMMENRISGLKCDTDVFATFEGDDVVMLQVVGRELLAQY 393
Cdd:PRK12341 341 GYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKDY 380
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
60-268 |
3.27e-07 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 52.63 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 60 LFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDlSAQEFVIdtpceNAEKMYIGNAMYGNY 139
Cdd:PTZ00461 125 LFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKD-SNGNYVL-----NGSKIWITNGTVADV 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918701 140 AAVFAQliIDGRSQGphcFIVpvrdENGSlyPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSvapdgqyhs 219
Cdd:PTZ00461 199 FLIYAK--VDGKITA---FVV----ERGT--KGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGK--------- 258
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767918701 220 pirnksaRFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFG 268
Cdd:PTZ00461 259 -------GMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFG 300
|
|
| |
