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Conserved domains on  [gi|767918697|ref|XP_011509713|]
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acyl-coenzyme A oxidase-like protein isoform X4 [Homo sapiens]

Protein Classification

acyl-CoA dehydrogenase family protein( domain architecture ID 550)

acyl-CoA dehydrogenase (ACAD) family protein similar to acyl-CoA dehydrogenase that catalyzes the alpha,beta dehydrogenation of an acyl-CoA to form 2,3-dehydroacyl-CoA; requires an acceptor such as FAD, which becomes reduced

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ACAD super family cl09933
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 2-536 9.93e-131

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)


The actual alignment was detected with superfamily member cd01150:

Pssm-ID: 447864 [Multi-domain]  Cd Length: 610  Bit Score: 395.16  E-value: 9.93e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697   2 RALTVQRV--KFAMDLPLLKRAGQDLAEKTknfvsrsLVIGEVLSMADMATGVKCGIIYWLFGGAIRNLGSPEHVTKWFQ 79
Cdd:cd01150   55 REELYEELkrKAKTDVERMGELMADDPEKM-------LALTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQ 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697  80 PLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVIDTPCENAEKMYIGN-AMYGNYAAVFAQLIIDGRSQGPHCF 158
Cdd:cd01150  128 GANNLEIIGCFAQTELGHGSNLQGLETTATYDPLTQEFVINTPDFTATKWWPGNlGKTATHAVVFAQLITPGKNHGLHAF 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 159 IVPVRDENG-SLYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSVAPDGQYHSPIRNKSARFNAMLAALTP 237
Cdd:cd01150  208 IVPIRDPKThQPLPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDPNKRYGAMLGTRSG 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 238 SRLAVAFQAMGAMKLGLTIAIRYS--HRYAG--------ALLDEDVFQ----------------GKELVN---------- 281
Cdd:cd01150  288 GRVGLIYDAAMSLKKAATIAIRYSavRRQFGpkpsdpevQILDYQLQQyrlfpqlaaayafhfaAKSLVEmyheiikell 367

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 282 ------SRSLQALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQVVGRELLAQYT 355
Cdd:cd01150  368 qgnselLAELHALSAGLKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYA 447

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 356 KQYEekplfgllqnwaesvgdklrtsflafnmdtvddLAFLLKAVKFRERVLQRGLVARIYYKVKTKKEDfFHAWNSCLH 435
Cdd:cd01150  448 QAFS---------------------------------LADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGS-FEARNNSQV 493

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 436 HVASLSLAHTHRVTLEQFSLAVKSCPDQEDQTLLMKFCLLYGTKLVFQERAWYLEHKYLTPMASTRIRNQLLDLCDSVKD 515
Cdd:cd01150  494 HLRCAAKAHTEYTVLQRFHESVEEIVDPSVRAVLKRLCDLYALWLLEEHIADFLEGGFLGGQDVKAVREALLALLPQLRP 573

                        570       580
                 ....*....|....*....|.
gi 767918697 516 DARRVISTFNIPHTYLHAPIA 536
Cdd:cd01150  574 DAVALVDAFDLPDFVLNSPIG 594
 
Name Accession Description Interval E-value
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 2-536 9.93e-131

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: 395.16  E-value: 9.93e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697   2 RALTVQRV--KFAMDLPLLKRAGQDLAEKTknfvsrsLVIGEVLSMADMATGVKCGIIYWLFGGAIRNLGSPEHVTKWFQ 79
Cdd:cd01150   55 REELYEELkrKAKTDVERMGELMADDPEKM-------LALTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQ 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697  80 PLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVIDTPCENAEKMYIGN-AMYGNYAAVFAQLIIDGRSQGPHCF 158
Cdd:cd01150  128 GANNLEIIGCFAQTELGHGSNLQGLETTATYDPLTQEFVINTPDFTATKWWPGNlGKTATHAVVFAQLITPGKNHGLHAF 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 159 IVPVRDENG-SLYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSVAPDGQYHSPIRNKSARFNAMLAALTP 237
Cdd:cd01150  208 IVPIRDPKThQPLPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDPNKRYGAMLGTRSG 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 238 SRLAVAFQAMGAMKLGLTIAIRYS--HRYAG--------ALLDEDVFQ----------------GKELVN---------- 281
Cdd:cd01150  288 GRVGLIYDAAMSLKKAATIAIRYSavRRQFGpkpsdpevQILDYQLQQyrlfpqlaaayafhfaAKSLVEmyheiikell 367

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 282 ------SRSLQALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQVVGRELLAQYT 355
Cdd:cd01150  368 qgnselLAELHALSAGLKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYA 447

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 356 KQYEekplfgllqnwaesvgdklrtsflafnmdtvddLAFLLKAVKFRERVLQRGLVARIYYKVKTKKEDfFHAWNSCLH 435
Cdd:cd01150  448 QAFS---------------------------------LADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGS-FEARNNSQV 493

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 436 HVASLSLAHTHRVTLEQFSLAVKSCPDQEDQTLLMKFCLLYGTKLVFQERAWYLEHKYLTPMASTRIRNQLLDLCDSVKD 515
Cdd:cd01150  494 HLRCAAKAHTEYTVLQRFHESVEEIVDPSVRAVLKRLCDLYALWLLEEHIADFLEGGFLGGQDVKAVREALLALLPQLRP 573

                        570       580
                 ....*....|....*....|.
gi 767918697 516 DARRVISTFNIPHTYLHAPIA 536
Cdd:cd01150  574 DAVALVDAFDLPDFVLNSPIG 594
PLN02312 PLN02312
acyl-CoA oxidase
 2-536 1.51e-109

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 342.52  E-value: 1.51e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697   2 RALTVQRVKFamdlpLLKRAGQD--LAEKTKNFVSRSLVIGEVLSMADMATGVKCGIIYWLFGGAIRNLGSPEHVTKWFQ 79
Cdd:PLN02312 104 REITMKRILY-----LLERGVFRgwLTETGPEAELRKLALLEVIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHDKWLK 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697  80 PLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVIDTPCENAEKMYIGNA-MYGNYAAVFAQLIIDGRSQGPHCF 158
Cdd:PLN02312 179 DTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFVINTPCESAQKYWIGGAaNHATHTIVFSQLHINGKNEGVHAF 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 159 IVPVRDENGSLYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSVAPDGQYHSPIRNKSARFNAMLAALTPS 238
Cdd:PLN02312 259 IAQIRDQDGNICPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNSVADVSPDGKYVSAIKDPDQRFGAFLAPLTSG 338

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 239 RLAVAFQAMGAMKLGLTIAIRYS-HRYAGA---------LLDEDVFQGKEL--------------------VN-----SR 283
Cdd:PLN02312 339 RVTIAVSAIYSSKVGLAIAIRYSlSRRAFSvtpngpevlLLDYPSHQRRLLpllaktyamsfaandlkmiyVKrtpesNK 418

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 284 SLQALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQVVGRELLAQY-TKQYEEKP 362
Cdd:PLN02312 419 AIHVVSSGFKAVLTWHNMRTLQECREACGGQGLKTENRVGQLKAEYDVQSTFEGDNNVLMQQVSKALLAEYvSAKKRNKP 498

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 363 LFGL----LQNWAESVGDKLRTSflafnmdTVDDLAFLLKAVKFRErvlqRGLVARIYYKVKT---KKEDFFHAWNSCLH 435
Cdd:PLN02312 499 FKGLglehMNGPRPVIPTQLTSS-------TLRDSQFQLNLFCLRE----RDLLERFASEVSElqsKGESREFAFLLSYQ 567

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 436 HVASLSLAHTHRVTLEQFSLAVKSCPDQEDQTLLMKFCLLYgTKLVFQERAWYLEHKYLTPMASTRIRNQLLDLCDSVKD 515
Cdd:PLN02312 568 LAEDLGRAFSERAILQTFLDAEANLPTGSLKDVLGLLRSLY-VLISLDEDPSFLRYGYLSPDNVALVRKEVAKLCGELRP 646

                        570       580
                 ....*....|....*....|.
gi 767918697 516 DARRVISTFNIPHTYLhAPIA 536
Cdd:PLN02312 647 HALALVSSFGIPDAFL-SPIA 666
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 37-354 2.09e-48

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: 172.72  E-value: 2.09e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697  37 LVIGEVLSMADMATGVKCGIiYWLFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDlsAQE 116
Cdd:COG1960   70 ALVLEELARADASLALPVGV-HNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRD--GDG 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 117 FVIdtpceNAEKMYIGNAMYGNYAAVFAQLIIDGRSQGPHCFIVPvRDEngslyPGVTAIDMMYKEGLHGVDNGILIFDK 196
Cdd:COG1960  147 YVL-----NGQKTFITNAPVADVILVLARTDPAAGHRGISLFLVP-KDT-----PGVTVGRIEDKMGLRGSDTGELFFDD 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 197 VRIPRENLLDKFGsvapdgqyhspirnksARFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYS---HRYAGALLDEDV 273
Cdd:COG1960  216 VRVPAENLLGEEG----------------KGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYArerEQFGRPIADFQA 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 274 FQGK------ELVNSRSL--------------QALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFA 333
Cdd:COG1960  280 VQHRladmaaELEAARALvyraawlldagedaALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILT 359

                        330       340
                 ....*....|....*....|.
gi 767918697 334 TFEGDDVVMLQVVGRELLAQY 354
Cdd:COG1960  360 IYEGTNEIQRLIIARRLLGRP 380
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 90-195 8.81e-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: 8.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697   90 FAMTERGHGSNARGIQTEAtFDLSAQEFVIdtpceNAEKMYIGNAMYGNYAAVFAQLIIDGRSQGPHCFIVPVRDengsl 169
Cdd:pfam02770   2 FALTEPGAGSDVASLKTTA-ADGDGGGWVL-----NGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDA----- 70

                          90       100
                  ....*....|....*....|....*.
gi 767918697  170 yPGVTAIDMMYKEGLHGVDNGILIFD 195
Cdd:pfam02770  71 -PGVSVRRIETKLGVRGLPTGELVFD 95
 
Name Accession Description Interval E-value
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 2-536 9.93e-131

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: 395.16  E-value: 9.93e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697   2 RALTVQRV--KFAMDLPLLKRAGQDLAEKTknfvsrsLVIGEVLSMADMATGVKCGIIYWLFGGAIRNLGSPEHVTKWFQ 79
Cdd:cd01150   55 REELYEELkrKAKTDVERMGELMADDPEKM-------LALTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQ 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697  80 PLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVIDTPCENAEKMYIGN-AMYGNYAAVFAQLIIDGRSQGPHCF 158
Cdd:cd01150  128 GANNLEIIGCFAQTELGHGSNLQGLETTATYDPLTQEFVINTPDFTATKWWPGNlGKTATHAVVFAQLITPGKNHGLHAF 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 159 IVPVRDENG-SLYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSVAPDGQYHSPIRNKSARFNAMLAALTP 237
Cdd:cd01150  208 IVPIRDPKThQPLPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDPNKRYGAMLGTRSG 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 238 SRLAVAFQAMGAMKLGLTIAIRYS--HRYAG--------ALLDEDVFQ----------------GKELVN---------- 281
Cdd:cd01150  288 GRVGLIYDAAMSLKKAATIAIRYSavRRQFGpkpsdpevQILDYQLQQyrlfpqlaaayafhfaAKSLVEmyheiikell 367

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 282 ------SRSLQALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQVVGRELLAQYT 355
Cdd:cd01150  368 qgnselLAELHALSAGLKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYA 447

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 356 KQYEekplfgllqnwaesvgdklrtsflafnmdtvddLAFLLKAVKFRERVLQRGLVARIYYKVKTKKEDfFHAWNSCLH 435
Cdd:cd01150  448 QAFS---------------------------------LADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGS-FEARNNSQV 493

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 436 HVASLSLAHTHRVTLEQFSLAVKSCPDQEDQTLLMKFCLLYGTKLVFQERAWYLEHKYLTPMASTRIRNQLLDLCDSVKD 515
Cdd:cd01150  494 HLRCAAKAHTEYTVLQRFHESVEEIVDPSVRAVLKRLCDLYALWLLEEHIADFLEGGFLGGQDVKAVREALLALLPQLRP 573

                        570       580
                 ....*....|....*....|.
gi 767918697 516 DARRVISTFNIPHTYLHAPIA 536
Cdd:cd01150  574 DAVALVDAFDLPDFVLNSPIG 594
PLN02312 PLN02312
acyl-CoA oxidase
 2-536 1.51e-109

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 342.52  E-value: 1.51e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697   2 RALTVQRVKFamdlpLLKRAGQD--LAEKTKNFVSRSLVIGEVLSMADMATGVKCGIIYWLFGGAIRNLGSPEHVTKWFQ 79
Cdd:PLN02312 104 REITMKRILY-----LLERGVFRgwLTETGPEAELRKLALLEVIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHDKWLK 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697  80 PLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVIDTPCENAEKMYIGNA-MYGNYAAVFAQLIIDGRSQGPHCF 158
Cdd:PLN02312 179 DTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFVINTPCESAQKYWIGGAaNHATHTIVFSQLHINGKNEGVHAF 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 159 IVPVRDENGSLYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSVAPDGQYHSPIRNKSARFNAMLAALTPS 238
Cdd:PLN02312 259 IAQIRDQDGNICPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNSVADVSPDGKYVSAIKDPDQRFGAFLAPLTSG 338

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 239 RLAVAFQAMGAMKLGLTIAIRYS-HRYAGA---------LLDEDVFQGKEL--------------------VN-----SR 283
Cdd:PLN02312 339 RVTIAVSAIYSSKVGLAIAIRYSlSRRAFSvtpngpevlLLDYPSHQRRLLpllaktyamsfaandlkmiyVKrtpesNK 418

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 284 SLQALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQVVGRELLAQY-TKQYEEKP 362
Cdd:PLN02312 419 AIHVVSSGFKAVLTWHNMRTLQECREACGGQGLKTENRVGQLKAEYDVQSTFEGDNNVLMQQVSKALLAEYvSAKKRNKP 498

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 363 LFGL----LQNWAESVGDKLRTSflafnmdTVDDLAFLLKAVKFRErvlqRGLVARIYYKVKT---KKEDFFHAWNSCLH 435
Cdd:PLN02312 499 FKGLglehMNGPRPVIPTQLTSS-------TLRDSQFQLNLFCLRE----RDLLERFASEVSElqsKGESREFAFLLSYQ 567

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 436 HVASLSLAHTHRVTLEQFSLAVKSCPDQEDQTLLMKFCLLYgTKLVFQERAWYLEHKYLTPMASTRIRNQLLDLCDSVKD 515
Cdd:PLN02312 568 LAEDLGRAFSERAILQTFLDAEANLPTGSLKDVLGLLRSLY-VLISLDEDPSFLRYGYLSPDNVALVRKEVAKLCGELRP 646

                        570       580
                 ....*....|....*....|.
gi 767918697 516 DARRVISTFNIPHTYLhAPIA 536
Cdd:PLN02312 647 HALALVSSFGIPDAFL-SPIA 666
PLN02636 PLN02636
acyl-coenzyme A oxidase
 34-536 5.46e-103

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 325.66  E-value: 5.46e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697  34 SRSLVIGEVLSMADMATGVKCGIIYWLFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDLS 113
Cdd:PLN02636 121 AKYFAITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPL 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 114 AQEFVIDTPCENAEKMYIGN-AMYGNYAAVFAQLIIDG------RSQGPHCFIVPVRD-ENGSLYPGVTAIDMMYKEGLH 185
Cdd:PLN02636 201 TDEFVINTPNDGAIKWWIGNaAVHGKFATVFARLKLPThdskgvSDMGVHAFIVPIRDmKTHQVLPGVEIRDCGHKVGLN 280

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 186 GVDNGILIFDKVRIPRENLLDKFGSVAPDGQYHSPIRNKSARFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYS---- 261
Cdd:PLN02636 281 GVDNGALRFRSVRIPRDNLLNRFGDVSRDGKYTSSLPTINKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSllrq 360

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 262 -----HRYAGALLDEDVFQGK----------------ELVNSRS-------------LQALVAGLKAYSTWENIRCLQDC 307
Cdd:PLN02636 361 qfgppKQPEISILDYQSQQHKlmpmlastyafhfateYLVERYSemkkthddqlvadVHALSAGLKAYITSYTAKALSTC 440

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 308 RECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQVVGRELLAQYTKQYEEKPLFGLLQNWAESVGDKL-RTSFLAFN 386
Cdd:PLN02636 441 REACGGHGYAAVNRFGSLRNDHDIFQTFEGDNTVLLQQVAADLLKQYKEKFQGGTLSVTWNYLRESMNTYLsQPNPVTTR 520

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 387 MDTVD---DLAFLLKAVKFR-ERVLQRglvARIYYKVKTKKEDFFHAWNSCLHHVASLSLAHTHRVTLEQFSLAVKSCPD 462
Cdd:PLN02636 521 WEGEEhlrDPKFQLDAFRYRtSRLLQT---AALRLRKHSKTLGSFGAWNRCLNHLLTLAESHIESVILAKFIEAVERCPD 597

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767918697 463 QEDQTLLMKFCLLYGTKLVFQERAWYLEHKYLTPMASTRIRNQLLDLCDSVKDDARRVISTFNIPHTYLHAPIA 536
Cdd:PLN02636 598 RSTRAALKLVCDLYALDRIWKDIGTYRNVDYVAPNKAKAIHKLTEYLSFQVRNVAKELVDAFGLPDHVTRAPIA 671
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 37-354 2.09e-48

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: 172.72  E-value: 2.09e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697  37 LVIGEVLSMADMATGVKCGIiYWLFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDlsAQE 116
Cdd:COG1960   70 ALVLEELARADASLALPVGV-HNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRD--GDG 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 117 FVIdtpceNAEKMYIGNAMYGNYAAVFAQLIIDGRSQGPHCFIVPvRDEngslyPGVTAIDMMYKEGLHGVDNGILIFDK 196
Cdd:COG1960  147 YVL-----NGQKTFITNAPVADVILVLARTDPAAGHRGISLFLVP-KDT-----PGVTVGRIEDKMGLRGSDTGELFFDD 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 197 VRIPRENLLDKFGsvapdgqyhspirnksARFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYS---HRYAGALLDEDV 273
Cdd:COG1960  216 VRVPAENLLGEEG----------------KGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYArerEQFGRPIADFQA 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 274 FQGK------ELVNSRSL--------------QALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFA 333
Cdd:COG1960  280 VQHRladmaaELEAARALvyraawlldagedaALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILT 359

                        330       340
                 ....*....|....*....|.
gi 767918697 334 TFEGDDVVMLQVVGRELLAQY 354
Cdd:COG1960  360 IYEGTNEIQRLIIARRLLGRP 380
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 64-398 5.49e-43

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 163.09  E-value: 5.49e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697  64 AIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVIDTPCENAEKMYIGN-AMYGNYAAV 142
Cdd:PTZ00460 105 AFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHTPSVEAVKFWPGElGFLCNFALV 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 143 FAQLIIDGRSQGPHCFIVPVRDENG-SLYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSVAPDGQYhspI 221
Cdd:PTZ00460 185 YAKLIVNGKNKGVHPFMVRIRDKEThKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLARYIKVSEDGQV---E 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 222 R--NKSARFNAMLAaltpSRLAVAFQAMGAMKLGLTIAIRYS---------HRYAGALLDED----------------VF 274
Cdd:PTZ00460 262 RqgNPKVSYASMMY----MRNLIIDQYPRFAAQALTVAIRYSiyrqqftndNKQENSVLEYQtqqqkllpllaefyacIF 337

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 275 QG---KELVNSR---------SL----QALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGD 338
Cdd:PTZ00460 338 GGlkiKELVDDNfnrvqkndfSLlqltHAILSAAKANYTYFVSNCAEWCRLSCGGHGYAHYSGLPAIYFDMSPNITLEGE 417

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767918697 339 DVVMLQVVGRELLAQYtKQYEEKP-----LFGLLQNWAESVGDKlrtsflafnmDTVDDLAFLLK 398
Cdd:PTZ00460 418 NQIMYLQLARYLLKQL-QHAVQKPekvpeYFNFLSHITEKLADQ----------TTIESLGQLLG 471
PLN02443 PLN02443
acyl-coenzyme A oxidase
 57-531 2.54e-39

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 152.68  E-value: 2.54e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697  57 IYW-LFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVIDTPCENAEKMYIGN-A 134
Cdd:PLN02443 101 LHWgMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFVIHSPTLTSSKWWPGGlG 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 135 MYGNYAAVFAQLIIDGRSQGPHCFIVPVRD-ENGSLYPGVTAIDMMYKEGLHG---VDNGILIFDKVRIPRENLLDKFGS 210
Cdd:PLN02443 181 KVSTHAVVYARLITNGKDHGIHGFIVQLRSlDDHSPLPGVTVGDIGMKFGNGAyntMDNGFLRFDHVRIPRDQMLMRLSK 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 211 VAPDGQYHSPIRNKSARFNAMLAAltpsRLAVAFQAMGAMKLGLTIAIRYS----------------------------- 261
Cdd:PLN02443 261 VTREGKYVQSDVPRQLVYGTMVYV----RQTIVADASTALSRAVCIATRYSavrrqfgsqdggpetqvidyktqqsrlfp 336

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 262 -------HRYAGALLD---EDVFQGKELVNSRSLQ---ALVAGLKAYSTWENIRCLQDCRECTGGMGYMMEnriSGLKcd 328
Cdd:PLN02443 337 llasayaFRFVGEWLKwlyTDVTQRLEANDFSTLPeahACTAGLKSLTTSATADGIEECRKLCGGHGYLCS---SGLP-- 411

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 329 tDVFA------TFEGDDVVMLQVVGRELLAQYTKQYEEKPLFGLLQnWAESVGDKLRTSFLAFNMDTVDDLAFLLKAvkF 402
Cdd:PLN02443 412 -ELFAvyvpacTYEGDNVVLLLQVARFLMKTVSQLGSGKKPVGTTA-YMGRVQHLLQCRCGVQTAEDWLNPSVVLEA--F 487

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 403 RERVLQRGLVARIYYKVKTKKEDFFHAWNSCLHHVAslsLAHTHRVTLEQFSLAVKS-CPDQEDQTLLMKFCLLYGTKLV 481
Cdd:PLN02443 488 EARAARMAVTCAQNLSKFENQEAGFQELSADLVEAA---VAHCQLIVVSKFIEKLQQdIPGKGVKKQLQNLCYIYALYLL 564

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 767918697 482 FQERAWYLEHKYLTPMASTRIRNQLLDLCDSVKDDARRVISTFNIPHTYL 531
Cdd:PLN02443 565 HKHLGDFLSTGCITPKQASLANDQLRSLYSQVRPNAVALVDAFNYTDHYL 614
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 58-348 3.19e-34

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: 132.41  E-value: 3.19e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697  58 YWLFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDlsAQEFVIdtpceNAEKMYIGNAMYG 137
Cdd:cd00567   41 LLLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKD--GDGYVL-----NGRKIFISNGGDA 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 138 NYAAVFAQLIIDG-RSQGPHCFIVPvRDEngslyPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSVapdgq 216
Cdd:cd00567  114 DLFIVLARTDEEGpGHRGISAFLVP-ADT-----PGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGG----- 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 217 yhspirnksarFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSH---RYAGALLDedvFQGK---------ELVNSRS 284
Cdd:cd00567  183 -----------FELAMKGLNVGRLLLAAVALGAARAALDEAVEYAKqrkQFGKPLAE---FQAVqfkladmaaELEAARL 248

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767918697 285 LQ---------------ALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQVVGR 348
Cdd:cd00567  249 LLyraawlldqgpdearLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 31-352 3.60e-24

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: 104.27  E-value: 3.60e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697  31 NFVSRSLVIGEvLSMADMATGVKCGIIYWLFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATF 110
Cdd:cd01158   59 DFLAYAIAIEE-LAKVDASVAVIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKK 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 111 DlsAQEFVIdtpceNAEKMYIGNAMYGNYAAVFAQLIIDGRSQGPHCFIVPvRDEngslyPGVTAIDMMYKEGLHGVDNG 190
Cdd:cd01158  138 D--GDDYVL-----NGSKMWITNGGEADFYIVFAVTDPSKGYRGITAFIVE-RDT-----PGLSVGKKEDKLGIRGSSTT 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 191 ILIFDKVRIPRENLLDKFGsvapDGqyhspirnksarFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYshryagaLLD 270
Cdd:cd01158  205 ELIFEDVRVPKENILGEEG----EG------------FKIAMQTLDGGRIGIAAQALGIAQAALDAAVDY-------AKE 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 271 EDVFqGKELVNSRSLQALVA------------GLKAYSTWEN-------------------IRCLQDCRECTGGMGYMME 319
Cdd:cd01158  262 RKQF-GKPIADFQGIQFKLAdmateieaarllTYKAARLKDNgepfikeaamaklfasevaMRVTTDAVQIFGGYGYTKD 340

                        330       340       350
                 ....*....|....*....|....*....|...
gi 767918697 320 NRISGLKCDTDVFATFEGDDVVMLQVVGRELLA 352
Cdd:cd01158  341 YPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 65-351 1.76e-21

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: 96.42  E-value: 1.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697  65 IRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDlsAQEFVIdtpceNAEKMYIGNAMYGNYAAVFA 144
Cdd:cd01160   91 ITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKD--GDHYVL-----NGSKTFITNGMLADVVIVVA 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 145 QLIIDGRSQ-GPHCFIVpvrdENGSlyPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLdkfgsvapdGQyhspiRN 223
Cdd:cd01160  164 RTGGEARGAgGISLFLV----ERGT--PGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLL---------GE-----EN 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 224 KSarFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSH---------------RYAGALLDEDVFQGKELVNsRSLQAL 288
Cdd:cd01160  224 KG--FYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKqrkafgktlaqlqvvRHKIAELATKVAVTRAFLD-NCAWRH 300

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767918697 289 VAG---------LKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQVVGRELL 351
Cdd:cd01160  301 EQGrldvaeasmAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 90-195 8.81e-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: 8.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697   90 FAMTERGHGSNARGIQTEAtFDLSAQEFVIdtpceNAEKMYIGNAMYGNYAAVFAQLIIDGRSQGPHCFIVPVRDengsl 169
Cdd:pfam02770   2 FALTEPGAGSDVASLKTTA-ADGDGGGWVL-----NGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDA----- 70

                          90       100
                  ....*....|....*....|....*.
gi 767918697  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 ...
 392-535 9.04e-16

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: 75.66  E-value: 9.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697  392 DLAFLLKAvkFRERVlqRGLVARIYYKVKTKKE---DFFHAWNSCLHHVASLSLAHTHRVTLEQFSLAVKSCPDQEDQTL 468
Cdd:pfam01756   1 DPEVLLKA--FEWRA--ARLLREAAEKLQALLKsgkSQFEAWNNQSVELVRAAKAHAEYFVLRTFVERLSTSLDPPLKPV 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767918697  469 LMKFCLLYGTKLVFQERAWYLEHKYLTPMASTRIRNQLLDLCDSVKDDARRVISTFNIPHTYLHAPI 535
Cdd:pfam01756  77 LKKLCKLYALWTIEKHLGDFLQGGYLSPEQIDLIREAILELLAELRPNAVALVDAFDFPDFILNSAL 143
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 66-352 2.90e-15

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: 77.84  E-value: 2.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697  66 RNlGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDlsAQEFVIdtpceNAEKMYIGNAMYGNYAAVFAQ 145
Cdd:cd01156   97 RN-GSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKK--GDRYVL-----NGSKMWITNGPDADTLVVYAK 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 146 LIIDGRSQGPHCFIVpvrdENGslYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSvapdGQYhspirnks 225
Cdd:cd01156  169 TDPSAGAHGITAFIV----EKG--MPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENK----GVY-------- 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 226 arfnAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSH--RYAGALLDE-DVFQGK------ELVNSRSLQALV------- 289
Cdd:cd01156  231 ----VLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHqrKQFGQPIGEfQLVQGKladmytRLNASRSYLYTVakacdrg 306

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 290 -------AGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQVVGRELLA 352
Cdd:cd01156  307 nmdpkdaAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 38-353 1.38e-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: 69.39  E-value: 1.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697  38 VIGEVLSMADMATGVKCGIiYWLFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATfdLSAQEF 117
Cdd:cd01162   67 IIFEALSTGCVSTAAYISI-HNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAV--REGDHY 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 118 VIdtpceNAEKMYIGNAMYGNYAAVFAQLIIDGrSQGPHCFIVpvrdENGSlyPGVTAIDMMYKEGLHGVDNGILIFDKV 197
Cdd:cd01162  144 VL-----NGSKAFISGAGDSDVYVVMARTGGEG-PKGISCFVV----EKGT--PGLSFGANEKKMGWNAQPTRAVIFEDC 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 198 RIPRENLLdkfgsvAPDGQyhspirnksaRFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRY---SHRYAGALLDEDVF 274
Cdd:cd01162  212 RVPVENRL------GGEGQ----------GFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYleeRKQFGKPLADFQAL 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 275 QGK------ELVNSR--------SLQ-------ALVAGLKAYSTwenIRCLQDCRECT---GGMGYMMENRISGLKCDTD 330
Cdd:cd01162  276 QFKladmatELVASRlmvrraasALDrgdpdavKLCAMAKRFAT---DECFDVANQALqlhGGYGYLKDYPVEQYVRDLR 352

                        330       340
                 ....*....|....*....|...
gi 767918697 331 VFATFEGDDVVMLQVVGRELLAQ 353
Cdd:cd01162  353 VHQILEGTNEIMRLIIARALLTR 375
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 65-353 3.23e-10

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 62.20  E-value: 3.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697  65 IRNlGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEAtfDLSAQEFVIdtpceNAEKMYIGNAMYGNYAAVFA 144
Cdd:PLN02519 122 VRN-GTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKA--ERVDGGYVL-----NGNKMWCTNGPVAQTLVVYA 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 145 QLIIDGRSQGPHCFIVpvrdENGslYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSvapdGQYhspirnk 224
Cdd:PLN02519 194 KTDVAAGSKGITAFII----EKG--MPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGK----GVY------- 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 225 sarfnAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYS---HRYAGALLDEDVFQGK------ELVNSRSLQALV------ 289
Cdd:PLN02519 257 -----VMMSGLDLERLVLAAGPLGLMQACLDVVLPYVrqrEQFGRPIGEFQFIQGKladmytSLQSSRSYVYSVardcdn 331

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767918697 290 --------AGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQVVGRELLAQ 353
Cdd:PLN02519 332 gkvdrkdcAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
PLN02526 PLN02526
acyl-coenzyme A oxidase
 65-350 4.81e-10

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 61.79  E-value: 4.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697  65 IRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATfdLSAQEFVIdtpceNAEKMYIGNAMYGNYAAVFA 144
Cdd:PLN02526 121 IALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTAT--KVEGGWIL-----NGQKRWIGNSTFADVLVIFA 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 145 QLIIDGRSQGphcFIVpvrdENGSlyPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLdkfgsvapdgqyhsPIRNK 224
Cdd:PLN02526 194 RNTTTNQING---FIV----KKGA--PGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRL--------------PGVNS 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 225 SARFNAMLAAltpSRLAVAFQAMGaMKLGLTIAirySHRYA------GALLDEDVFQGKELVNSR-SLQALV-------- 289
Cdd:PLN02526 251 FQDTNKVLAV---SRVMVAWQPIG-ISMGVYDM---CHRYLkerkqfGAPLAAFQINQEKLVRMLgNIQAMFlvgwrlck 323

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767918697 290 -----------AGL-KAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQVVGREL 350
Cdd:PLN02526 324 lyesgkmtpghASLgKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREI 396
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 69-351 3.25e-09

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: 59.14  E-value: 3.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697  69 GSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEAtfDLSAQEFVIdtpceNAEKMYIGNAMYGNYAAVFAQLII 148
Cdd:cd01157   97 GNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYII-----NGQKMWITNGGKANWYFLLARSDP 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 149 DGR---SQGPHCFIVPvRDENGsLYPGVTAIDMmykeGLHGVDNGILIFDKVRIPRENLLDKFGsvapdgqyhspirnks 225
Cdd:cd01157  170 DPKcpaSKAFTGFIVE-ADTPG-IQPGRKELNM----GQRCSDTRGITFEDVRVPKENVLIGEG---------------- 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 226 ARFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYShryagalLDEDVFqGKELVNSRSLQALVAGLK--------AY-- 295
Cdd:cd01157  228 AGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYA-------LERKTF-GKLIAEHQAVSFMLADMAmkvelarlAYqr 299

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767918697 296 STWE-----------NI----------RCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQVVGRELL 351
Cdd:cd01157  300 AAWEvdsgrrntyyaSIakafaadianQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 228-350 7.61e-08

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: 51.87  E-value: 7.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697  228 FNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHR---YAGALLDEDVFQGK------ELVNSRSL------------- 285
Cdd:pfam00441   4 FRVAMETLNHERLAIAAMALGLARRALDEALAYARRrkaFGRPLIDFQLVRHKlaemaaEIEAARLLvyraaealdaggp 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767918697  286 -QALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQVVGREL 350
Cdd:pfam00441  84 dGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 63-348 1.19e-07

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: 54.30  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697  63 GAIRNLGsPEHVTKWFQPLQEQKY-TGMFA---MTERGHGSNARGIQTEATFDLSaqefviDTPCENAEKMYIGNAMyGN 138
Cdd:cd01154  121 YALRKYG-PEELKQYLPGLLSDRYkTGLLGgtwMTEKQGGSDLGANETTAERSGG------GVYRLNGHKWFASAPL-AD 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 139 YAAVFAQLI-IDGRSQGPHCFIVPVRDENGSLypgvtaidmmykeglhgvdNGILIfdkvriprENLLDKFG--SVAP-- 213
Cdd:cd01154  193 AALVLARPEgAPAGARGLSLFLVPRLLEDGTR-------------------NGYRI--------RRLKDKLGtrSVATge 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 214 ---DGQYHSPIRNKSARFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHR---YAGALLDED--------------- 272
Cdd:cd01154  246 vefDDAEAYLIGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHrraFGKPLIDHPlmrrdlaemevdvea 325

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 273 ----VFQGKELVNSRS---------LQALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDD 339
Cdd:cd01154  326 atalTFRAARAFDRAAadkpveahmARLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTG 405

                        330
                 ....*....|...
gi 767918697 340 VV----MLQVVGR 348
Cdd:cd01154  406 NIqaldVLRVLVK 418
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 59-265 2.52e-05

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: 47.00  E-value: 2.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697  59 WLFGGAIRNL---GSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVidtpceNAEKMYIGN-- 133
Cdd:cd01153   87 SGTQGAAATLlahGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSWRI------NGVKRFISAge 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 134 -AMYGNyaavfAQLIIDGRSQGP-------HCFIVPVRDENGSlYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPrenLL 205
Cdd:cd01153  161 hDMSEN-----IVHLVLARSEGAppgvkglSLFLVPKFLDDGE-RNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LI 231

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 206 dkfgsvapdGQYHSPIRnksarfnAMLAALTPSRLAVAFQAMGAmklgLTIAIRYSHRYA 265
Cdd:cd01153  232 ---------GEEGMGLA-------QMFAMMNGARLGVGTQGTGL----AEAAYLNALAYA 271
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 60-209 3.72e-05

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 46.47  E-value: 3.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697  60 LFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDlSAQEFVIdtpceNAEKMYIGNAMYGNY 139
Cdd:PTZ00461 125 LFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKD-SNGNYVL-----NGSKIWITNGTVADV 198

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 140 AAVFAQliIDGRSQGphcFIVpvrdENGSlyPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFG 209
Cdd:PTZ00461 199 FLIYAK--VDGKITA---FVV----ERGT--KGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEG 257
PRK12341 PRK12341
acyl-CoA dehydrogenase;
53-354 4.08e-04

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 42.79  E-value: 4.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697  53 KCGIIYWLFGGA-----IRNLGSPEHVTKWFQplqEQKYTG----MFAMTERGHGSNARGIQTEATFDlSAQEFVidtpc 123
Cdd:PRK12341  79 KCGAPAFLITNGqcihsMRRFGSAEQLRKTAE---STLETGdpayALALTEPGAGSDNNSATTTYTRK-NGKVYL----- 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 124 eNAEKMYIGNAMYGNYAAVFAQliiDGRSQGPH-CF---IVPVRDengslyPGVTaIDMMYKEGLHGVDNGILIFDKVRI 199
Cdd:PRK12341 150 -NGQKTFITGAKEYPYMLVLAR---DPQPKDPKkAFtlwWVDSSK------PGIK-INPLHKIGWHMLSTCEVYLDNVEV 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 200 PRENLLDKFGsvapDGqyhspirnksarFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHR---YAGALLDEDVFQG 276
Cdd:PRK12341 219 EESDLVGEEG----MG------------FLNVMYNFEMERLINAARSLGFAECAFEDAARYANQriqFGKPIGHNQLIQE 282

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918697 277 K--------------------ELVNSRSLQALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFE 336
Cdd:PRK12341 283 KltlmaikienmrnmvykvawQADNGQSLRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGG 362

                        330
                 ....*....|....*...
gi 767918697 337 GDDVVMLQVVGRELLAQY 354
Cdd:PRK12341 363 GTDEIMIYIAGRQILKDY 380
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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