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Conserved domains on  [gi|1771853648|ref|NP_001362715|]
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peroxisomal acyl-coenzyme A oxidase 3 isoform d [Homo sapiens]

Protein Classification

acyl-CoA oxidase( domain architecture ID 10100166)

acyl-CoA oxidase catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
19-636 0e+00

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: 848.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648  19 GPLDAYRARASFSWKELALFTEG-EGMLRFKKTIFSALENDPLFARspgADLSLEKYRELNFLRCKRIFEYDFLSVEDMF 97
Cdd:cd01150     1 PDLDKERASATFDWKALTHILEGgEENLRRKREVERELESDPLFQR---ELPSKHLSREELYEELKRKAKTDVERMGELM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648  98 KS-PLKVPALIQCLGMYDSSLAAKYLLHSLVFGSAVYSSGSERHLTYIQKIFRM-EIFGCFALTELSHGSNTKAIRTTAH 175
Cdd:cd01150    78 ADdPEKMLALTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNlEIIGCFAQTELGHGSNLQGLETTAT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 176 YDPATEEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGdQCHGLHPFIVQIRDPKTLLPMPGVMVGDIGKKLGQNG 255
Cdd:cd01150   158 YDPLTQEFVINTPDFTATKWWPGNLGKTATHAVVFAQLITPG-KNHGLHAFIVPIRDPKTHQPLPGVTVGDIGPKMGLNG 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 256 LDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYVSPFKDVRQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQ 335
Cdd:cd01150   237 VDNGFLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQ 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 336 FGPT-EEEEIPVLEYPMQQWRLLPYLAAVYALDHFSKSLFLDLVELQRGLASGDrsarqAELGREIHALASASKPLASWT 414
Cdd:cd01150   317 FGPKpSDPEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKELLQGN-----SELLAELHALSAGLKAVATWT 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 415 TQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGLLAHQVHdgacfrsplksvdfldaypg 494
Cdd:cd01150   392 AAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQAFS-------------------- 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 495 ildqkfevssvadcldSAVALAAYKWLVCYLLRETYQKLNQEKRSGSSDFEARNKCQVsHGRPLALAFVELTVVQRFHEH 574
Cdd:cd01150   452 ----------------LADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGSFEARNNSQV-HLRCAAKAHTEYTVLQRFHES 514
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1771853648 575 VHQpSVPPSLRAVLGRLSALYALWSLSRHAALLYRgGYFSGEQAGEVLESAVLALCSQLYKN 636
Cdd:cd01150   515 VEE-IVDPSVRAVLKRLCDLYALWLLEEHIADFLE-GGFLGGQDVKAVREALLALLPQLRPD 574
 
Name Accession Description Interval E-value
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
19-636 0e+00

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: 848.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648  19 GPLDAYRARASFSWKELALFTEG-EGMLRFKKTIFSALENDPLFARspgADLSLEKYRELNFLRCKRIFEYDFLSVEDMF 97
Cdd:cd01150     1 PDLDKERASATFDWKALTHILEGgEENLRRKREVERELESDPLFQR---ELPSKHLSREELYEELKRKAKTDVERMGELM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648  98 KS-PLKVPALIQCLGMYDSSLAAKYLLHSLVFGSAVYSSGSERHLTYIQKIFRM-EIFGCFALTELSHGSNTKAIRTTAH 175
Cdd:cd01150    78 ADdPEKMLALTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNlEIIGCFAQTELGHGSNLQGLETTAT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 176 YDPATEEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGdQCHGLHPFIVQIRDPKTLLPMPGVMVGDIGKKLGQNG 255
Cdd:cd01150   158 YDPLTQEFVINTPDFTATKWWPGNLGKTATHAVVFAQLITPG-KNHGLHAFIVPIRDPKTHQPLPGVTVGDIGPKMGLNG 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 256 LDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYVSPFKDVRQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQ 335
Cdd:cd01150   237 VDNGFLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQ 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 336 FGPT-EEEEIPVLEYPMQQWRLLPYLAAVYALDHFSKSLFLDLVELQRGLASGDrsarqAELGREIHALASASKPLASWT 414
Cdd:cd01150   317 FGPKpSDPEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKELLQGN-----SELLAELHALSAGLKAVATWT 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 415 TQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGLLAHQVHdgacfrsplksvdfldaypg 494
Cdd:cd01150   392 AAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQAFS-------------------- 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 495 ildqkfevssvadcldSAVALAAYKWLVCYLLRETYQKLNQEKRSGSSDFEARNKCQVsHGRPLALAFVELTVVQRFHEH 574
Cdd:cd01150   452 ----------------LADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGSFEARNNSQV-HLRCAAKAHTEYTVLQRFHES 514
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1771853648 575 VHQpSVPPSLRAVLGRLSALYALWSLSRHAALLYRgGYFSGEQAGEVLESAVLALCSQLYKN 636
Cdd:cd01150   515 VEE-IVDPSVRAVLKRLCDLYALWLLEEHIADFLE-GGFLGGQDVKAVREALLALLPQLRPD 574
PLN02312 PLN02312
acyl-CoA oxidase
28-633 7.33e-117

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 364.86  E-value: 7.33e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648  28 ASFSWKELALFTEGEGmLRFKKTIFSALENDPLFAR---------SPGADLSLEKYRELNFlrcKRIFeydFLSVEDMFK 98
Cdd:PLN02312   49 YAFDVKEMRKLLDGHN-LEDRDWLFGLMMQSDLFNSkrrggrvfvSPDYNQTMEQQREITM---KRIL---YLLERGVFR 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648  99 ---------SPLKVPALIQCLGMYDSSLAAKYLLHSLVFGSAVYSSGSERHL-TYIQKIFRMEIFGCFALTELSHGSNTK 168
Cdd:PLN02312  122 gwltetgpeAELRKLALLEVIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHdKWLKDTEDYVVKGCFAMTELGHGSNVR 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 169 AIRTTAHYDPATEEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGDQcHGLHPFIVQIRDPKTLLpMPGVMVGDIG 248
Cdd:PLN02312  202 GIETVTTYDPKTEEFVINTPCESAQKYWIGGAANHATHTIVFSQLHINGKN-EGVHAFIAQIRDQDGNI-CPNIRIADCG 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 249 KKLGQNGLDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYVSPFKDVRQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALR 328
Cdd:PLN02312  280 HKIGLNGVDNGRIWFDNLRIPRENLLNSVADVSPDGKYVSAIKDPDQRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIR 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 329 FSATRRQFGPTEEE-EIPVLEYPMQQWRLLPYLAAVYALD---HFSKSLFLDlvelqrglasgdrsaRQAELGREIHALA 404
Cdd:PLN02312  360 YSLSRRAFSVTPNGpEVLLLDYPSHQRRLLPLLAKTYAMSfaaNDLKMIYVK---------------RTPESNKAIHVVS 424
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 405 SASKPLASWTTQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGLLAhqvhdgACFR--SP 482
Cdd:PLN02312  425 SGFKAVLTWHNMRTLQECREACGGQGLKTENRVGQLKAEYDVQSTFEGDNNVLMQQVSKALLAEYV------SAKKrnKP 498
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 483 LK--SVDFLDAYPGILDQKFEVSSVAdclDSAVALAAYkwlvCYLLRETYQKLNQEKRSGSSDFEARNKCQVSH---GRP 557
Cdd:PLN02312  499 FKglGLEHMNGPRPVIPTQLTSSTLR---DSQFQLNLF----CLRERDLLERFASEVSELQSKGESREFAFLLSyqlAED 571
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853648 558 LALAFVELTVVQRFHEhVHQPSVPPSLRAVLGRLSALYALWSLSRHAALLyRGGYFSGEQAGEVlESAVLALCSQL 633
Cdd:PLN02312  572 LGRAFSERAILQTFLD-AEANLPTGSLKDVLGLLRSLYVLISLDEDPSFL-RYGYLSPDNVALV-RKEVAKLCGEL 644
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
110-468 8.86e-41

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: 153.07  E-value: 8.86e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 110 LGMYDSSLAAKYLLHSlVFGSAVYSSGSERHL-TYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPatEEFIIHsp 188
Cdd:COG1960    76 LARADASLALPVGVHN-GAAEALLRFGTEEQKeRYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDG--DGYVLN-- 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 189 dfeAAKFWVGNmGKTATHAVVFAKLcVPGDQCHGLHPFIVqirdPKtllPMPGVMVGDIGKKLGQNGLDNGFAMFHKVRV 268
Cdd:COG1960   151 ---GQKTFITN-APVADVILVLART-DPAAGHRGISLFLV----PK---DTPGVTVGRIEDKMGLRGSDTGELFFDDVRV 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 269 PRQsllNRMGDvtpEGtyvspfkdvrQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLE 348
Cdd:COG1960   219 PAE---NLLGE---EG----------KGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGR------PIAD 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 349 YPMQQWRLLPYLAAVYALdhfskslfldlvelqRGLAsgDRSARQAELGREIHALASASKPLASWTTQQGIQECREACGG 428
Cdd:COG1960   277 FQAVQHRLADMAAELEAA---------------RALV--YRAAWLLDAGEDAALEAAMAKLFATEAALEVADEALQIHGG 339
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1771853648 429 HGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGL 468
Cdd:COG1960   340 YGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGR 379
ACOX pfam01756
Acyl-CoA oxidase; This is a family of Acyl-CoA oxidases EC:1.3.3.6. Acyl-coA oxidase converts ...
510-665 9.74e-39

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: 141.14  E-value: 9.74e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 510 DSAVALAAYKWLVCYLLRETYQKLNQEKRSGSSDFEARNKCQVSHgRPLALAFVELTVVQRFHEHVHQpSVPPSLRAVLG 589
Cdd:pfam01756   1 DPEVLLKAFEWRAARLLREAAEKLQALLKSGKSQFEAWNNQSVEL-VRAAKAHAEYFVLRTFVERLST-SLDPPLKPVLK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 590 RLSALYALWSLSRHAALLYRGGYFSGEQAGEVLEsAVLALCSQL-----------------------------YKNLWGA 640
Cdd:pfam01756  79 KLCKLYALWTIEKHLGDFLQGGYLSPEQIDLIRE-AILELLAELrpnavalvdafdfpdfilnsalgrydgnvYENLFEW 157
                         170       180
                  ....*....|....*....|....*
gi 1771853648 641 VLQESKVLERASWWPEFSvnKPVIG 665
Cdd:pfam01756 158 AKKNPLNTEVPPSYHEYL--KPLLK 180
 
Name Accession Description Interval E-value
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
19-636 0e+00

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: 848.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648  19 GPLDAYRARASFSWKELALFTEG-EGMLRFKKTIFSALENDPLFARspgADLSLEKYRELNFLRCKRIFEYDFLSVEDMF 97
Cdd:cd01150     1 PDLDKERASATFDWKALTHILEGgEENLRRKREVERELESDPLFQR---ELPSKHLSREELYEELKRKAKTDVERMGELM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648  98 KS-PLKVPALIQCLGMYDSSLAAKYLLHSLVFGSAVYSSGSERHLTYIQKIFRM-EIFGCFALTELSHGSNTKAIRTTAH 175
Cdd:cd01150    78 ADdPEKMLALTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNlEIIGCFAQTELGHGSNLQGLETTAT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 176 YDPATEEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGdQCHGLHPFIVQIRDPKTLLPMPGVMVGDIGKKLGQNG 255
Cdd:cd01150   158 YDPLTQEFVINTPDFTATKWWPGNLGKTATHAVVFAQLITPG-KNHGLHAFIVPIRDPKTHQPLPGVTVGDIGPKMGLNG 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 256 LDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYVSPFKDVRQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQ 335
Cdd:cd01150   237 VDNGFLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQ 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 336 FGPT-EEEEIPVLEYPMQQWRLLPYLAAVYALDHFSKSLFLDLVELQRGLASGDrsarqAELGREIHALASASKPLASWT 414
Cdd:cd01150   317 FGPKpSDPEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKELLQGN-----SELLAELHALSAGLKAVATWT 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 415 TQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGLLAHQVHdgacfrsplksvdfldaypg 494
Cdd:cd01150   392 AAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQAFS-------------------- 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 495 ildqkfevssvadcldSAVALAAYKWLVCYLLRETYQKLNQEKRSGSSDFEARNKCQVsHGRPLALAFVELTVVQRFHEH 574
Cdd:cd01150   452 ----------------LADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGSFEARNNSQV-HLRCAAKAHTEYTVLQRFHES 514
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1771853648 575 VHQpSVPPSLRAVLGRLSALYALWSLSRHAALLYRgGYFSGEQAGEVLESAVLALCSQLYKN 636
Cdd:cd01150   515 VEE-IVDPSVRAVLKRLCDLYALWLLEEHIADFLE-GGFLGGQDVKAVREALLALLPQLRPD 574
PLN02312 PLN02312
acyl-CoA oxidase
28-633 7.33e-117

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 364.86  E-value: 7.33e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648  28 ASFSWKELALFTEGEGmLRFKKTIFSALENDPLFAR---------SPGADLSLEKYRELNFlrcKRIFeydFLSVEDMFK 98
Cdd:PLN02312   49 YAFDVKEMRKLLDGHN-LEDRDWLFGLMMQSDLFNSkrrggrvfvSPDYNQTMEQQREITM---KRIL---YLLERGVFR 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648  99 ---------SPLKVPALIQCLGMYDSSLAAKYLLHSLVFGSAVYSSGSERHL-TYIQKIFRMEIFGCFALTELSHGSNTK 168
Cdd:PLN02312  122 gwltetgpeAELRKLALLEVIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHdKWLKDTEDYVVKGCFAMTELGHGSNVR 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 169 AIRTTAHYDPATEEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGDQcHGLHPFIVQIRDPKTLLpMPGVMVGDIG 248
Cdd:PLN02312  202 GIETVTTYDPKTEEFVINTPCESAQKYWIGGAANHATHTIVFSQLHINGKN-EGVHAFIAQIRDQDGNI-CPNIRIADCG 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 249 KKLGQNGLDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYVSPFKDVRQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALR 328
Cdd:PLN02312  280 HKIGLNGVDNGRIWFDNLRIPRENLLNSVADVSPDGKYVSAIKDPDQRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIR 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 329 FSATRRQFGPTEEE-EIPVLEYPMQQWRLLPYLAAVYALD---HFSKSLFLDlvelqrglasgdrsaRQAELGREIHALA 404
Cdd:PLN02312  360 YSLSRRAFSVTPNGpEVLLLDYPSHQRRLLPLLAKTYAMSfaaNDLKMIYVK---------------RTPESNKAIHVVS 424
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 405 SASKPLASWTTQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGLLAhqvhdgACFR--SP 482
Cdd:PLN02312  425 SGFKAVLTWHNMRTLQECREACGGQGLKTENRVGQLKAEYDVQSTFEGDNNVLMQQVSKALLAEYV------SAKKrnKP 498
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 483 LK--SVDFLDAYPGILDQKFEVSSVAdclDSAVALAAYkwlvCYLLRETYQKLNQEKRSGSSDFEARNKCQVSH---GRP 557
Cdd:PLN02312  499 FKglGLEHMNGPRPVIPTQLTSSTLR---DSQFQLNLF----CLRERDLLERFASEVSELQSKGESREFAFLLSyqlAED 571
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853648 558 LALAFVELTVVQRFHEhVHQPSVPPSLRAVLGRLSALYALWSLSRHAALLyRGGYFSGEQAGEVlESAVLALCSQL 633
Cdd:PLN02312  572 LGRAFSERAILQTFLD-AEANLPTGSLKDVLGLLRSLYVLISLDEDPSFL-RYGYLSPDNVALV-RKEVAKLCGEL 644
PLN02636 PLN02636
acyl-coenzyme A oxidase
68-597 1.96e-101

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 324.89  E-value: 1.96e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648  68 DLSLEKYRELNFLRCKRIF-EYDFLSVEDMFKSPLKVPALIQCLGMYDSSLAAKYLLHSLVFGSAVYSSGSERHL-TYIQ 145
Cdd:PLN02636   87 EISKDEHRELCMRQLTGLVrEAGIRPMKYLVEDPAKYFAITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRdKYFD 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 146 KIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPATEEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVP-----GDQC 220
Cdd:PLN02636  167 GIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLTDEFVINTPNDGAIKWWIGNAAVHGKFATVFARLKLPthdskGVSD 246
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 221 HGLHPFIVQIRDPKTLLPMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYVSPFKDVRQRFGAS 300
Cdd:PLN02636  247 MGVHAFIVPIRDMKTHQVLPGVEIRDCGHKVGLNGVDNGALRFRSVRIPRDNLLNRFGDVSRDGKYTSSLPTINKRFAAT 326
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 301 LGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPTEEEEIPVLEYPMQQWRLLPYLAAVYALdHFSKSLfldLVEL 380
Cdd:PLN02636  327 LGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPKQPEISILDYQSQQHKLMPMLASTYAF-HFATEY---LVER 402
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 381 QrglaSGDRSARQAELGREIHALASASKPLASWTTQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQ 460
Cdd:PLN02636  403 Y----SEMKKTHDDQLVADVHALSAGLKAYITSYTAKALSTCREACGGHGYAAVNRFGSLRNDHDIFQTFEGDNTVLLQQ 478
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 461 TSNYLLGLLAHQVHDGACFRSPLKSVDFLDAYpgiLDQKFEVSS----VADCLDSAVALAAYKWLVCYLLRETYQKLNQE 536
Cdd:PLN02636  479 VAADLLKQYKEKFQGGTLSVTWNYLRESMNTY---LSQPNPVTTrwegEEHLRDPKFQLDAFRYRTSRLLQTAALRLRKH 555
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1771853648 537 -KRSGSsdFEARNKCqVSHGRPLALAFVELTVVQRFHEHVhQPSVPPSLRAVLGRLSALYAL 597
Cdd:PLN02636  556 sKTLGS--FGAWNRC-LNHLLTLAESHIESVILAKFIEAV-ERCPDRSTRAALKLVCDLYAL 613
PLN02443 PLN02443
acyl-coenzyme A oxidase
57-641 4.11e-97

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 312.54  E-value: 4.11e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648  57 NDPLFARSPGADLSLEkyrEL--NFLR-----CKRIFEYDfLSVEDMFKSPLKV--PALIQclgmydsslaakylLHSLV 127
Cdd:PLN02443   44 SDPVFSKDNRTRLSRK---ELfkNTLRkaahaWKRIIELR-LTEEEAGKLRSFVdePGYTD--------------LHWGM 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 128 FGSAVYSSGS-ERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPATEEFIIHSPDFEAAKFWVGNMGKTATH 206
Cdd:PLN02443  106 FVPAIKGQGTeEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFVIHSPTLTSSKWWPGGLGKVSTH 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 207 AVVFAKLCVPGDQcHGLHPFIVQIRDPKTLLPMPGVMVGDIGKKLGQ---NGLDNGFAMFHKVRVPRQSLLNRMGDVTPE 283
Cdd:PLN02443  186 AVVYARLITNGKD-HGIHGFIVQLRSLDDHSPLPGVTVGDIGMKFGNgayNTMDNGFLRFDHVRIPRDQMLMRLSKVTRE 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 284 GTYVSpfKDVRQRFGasLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPTEEE-EIPVLEYPMQQWRLLPYLAA 362
Cdd:PLN02443  265 GKYVQ--SDVPRQLV--YGTMVYVRQTIVADASTALSRAVCIATRYSAVRRQFGSQDGGpETQVIDYKTQQSRLFPLLAS 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 363 VYA---LDHFSKSLFLDLVelQRgLASGDRSARQaelgrEIHALASASKPLASWTTQQGIQECREACGGHGYLAMNRLGV 439
Cdd:PLN02443  341 AYAfrfVGEWLKWLYTDVT--QR-LEANDFSTLP-----EAHACTAGLKSLTTSATADGIEECRKLCGGHGYLCSSGLPE 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 440 LRDDNDPNCTYEGDNNILLQQTSNYLLGLLAhQVHDGacfRSPLKSVDFLDAYPGILDQKFEVSSVADCLDSAVALAAYK 519
Cdd:PLN02443  413 LFAVYVPACTYEGDNVVLLLQVARFLMKTVS-QLGSG---KKPVGTTAYMGRVQHLLQCRCGVQTAEDWLNPSVVLEAFE 488
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 520 WLVCYLLRETYQKLNQeKRSGSSDFEARNKCQVShgrpLALAFVELTVVQRFHEHVHQPSVPPSLRAVLGRLSALYALWS 599
Cdd:PLN02443  489 ARAARMAVTCAQNLSK-FENQEAGFQELSADLVE----AAVAHCQLIVVSKFIEKLQQDIPGKGVKKQLQNLCYIYALYL 563
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|..
gi 1771853648 600 LSRHAALLYRGGYFSGEQAgevlesavlALCSQLYKNLWGAV 641
Cdd:PLN02443  564 LHKHLGDFLSTGCITPKQA---------SLANDQLRSLYSQV 596
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
146-617 4.16e-73

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 248.61  E-value: 4.16e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 146 KIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPATEEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGdQCHGLHP 225
Cdd:PTZ00460  121 SLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHTPSVEAVKFWPGELGFLCNFALVYAKLIVNG-KNKGVHP 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 226 FIVQIRDPKTLLPMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYvspfkdvrQRFG---ASLG 302
Cdd:PTZ00460  200 FMVRIRDKETHKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLARYIKVSEDGQV--------ERQGnpkVSYA 271
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 303 SLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPTEEEEIPVLEYPMQQWRLLPYLAAVYALDhFSKSLFLDLVELQ- 381
Cdd:PTZ00460  272 SMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQFTNDNKQENSVLEYQTQQQKLLPLLAEFYACI-FGGLKIKELVDDNf 350
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 382 RGLASGDRSARQaelgrEIHALASASKPLASWTTQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQT 461
Cdd:PTZ00460  351 NRVQKNDFSLLQ-----LTHAILSAAKANYTYFVSNCAEWCRLSCGGHGYAHYSGLPAIYFDMSPNITLEGENQIMYLQL 425
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 462 SNYLLGLLAHQVhdgacfrSPLKSV----DFLDAYPGILDQKFEVSSVADCLDSAVALaaykwlvcyLLRETYQKLNQEK 537
Cdd:PTZ00460  426 ARYLLKQLQHAV-------QKPEKVpeyfNFLSHITEKLADQTTIESLGQLLGLNCTI---------LTIYAAKKIMDHI 489
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 538 RSGSSDFEARNKCQVSHGRPLALAFVELTVVQRFHEHVHQPSvpPSLRAVLGRLSALYALWSLSRHAALLYRGGYFSGEQ 617
Cdd:PTZ00460  490 NTGKDFQQSWDTKSGIALASAASRFIEYFNYLCFLDTINNAN--KSTKEILTQLADLYGITMLLNNPQGLIEKGQITVEQ 567
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
110-468 8.86e-41

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: 153.07  E-value: 8.86e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 110 LGMYDSSLAAKYLLHSlVFGSAVYSSGSERHL-TYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPatEEFIIHsp 188
Cdd:COG1960    76 LARADASLALPVGVHN-GAAEALLRFGTEEQKeRYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDG--DGYVLN-- 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 189 dfeAAKFWVGNmGKTATHAVVFAKLcVPGDQCHGLHPFIVqirdPKtllPMPGVMVGDIGKKLGQNGLDNGFAMFHKVRV 268
Cdd:COG1960   151 ---GQKTFITN-APVADVILVLART-DPAAGHRGISLFLV----PK---DTPGVTVGRIEDKMGLRGSDTGELFFDDVRV 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 269 PRQsllNRMGDvtpEGtyvspfkdvrQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLE 348
Cdd:COG1960   219 PAE---NLLGE---EG----------KGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGR------PIAD 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 349 YPMQQWRLLPYLAAVYALdhfskslfldlvelqRGLAsgDRSARQAELGREIHALASASKPLASWTTQQGIQECREACGG 428
Cdd:COG1960   277 FQAVQHRLADMAAELEAA---------------RALV--YRAAWLLDAGEDAALEAAMAKLFATEAALEVADEALQIHGG 339
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1771853648 429 HGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGL 468
Cdd:COG1960   340 YGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGR 379
ACOX pfam01756
Acyl-CoA oxidase; This is a family of Acyl-CoA oxidases EC:1.3.3.6. Acyl-coA oxidase converts ...
510-665 9.74e-39

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: 141.14  E-value: 9.74e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 510 DSAVALAAYKWLVCYLLRETYQKLNQEKRSGSSDFEARNKCQVSHgRPLALAFVELTVVQRFHEHVHQpSVPPSLRAVLG 589
Cdd:pfam01756   1 DPEVLLKAFEWRAARLLREAAEKLQALLKSGKSQFEAWNNQSVEL-VRAAKAHAEYFVLRTFVERLST-SLDPPLKPVLK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 590 RLSALYALWSLSRHAALLYRGGYFSGEQAGEVLEsAVLALCSQL-----------------------------YKNLWGA 640
Cdd:pfam01756  79 KLCKLYALWTIEKHLGDFLQGGYLSPEQIDLIRE-AILELLAELrpnavalvdafdfpdfilnsalgrydgnvYENLFEW 157
                         170       180
                  ....*....|....*....|....*
gi 1771853648 641 VLQESKVLERASWWPEFSvnKPVIG 665
Cdd:pfam01756 158 AKKNPLNTEVPPSYHEYL--KPLLK 180
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
143-460 2.23e-32

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: 127.79  E-value: 2.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 143 YIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPatEEFIIHSpdfeaAKFWVGNmGKTATHAVVFAKLCVPGDQCHG 222
Cdd:cd00567    60 YLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDG--DGYVLNG-----RKIFISN-GGDADLFIVLARTDEEGPGHRG 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 223 LHPFIVqirdPKTllpMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLNRMGDVtpegtyvspfkdvrqrFGASLG 302
Cdd:cd00567   132 ISAFLV----PAD---TPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGG----------------FELAMK 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 303 SLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLEYPMQQWRLLPYLAAVYALDHFskslfldlvelqr 382
Cdd:cd00567   189 GLNVGRLLLAAVALGAARAALDEAVEYAKQRKQFGK------PLAEFQAVQFKLADMAAELEAARLL------------- 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 383 glasGDRSARQAELGR-EIHALASASKPLASWTTQQGIQECREACGGHGYLAMNRLG-VLRDDNdPNCTYEGDNNILLQQ 460
Cdd:cd00567   250 ----LYRAAWLLDQGPdEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVErYLRDAR-AARIAEGTAEIQRLI 324
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
114-337 1.63e-17

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: 85.10  E-value: 1.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 114 DSSLAAKYLLH-SLVFGsAVYSSGSE-RHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPATeeFIIHspdfe 191
Cdd:cd01151    87 DSGYRSFMSVQsSLVML-PIYDFGSEeQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGG--YKLN----- 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 192 AAKFWVGNmGKTATHAVVFAKlCVPGDQCHGlhpFIVQiRDpktllpMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQ 271
Cdd:cd01151   159 GSKTWITN-SPIADVFVVWAR-NDETGKIRG---FILE-RG------MKGLSAPKIQGKFSLRASITGEIVMDNVFVPEE 226
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853648 272 SLLnrmgdvtPEGTYvspfkdvrqrFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFG 337
Cdd:cd01151   227 NLL-------PGAEG----------LRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFG 275
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
113-467 1.75e-17

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: 84.63  E-value: 1.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 113 YDSSLAAKYLLHSLVFGSAVYSSGSE-RHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDpaTEEFIIHspdfe 191
Cdd:cd01158    73 VDASVAVIVSVHNSLGANPIIKFGTEeQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKD--GDDYVLN----- 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 192 AAKFWVGNMGKtATHAVVFAKlCVPGDQCHGLHPFIVqirdPKtllPMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQ 271
Cdd:cd01158   146 GSKMWITNGGE-ADFYIVFAV-TDPSKGYRGITAFIV----ER---DTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKE 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 272 SLLNRMGdvtpEGtyvspfkdvrqrFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLEYPM 351
Cdd:cd01158   217 NILGEEG----EG------------FKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGK------PIADFQG 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 352 QQWRLlpylaAVYALDhfskslfldlVELQRGLasGDRSARQAELGREIHALASASKPLASWTTQQGIQECREACGGHGY 431
Cdd:cd01158   275 IQFKL-----ADMATE----------IEAARLL--TYKAARLKDNGEPFIKEAAMAKLFASEVAMRVTTDAVQIFGGYGY 337
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1771853648 432 laMNRLGVLRDDNDPNCT--YEGDNNILLQQTSNYLLG 467
Cdd:cd01158   338 --TKDYPVERYYRDAKITeiYEGTSEIQRLVIAKHLLK 373
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
113-457 1.98e-16

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: 81.75  E-value: 1.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 113 YDSSLAAKYLLHSLV-FGSAVYSSGSERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPATEEFIIHspdfe 191
Cdd:cd01161    98 MDLGFSVTLGAHQSIgFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSEDGKHYVLN----- 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 192 AAKFWVGNmGKTATHAVVFAKLCV---PGDQCHGLHPFIVQiRDPKtllpmpGVMVGDIGKKLGQNGLDNGFAMFHKVRV 268
Cdd:cd01161   173 GSKIWITN-GGIADIFTVFAKTEVkdaTGSVKDKITAFIVE-RSFG------GVTNGPPEKKMGIKGSNTAEVYFEDVKI 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 269 PRQSLLNRMGDvtpegtyvspfkdvrqRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLE 348
Cdd:cd01161   245 PVENVLGEVGD----------------GFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGK------KIHE 302
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 349 YPMQQWRLLPYLAAVYALDhfsKSLFLDLVELQRGlasgdrsarqaeLGREIHALASASKPLASWTTQQGIQECREACGG 428
Cdd:cd01161   303 FGLIQEKLANMAILQYATE---SMAYMTSGNMDRG------------LKAEYQIEAAISKVFASEAAWLVVDEAIQIHGG 367
                         330       340
                  ....*....|....*....|....*....
gi 1771853648 429 HGYLAMNRLGVLRDDNDPNCTYEGDNNIL 457
Cdd:cd01161   368 MGFMREYGVERVLRDLRIFRIFEGTNEIL 396
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
112-466 2.53e-11

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: 65.98  E-value: 2.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 112 MYDSSLAAKYLLHSLVFGSAVYSSGSERHLT-YIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDpaTEEFIIHspdf 190
Cdd:cd01160    71 ARAGGSGPGLSLHTDIVSPYITRAGSPEQKErVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKD--GDHYVLN---- 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 191 eAAKFWVGNmGKTATHAVVFAKLCVPGDQCHGLHPFIVQiRDpktllpMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPR 270
Cdd:cd01160   145 -GSKTFITN-GMLADVVIVVARTGGEARGAGGISLFLVE-RG------TPGFSRGRKLKKMGWKAQDTAELFFDDCRVPA 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 271 QSLLNRMGdvtpegtyvspfkdvrQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPTeeeeipvleyp 350
Cdd:cd01160   216 ENLLGEEN----------------KGFYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFGKT----------- 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 351 mqqwrllpyLAAVYALDHfskslflDLVELQRGLASG----DRSARQAELGREIHALASASKPLASWTTQQGIQECREAC 426
Cdd:cd01160   269 ---------LAQLQVVRH-------KIAELATKVAVTraflDNCAWRHEQGRLDVAEASMAKYWATELQNRVAYECVQLH 332
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1771853648 427 GGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLL 466
Cdd:cd01160   333 GGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
PLN02526 PLN02526
acyl-coenzyme A oxidase
114-456 1.24e-10

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 64.10  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 114 DSSLAAKYLLHSLVFGSAVYSSGSE-RHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPATeeFIIhspdfEA 192
Cdd:PLN02526  103 DASCSTFILVHSSLAMLTIALCGSEaQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGG--WIL-----NG 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 193 AKFWVGNmGKTATHAVVFAKlCVPGDQCHGlhpFIVQiRDPktllpmPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQS 272
Cdd:PLN02526  176 QKRWIGN-STFADVLVIFAR-NTTTNQING---FIVK-KGA------PGLKATKIENKIGLRMVQNGDIVLKDVFVPDED 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 273 LLnrmgdvtpegTYVSPFKDVRQrfgaslgSLSSGRVsIVSLAILNLKLAV-AIALRFSATRRQFGpteeeeIPVLEYPM 351
Cdd:PLN02526  244 RL----------PGVNSFQDTNK-------VLAVSRV-MVAWQPIGISMGVyDMCHRYLKERKQFG------APLAAFQI 299
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 352 QQWRLLPYLAAVYAldhfsksLFLDLVELQRGLASGDRSARQAELGReihalasaskplaSWTTQQGIQEC---REACGG 428
Cdd:PLN02526  300 NQEKLVRMLGNIQA-------MFLVGWRLCKLYESGKMTPGHASLGK-------------AWITKKARETValgRELLGG 359
                         330       340
                  ....*....|....*....|....*...
gi 1771853648 429 HGYLAMNRLGVLRDDNDPNCTYEGDNNI 456
Cdd:PLN02526  360 NGILADFLVAKAFCDLEPIYTYEGTYDI 387
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
155-259 4.09e-09

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: 54.21  E-value: 4.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 155 CFALTELSHGSNTKAIRTTAhYDPATEEFIIHspdfeAAKFWVGNmGKTATHAVVFAKLcVPGDQCHGLHPFIVqirdPK 234
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTA-ADGDGGGWVLN-----GTKWWITN-AGIADLFLVLART-GGDDRHGGISLFLV----PK 68
                          90       100
                  ....*....|....*....|....*
gi 1771853648 235 TllpMPGVMVGDIGKKLGQNGLDNG 259
Cdd:pfam02770  69 D---APGVSVRRIETKLGVRGLPTG 90
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
99-433 3.39e-08

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: 55.91  E-value: 3.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648  99 SPLKVPALIQCLGMYDSSLAAKYLLHSLVFGS-AVYSSGSERHlTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYD 177
Cdd:cd01162    61 SRLDASIIFEALSTGCVSTAAYISIHNMCAWMiDSFGNDEQRE-RFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVRE 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 178 paTEEFIIhspdfEAAKFWVGNMGKTATHaVVFAKlcVPGDQCHGLHPFIVqirdPKTllpMPGVMVGDIGKKLGQNGLD 257
Cdd:cd01162   140 --GDHYVL-----NGSKAFISGAGDSDVY-VVMAR--TGGEGPKGISCFVV----EKG---TPGLSFGANEKKMGWNAQP 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 258 NGFAMFHKVRVPRQsllNRMGdvtPEGtyvspfkdvrQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFG 337
Cdd:cd01162   203 TRAVIFEDCRVPVE---NRLG---GEG----------QGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFG 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 338 PteeeeiPVLEYPMQQWRLlpylaAVYALDHFSKSLFLDLVELQrgLASGDRSARqaelgreihALASASKPLAswtTQQ 417
Cdd:cd01162   267 K------PLADFQALQFKL-----ADMATELVASRLMVRRAASA--LDRGDPDAV---------KLCAMAKRFA---TDE 321
                         330
                  ....*....|....*....
gi 1771853648 418 GIQECREAC---GGHGYLA 433
Cdd:cd01162   322 CFDVANQALqlhGGYGYLK 340
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
116-442 1.00e-07

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: 54.72  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 116 SLAAKYLLHSLVFGSAVYSSGSE-RHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAhyDPATEEFIIHspdfeAAK 194
Cdd:cd01156    79 SVALSYGAHSNLCINQIYRNGSAaQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRA--EKKGDRYVLN-----GSK 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 195 FWVGNmGKTATHAVVFAKlCVPGDQCHGLHPFIVQirdpktlLPMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLL 274
Cdd:cd01156   152 MWITN-GPDADTLVVYAK-TDPSAGAHGITAFIVE-------KGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENIL 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 275 NRMGdvtpEGTYVspfkdvrqrfgaSLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLEYPMQQW 354
Cdd:cd01156   223 GGEN----KGVYV------------LMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQ------PIGEFQLVQG 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 355 RllpyLAAVYALDHFSKSLfldLVELQRGLASGDRSARQAelgreihalASA---SKPLASWTTQQGIQecreACGGHGY 431
Cdd:cd01156   281 K----LADMYTRLNASRSY---LYTVAKACDRGNMDPKDA---------AGVilyAAEKATQVALDAIQ----ILGGNGY 340
                         330
                  ....*....|....
gi 1771853648 432 L---AMNRLgvLRD 442
Cdd:cd01156   341 IndyPTGRL--LRD 352
Acyl-CoA_ox_N pfam14749
Acyl-coenzyme A oxidase N-terminal; Acyl-coenzyme A oxidase consists of three domains. An ...
31-153 1.79e-05

Acyl-coenzyme A oxidase N-terminal; Acyl-coenzyme A oxidase consists of three domains. An N-terminal alpha-helical domain, a beta sheet domain (pfam02770) and a C-terminal catalytic domain (pfam01756). This entry represents the N-terminal alpha-helical domain.


Pssm-ID: 464295 [Multi-domain]  Cd Length: 120  Bit Score: 44.51  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648  31 SWKELALFTEG-EGMLRFKKTIFSALENDPLFA-RSPGADLSLEKYRELNFLRCKRIFEYdflsVEDMFKSPLKVPALIQ 108
Cdd:pfam14749   1 DVEELTALLYGgEEKLERRREIESLIESDPEFSkPEDYYFLSREERYERALRKAKRLVKK----LRELQIEDPEETLLLY 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1771853648 109 CLGMYDSSLAakYLLHSLVFGSAVYSSGSERHLTY-IQKIFRMEIF 153
Cdd:pfam14749  77 LRGLLDEGLP--LGLHFGMFIPTLKGQGTDEQQAKwLPLAENFEII 120
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
297-458 2.19e-05

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: 44.94  E-value: 2.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 297 FGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLEYPMQQWRLLPYLAAVYALdhfsKSLFLd 376
Cdd:pfam00441   4 FRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGR------PLIDFQLVRHKLAEMAAEIEAA----RLLVY- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 377 lvelqrglasgdRSARQAELGREIHALASASKPLASWTTQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNI 456
Cdd:pfam00441  73 ------------RAAEALDAGGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEI 140

                  ..
gi 1771853648 457 LL 458
Cdd:pfam00441 141 QR 142
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
110-431 3.96e-05

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 46.47  E-value: 3.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 110 LGMYDSSLAAKYLLHSLVFGSAVYSSGS-ERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDpATEEFIIHsp 188
Cdd:PTZ00461  108 LSKYDPGFCLAYLAHSMLFVNNFYYSASpAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKD-SNGNYVLN-- 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 189 dfeAAKFWVGNmGKTATHAVVFAKlcVPGDqchgLHPFIVQirdpktlLPMPGVMVGDIGKKLGQNGLDNGFAMFHKVRV 268
Cdd:PTZ00461  185 ---GSKIWITN-GTVADVFLIYAK--VDGK----ITAFVVE-------RGTKGFTQGPKIDKCGMRASHMCQLFFEDVVV 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 269 PRQSLLNRMGdvtpegtyvspfkdvrQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLE 348
Cdd:PTZ00461  248 PAENLLGEEG----------------KGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGK------PISN 305
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 349 YPMQQwrllPYLAAVYALDHFSKSLfldLVELQRGLASGDrsarQAELGREIHALASAskPLASWTTQQGIQecreACGG 428
Cdd:PTZ00461  306 FGQIQ----RYIAEGYADTEAAKAL---VYSVSHNVHPGN----KNRLGSDAAKLFAT--PIAKKVADSAIQ----VMGG 368

                  ...
gi 1771853648 429 HGY 431
Cdd:PTZ00461  369 MGY 371
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
132-456 2.31e-04

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: 44.11  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 132 VYSSGS-ERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAhyDPATEEFIIHspdfeAAKFWVGNMGKtATHAVVF 210
Cdd:cd01157    93 VIISGNdEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKMWITNGGK-ANWYFLL 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 211 AKlCVPGDQCHGLHPFIVQIRDPKTllpmPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLnrmgdvTPEGTyvspf 290
Cdd:cd01157   165 AR-SDPDPKCPASKAFTGFIVEADT----PGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVL------IGEGA----- 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 291 kdvrqRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeipvleyPMQQWRLLPYLAAVYALDhfs 370
Cdd:cd01157   229 -----GFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGK-----------LIAEHQAVSFMLADMAMK--- 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 371 kslfldlVELQRglASGDRSARQAELGREIHALASASKPLASWTTQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTY 450
Cdd:cd01157   290 -------VELAR--LAYQRAAWEVDSGRRNTYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIY 360

                  ....*.
gi 1771853648 451 EGDNNI 456
Cdd:cd01157   361 EGTSQI 366
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
106-356 4.90e-03

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 39.86  E-value: 4.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 106 LIQCLGMYDSSLAA-----KYLLHS-LVFGSAVYSSGSERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAhyDPA 179
Cdd:PLN02519   90 LYHCIAMEEISRASgsvglSYGAHSnLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKA--ERV 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 180 TEEFIIHspdfeAAKFWVGNmGKTATHAVVFAKLCVPGDQcHGLHPFIVQirdpktlLPMPGVMVGDIGKKLGQNGLDNG 259
Cdd:PLN02519  168 DGGYVLN-----GNKMWCTN-GPVAQTLVVYAKTDVAAGS-KGITAFIIE-------KGMPGFSTAQKLDKLGMRGSDTC 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 260 FAMFHKVRVPRQSLLNRMGdvtpEGTYVspfkdvrqrfgaSLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPt 339
Cdd:PLN02519  234 ELVFENCFVPEENVLGQEG----KGVYV------------MMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGR- 296
                         250
                  ....*....|....*..
gi 1771853648 340 eeeeiPVLEYPMQQWRL 356
Cdd:PLN02519  297 -----PIGEFQFIQGKL 308
 
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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