|
Name |
Accession |
Description |
Interval |
E-value |
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
16-670 |
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: 869.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 16 GPLAVYRKRANFDWKRLRLIFEK-EQGLRIKYKVWRRLENDPLF------AHPSRTLPMDEQKRLCAMQVNRMKHLDLV- 87
Cdd:cd01150 1 PDLDKERASATFDWKALTHILEGgEENLRRKREVERELESDPLFqrelpsKHLSREELYEELKRKAKTDVERMGELMADd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 88 PKEIESLSFSAKTKYLmyinealacyspSLSVKIALGVGLFNNAIRAMGTEKHQKYIEA-AWNREVITCLAITELSHGSN 166
Cdd:cd01150 81 PEKMLALTNSLGGYDL------------SLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQgANNLEIIGCFAQTELGHGSN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 167 TKSIRTTATYDPTTQEFVINTPDFEAAKCWVGNLGKTATVAMTFANLYTaDGQNHGLHGFLIPIRDPKTLLSYPGVLVGD 246
Cdd:cd01150 149 LQGLETTATYDPLTQEFVINTPDFTATKWWPGNLGKTATHAVVFAQLIT-PGKNHGLHAFIVPIRDPKTHQPLPGVTVGD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 247 IGEKCGLNGIDNGFVVFTNYRIPRDNLLNRTSDVTPEGVYESVFTEPGKVLGAALESFSAGRIGIMQESANTLCSAAVIA 326
Cdd:cd01150 228 IGPKMGLNGVDNGFLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 327 VRYSAVRKQFGPERHGEEMAILEYQLHQYRIFPYLAAACVQKIATEELTSTYMEIIARSQADsngfdvLTQNAAEIHALI 406
Cdd:cd01150 308 IRYSAVRRQFGPKPSDPEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKELLQG------NSELLAELHALS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 407 SSSKPLITWAARDAIQEAREACGGHGYLQAAKLGQMRTDHDPLCTYEGDNNVLGQQASNWLLRQWSAKEletpigsvkfl 486
Cdd:cd01150 382 AGLKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQAF----------- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 487 errsellalnyaslaqktpiaSWQFSLRCYEWLLCHLMAKTTAHIEGQLAAGSSKFEARNNSQVAgARELSLAYAEYYAL 566
Cdd:cd01150 451 ---------------------SLADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGSFEARNNSQVH-LRCAAKAHTEYTVL 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 567 TRYVDHVSTlTVEAPYASVLRLLFDVYAMWLLEKHMTTFYVGGFAaGRDFSAAVRQLLLDSCLKLKDVAVSVADAISPPD 646
Cdd:cd01150 509 QRFHESVEE-IVDPSVRAVLKRLCDLYALWLLEEHIADFLEGGFL-GGQDVKAVREALLALLPQLRPDAVALVDAFDLPD 586
|
650 660
....*....|....*....|....
gi 24585193 647 FALNSVIARADGLLYENLQNEFMT 670
Cdd:cd01150 587 FVLNSPIGRYDGDVYENLFEEARK 610
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
18-687 |
1.84e-102 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 327.56 E-value: 1.84e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 18 LAVYRKRANFDWKRLRLIFE-KEQGLRIKYKVWRRLENDPLFAHPSRT-LPMDE----QKRLCAMQVNRMKHLDLVPKEI 91
Cdd:PLN02443 7 LAGERNKAQFDVDAMKIVWAgSRHAFEVSDRMARLVASDPVFSKDNRTrLSRKElfknTLRKAAHAWKRIIELRLTEEEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 92 ESLSFsaktkylmYINEalacysPSLsvkIALGVGLFNNAIRAMGTEKHQ-KYIEAAWNREVITCLAITELSHGSNTKSI 170
Cdd:PLN02443 87 GKLRS--------FVDE------PGY---TDLHWGMFVPAIKGQGTEEQQkKWLPLAYKMQIIGCYAQTELGHGSNVQGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 171 RTTATYDPTTQEFVINTPDFEAAKCWVGNLGKTATVAMTFANLYTaDGQNHGLHGFLIPIRDPKTLLSYPGVLVGDIGEK 250
Cdd:PLN02443 150 ETTATFDPKTDEFVIHSPTLTSSKWWPGGLGKVSTHAVVYARLIT-NGKDHGIHGFIVQLRSLDDHSPLPGVTVGDIGMK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 251 CG---LNGIDNGFVVFTNYRIPRDNLLNRTSDVTPEGVYesVFTEPGKVLGAALESFSagRIGIMQESANTLCSAAVIAV 327
Cdd:PLN02443 229 FGngaYNTMDNGFLRFDHVRIPRDQMLMRLSKVTREGKY--VQSDVPRQLVYGTMVYV--RQTIVADASTALSRAVCIAT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 328 RYSAVRKQFGPERHGEEMAILEYQLHQYRIFPYLAAACVQKIATEELTSTYMEIIARSQAdsNGFDVLtqnaAEIHALIS 407
Cdd:PLN02443 305 RYSAVRRQFGSQDGGPETQVIDYKTQQSRLFPLLASAYAFRFVGEWLKWLYTDVTQRLEA--NDFSTL----PEAHACTA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 408 SSKPLITWAARDAIQEAREACGGHGYLQAAKLGQMRTDHDPLCTYEGDNNVLGQQASNWLLRQWSakELET---PIGSVK 484
Cdd:PLN02443 379 GLKSLTTSATADGIEECRKLCGGHGYLCSSGLPELFAVYVPACTYEGDNVVLLLQVARFLMKTVS--QLGSgkkPVGTTA 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 485 FLERRSELL----ALNYASLAQKTPIASWQFSLRCYEwllchlMAKTTAHIEGQLAAGSSKFEARNNSQVAGARelslAY 560
Cdd:PLN02443 457 YMGRVQHLLqcrcGVQTAEDWLNPSVVLEAFEARAAR------MAVTCAQNLSKFENQEAGFQELSADLVEAAV----AH 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 561 AEYYALTRYVDHVSTLTVEAPYASVLRLLFDVYAMWLLEKHMTTFYVGGFAAGRDFSAAVRQL--LLDsclKLKDVAVSV 638
Cdd:PLN02443 527 CQLIVVSKFIEKLQQDIPGKGVKKQLQNLCYIYALYLLHKHLGDFLSTGCITPKQASLANDQLrsLYS---QVRPNAVAL 603
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 24585193 639 ADAISPPDFALNSVIARADGLLYENLQnefmtnEGAFQRPswWRDVIIP 687
Cdd:PLN02443 604 VDAFNYTDHYLGSVLGRYDGNVYPKLY------EEAWKDP--LNDSVVP 644
|
|
| ACOX |
pfam01756 |
Acyl-CoA oxidase; This is a family of Acyl-CoA oxidases EC:1.3.3.6. Acyl-coA oxidase converts ... |
508-687 |
7.02e-51 |
|
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: 174.66 E-value: 7.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 508 SWQFSLRCYEWLLCHLMAKTTAHIEGQLAAGSSKFEARNNsQVAGARELSLAYAEYYALTRYVDHVSTlTVEAPYASVLR 587
Cdd:pfam01756 1 DPEVLLKAFEWRAARLLREAAEKLQALLKSGKSQFEAWNN-QSVELVRAAKAHAEYFVLRTFVERLST-SLDPPLKPVLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 588 LLFDVYAMWLLEKHMTTFYVGGFAAGRDFsAAVRQLLLDSCLKLKDVAVSVADAISPPDFALNSVIARADGLLYENLQNE 667
Cdd:pfam01756 79 KLCKLYALWTIEKHLGDFLQGGYLSPEQI-DLIREAILELLAELRPNAVALVDAFDFPDFILNSALGRYDGNVYENLFEW 157
|
170 180
....*....|....*....|
gi 24585193 668 FMTNEGAFQRPSWWRDVIIP 687
Cdd:pfam01756 158 AKKNPLNTEVPPSYHEYLKP 177
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
63-469 |
3.86e-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: 154.23 E-value: 3.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 63 RTLPMDEQKRLCAMQVNRMkhldLVPKEIESLSFSAKTkyLMYINEALACYSPSLSVKIALGVGlFNNAIRAMGTEKH-Q 141
Cdd:COG1960 35 GEFPRELWRKLAELGLLGL----TIPEEYGGLGLSLVE--LALVLEELARADASLALPVGVHNG-AAEALLRFGTEEQkE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 142 KYIEAAWNREVITCLAITELSHGSNTKSIRTTATYDPttQEFVINtpdfeAAKCWVGNlGKTATVAMTFANLYTADGQnH 221
Cdd:COG1960 108 RYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDG--DGYVLN-----GQKTFITN-APVADVILVLARTDPAAGH-R 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 222 GLHGFLIPIRDPktllsypGVLVGDIGEKCGLNGIDNGFVVFTNYRIPRDNLLnrtsdvtpeGvyesvftEPGKVLGAAL 301
Cdd:COG1960 179 GISLFLVPKDTP-------GVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLL---------G-------EEGKGFKIAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 302 ESFSAGRIGIMQESANTLCSAAVIAVRYSAVRKQFGperhgeeMAILEYQLHQYRifpyLAAAcvqKIATEELTSTYMEI 381
Cdd:COG1960 236 STLNAGRLGLAAQALGIAEAALELAVAYAREREQFG-------RPIADFQAVQHR----LADM---AAELEAARALVYRA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 382 IARSQAdsngfdvltqnAAEIHALISSSKPLITWAARDAIQEAREACGGHGYLQAAKLGQMRTDHDPLCTYEGDNNVLGQ 461
Cdd:COG1960 302 AWLLDA-----------GEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRL 370
|
....*...
gi 24585193 462 QASNWLLR 469
Cdd:COG1960 371 IIARRLLG 378
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
16-670 |
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: 869.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 16 GPLAVYRKRANFDWKRLRLIFEK-EQGLRIKYKVWRRLENDPLF------AHPSRTLPMDEQKRLCAMQVNRMKHLDLV- 87
Cdd:cd01150 1 PDLDKERASATFDWKALTHILEGgEENLRRKREVERELESDPLFqrelpsKHLSREELYEELKRKAKTDVERMGELMADd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 88 PKEIESLSFSAKTKYLmyinealacyspSLSVKIALGVGLFNNAIRAMGTEKHQKYIEA-AWNREVITCLAITELSHGSN 166
Cdd:cd01150 81 PEKMLALTNSLGGYDL------------SLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQgANNLEIIGCFAQTELGHGSN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 167 TKSIRTTATYDPTTQEFVINTPDFEAAKCWVGNLGKTATVAMTFANLYTaDGQNHGLHGFLIPIRDPKTLLSYPGVLVGD 246
Cdd:cd01150 149 LQGLETTATYDPLTQEFVINTPDFTATKWWPGNLGKTATHAVVFAQLIT-PGKNHGLHAFIVPIRDPKTHQPLPGVTVGD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 247 IGEKCGLNGIDNGFVVFTNYRIPRDNLLNRTSDVTPEGVYESVFTEPGKVLGAALESFSAGRIGIMQESANTLCSAAVIA 326
Cdd:cd01150 228 IGPKMGLNGVDNGFLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 327 VRYSAVRKQFGPERHGEEMAILEYQLHQYRIFPYLAAACVQKIATEELTSTYMEIIARSQADsngfdvLTQNAAEIHALI 406
Cdd:cd01150 308 IRYSAVRRQFGPKPSDPEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKELLQG------NSELLAELHALS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 407 SSSKPLITWAARDAIQEAREACGGHGYLQAAKLGQMRTDHDPLCTYEGDNNVLGQQASNWLLRQWSAKEletpigsvkfl 486
Cdd:cd01150 382 AGLKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQAF----------- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 487 errsellalnyaslaqktpiaSWQFSLRCYEWLLCHLMAKTTAHIEGQLAAGSSKFEARNNSQVAgARELSLAYAEYYAL 566
Cdd:cd01150 451 ---------------------SLADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGSFEARNNSQVH-LRCAAKAHTEYTVL 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 567 TRYVDHVSTlTVEAPYASVLRLLFDVYAMWLLEKHMTTFYVGGFAaGRDFSAAVRQLLLDSCLKLKDVAVSVADAISPPD 646
Cdd:cd01150 509 QRFHESVEE-IVDPSVRAVLKRLCDLYALWLLEEHIADFLEGGFL-GGQDVKAVREALLALLPQLRPDAVALVDAFDLPD 586
|
650 660
....*....|....*....|....
gi 24585193 647 FALNSVIARADGLLYENLQNEFMT 670
Cdd:cd01150 587 FVLNSPIGRYDGDVYENLFEEARK 610
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
18-687 |
1.84e-102 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 327.56 E-value: 1.84e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 18 LAVYRKRANFDWKRLRLIFE-KEQGLRIKYKVWRRLENDPLFAHPSRT-LPMDE----QKRLCAMQVNRMKHLDLVPKEI 91
Cdd:PLN02443 7 LAGERNKAQFDVDAMKIVWAgSRHAFEVSDRMARLVASDPVFSKDNRTrLSRKElfknTLRKAAHAWKRIIELRLTEEEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 92 ESLSFsaktkylmYINEalacysPSLsvkIALGVGLFNNAIRAMGTEKHQ-KYIEAAWNREVITCLAITELSHGSNTKSI 170
Cdd:PLN02443 87 GKLRS--------FVDE------PGY---TDLHWGMFVPAIKGQGTEEQQkKWLPLAYKMQIIGCYAQTELGHGSNVQGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 171 RTTATYDPTTQEFVINTPDFEAAKCWVGNLGKTATVAMTFANLYTaDGQNHGLHGFLIPIRDPKTLLSYPGVLVGDIGEK 250
Cdd:PLN02443 150 ETTATFDPKTDEFVIHSPTLTSSKWWPGGLGKVSTHAVVYARLIT-NGKDHGIHGFIVQLRSLDDHSPLPGVTVGDIGMK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 251 CG---LNGIDNGFVVFTNYRIPRDNLLNRTSDVTPEGVYesVFTEPGKVLGAALESFSagRIGIMQESANTLCSAAVIAV 327
Cdd:PLN02443 229 FGngaYNTMDNGFLRFDHVRIPRDQMLMRLSKVTREGKY--VQSDVPRQLVYGTMVYV--RQTIVADASTALSRAVCIAT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 328 RYSAVRKQFGPERHGEEMAILEYQLHQYRIFPYLAAACVQKIATEELTSTYMEIIARSQAdsNGFDVLtqnaAEIHALIS 407
Cdd:PLN02443 305 RYSAVRRQFGSQDGGPETQVIDYKTQQSRLFPLLASAYAFRFVGEWLKWLYTDVTQRLEA--NDFSTL----PEAHACTA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 408 SSKPLITWAARDAIQEAREACGGHGYLQAAKLGQMRTDHDPLCTYEGDNNVLGQQASNWLLRQWSakELET---PIGSVK 484
Cdd:PLN02443 379 GLKSLTTSATADGIEECRKLCGGHGYLCSSGLPELFAVYVPACTYEGDNVVLLLQVARFLMKTVS--QLGSgkkPVGTTA 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 485 FLERRSELL----ALNYASLAQKTPIASWQFSLRCYEwllchlMAKTTAHIEGQLAAGSSKFEARNNSQVAGARelslAY 560
Cdd:PLN02443 457 YMGRVQHLLqcrcGVQTAEDWLNPSVVLEAFEARAAR------MAVTCAQNLSKFENQEAGFQELSADLVEAAV----AH 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 561 AEYYALTRYVDHVSTLTVEAPYASVLRLLFDVYAMWLLEKHMTTFYVGGFAAGRDFSAAVRQL--LLDsclKLKDVAVSV 638
Cdd:PLN02443 527 CQLIVVSKFIEKLQQDIPGKGVKKQLQNLCYIYALYLLHKHLGDFLSTGCITPKQASLANDQLrsLYS---QVRPNAVAL 603
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 24585193 639 ADAISPPDFALNSVIARADGLLYENLQnefmtnEGAFQRPswWRDVIIP 687
Cdd:PLN02443 604 VDAFNYTDHYLGSVLGRYDGNVYPKLY------EEAWKDP--LNDSVVP 644
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
44-658 |
7.83e-92 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 299.85 E-value: 7.83e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 44 IKYKVWRRLENDPLFAHPSRtLPMDEQKRLCAMQ---------VNRMKHLDLVPkeieslsfsakTKYLMyINEALACYS 114
Cdd:PLN02636 68 IQEKIYEFFNSRPDLQTPVE-ISKDEHRELCMRQltglvreagIRPMKYLVEDP-----------AKYFA-ITEAVGSVD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 115 PSLSVKIALGVGLFNNAIRAMGTEKHQ-KYIEAAWNREVITCLAITELSHGSNTKSIRTTATYDPTTQEFVINTPDFEAA 193
Cdd:PLN02636 135 MSLGIKLGVQYSLWGGSVINLGTKKHRdKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLTDEFVINTPNDGAI 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 194 KCWVGNL---GKTATVamtFANLYTADGQNH-----GLHGFLIPIRDPKTLLSYPGVLVGDIGEKCGLNGIDNGFVVFTN 265
Cdd:PLN02636 215 KWWIGNAavhGKFATV---FARLKLPTHDSKgvsdmGVHAFIVPIRDMKTHQVLPGVEIRDCGHKVGLNGVDNGALRFRS 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 266 YRIPRDNLLNRTSDVTPEGVYESVFTEPGKVLGAALESFSAGRIGIMQESANTLCSAAVIAVRYSAVRKQFGPERHgEEM 345
Cdd:PLN02636 292 VRIPRDNLLNRFGDVSRDGKYTSSLPTINKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPKQ-PEI 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 346 AILEYQLHQYRIFPYLAAACVQKIATEELTSTYMEiIARSQADsngfdvltQNAAEIHALISSSKPLITWAARDAIQEAR 425
Cdd:PLN02636 371 SILDYQSQQHKLMPMLASTYAFHFATEYLVERYSE-MKKTHDD--------QLVADVHALSAGLKAYITSYTAKALSTCR 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 426 EACGGHGYLQAAKLGQMRTDHDPLCTYEGDNNVLGQQASNWLLRQWSAKeLETPIGSVKFLERRSELlaLNYasLAQKTP 505
Cdd:PLN02636 442 EACGGHGYAAVNRFGSLRNDHDIFQTFEGDNTVLLQQVAADLLKQYKEK-FQGGTLSVTWNYLRESM--NTY--LSQPNP 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 506 IAS-WQ---------FSLRCYEWLLCHLMAKTTAHIegqlaagsskfeaRNNSQVAGA---------RELSLA--YAEYY 564
Cdd:PLN02636 517 VTTrWEgeehlrdpkFQLDAFRYRTSRLLQTAALRL-------------RKHSKTLGSfgawnrclnHLLTLAesHIESV 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 565 ALTRYVDHVSTLTvEAPYASVLRLLFDVYAMWLLEKHMTTFYVGGFAAGRDfSAAVRQLLLDSCLKLKDVAVSVADAISP 644
Cdd:PLN02636 584 ILAKFIEAVERCP-DRSTRAALKLVCDLYALDRIWKDIGTYRNVDYVAPNK-AKAIHKLTEYLSFQVRNVAKELVDAFGL 661
|
650
....*....|....
gi 24585193 645 PDFALNSVIARADG 658
Cdd:PLN02636 662 PDHVTRAPIAMQSG 675
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
108-654 |
1.42e-89 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 293.99 E-value: 1.42e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 108 EALACYSPSLSVKIALGVGLFNNAIRAMGTEKHQ-KYIEAAWNREVITCLAITELSHGSNTKSIRTTATYDPTTQEFVIN 186
Cdd:PLN02312 140 EVIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHdKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFVIN 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 187 TPDFEAAKCWVGNLGKTATVAMTFANLYTaDGQNHGLHGFLIPIRDPKTLLSyPGVLVGDIGEKCGLNGIDNGFVVFTNY 266
Cdd:PLN02312 220 TPCESAQKYWIGGAANHATHTIVFSQLHI-NGKNEGVHAFIAQIRDQDGNIC-PNIRIADCGHKIGLNGVDNGRIWFDNL 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 267 RIPRDNLLNRTSDVTPEGVYESVFTEPGKVLGAALESFSAGRIGImqeSANTLCSAAV---IAVRYSAVRKQFGPERHGE 343
Cdd:PLN02312 298 RIPRENLLNSVADVSPDGKYVSAIKDPDQRFGAFLAPLTSGRVTI---AVSAIYSSKVglaIAIRYSLSRRAFSVTPNGP 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 344 EMAILEYQLHQYRIFPYLAAACVQKIATEELTSTYmeiIARSQADSNGfdvltqnaaeIHALISSSKPLITWAARDAIQE 423
Cdd:PLN02312 375 EVLLLDYPSHQRRLLPLLAKTYAMSFAANDLKMIY---VKRTPESNKA----------IHVVSSGFKAVLTWHNMRTLQE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 424 AREACGGHGYLQAAKLGQMRTDHDPLCTYEGDNNVLGQQASNWLLRQW-SAKELETPigsvkflerrseLLALNYASLAQ 502
Cdd:PLN02312 442 CREACGGQGLKTENRVGQLKAEYDVQSTFEGDNNVLMQQVSKALLAEYvSAKKRNKP------------FKGLGLEHMNG 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 503 KTPIASWQFS---LRCYEW---LLC----HLMAKTTAHIEGQLAAGSSKFEARNNS-QVagARELSLAYAEYYALTRYVD 571
Cdd:PLN02312 510 PRPVIPTQLTsstLRDSQFqlnLFClrerDLLERFASEVSELQSKGESREFAFLLSyQL--AEDLGRAFSERAILQTFLD 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 572 HVSTLTvEAPYASVLRLLFDVYAMWLLEKHmTTFYVGGFAAgRDFSAAVRQLLLDSCLKLKDVAVSVADAISPPDfALNS 651
Cdd:PLN02312 588 AEANLP-TGSLKDVLGLLRSLYVLISLDED-PSFLRYGYLS-PDNVALVRKEVAKLCGELRPHALALVSSFGIPD-AFLS 663
|
...
gi 24585193 652 VIA 654
Cdd:PLN02312 664 PIA 666
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
22-672 |
1.39e-74 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 252.84 E-value: 1.39e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 22 RKRANFDWKRL-RLIFEKEQGLRIKYKVWRRLENDPLF-AHP-----SRtlpmDEQKRLCAMQ-VNRMKHLDLvpkeies 93
Cdd:PTZ00460 8 RKQVQFPVLEMtHLLYGNKEQFETFLERQKFIDNEPMFkVHPdyynwSR----QDQILLNAEKtREAHKHLNL------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 94 lsfsAKTKYlmyinealacYSPSLSVK-----IALGVGLFNNAIRAMGT-EKHQKYIEAAWNREVITCLAITELSHGSNT 167
Cdd:PTZ00460 77 ----ANPNY----------YTPNLLCPqgtfiSTVHFAMVIPAFQVLGTdEQINLWMPSLLNFEIVGCYAQTELGHGSDV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 168 KSIRTTATYDPTTQEFVINTPDFEAAKCWVGNLGKTATVAMTFANLyTADGQNHGLHGFLIPIRDPKTLLSYPGVLVGDI 247
Cdd:PTZ00460 143 QNLETTATYDKQTNEFVIHTPSVEAVKFWPGELGFLCNFALVYAKL-IVNGKNKGVHPFMVRIRDKETHKPLQGVEVGDI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 248 GEKCGLNGIDNGFVVFTNYRIPRDNLLNRTSDVTPEGVYESVFTEpgKVlgaaleSFSAgrigiMQESANTLC------- 320
Cdd:PTZ00460 222 GPKMGYAVKDNGFLSFDHYRIPLDSLLARYIKVSEDGQVERQGNP--KV------SYAS-----MMYMRNLIIdqyprfa 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 321 -SAAVIAVRYSAVRKQFGPERhGEEMAILEYQLHQYRIFPYLAA--ACV-QKIATEELTSTYMeiiarSQADSNGFDVLT 396
Cdd:PTZ00460 289 aQALTVAIRYSIYRQQFTNDN-KQENSVLEYQTQQQKLLPLLAEfyACIfGGLKIKELVDDNF-----NRVQKNDFSLLQ 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 397 QNaaeiHALISSSKPLITWAARDAIQEAREACGGHGYLQAAKLGQMRTDHDPLCTYEGDNNVLGQQASNWLLRQWsaKEL 476
Cdd:PTZ00460 363 LT----HAILSAAKANYTYFVSNCAEWCRLSCGGHGYAHYSGLPAIYFDMSPNITLEGENQIMYLQLARYLLKQL--QHA 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 477 ETPIGSVKFLERRSELLALNYASLAQKTPIASWqfsLRCYewlLCHLMAKTTAHIEGQLAAGSSKFEARNnsQVAGAREL 556
Cdd:PTZ00460 437 VQKPEKVPEYFNFLSHITEKLADQTTIESLGQL---LGLN---CTILTIYAAKKIMDHINTGKDFQQSWD--TKSGIALA 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 557 SLA--YAEYYALTRYVDHVSTLTVEApyASVLRLLFDVYAMWLLEKHMTTFYVGGFAAGRDFSaAVRQLLLDSCLKLKDV 634
Cdd:PTZ00460 509 SAAsrFIEYFNYLCFLDTINNANKST--KEILTQLADLYGITMLLNNPQGLIEKGQITVEQIK-LLQETREQLYPIIKPN 585
|
650 660 670
....*....|....*....|....*....|....*...
gi 24585193 635 AVSVADAISPPDFALNSVIARADGLLYENLQNeFMTNE 672
Cdd:PTZ00460 586 ALGLVEAFGLSDNSLRSLIGCHDGDPYENMYN-WASKE 622
|
|
| ACOX |
pfam01756 |
Acyl-CoA oxidase; This is a family of Acyl-CoA oxidases EC:1.3.3.6. Acyl-coA oxidase converts ... |
508-687 |
7.02e-51 |
|
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: 174.66 E-value: 7.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 508 SWQFSLRCYEWLLCHLMAKTTAHIEGQLAAGSSKFEARNNsQVAGARELSLAYAEYYALTRYVDHVSTlTVEAPYASVLR 587
Cdd:pfam01756 1 DPEVLLKAFEWRAARLLREAAEKLQALLKSGKSQFEAWNN-QSVELVRAAKAHAEYFVLRTFVERLST-SLDPPLKPVLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 588 LLFDVYAMWLLEKHMTTFYVGGFAAGRDFsAAVRQLLLDSCLKLKDVAVSVADAISPPDFALNSVIARADGLLYENLQNE 667
Cdd:pfam01756 79 KLCKLYALWTIEKHLGDFLQGGYLSPEQI-DLIREAILELLAELRPNAVALVDAFDFPDFILNSALGRYDGNVYENLFEW 157
|
170 180
....*....|....*....|
gi 24585193 668 FMTNEGAFQRPSWWRDVIIP 687
Cdd:pfam01756 158 AKKNPLNTEVPPSYHEYLKP 177
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
63-469 |
3.86e-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: 154.23 E-value: 3.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 63 RTLPMDEQKRLCAMQVNRMkhldLVPKEIESLSFSAKTkyLMYINEALACYSPSLSVKIALGVGlFNNAIRAMGTEKH-Q 141
Cdd:COG1960 35 GEFPRELWRKLAELGLLGL----TIPEEYGGLGLSLVE--LALVLEELARADASLALPVGVHNG-AAEALLRFGTEEQkE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 142 KYIEAAWNREVITCLAITELSHGSNTKSIRTTATYDPttQEFVINtpdfeAAKCWVGNlGKTATVAMTFANLYTADGQnH 221
Cdd:COG1960 108 RYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDG--DGYVLN-----GQKTFITN-APVADVILVLARTDPAAGH-R 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 222 GLHGFLIPIRDPktllsypGVLVGDIGEKCGLNGIDNGFVVFTNYRIPRDNLLnrtsdvtpeGvyesvftEPGKVLGAAL 301
Cdd:COG1960 179 GISLFLVPKDTP-------GVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLL---------G-------EEGKGFKIAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 302 ESFSAGRIGIMQESANTLCSAAVIAVRYSAVRKQFGperhgeeMAILEYQLHQYRifpyLAAAcvqKIATEELTSTYMEI 381
Cdd:COG1960 236 STLNAGRLGLAAQALGIAEAALELAVAYAREREQFG-------RPIADFQAVQHR----LADM---AAELEAARALVYRA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 382 IARSQAdsngfdvltqnAAEIHALISSSKPLITWAARDAIQEAREACGGHGYLQAAKLGQMRTDHDPLCTYEGDNNVLGQ 461
Cdd:COG1960 302 AWLLDA-----------GEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRL 370
|
....*...
gi 24585193 462 QASNWLLR 469
Cdd:COG1960 371 IIARRLLG 378
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
98-462 |
1.30e-39 |
|
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: 148.59 E-value: 1.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 98 AKTKYLMYINEALACYSPSLSVKIALGVGLFNNAIRAMGTEKHQ-KYIEAAWNREVITCLAITELSHGSNTKSIRTTATY 176
Cdd:cd00567 14 AAEELEPYARERRETPEEPWELLAELGLLLGAALLLAYGTEEQKeRYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 177 DPttQEFVINtpdfeAAKCWVGNlGKTATVAMTFANLYTADGQNHGLHGFLIPIRDPktllsypGVLVGDIGEKCGLNGI 256
Cdd:cd00567 94 DG--DGYVLN-----GRKIFISN-GGDADLFIVLARTDEEGPGHRGISAFLVPADTP-------GVTVGRIWDKMGMRGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 257 DNGFVVFTNYRIPRDNLLnrtsdvtpegvyesvfTEPGKVLGAALESFSAGRIGImqeSANTL--CSAAV-IAVRYSAVR 333
Cdd:cd00567 159 GTGELVFDDVRVPEDNLL----------------GEEGGGFELAMKGLNVGRLLL---AAVALgaARAALdEAVEYAKQR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 334 KQFGperhgeeMAILEYQLHQYRIFPylAAACVQkiateeltstymeiIARSqadsngfdvLTQNAA--------EIHAL 405
Cdd:cd00567 220 KQFG-------KPLAEFQAVQFKLAD--MAAELE--------------AARL---------LLYRAAwlldqgpdEARLE 267
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 24585193 406 ISSSKPLITWAARDAIQEAREACGGHGYLQAAKLGQMRTDHDPLCTYEGDNNVLGQQ 462
Cdd:cd00567 268 AAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLI 324
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
67-459 |
4.89e-23 |
|
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: 101.58 E-value: 4.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 67 MDEQKRLCAMQVNRMKHLDL----VPKEI--ESLSFSAktkYLMYINEaLACYSPSLSVKIALGVGLFNNAIRAMGTEKH 140
Cdd:cd01158 25 MDEKGEFPREVIKEMAELGLmgipIPEEYggAGLDFLA---YAIAIEE-LAKVDASVAVIVSVHNSLGANPIIKFGTEEQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 141 -QKYIEAAWNREVITCLAITELSHGSNTKSIRTTATYDptTQEFVINtpdfeAAKCWVGNlGKTATVAMTFANLYTADGq 219
Cdd:cd01158 101 kKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKD--GDDYVLN-----GSKMWITN-GGEADFYIVFAVTDPSKG- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 220 NHGLHGFLIPiRDpktllsYPGVLVGDIGEKCGLNGIDNGFVVFTNYRIPRDNLLNrtsdvtpegvyesvftEPGKVLGA 299
Cdd:cd01158 172 YRGITAFIVE-RD------TPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILG----------------EEGEGFKI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 300 ALESFSAGRIGIMQESANTLCSAAVIAVRYSAVRKQFGPerhgeemAILEYQLHQYrifpylaaacvqKIATeeltsTYM 379
Cdd:cd01158 229 AMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGK-------PIADFQGIQF------------KLAD-----MAT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 380 EI-IARsqadsngfdVLTQNAAEihaLISSSKPLI----------TWAARDAIQEAREACGGHGYLQA---------AKL 439
Cdd:cd01158 285 EIeAAR---------LLTYKAAR---LKDNGEPFIkeaamaklfaSEVAMRVTTDAVQIFGGYGYTKDypveryyrdAKI 352
|
410 420
....*....|....*....|
gi 24585193 440 GQMrtdhdplctYEGDNNVL 459
Cdd:cd01158 353 TEI---------YEGTSEIQ 363
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
54-459 |
3.32e-18 |
|
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: 87.52 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 54 NDPLFAHPSRTLpmDEQKRLCAMQVnrmkhldLVPKEIESLSFSaKTKYLMyINEALAcYSPSLSVKIALGVGLFNNAIR 133
Cdd:cd01161 51 NDQLEKIPRKTL--TQLKELGLFGL-------QVPEEYGGLGLN-NTQYAR-LAEIVG-MDLGFSVTLGAHQSIGFKGIL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 134 AMGTE-KHQKYIEAAWNREVITCLAITELSHGSNTKSIRTTATYDPTTQEFVINtpdfeAAKCWVGNlGKTATVAMTFAN 212
Cdd:cd01161 119 LFGTEaQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSEDGKHYVLN-----GSKIWITN-GGIADIFTVFAK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 213 LYTADGQNHGLHGF--LIPIRDpktllsYPGVLVGDIGEKCGLNGIDNGFVVFTNYRIPRDNLLNrtsdvtpegvyesvf 290
Cdd:cd01161 193 TEVKDATGSVKDKItaFIVERS------FGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLG--------------- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 291 tEPGKVLGAALESFSAGRIGIMQESANTLCSAAVIAVRYSAVRKQFGPErhgeemaILEYQLHQYRifpyLAAACVQKIA 370
Cdd:cd01161 252 -EVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKK-------IHEFGLIQEK----LANMAILQYA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 371 TEelTSTYMeiiARSQADSNGFdvltqnaAEIHALISSSKPLITWAARDAIQEAREACGGHGYLQAAKLGQMRTDHDPLC 450
Cdd:cd01161 320 TE--SMAYM---TSGNMDRGLK-------AEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFR 387
|
....*....
gi 24585193 451 TYEGDNNVL 459
Cdd:cd01161 388 IFEGTNEIL 396
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
113-458 |
1.48e-15 |
|
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: 78.94 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 113 YSPSLSVKIALGVGlfnnAIRAMGTEKH-QKYIEAAWNREVITCLAITELSHGSNTKSIRTTATYDptTQEFVINtpdfe 191
Cdd:cd01151 90 YRSFMSVQSSLVML----PIYDFGSEEQkQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKD--GGGYKLN----- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 192 AAKCWVGNlGKTATVAMTFANLYTADgqnhGLHGFLIPiRDPKTlLSYPgvlvgDIGEKCGLNGIDNGFVVFTNYRIPRD 271
Cdd:cd01151 159 GSKTWITN-SPIADVFVVWARNDETG----KIRGFILE-RGMKG-LSAP-----KIQGKFSLRASITGEIVMDNVFVPEE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 272 NLLNRTSDvtpegvyesvFTEPGKVLGAAlesfsagRIGIMQESANTLCSAAVIAVRYSAVRKQFG-PerhgeemaILEY 350
Cdd:cd01151 227 NLLPGAEG----------LRGPFKCLNNA-------RYGIAWGALGAAEDCYHTARQYVLDRKQFGrP--------LAAF 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 351 QLHQYRifpyLAAACVqkiateeltstymEIIARSQADSNGFDVLTQNAAEIHAlISSSKPLITWAARDAIQEAREACGG 430
Cdd:cd01151 282 QLVQKK----LADMLT-------------EIALGLLACLRVGRLKDQGKATPEQ-ISLLKRNNCGKALEIARTAREMLGG 343
|
330 340
....*....|....*....|....*...
gi 24585193 431 HGYLQAAKLGQMRTDHDPLCTYEGDNNV 458
Cdd:cd01151 344 NGISDEYHIIRHMVNLESVNTYEGTHDI 371
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
132-459 |
6.68e-11 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 64.87 E-value: 6.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 132 IRAMGTE-KHQKYIEAAWNREVITCLAITELSHGSNTKSIRTTATYDPTTqeFVINtpdfeAAKCWVGNlGKTATVAMTF 210
Cdd:PLN02526 121 IALCGSEaQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGG--WILN-----GQKRWIGN-STFADVLVIF 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 211 ANlytaDGQNHGLHGFLIPirdpktlLSYPGVLVGDIGEKCGLNGIDNGFVVFTNYRIPRDNLLnrtsdvtpEGVyeSVF 290
Cdd:PLN02526 193 AR----NTTTNQINGFIVK-------KGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRL--------PGV--NSF 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 291 TEPGKVLGAALESFSAGRIGImQESANTLCSaaviavRYSAVRKQFGperhgeeMAILEYQLHQYRIFPYLAAACVQKIA 370
Cdd:PLN02526 252 QDTNKVLAVSRVMVAWQPIGI-SMGVYDMCH------RYLKERKQFG-------APLAAFQINQEKLVRMLGNIQAMFLV 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 371 TEELTSTYMeiiarsqadsngfdvlTQNAAEIHAliSSSKPLITWAARDAIQEAREACGGHGYLQAAKLGQMRTDHDPLC 450
Cdd:PLN02526 318 GWRLCKLYE----------------SGKMTPGHA--SLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIY 379
|
330
....*....|.
gi 24585193 451 TYEG--DNNVL 459
Cdd:PLN02526 380 TYEGtyDINAL 390
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
155-263 |
1.07e-10 |
|
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: 58.83 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 155 CLAITELSHGSNTKSIRTTAtYDPTTQEFVINtpdfeAAKCWVGNlGKTATVAMTFANLYTADGQnHGLHGFLIPirdpk 234
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTA-ADGDGGGWVLN-----GTKWWITN-AGIADLFLVLARTGGDDRH-GGISLFLVP----- 67
|
90 100
....*....|....*....|....*....
gi 24585193 235 tlLSYPGVLVGDIGEKCGLNGIDNGFVVF 263
Cdd:pfam02770 68 --KDAPGVSVRRIETKLGVRGLPTGELVF 94
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
106-459 |
1.90e-06 |
|
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: 50.52 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 106 INEALACYSPSLSVKIALgvglfNNAIRAM----GTEKH-QKYIEAAWNREVITCLAITELSHGSNTKSIRTTATYDptT 180
Cdd:cd01162 68 IFEALSTGCVSTAAYISI-----HNMCAWMidsfGNDEQrERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVRE--G 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 181 QEFVINtpdfeAAKCWVGNLGKTAT-VAMTFANlytADGQNhGLHGFLIPirdpktlLSYPGVLVGDIGEKCGLNGIDNG 259
Cdd:cd01162 141 DHYVLN-----GSKAFISGAGDSDVyVVMARTG---GEGPK-GISCFVVE-------KGTPGLSFGANEKKMGWNAQPTR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 260 FVVFTNYRIPRDNLLNrtsdvtPEGvyesvftepgKVLGAALESFSAGRIGIMQESANTLCSAAVIAVRYSAVRKQFGPe 339
Cdd:cd01162 205 AVIFEDCRVPVENRLG------GEG----------QGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGK- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 340 rhgeemAILEYQLHQYRifpyLAaacvqKIATEELTStymEIIARSQADSngfdvLTQNAAEIHALISSSKPLITWAARD 419
Cdd:cd01162 268 ------PLADFQALQFK----LA-----DMATELVAS---RLMVRRAASA-----LDRGDPDAVKLCAMAKRFATDECFD 324
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 24585193 420 AIQEAREACGGHGYLQAAKLGQMRTD---HDPLctyEGDNNVL 459
Cdd:cd01162 325 VANQALQLHGGYGYLKDYPVEQYVRDlrvHQIL---EGTNEIM 364
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
112-464 |
2.00e-06 |
|
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: 50.58 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 112 CYSPSLSVKIALGVGLFNNAIRAmgtEKHQKYIEAAWNREVITCLAITELSHGSNTKSIRTTATYDPTtqEFVINtpdfe 191
Cdd:cd01160 75 GSGPGLSLHTDIVSPYITRAGSP---EQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGD--HYVLN----- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 192 AAKCWVGN--LGKTATVAMtfanlyTADGQNHGLHGFLIPIRDPKTllsyPGVLVGDIGEKCGLNGIDNGFVVFTNYRIP 269
Cdd:cd01160 145 GSKTFITNgmLADVVIVVA------RTGGEARGAGGISLFLVERGT----PGFSRGRKLKKMGWKAQDTAELFFDDCRVP 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 270 RDNLLNrtsdvtpegvyesvftEPGKVLGAALESFSAGRIGIMQESANTLCSAAVIAVRYSAVRKQFGperhgeeMAILE 349
Cdd:cd01160 215 AENLLG----------------EENKGFYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFG-------KTLAQ 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 350 YQLHQYRIFPYLAAACVqkiateelTSTYMEIIArsQADSNGfdvltqnaaeihALISSSKPLITWAARDAIQEAREAC- 428
Cdd:cd01160 272 LQVVRHKIAELATKVAV--------TRAFLDNCA--WRHEQG------------RLDVAEASMAKYWATELQNRVAYECv 329
|
330 340 350
....*....|....*....|....*....|....*....
gi 24585193 429 ---GGHGYLQAAKLGQMRTDHDPLCTYEGDNNVLGQQAS 464
Cdd:cd01160 330 qlhGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELIS 368
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
294-459 |
1.28e-03 |
|
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: 39.93 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 294 GKVLGAALESFSAGRIGIMQESANTLCSAAVIAVRYSAVRKQFGperhgeeMAILEYQLHQYRIFPYLAAACVQKIATEE 373
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFG-------RPLIDFQLVRHKLAEMAAEIEAARLLVYR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 374 LTSTYmeiiarsqadsngfdvltQNAAEIHALISSSKPLITWAARDAIQEAREACGGHGYLQAAKLGQMRTDHDPLCTYE 453
Cdd:pfam00441 74 AAEAL------------------DAGGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGE 135
|
....*.
gi 24585193 454 GDNNVL 459
Cdd:pfam00441 136 GTSEIQ 141
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
138-337 |
1.51e-03 |
|
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: 41.42 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 138 EKHQKYIEAAWNREVITCLAITELSHGSNTKSIRTTAtyDPTTQEFVINtpdfeAAKCWVGNLGKtatvamtfANLYtad 217
Cdd:cd01157 100 EQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKMWITNGGK--------ANWY--- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 218 gqnhglhgFLIPIRDP-------KTLLSY------PGVLVG----DIGEKCGlngiDNGFVVFTNYRIPRDNLLnrtsdv 280
Cdd:cd01157 162 --------FLLARSDPdpkcpasKAFTGFiveadtPGIQPGrkelNMGQRCS----DTRGITFEDVRVPKENVL------ 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24585193 281 tpegvyesvfTEPGKVLGAALESF-------SAGRIGIMQESANTlcsaaviAVRYSAVRKQFG 337
Cdd:cd01157 224 ----------IGEGAGFKIAMGAFdktrppvAAGAVGLAQRALDE-------ATKYALERKTFG 270
|
|
| Acyl-CoA_ox_N |
pfam14749 |
Acyl-coenzyme A oxidase N-terminal; Acyl-coenzyme A oxidase consists of three domains. An ... |
52-153 |
9.94e-03 |
|
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: 36.42 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585193 52 LENDPLFAHP------SRtlpmdEQKRLCAMQvnRMKHLdlvPKEIESLSFSAKTKYLMYINEALACYSPSLsvkiALGV 125
Cdd:pfam14749 26 IESDPEFSKPedyyflSR-----EERYERALR--KAKRL---VKKLRELQIEDPEETLLLYLRGLLDEGLPL----GLHF 91
|
90 100
....*....|....*....|....*....
gi 24585193 126 GLFNNAIRAMGTEKHQKY-IEAAWNREVI 153
Cdd:pfam14749 92 GMFIPTLKGQGTDEQQAKwLPLAENFEII 120
|
|
| |
