|
Name |
Accession |
Description |
Interval |
E-value |
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
19-672 |
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: 808.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 19 GPLSAYRARASFNSGELLLFWDGQDV-IHFKKTIFSTLENDPLFARsygADLPLEKLRELNFLRCKRVFEYGFFKVEELL 97
Cdd:cd01150 1 PDLDKERASATFDWKALTHILEGGEEnLRRKREVERELESDPLFQR---ELPSKHLSREELYEELKRKAKTDVERMGELM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 98 K-NPLKILVLINCLGMYDWSLANKCVLHMLVFGTTVFVSGSEKHFKY-LEKIYSLEIFGCFALTELSHGSNTKAMRTTAH 175
Cdd:cd01150 78 AdDPEKMLALTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYwLQGANNLEIIGCFAQTELGHGSNLQGLETTAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 176 YDPDTQEFILHSPDFEAAKFWVGNLGKTATHAVVFAQLYMPdGQCHGLHSFLVQIRDTKTLLPMTGVMVGDIGKKLGQNG 255
Cdd:cd01150 158 YDPLTQEFVINTPDFTATKWWPGNLGKTATHAVVFAQLITP-GKNHGLHAFIVPIRDPKTHQPLPGVTVGDIGPKMGLNG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 256 LDNGFAMFNKVRIPRQNLLDRTGNITSEGTYNSPFKDVRQRLGASLGSLSSGRISIISMSVVNLKLAVSIAIRFSATRCQ 335
Cdd:cd01150 237 VDNGFLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 336 FGPTDKE-EIPVLEYPLQQWRILPYLAAAYALDHFSKTIFMDLIEVQSarlrgDHSDQQAELGREIHALASAGKPLASWT 414
Cdd:cd01150 317 FGPKPSDpEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIK-----ELLQGNSELLAELHALSAGLKAVATWT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 415 AQRGIQECREACGGHGYLAMNRFGDLRNDNDPNCTYEGDNNVLLQQTSNYLLsllepplqdgahftsplktvdfleaypG 494
Cdd:cd01150 392 AAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLL---------------------------K 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 495 ILGQKFLgsskadwmdSAAPLAAYRWLVCYLLQESHRRYCQEKKSRGSDFEARNNSQVYgCRPLALAFMELTVMQRFHEH 574
Cdd:cd01150 445 KYAQAFS---------LADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGSFEARNNSQVH-LRCAAKAHTEYTVLQRFHES 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 575 IHSSgLSPSLRTVLGRLSTLYGLWCLSQHMALLYRGGYiSGEQTGRAMEDAILTLCEQLKDDAVALVDVIAPSDFVLNSP 654
Cdd:cd01150 515 VEEI-VDPSVRAVLKRLCDLYALWLLEEHIADFLEGGF-LGGQDVKAVREALLALLPQLRPDAVALVDAFDLPDFVLNSP 592
|
650
....*....|....*...
gi 1257171101 655 IAKADGELYKNLWAAVLQ 672
Cdd:cd01150 593 IGRYDGDVYENLFEEARK 610
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
28-656 |
3.15e-109 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 345.99 E-value: 3.15e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 28 ASFNSGELLLFWDGQDViHFKKTIFSTLENDPLFARS-------YGADL--PLEKLRELNFLRCKRVFEYGFFK---VEE 95
Cdd:PLN02312 49 YAFDVKEMRKLLDGHNL-EDRDWLFGLMMQSDLFNSKrrggrvfVSPDYnqTMEQQREITMKRILYLLERGVFRgwlTET 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 96 LLKNPLKILVLINCLGMYDWSLANKCVLHMLVFGTTVFVSGSEKHF-KYLEKIYSLEIFGCFALTELSHGSNTKAMRTTA 174
Cdd:PLN02312 128 GPEAELRKLALLEVIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHdKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 175 HYDPDTQEFILHSPDFEAAKFWVGNLGKTATHAVVFAQLYMpDGQCHGLHSFLVQIRDTK-TLLPmtGVMVGDIGKKLGQ 253
Cdd:PLN02312 208 TYDPKTEEFVINTPCESAQKYWIGGAANHATHTIVFSQLHI-NGKNEGVHAFIAQIRDQDgNICP--NIRIADCGHKIGL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 254 NGLDNGFAMFNKVRIPRQNLLDRTGNITSEGTYNSPFKDVRQRLGASLGSLSSGRISIISMSVVNLKLAVSIAIRFSATR 333
Cdd:PLN02312 285 NGVDNGRIWFDNLRIPRENLLNSVADVSPDGKYVSAIKDPDQRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSR 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 334 CQFGPT-DKEEIPVLEYPLQQWRILPYLAAAYALDhfSKTIFMDLIEVQsarlrgdhsdQQAELGREIHALASAGKPLAS 412
Cdd:PLN02312 365 RAFSVTpNGPEVLLLDYPSHQRRLLPLLAKTYAMS--FAANDLKMIYVK----------RTPESNKAIHVVSSGFKAVLT 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 413 WTAQRGIQECREACGGHGYLAMNRFGDLRNDNDPNCTYEGDNNVLLQQTSNYLLSLL------EPPLQDGA--HFTSPLK 484
Cdd:PLN02312 433 WHNMRTLQECREACGGQGLKTENRVGQLKAEYDVQSTFEGDNNVLMQQVSKALLAEYvsakkrNKPFKGLGleHMNGPRP 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 485 TVdfleayPGILGQKFLGSSKADwMDsaaplaayrwLVCYLLQESHRRYCQEKKSRGSDFEARNNSQVYG---CRPLALA 561
Cdd:PLN02312 513 VI------PTQLTSSTLRDSQFQ-LN----------LFCLRERDLLERFASEVSELQSKGESREFAFLLSyqlAEDLGRA 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 562 FMELTVMQRF--HEHIHSSGlspSLRTVLGRLSTLYGLWCLSQHMALLyRGGYISGEQTGrAMEDAILTLCEQLKDDAVA 639
Cdd:PLN02312 576 FSERAILQTFldAEANLPTG---SLKDVLGLLRSLYVLISLDEDPSFL-RYGYLSPDNVA-LVRKEVAKLCGELRPHALA 650
|
650
....*....|....*..
gi 1257171101 640 LVDVIAPSDFVLnSPIA 656
Cdd:PLN02312 651 LVSSFGIPDAFL-SPIA 666
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
75-661 |
1.94e-103 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 330.67 E-value: 1.94e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 75 RELNFLRCKR-VFEYGFFKVEELLKNPLKILVLINCLGMYDWSLANKCVLHMLVFGTTVFVSGSEKHF-KYLEKIYSLEI 152
Cdd:PLN02636 94 RELCMRQLTGlVREAGIRPMKYLVEDPAKYFAITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRdKYFDGIDNLDY 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 153 FGCFALTELSHGSNTKAMRTTAHYDPDTQEFILHSPDFEAAKFWVGNLGKTATHAVVFAQLYMPDGQCH-----GLHSFL 227
Cdd:PLN02636 174 PGCFAMTELHHGSNVQGLQTTATFDPLTDEFVINTPNDGAIKWWIGNAAVHGKFATVFARLKLPTHDSKgvsdmGVHAFI 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 228 VQIRDTKTLLPMTGVMVGDIGKKLGQNGLDNGFAMFNKVRIPRQNLLDRTGNITSEGTYNSPFKDVRQRLGASLGSLSSG 307
Cdd:PLN02636 254 VPIRDMKTHQVLPGVEIRDCGHKVGLNGVDNGALRFRSVRIPRDNLLNRFGDVSRDGKYTSSLPTINKRFAATLGELVGG 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 308 RISIISMSVVNLKLAVSIAIRFSATRCQFGPTDKEEIPVLEYPLQQWRILPYLAAAYALdHFSkTIFmdLIEVQSaRLRG 387
Cdd:PLN02636 334 RVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPKQPEISILDYQSQQHKLMPMLASTYAF-HFA-TEY--LVERYS-EMKK 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 388 DHSDQqaeLGREIHALASAGKP-LASWTAqRGIQECREACGGHGYLAMNRFGDLRNDNDPNCTYEGDNNVLLQQTSNYLL 466
Cdd:PLN02636 409 THDDQ---LVADVHALSAGLKAyITSYTA-KALSTCREACGGHGYAAVNRFGSLRNDHDIFQTFEGDNTVLLQQVAADLL 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 467 SLLEPPLQDGA--------------HFTSPLKTVDFLEAYPGILGQKFlgsskadwmdsaaPLAAYRWLVCYLLQESHRR 532
Cdd:PLN02636 485 KQYKEKFQGGTlsvtwnylresmntYLSQPNPVTTRWEGEEHLRDPKF-------------QLDAFRYRTSRLLQTAALR 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 533 YCQEKKSRGSdFEARNNSqVYGCRPLALAFMELTVMQRFHEHIHSSGlSPSLRTVLGRLSTLYGLWCLSQHMALLYRGGY 612
Cdd:PLN02636 552 LRKHSKTLGS-FGAWNRC-LNHLLTLAESHIESVILAKFIEAVERCP-DRSTRAALKLVCDLYALDRIWKDIGTYRNVDY 628
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1257171101 613 ISGEQtGRAMEDAILTLCEQLKDDAVALVDVIAPSDFVLNSPIAKADGE 661
Cdd:PLN02636 629 VAPNK-AKAIHKLTEYLSFQVRNVAKELVDAFGLPDHVTRAPIAMQSGA 676
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
21-667 |
5.11e-100 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 321.40 E-value: 5.11e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 21 LSAYRARASFNSGELLLFWDG-QDVIHFKKTIFSTLENDPLFARSYGADLPLEKLRElNFLR-----CKRVFEYGFFKVE 94
Cdd:PLN02443 7 LAGERNKAQFDVDAMKIVWAGsRHAFEVSDRMARLVASDPVFSKDNRTRLSRKELFK-NTLRkaahaWKRIIELRLTEEE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 95 ellknPLKILVLINCLGMYDwslankcvLHMLVFGTTVFVSGS-EKHFKYLEKIYSLEIFGCFALTELSHGSNTKAMRTT 173
Cdd:PLN02443 86 -----AGKLRSFVDEPGYTD--------LHWGMFVPAIKGQGTeEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 174 AHYDPDTQEFILHSPDFEAAKFWVGNLGKTATHAVVFAQLyMPDGQCHGLHSFLVQIRDTKTLLPMTGVMVGDIGKKLGQ 253
Cdd:PLN02443 153 ATFDPKTDEFVIHSPTLTSSKWWPGGLGKVSTHAVVYARL-ITNGKDHGIHGFIVQLRSLDDHSPLPGVTVGDIGMKFGN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 254 ---NGLDNGFAMFNKVRIPRQNLLDRTGNITSEGTYNSpfKDVRQRLGasLGSLSSGRISIISMSVVNLKLAVSIAIRFS 330
Cdd:PLN02443 232 gayNTMDNGFLRFDHVRIPRDQMLMRLSKVTREGKYVQ--SDVPRQLV--YGTMVYVRQTIVADASTALSRAVCIATRYS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 331 ATRCQFGPTDKE-EIPVLEYPLQQWRILPYLAAAYA---LDHFSKTIFMDLIEvqsaRLRG-DHSDQQaelgrEIHALAS 405
Cdd:PLN02443 308 AVRRQFGSQDGGpETQVIDYKTQQSRLFPLLASAYAfrfVGEWLKWLYTDVTQ----RLEAnDFSTLP-----EAHACTA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 406 AGKPLASWTAQRGIQECREACGGHGYLAMNRFGDLRNDNDPNCTYEGDNNVLLQQTSNYLLSLLEpPLQDGahfTSPLKT 485
Cdd:PLN02443 379 GLKSLTTSATADGIEECRKLCGGHGYLCSSGLPELFAVYVPACTYEGDNVVLLLQVARFLMKTVS-QLGSG---KKPVGT 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 486 VDFLEAYPGILGQKFLGSSKADWMDSAAPLAAYRwlvcyllQESHRR--YCQEKKSRGSDFEARNNSQVYGCRPLALAFM 563
Cdd:PLN02443 455 TAYMGRVQHLLQCRCGVQTAEDWLNPSVVLEAFE-------ARAARMavTCAQNLSKFENQEAGFQELSADLVEAAVAHC 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 564 ELTVMQRFHEHIHSSGLSPSLRTVLGRLSTLYGLWCLSQHMALLYRGGYISGEQTGRAmEDAILTLCEQLKDDAVALVDV 643
Cdd:PLN02443 528 QLIVVSKFIEKLQQDIPGKGVKKQLQNLCYIYALYLLHKHLGDFLSTGCITPKQASLA-NDQLRSLYSQVRPNAVALVDA 606
|
650 660
....*....|....*....|....
gi 1257171101 644 IAPSDFVLNSPIAKADGELYKNLW 667
Cdd:PLN02443 607 FNYTDHYLGSVLGRYDGNVYPKLY 630
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
128-676 |
2.91e-80 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 268.25 E-value: 2.91e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 128 FGTTV----FVSGSEKHFKYLEKIYSLEIFGCFALTELSHGSNTKAMRTTAHYDPDTQEFILHSPDFEAAKFWVGNLGKT 203
Cdd:PTZ00460 99 FAMVIpafqVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHTPSVEAVKFWPGELGFL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 204 ATHAVVFAQLYMpDGQCHGLHSFLVQIRDTKTLLPMTGVMVGDIGKKLGQNGLDNGFAMFNKVRIPRQNLLDRTGNITSE 283
Cdd:PTZ00460 179 CNFALVYAKLIV-NGKNKGVHPFMVRIRDKETHKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLARYIKVSED 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 284 GTYnspfkdvrQRLG---ASLGSLSSGRISIISMSVVNLKLAVSIAIRFSATRCQFGPTDKEEIPVLEYPLQQWRILPYL 360
Cdd:PTZ00460 258 GQV--------ERQGnpkVSYASMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQFTNDNKQENSVLEYQTQQQKLLPLL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 361 AAAYALDhFSKTIFMDLIEVQSARLRgdhsDQQAELGREIHALASAGKPLASWTAQRGIQECREACGGHGYLAMNRFGDL 440
Cdd:PTZ00460 330 AEFYACI-FGGLKIKELVDDNFNRVQ----KNDFSLLQLTHAILSAAKANYTYFVSNCAEWCRLSCGGHGYAHYSGLPAI 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 441 RNDNDPNCTYEGDNNVLLQQTSNYLLSLLEPPLQDGAHFTSPLKtvdFLEAYPGILGQKFLGSSKADWMDsaaplaayrw 520
Cdd:PTZ00460 405 YFDMSPNITLEGENQIMYLQLARYLLKQLQHAVQKPEKVPEYFN---FLSHITEKLADQTTIESLGQLLG---------- 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 521 LVCYLLQESHRRYCQEKKSRGSDFEARNNSQVyGCRPLALA--FMELTVMQRFHEHIHSSglSPSLRTVLGRLSTLYGLW 598
Cdd:PTZ00460 472 LNCTILTIYAAKKIMDHINTGKDFQQSWDTKS-GIALASAAsrFIEYFNYLCFLDTINNA--NKSTKEILTQLADLYGIT 548
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1257171101 599 CLSQHMALLYRGGYISGEQTgRAMEDAILTLCEQLKDDAVALVDVIAPSDFVLNSPIAKADGELYKNLWAAVLQQNGV 676
Cdd:PTZ00460 549 MLLNNPQGLIEKGQITVEQI-KLLQETREQLYPIIKPNALGLVEAFGLSDNSLRSLIGCHDGDPYENMYNWASKENSL 625
|
|
| ACOX |
pfam01756 |
Acyl-CoA oxidase; This is a family of Acyl-CoA oxidases EC:1.3.3.6. Acyl-coA oxidase converts ... |
510-686 |
2.60e-59 |
|
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: 197.77 E-value: 2.60e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 510 DSAAPLAAYRWLVCYLLQESHRRYCQEKKSRGSDFEARNNsQVYGCRPLALAFMELTVMQRFHEHIHSSgLSPSLRTVLG 589
Cdd:pfam01756 1 DPEVLLKAFEWRAARLLREAAEKLQALLKSGKSQFEAWNN-QSVELVRAAKAHAEYFVLRTFVERLSTS-LDPPLKPVLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 590 RLSTLYGLWCLSQHMALLYRGGYISGEQTgRAMEDAILTLCEQLKDDAVALVDVIAPSDFVLNSPIAKADGELYKNLWAA 669
Cdd:pfam01756 79 KLCKLYALWTIEKHLGDFLQGGYLSPEQI-DLIREAILELLAELRPNAVALVDAFDFPDFILNSALGRYDGNVYENLFEW 157
|
170
....*....|....*..
gi 1257171101 670 VLQQNGVLERAAWWPEF 686
Cdd:pfam01756 158 AKKNPLNTEVPPSYHEY 174
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
110-466 |
1.37e-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: 155.77 E-value: 1.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 110 LGMYDWSLANKCVLHmLVFGTTVFVSGSEKHF-KYLEKIYSLEIFGCFALTELSHGSNTKAMRTTAHYDPDtqEFILHsp 188
Cdd:COG1960 76 LARADASLALPVGVH-NGAAEALLRFGTEEQKeRYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGD--GYVLN-- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 189 dfeAAKFWVGNlGKTATHAVVFAQLyMPDGQCHGLHSFLVQiRDTKtllpmtGVMVGDIGKKLGQNGLDNGFAMFNKVRI 268
Cdd:COG1960 151 ---GQKTFITN-APVADVILVLART-DPAAGHRGISLFLVP-KDTP------GVTVGRIEDKMGLRGSDTGELFFDDVRV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 269 PRQNLLdrtgnitseGTYNSPFKDVRQRLGAslgslssGRISIISMSVVNLKLAVSIAIRFSATRCQFGPtdkeeiPVLE 348
Cdd:COG1960 219 PAENLL---------GEEGKGFKIAMSTLNA-------GRLGLAAQALGIAEAALELAVAYAREREQFGR------PIAD 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 349 YPLQQWRilpyLAAAYAldhfsktifmdliEVQSARLRGDHSDQQAELGREIHALASAGKPLASWTAQRGIQECREACGG 428
Cdd:COG1960 277 FQAVQHR----LADMAA-------------ELEAARALVYRAAWLLDAGEDAALEAAMAKLFATEAALEVADEALQIHGG 339
|
330 340 350
....*....|....*....|....*....|....*...
gi 1257171101 429 HGYLAMNRFGDLRNDNDPNCTYEGDNNVLLQQTSNYLL 466
Cdd:COG1960 340 YGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLL 377
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
142-460 |
3.74e-35 |
|
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: 135.87 E-value: 3.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 142 KYLEKIYSLEIFGCFALTELSHGSNTKAMRTTAHYDPDtqEFILHSpdfeaAKFWVGNlGKTATHAVVFAQLYMPDGQCH 221
Cdd:cd00567 59 RYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGD--GYVLNG-----RKIFISN-GGDADLFIVLARTDEEGPGHR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 222 GLHSFLVQiRDTKtllpmtGVMVGDIGKKLGQNGLDNGFAMFNKVRIPRQNLLDRTGnitsEGtynspfkdvrqrLGASL 301
Cdd:cd00567 131 GISAFLVP-ADTP------GVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEG----GG------------FELAM 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 302 GSLSSGRISIISMSVVNLKLAVSIAIRFSATRCQFGPtdkeeiPVLEYPLQQWRILPYLAAAYALDHFsktifmdlieVQ 381
Cdd:cd00567 188 KGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQFGK------PLAEFQAVQFKLADMAAELEAARLL----------LY 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1257171101 382 SARLRGDHSDqqaelgREIHALASAGKPLASWTAQRGIQECREACGGHGYLAMNRFGDLRNDNDPNCTYEGDNNVLLQQ 460
Cdd:cd00567 252 RAAWLLDQGP------DEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLI 324
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
113-466 |
2.98e-19 |
|
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: 90.02 E-value: 2.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 113 YDWSLANKCVLHMLVFGTTVFVSGSE--KHfKYLEKIYSLEIFGCFALTELSHGSNTKAMRTTAHYDPDtqEFILHspdf 190
Cdd:cd01158 73 VDASVAVIVSVHNSLGANPIIKFGTEeqKK-KYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGD--DYVLN---- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 191 eAAKFWVGNlGKTATHAVVFAQLyMPDGQCHGLHSFLVQiRDTKtllpmtGVMVGDIGKKLGQNGLDNGFAMFNKVRIPR 270
Cdd:cd01158 146 -GSKMWITN-GGEADFYIVFAVT-DPSKGYRGITAFIVE-RDTP------GLSVGKKEDKLGIRGSSTTELIFEDVRVPK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 271 QNLLdrtgnitseGTYNSPFKdvrqrlgASLGSLSSGRISIISMSVVNLKLAVSIAIRFSATRCQFGPtdkeeiPVLEYP 350
Cdd:cd01158 216 ENIL---------GEEGEGFK-------IAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGK------PIADFQ 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 351 LQQWRIlpylaAAYALdhfsktifmdliEVQSARLRGDHSDQQAELGREIHALASAGKPLASWTAQRGIQECREACGGHG 430
Cdd:cd01158 274 GIQFKL-----ADMAT------------EIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEVAMRVTTDAVQIFGGYG 336
|
330 340 350
....*....|....*....|....*....|....*....
gi 1257171101 431 Y---LAMNRFgdLRnDNDPNCTYEGDNNVLLQQTSNYLL 466
Cdd:cd01158 337 YtkdYPVERY--YR-DAKITEIYEGTSEIQRLVIAKHLL 372
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
126-457 |
6.42e-19 |
|
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: 89.83 E-value: 6.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 126 LVFGTtvfvsgSEKHFKYLEKIYSLEIFGCFALTELSHGSNTKAMRTTAHYDPDTQEFILHspdfeAAKFWVGNlGKTAT 205
Cdd:cd01161 118 LLFGT------EAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSEDGKHYVLN-----GSKIWITN-GGIAD 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 206 HAVVFAQ--LYMPDGQC-HGLHSFLVQiRDTKtllpmtGVMVGDIGKKLGQNGLDNGFAMFNKVRIPRQNLLDRTGnits 282
Cdd:cd01161 186 IFTVFAKteVKDATGSVkDKITAFIVE-RSFG------GVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVG---- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 283 EGtynspFKdvrqrlgASLGSLSSGRISIISMSVVNLKLAVSIAIRFSATRCQFGPtdkeeiPVLEYPLQQWRILPYLAA 362
Cdd:cd01161 255 DG-----FK-------VAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGK------KIHEFGLIQEKLANMAIL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 363 AYALDhfsktifmdlievQSARLRGDHSDQQaeLGREIHALASAGKPLASWTAQRGIQECREACGGHGYLAMNRFGDLRN 442
Cdd:cd01161 317 QYATE-------------SMAYMTSGNMDRG--LKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLR 381
|
330
....*....|....*
gi 1257171101 443 DNDPNCTYEGDNNVL 457
Cdd:cd01161 382 DLRIFRIFEGTNEIL 396
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
122-456 |
1.74e-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: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 122 VLHMLVFGTtVFVSGSEKHF-KYLEKIYSLEIFGCFALTELSHGSNTKAMRTTAHYDPDTqeFILHspdfeAAKFWVGNl 200
Cdd:cd01151 96 VQSSLVMLP-IYDFGSEEQKqKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGG--YKLN-----GSKTWITN- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 201 GKTATHAVVFAQLyMPDGQCHGlhsFLVQiRDTKTLLPMTgvmvgdIGKKLGQNGLDNGFAMFNKVRIPRQNLLDrtgNI 280
Cdd:cd01151 167 SPIADVFVVWARN-DETGKIRG---FILE-RGMKGLSAPK------IQGKFSLRASITGEIVMDNVFVPEENLLP---GA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 281 TSegtynspfkdvrqrLGASLGSLSSGRISIISMSVVNLKLAVSIAIRFSATRCQFGPtdkeeiPVLEYPLQQWRIlpyl 360
Cdd:cd01151 233 EG--------------LRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGR------PLAAFQLVQKKL---- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 361 aaAYALDHFSKTIFMDLievQSARL--RGDHSDQQAELGReihaLASAGKplASWTAQRGiqecREACGGHG----YLAM 434
Cdd:cd01151 289 --ADMLTEIALGLLACL---RVGRLkdQGKATPEQISLLK----RNNCGK--ALEIARTA----REMLGGNGisdeYHII 353
|
330 340
....*....|....*....|..
gi 1257171101 435 NRFGDLRNDNdpncTYEGDNNV 456
Cdd:cd01151 354 RHMVNLESVN----TYEGTHDI 371
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
142-466 |
9.14e-12 |
|
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: 67.14 E-value: 9.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 142 KYLEKIYSLEIFGCFALTELSHGSNTKAMRTTAHYDPDtqEFILHspdfeAAKFWVGNlGKTATHAVVFAQLYMPDGQCH 221
Cdd:cd01160 102 RVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGD--HYVLN-----GSKTFITN-GMLADVVIVVARTGGEARGAG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 222 GLHSFLVQiRDTKtllpmtGVMVGDIGKKLGQNGLDNGFAMFNKVRIPRQNLLdrtgnitseGTYNSPFKDVrqrlgasL 301
Cdd:cd01160 174 GISLFLVE-RGTP------GFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLL---------GEENKGFYYL-------M 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 302 GSLSSGRISIISMSVVNLKLAVSIAIRFSATRCQFGPTdkeeipvleyplqqwrilpyLAAAYALDHfskTIFMDLIEVQ 381
Cdd:cd01160 231 QNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFGKT--------------------LAQLQVVRH---KIAELATKVA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 382 SARLRGDHSDQQAELGREIHALASAGKPLASWTAQRGIQECREACGGHGYLAMNRFGDLRNDNDPNCTYEGDNNVLLQQT 461
Cdd:cd01160 288 VTRAFLDNCAWRHEQGRLDVAEASMAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELI 367
|
....*
gi 1257171101 462 SNYLL 466
Cdd:cd01160 368 SRQMV 372
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
114-458 |
1.39e-10 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 63.72 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 114 DWSLANKCVLHMLVFGTTVFVSGSE-KHFKYLEKIYSLEIFGCFALTELSHGSNTKAMRTTAHYDPDTqeFILhspdfEA 192
Cdd:PLN02526 103 DASCSTFILVHSSLAMLTIALCGSEaQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGG--WIL-----NG 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 193 AKFWVGNlGKTATHAVVFAQlympDGQCHGLHSFLVQiRDTktllpmTGVMVGDIGKKLGQNGLDNGFAMFNKVRIPRQn 272
Cdd:PLN02526 176 QKRWIGN-STFADVLVIFAR----NTTTNQINGFIVK-KGA------PGLKATKIENKIGLRMVQNGDIVLKDVFVPDE- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 273 llDRTGNITSegtynspFKDVRQRLGASlgslssgRISI------ISMSVVNlklavsIAIRFSATRCQFGptdkeeIPV 346
Cdd:PLN02526 243 --DRLPGVNS-------FQDTNKVLAVS-------RVMVawqpigISMGVYD------MCHRYLKERKQFG------APL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 347 LEYPLQQWRILPYLAaayaldhfsktifmdliEVQSARLRGDHSDQQAELGREIHALASAGKPLASWTAQRGIQECREAC 426
Cdd:PLN02526 295 AAFQINQEKLVRMLG-----------------NIQAMFLVGWRLCKLYESGKMTPGHASLGKAWITKKARETVALGRELL 357
|
330 340 350
....*....|....*....|....*....|....*...
gi 1257171101 427 GGHGYLA----MNRFGDLrndnDPNCTYEG--DNNVLL 458
Cdd:PLN02526 358 GGNGILAdflvAKAFCDL----EPIYTYEGtyDINALV 391
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
155-259 |
8.23e-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: 56.13 E-value: 8.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 155 CFALTELSHGSNTKAMRTTAhYDPDTQEFILHspdfeAAKFWVGNlGKTATHAVVFAQLYMPDGQcHGLHSFLVQIRdtk 234
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTA-ADGDGGGWVLN-----GTKWWITN-AGIADLFLVLARTGGDDRH-GGISLFLVPKD--- 69
|
90 100
....*....|....*....|....*
gi 1257171101 235 tllpMTGVMVGDIGKKLGQNGLDNG 259
Cdd:pfam02770 70 ----APGVSVRRIETKLGVRGLPTG 90
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
142-278 |
9.32e-10 |
|
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: 60.89 E-value: 9.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 142 KYLEKIYSLEIFGCFALTELSHGSNTKAMRTTAHYDPDtqEFILHspdfeAAKFWVGNlGKTATHAVVFAQLyMPDGQCH 221
Cdd:cd01156 106 KYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGD--RYVLN-----GSKMWITN-GPDADTLVVYAKT-DPSAGAH 176
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1257171101 222 GLHSFLVQirdtktlLPMTGVMVGDIGKKLGQNGLDNGFAMFNKVRIPRQNLLDRTG 278
Cdd:cd01156 177 GITAFIVE-------KGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGEN 226
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
297-458 |
4.18e-07 |
|
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: 49.95 E-value: 4.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 297 LGASLGSLSSGRISIISMSVVNLKLAVSIAIRFSATRCQFGPtdkeeiPVLEYPLQQWRILPYLAaayaldhfsktifmd 376
Cdd:pfam00441 4 FRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGR------PLIDFQLVRHKLAEMAA--------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 377 liEVQSARLRGDHSDQQAELGREIHALASAGKPLASWTAQRGIQECREACGGHGYLAMNRFGDLRNDNDPNCTYEGDNNV 456
Cdd:pfam00441 63 --EIEAARLLVYRAAEALDAGGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEI 140
|
..
gi 1257171101 457 LL 458
Cdd:pfam00441 141 QR 142
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
116-367 |
6.73e-07 |
|
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: 52.06 E-value: 6.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 116 SLANKCVLHMLVFGTtvfvsgSEKHFKYLEKIYSLEIFGCFALTELSHGSNTKAMRTTAHYDPDtqEFILhspdfEAAKF 195
Cdd:cd01162 84 SIHNMCAWMIDSFGN------DEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGD--HYVL-----NGSKA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 196 WVGNLGKTATHAVVFAQlympDGQ-CHGLHSFLVQiRDTKtllpmtGVMVGDIGKKLGQNGLDNGFAMFNKVRIPRQNLl 274
Cdd:cd01162 151 FISGAGDSDVYVVMART----GGEgPKGISCFVVE-KGTP------GLSFGANEKKMGWNAQPTRAVIFEDCRVPVENR- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 275 drtgnITSEGtynspfkdvrQRLGASLGSLSSGRISIISMSVVNLKLAVSIAIRFSATRCQFGPTDKEEiPVLEYP---- 350
Cdd:cd01162 219 -----LGGEG----------QGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADF-QALQFKladm 282
|
250 260
....*....|....*....|
gi 1257171101 351 ---LQQWRILPYlAAAYALD 367
Cdd:cd01162 283 ateLVASRLMVR-RAASALD 301
|
|
| Acyl-CoA_ox_N |
pfam14749 |
Acyl-coenzyme A oxidase N-terminal; Acyl-coenzyme A oxidase consists of three domains. An ... |
31-153 |
5.43e-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: 42.97 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 31 NSGELLLFWDG-QDVIHFKKTIFSTLENDPLFARSYG-ADLPLEKLRELNFLRCKRVFEygffKVEELLKNPLKILVLIN 108
Cdd:pfam14749 1 DVEELTALLYGgEEKLERRREIESLIESDPEFSKPEDyYFLSREERYERALRKAKRLVK----KLRELQIEDPEETLLLY 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1257171101 109 CLGMYDWSLANKcvLHMLVFGTTVFVSGSEKHFKY-LEKIYSLEIF 153
Cdd:pfam14749 77 LRGLLDEGLPLG--LHFGMFIPTLKGQGTDEQQAKwLPLAENFEII 120
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
130-431 |
3.58e-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: 43.34 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 130 TTVFVSGS-EKHFKYLEKIYSLEIFGCFALTELSHGSNTKAMRTTAHYDPDtqEFILHspdfeAAKFWVGNLGKtATHAV 208
Cdd:cd01157 91 MPVIISGNdEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGD--EYIIN-----GQKMWITNGGK-ANWYF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 209 VFAQlYMPDGQCHGLHSFLVQIRDTKTllpmTGVMVGDIGKKLGQNGLDNGFAMFNKVRIPRQNLLdrtgniTSEGtynS 288
Cdd:cd01157 163 LLAR-SDPDPKCPASKAFTGFIVEADT----PGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVL------IGEG---A 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 289 PFKdvrqrlgASLGSLSSGRISIISMSVVNLKLAVSIAIRFSATRCQFGPtdkeeipvleyPLQQWRILPYLAAAYAldh 368
Cdd:cd01157 229 GFK-------IAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGK-----------LIAEHQAVSFMLADMA--- 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1257171101 369 fsktifmdlIEVQSARLRGDHSDQQAELGREIHALASAGKPLASWTAQRGIQECREACGGHGY 431
Cdd:cd01157 288 ---------MKVELARLAYQRAAWEVDSGRRNTYYASIAKAFAADIANQLATDAVQIFGGNGF 341
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
142-278 |
1.78e-03 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 41.40 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171101 142 KYLEKIYSLEIFGCFALTELSHGSNTKAMRTTAhyDPDTQEFILHspdfeAAKFWVGNlGKTATHAVVFAQLYMPDGQcH 221
Cdd:PLN02519 132 KYLPKLISGEHVGALAMSEPNSGSDVVSMKCKA--ERVDGGYVLN-----GNKMWCTN-GPVAQTLVVYAKTDVAAGS-K 202
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1257171101 222 GLHSFLVQirdtktlLPMTGVMVGDIGKKLGQNGLDNGFAMFNKVRIPRQNLLDRTG 278
Cdd:PLN02519 203 GITAFIIE-------KGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEG 252
|
|
| |
