|
Name |
Accession |
Description |
Interval |
E-value |
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
72-481 |
0e+00 |
|
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: 754.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 72 SFAVGTFKGQLTTDQVFPYPSVLNEDQTQFLKELVGPVTRFFEEVNDAAKNDMLERVEETTMQGLKELGAFGLQVPNELG 151
Cdd:cd01161 1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 152 GVGLCNTQYARLVEIVGMyDLGVGIVLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETIAAFCLTEPSSGSDAASIRSS 231
Cdd:cd01161 81 GLGLNNTQYARLAEIVGM-DLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 232 AVPSPCGKYYTLNGSKIWISNGGLADIFTVFAKTPVTDtATGAVKEKITAFVVERSFGGVTHGPPEKKMGIKASNTAEVY 311
Cdd:cd01161 160 AVLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKD-ATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 312 FDGVRVPAENVLGEVGGGFKVAMHILNNGRFGMAAALAGTMKGIIAKAVDHAANRTQFGEKIHNFGLIQEKLARMAMLQY 391
Cdd:cd01161 239 FEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 392 VTESMAYMVSANMDQGST-DFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRL 470
Cdd:cd01161 319 ATESMAYMTSGNMDRGLKaEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRL 398
|
410
....*....|.
gi 27806205 471 FVALQGCMDKG 481
Cdd:cd01161 399 FIALTGLQHAG 409
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
94-473 |
9.20e-135 |
|
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: 399.98 E-value: 9.20e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 94 LNEDQTQFLKElvgpVTRFFEEVND--AAKNDMLERVEETTMQGLKELGAFGLQVPNELGGVGLCNTQYARLVEIVGMYD 171
Cdd:COG1960 5 LTEEQRALRDE----VREFAEEEIApeAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 172 LGVGIVLGAHQSIGfKGILLFGTKAQKEKYLPKLASGETIAAFCLTEPSSGSDAASIRSSAVPSpcGKYYTLNGSKIWIS 251
Cdd:COG1960 81 ASLALPVGVHNGAA-EALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRD--GDGYVLNGQKTFIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 252 NGGLADIFTVFAKTpvtDTATGAvkEKITAFVVERSFGGVTHGPPEKKMGIKASNTAEVYFDGVRVPAENVLGEVGGGFK 331
Cdd:COG1960 158 NAPVADVILVLART---DPAAGH--RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 332 VAMHILNNGRFGMAAALAGTMKGIIAKAVDHAANRTQFGEKIHNFGLIQEKLARMAMLQYVTESMAYMVSANMDQGsTDF 411
Cdd:COG1960 233 IAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAG-EDA 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27806205 412 QIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:COG1960 312 ALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIA 373
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
119-473 |
7.89e-120 |
|
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: 361.59 E-value: 7.89e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 119 AAKNDMLERVEETTMQGLKELGAFGLQVPNELGGVGLCNTQYARLVEIVGMYDLGVGIVLGAHQSIGFKGILLFGTKAQK 198
Cdd:cd01158 22 AAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVIVSVHNSLGANPIIKFGTEEQK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 199 EKYLPKLASGETIAAFCLTEPSSGSDAASIRSSAVPSpcGKYYTLNGSKIWISNGGLADIFTVFAktpVTDTATGavKEK 278
Cdd:cd01158 102 KKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKD--GDDYVLNGSKMWITNGGEADFYIVFA---VTDPSKG--YRG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 279 ITAFVVERSFGGVTHGPPEKKMGIKASNTAEVYFDGVRVPAENVLGEVGGGFKVAMHILNNGRFGMAAALAGTMKGIIAK 358
Cdd:cd01158 175 ITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGIAAQALGIAQAALDA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 359 AVDHAANRTQFGEKIHNFGLIQEKLARMAMLQYVTESMAYMVSANMDQGStDFQIEAAISKIFGSEAAWKVTDECIQIMG 438
Cdd:cd01158 255 AVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGE-PFIKEAAMAKLFASEVAMRVTTDAVQIFG 333
|
330 340 350
....*....|....*....|....*....|....*
gi 27806205 439 GMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:cd01158 334 GYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIA 368
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
189-473 |
9.58e-106 |
|
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: 323.47 E-value: 9.58e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 189 ILLFGTKAQKEKYLPKLASGETIAAFCLTEPSSGSDAASIRSSAVPSpcGKYYTLNGSKIWISNGGLADIFTVFAKTPvt 268
Cdd:cd00567 48 LLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKD--GDGYVLNGRKIFISNGGDADLFIVLARTD-- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 269 dtATGAVKEKITAFVVERSFGGVTHGPPEKKMGIKASNTAEVYFDGVRVPAENVLGEVGGGFKVAMHILNNGRFGMAAAL 348
Cdd:cd00567 124 --EEGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLLAAVA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 349 AGTMKGIIAKAVDHAANRTQFGEKIHNFGLIQEKLARMAMLQYVTESMAYMVSANMDQGSTDFQIEAAISKIFGSEAAWK 428
Cdd:cd00567 202 LGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFATEAARE 281
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 27806205 429 VTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:cd00567 282 VADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
94-473 |
5.35e-86 |
|
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: 274.29 E-value: 5.35e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 94 LNEDQTQfLKELVgpvTRFFEEvNDAAKNDMLERVEETTMQGLKELGAFGL---QVPNELGGVGLCNTQYARLVEIVGMY 170
Cdd:cd01156 2 LDDEIEM-LRQSV---REFAQK-EIAPLAAKIDRDNEFPRDLWRKMGKLGLlgiTAPEEYGGSGMGYLAHVIIMEEISRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 171 DLGVGIVLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETIAAFCLTEPSSGSDAASIRSSAvpSPCGKYYTLNGSKIWI 250
Cdd:cd01156 77 SGSVALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRA--EKKGDRYVLNGSKMWI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 251 SNGGLADIFTVFAKTpvtdtATGAVKEKITAFVVERSFGGVTHGPPEKKMGIKASNTAEVYFDGVRVPAENVLGEVGGGF 330
Cdd:cd01156 155 TNGPDADTLVVYAKT-----DPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 331 KVAMHILNNGRFGMAAALAGTMKGIIAKAVDHAANRTQFGEKIHNFGLIQEKLARMAMLQYVTESMAYMVSANMDQGSTD 410
Cdd:cd01156 230 YVLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMD 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27806205 411 fQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:cd01156 310 -PKDAAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIG 371
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
94-473 |
2.31e-79 |
|
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: 256.60 E-value: 2.31e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 94 LNEDQTQFLKelvgpVTRFF---EEVNDAAKNDMLERVEETTMQGLKELGAFGLQVPNELGGVGLCNTQYARLVEIVGMY 170
Cdd:cd01162 1 LNEEQRAIQE-----VARAFaakEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 171 DLGVGIVLGAHQSIGFKgILLFGTKAQKEKYLPKLASGETIAAFCLTEPSSGSDAASIRSSAVPSpcGKYYTLNGSKIWI 250
Cdd:cd01162 76 CVSTAAYISIHNMCAWM-IDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVRE--GDHYVLNGSKAFI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 251 SNGGLADIFTVFAKTpvtdTATGAvkEKITAFVVERSFGGVTHGPPEKKMGIKASNTAEVYFDGVRVPAENVLGEVGGGF 330
Cdd:cd01162 153 SGAGDSDVYVVMART----GGEGP--KGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 331 KVAMHILNNGRFGMAAALAGTMKGIIAKAVDHAANRTQFGEKIHNFGLIQEKLARMAMLQYVTESMAYMVSANMDQGSTD 410
Cdd:cd01162 227 GIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPD 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27806205 411 FQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:cd01162 307 AVKLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIA 369
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
138-475 |
2.39e-70 |
|
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: 232.78 E-value: 2.39e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 138 ELGAFGLQVPNELGGVGLcNTQYARLVEIVGMYDLGVGIVLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETIAAFCLT 217
Cdd:cd01160 41 EQGLLGVGFPEEYGGIGG-DLLSAAVLWEELARAGGSGPGLSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 218 EPSSGSDAASIRSSAVPSpcGKYYTLNGSKIWISNGGLADIFTVFAKTPVTDTATGAvkekITAFVVERSFGGVTHGPPE 297
Cdd:cd01160 120 EPGAGSDLQGIRTTARKD--GDHYVLNGSKTFITNGMLADVVIVVARTGGEARGAGG----ISLFLVERGTPGFSRGRKL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 298 KKMGIKASNTAEVYFDGVRVPAENVLGEVGGGFKVAMHILNNGRFGMAAALAGTMKGIIAKAVDHAANRTQFGEKIHNFG 377
Cdd:cd01160 194 KKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQ 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 378 LIQEKLARMAMLQYVTESMAYMVSANMDQGSTDfQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRI 457
Cdd:cd01160 274 VVRHKIAELATKVAVTRAFLDNCAWRHEQGRLD-VAEASMAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARV 352
|
330
....*....|....*...
gi 27806205 458 FRIFEGTNDILRLFVALQ 475
Cdd:cd01160 353 QPIYGGTTEIMKELISRQ 370
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
103-464 |
4.28e-62 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 212.10 E-value: 4.28e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 103 KELVGPVTRFFEEVND--AAKNDMLERVEETTMQGLKELGAFGLQVPNELGGVGLCNTQYARLVEIVGMYDLGVGIVLGA 180
Cdd:PTZ00461 42 AALRETVAKFSREVVDkhAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 181 HQSIGFKGILLFGTKAQKEKYLPKLASGETIAAFCLTEPSSGSDAASIRSSAVPSPCGKYyTLNGSKIWISNGGLADIFT 260
Cdd:PTZ00461 122 HSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGNY-VLNGSKIWITNGTVADVFL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 261 VFAKtpvtdtatgaVKEKITAFVVERSFGGVTHGPPEKKMGIKASNTAEVYFDGVRVPAENVLGEVGGGFKVAMHILNNG 340
Cdd:PTZ00461 201 IYAK----------VDGKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 341 RFGMAAALAGTMKGIIAKAVDHAANRTQFGEKIHNFGLIQEKLARMAMLQYVTESMAYMVSANMDQGSTDfQIEAAISKI 420
Cdd:PTZ00461 271 RVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKN-RLGSDAAKL 349
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 27806205 421 FGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGT 464
Cdd:PTZ00461 350 FATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGT 393
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
137-472 |
5.27e-62 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 211.66 E-value: 5.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 137 KELGAF---GLQVPNELGGVGLCNTQYARLVEIVGMYDLGVGIVLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETIAA 213
Cdd:PLN02519 66 KLMGDFnlhGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 214 FCLTEPSSGSDAASIRSSAVPSPCGkyYTLNGSKIWISNGGLADIFTVFAKTPVTDTATGavkekITAFVVERSFGGVTH 293
Cdd:PLN02519 146 LAMSEPNSGSDVVSMKCKAERVDGG--YVLNGNKMWCTNGPVAQTLVVYAKTDVAAGSKG-----ITAFIIEKGMPGFST 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 294 GPPEKKMGIKASNTAEVYFDGVRVPAENVLGEVGGGFKVAMHILNNGRFGMAAALAGTMKGIIAKAVDHAANRTQFGEKI 373
Cdd:PLN02519 219 AQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPI 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 374 HNFGLIQEKLARMAMLQYVTESMAYMVSANMDQGSTDFQiEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLR 453
Cdd:PLN02519 299 GEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRK-DCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLR 377
|
330
....*....|....*....
gi 27806205 454 DLRIFRIFEGTNDILRLFV 472
Cdd:PLN02519 378 DAKLYEIGAGTSEIRRMLI 396
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
94-473 |
5.87e-62 |
|
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: 210.91 E-value: 5.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 94 LNEDQTQFlKELVGPVTRFfEEVNDAAKNDMLERVEETTMQGLKELGAFGLQVPNELGGVGLCNTQYARLVEIVGMYDLG 173
Cdd:cd01157 1 LTEQQKEF-QETARKFARE-EIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 174 VGIVLGAHqSIGFKGILLFGTKAQKEKYLPKLASGETIAAFCLTEPSSGSDAASIRSSAVPSpcGKYYTLNGSKIWISNG 253
Cdd:cd01157 79 VQTAIEAN-SLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKK--GDEYIINGQKMWITNG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 254 GLADIFTVFAKTPvTDTATGAVKeKITAFVVERSFGGVTHGPPEKKMGIKASNTAEVYFDGVRVPAENVLGEVGGGFKVA 333
Cdd:cd01157 156 GKANWYFLLARSD-PDPKCPASK-AFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 334 MHILNNGRFGMAAALAGTMKGIIAKAVDHAANRTQFGEKIHNFGLIQEKLARMAMlQYVTESMAYMVSAN-MDQGSTDfQ 412
Cdd:cd01157 234 MGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAM-KVELARLAYQRAAWeVDSGRRN-T 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27806205 413 IEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:cd01157 312 YYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIIS 372
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
78-487 |
1.78e-61 |
|
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: 209.91 E-value: 1.78e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 78 FKGQLTTDQVfpypsVLNEDQTQFLKELVGP-VTRFFEEvndaakndmlervEETTMQGLKELGAFGL--QVPNELGGVG 154
Cdd:cd01151 9 LDDLLTEEER-----AIRDTAREFCQEELAPrVLEAYRE-------------EKFDRKIIEEMGELGLlgATIKGYGCAG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 155 LCNTQY---ARLVEIVgmyDLGVGIVLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETIAAFCLTEPSSGSDAASIRSS 231
Cdd:cd01151 71 LSSVAYgliAREVERV---DSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 232 AvpSPCGKYYTLNGSKIWISNGGLADIFTVFAKTPVTDtatgavkeKITAFVVERSFGGVTHGPPEKKMGIKASNTAEVY 311
Cdd:cd01151 148 A--RKDGGGYKLNGSKTWITNSPIADVFVVWARNDETG--------KIRGFILERGMKGLSAPKIQGKFSLRASITGEIV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 312 FDGVRVPAENVLGEV---GGGFKVamhiLNNGRFGMAAALAGTMKGIIAKAVDHAANRTQFGEKIHNFGLIQEKLARM-- 386
Cdd:cd01151 218 MDNVFVPEENLLPGAeglRGPFKC----LNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMlt 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 387 ---AMLQyvtesMAYMVSANMDQGS-TDFQIeaAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFE 462
Cdd:cd01151 294 eiaLGLL-----ACLRVGRLKDQGKaTPEQI--SLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYE 366
|
410 420
....*....|....*....|....*
gi 27806205 463 GTNDILRLFValqgcmdkGKELSGL 487
Cdd:cd01151 367 GTHDIHALIL--------GRAITGI 383
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
131-467 |
4.17e-53 |
|
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173842 [Multi-domain] Cd Length: 407 Bit Score: 187.60 E-value: 4.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 131 TTMQGLKEL-------GAFGLQVPNELGGVGLCNTQYARLVEIVGMYDLGVGIVLGAHQsiGFKGILLFGTKAQKEKYLP 203
Cdd:cd01153 33 VVPPPFKEAldafaeaGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMYASGTQG--AAATLLAHGTEAQREKWIP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 204 KLASGETIAAFCLTEPSSGSDAASIRSSAVPSPCGKYYtLNGSKIWISNG--GLAD--IFTVFAKTPvtDTATGAvkEKI 279
Cdd:cd01153 111 RLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSWR-INGVKRFISAGehDMSEniVHLVLARSE--GAPPGV--KGL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 280 TAFVV-------ERsfGGVTHGPPEKKMGIKASNTAEVYFDGVRVPaenVLGEVGGGFKVAMHILNNGRFGMAAALAGTM 352
Cdd:cd01153 186 SLFLVpkflddgER--NGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMGLAQMFAMMNGARLGVGTQGTGLA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 353 KGIIAKAVDHAANRTQFGEKIHNFGLIQEKLARMAMLQYVTESMAYMVSANMDQGSTDFQIEA----------------- 415
Cdd:cd01153 261 EAAYLNALAYAKERKQGGDLIKAAPAVTIIHHPDVRRSLMTQKAYAEGSRALDLYTATVQDLAerkategedrkalsala 340
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 27806205 416 ----AISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDI 467
Cdd:cd01153 341 dlltPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGI 396
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
94-468 |
2.76e-48 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 173.76 E-value: 2.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 94 LNEDQTQFLKELVGPVTRFFEEvNDAAKNDMLERVEETTMQGLKELGAFGLQVPNELGGVGLCNTQYARLVEIVGmyDLG 173
Cdd:PRK12341 5 LTEEQELLLASIRELITRNFPE-EYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVS--KCG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 174 VGI-VLGAHQSIgfKGILLFGTKAQKEK-YLPKLASGEtiAAFCL--TEPSSGSDAASIRSSAVPSPcGKYYtLNGSKIW 249
Cdd:PRK12341 82 APAfLITNGQCI--HSMRRFGSAEQLRKtAESTLETGD--PAYALalTEPGAGSDNNSATTTYTRKN-GKVY-LNGQKTF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 250 ISNGGLADIFTVFAKTPVTDTATGAvkekITAFVVERSFGGVTHGPPEKkMGIKASNTAEVYFDGVRVPAENVLGEVGGG 329
Cdd:PRK12341 156 ITGAKEYPYMLVLARDPQPKDPKKA----FTLWWVDSSKPGIKINPLHK-IGWHMLSTCEVYLDNVEVEESDLVGEEGMG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 330 FKVAMHILNNGRFGMAAALAGTMKGIIAKAVDHAANRTQFGEKIHNFGLIQEKLARMAMLQYVTESMAYMVSANMDQGST 409
Cdd:PRK12341 231 FLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQS 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 27806205 410 dFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDIL 468
Cdd:PRK12341 311 -LRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIM 368
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
130-470 |
5.49e-44 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 161.92 E-value: 5.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 130 ETTMQGLKELGAFGLQVPNELGGVGLCNTQYARLVEIVGMydLGVGIVLGAHQSIGFKGILLFGTKAQKEKYLPKLASGE 209
Cdd:PRK03354 40 ERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGR--LGAPTYVLYQLPGGFNTFLREGTQEQIDKIMAFRGTGK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 210 TIAAFCLTEPSSGSDAASIRSSAVPSPcGKYYtLNGSKIWISNGGLADIFTVFAKTPVTDTatgavKEKITAFVVERSFG 289
Cdd:PRK03354 118 QMWNSAITEPGAGSDVGSLKTTYTRRN-GKVY-LNGSKCFITSSAYTPYIVVMARDGASPD-----KPVYTEWFVDMSKP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 290 GVTHGPPEKkMGIKASNTAEVYFDGVRVPAENVLGEVGGGFKVAMHILNNGRFGMAAALAGTMKGIIAKAVDHAANRTQF 369
Cdd:PRK03354 191 GIKVTKLEK-LGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQF 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 370 GEKIHNFGLIQEKLARMAMLQYVTESMAYMVSANMDQGSTDfQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVE 449
Cdd:PRK03354 270 GEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTIT-SGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRIS 348
|
330 340
....*....|....*....|.
gi 27806205 450 RVLRDLRIFRIFEGTNDILRL 470
Cdd:PRK03354 349 RFWRDLRVDRVSGGSDEMQIL 369
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
327-473 |
2.61e-40 |
|
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: 144.32 E-value: 2.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 327 GGGFKVAMHILNNGRFGMAAALAGTMKGIIAKAVDHAANRTQFGEKIHNFGLIQEKLARMAMLQYVTESMAYMVSANMDQ 406
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27806205 407 GSTDfQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:pfam00441 81 GGPD-GAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
136-473 |
8.95e-38 |
|
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 144.41 E-value: 8.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 136 LKELGAFGLQVPNELGGVGLCNTQ---------YARLVEIVGMydlgVGIVLGAHQsigfkgILLFGTKAQKEKYLPKLA 206
Cdd:cd01152 44 LAAAGWAAPGWPKEYGGRGASLMEqlifreemaAAGAPVPFNQ----IGIDLAGPT------ILAYGTDEQKRRFLPPIL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 207 SGETIaaFCL--TEPSSGSDAASIRSSAVPSpcGKYYTLNGSKIWISNGGLADIFTVFAKTPvtdtaTGAVKEK-ITAFV 283
Cdd:cd01152 114 SGEEI--WCQgfSEPGAGSDLAGLRTRAVRD--GDDWVVNGQKIWTSGAHYADWAWLLVRTD-----PEAPKHRgISILL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 284 VERSFGGVTHGPPEKKMGikASNTAEVYFDGVRVPAENVLGEVGGGFKVAMHILNNGRfgmaAALAGTMKGIIAKAVDHA 363
Cdd:cd01152 185 VDMDSPGVTVRPIRSING--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFER----VSIGGSAATFFELLLARL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 364 ANRTQFGEKIHNFGLIQEKLARMAMLQYVTESMAYMVSANMDQGStDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFM 443
Cdd:cd01152 259 LLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGK-PPGAEASIAKLFGSELAQELAELALELLGTAALL 337
|
330 340 350
....*....|....*....|....*....|....*...
gi 27806205 444 KEPG--------VERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:cd01152 338 RDPApgaelagrWEADYLRSRATTIYGGTSEIQRNIIA 375
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
100-463 |
3.70e-34 |
|
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACAD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. ACAD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173844 [Multi-domain] Cd Length: 394 Bit Score: 134.44 E-value: 3.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 100 QFLKELVGPVTRFFEEVNDAAKNdmleRVEETT--MQGLKE----LGAFGLQVPNELGGVGLCNTQYARLVEIVGMYDLG 173
Cdd:cd01155 12 AFMEEHVYPAEQEFLEYYAEGGD----RWWTPPpiIEKLKAkakaEGLWNLFLPEVSGLSGLTNLEYAYLAEETGRSFFA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 174 VGIVLGAHQSIGFKGIL-LFGTKAQKEKYLPKLASGETIAAFCLTEPS-SGSDAASIRSSAVPSpcGKYYTLNGSKIWIS 251
Cdd:cd01155 88 PEVFNCQAPDTGNMEVLhRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERD--GDDYVINGRKWWSS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 252 NGGLAD--IFTVFAKTPVTDTATGAVKEKItafVVERSFGGVTHGPPEKKMGIKAS--NTAEVYFDGVRVPAENVLGEVG 327
Cdd:cd01155 166 GAGDPRckIAIVMGRTDPDGAPRHRQQSMI---LVPMDTPGVTIIRPLSVFGYDDAphGHAEITFDNVRVPASNLILGEG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 328 GGFKVAMHILNNGRFGMAAALAGTMKGIIAKAVDHAANRTQFGEKIHNFGLIQEKLA--RMA--MLQYVTESMAYMvsan 403
Cdd:cd01155 243 RGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAksRIEieQARLLVLKAAHM---- 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27806205 404 MDQ-GSTDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEG 463
Cdd:cd01155 319 IDTvGNKAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADG 379
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
81-487 |
1.29e-31 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 127.66 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 81 QLTTDQVFPyPSVLN----------EDQT------QFLKELVGPV-TRFFEEVndaakndmlerveETTMQGLKELGAFG 143
Cdd:PLN02526 8 QATPASIFP-PSVSDyyqfddlltpEEQAlrkrvrECMEKEVAPImTEYWEKA-------------EFPFHIIPKLGSLG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 144 LqvpneLGGV-------GLCNTQYARLVEIVGMYDLGVGIVLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETIAAFCL 216
Cdd:PLN02526 74 I-----AGGTikgygcpGLSITASAIATAEVARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 217 TEPSSGSDAASIRSSAVPSPCGkyYTLNGSKIWISNGGLADIFTVFAKTPVTDtatgavkeKITAFVVERSFGGVTHGPP 296
Cdd:PLN02526 149 TEPDYGSDASSLNTTATKVEGG--WILNGQKRWIGNSTFADVLVIFARNTTTN--------QINGFIVKKGAPGLKATKI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 297 EKKMGIKASNTAEVYFDGVRVPAENVLGEVgGGFKVAMHILNNGRFGMAAALAGTMKGIIAKAVDHAANRTQFGEKIHNF 376
Cdd:PLN02526 219 ENKIGLRMVQNGDIVLKDVFVPDEDRLPGV-NSFQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAF 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 377 GLIQEKLARM-----AMLQYVTESMAYMVSANMDQGstdfqiEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERV 451
Cdd:PLN02526 298 QINQEKLVRMlgniqAMFLVGWRLCKLYESGKMTPG------HASLGKAWITKKARETVALGRELLGGNGILADFLVAKA 371
|
410 420 430
....*....|....*....|....*....|....*.
gi 27806205 452 LRDLRIFRIFEGTNDILRLFValqgcmdkGKELSGL 487
Cdd:PLN02526 372 FCDLEPIYTYEGTYDINALVT--------GREITGI 399
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
199-470 |
5.21e-30 |
|
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of several genes involved in the SOS adaptive response to DNA alkylation damage, whose expression is activated by the Ada protein. Its function has not been entirely elucidated; however, it is similar in sequence and function to acyl-CoA dehydrogenases. It has been proposed that aidB directly destroys DNA alkylating agents such as nitrosoguanidines (nitrosated amides) or their reaction intermediates.
Pssm-ID: 173843 [Multi-domain] Cd Length: 418 Bit Score: 122.86 E-value: 5.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 199 EKYLPKLASGET----IAAFCLTEPSSGSDAASIRSSAVPSPcGKYYTLNGSKiWISNGGLADIFTVFAKTPVTDTATGA 274
Cdd:cd01154 132 KQYLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERSG-GGVYRLNGHK-WFASAPLADAALVLARPEGAPAGARG 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 275 vkekITAFVVERSFGGVTHGPPE-----KKMGIKASNTAEVYFDGvrvpAEN-VLGEVGGGFKVAMHILNNGRFGMAAAL 348
Cdd:cd01154 210 ----LSLFLVPRLLEDGTRNGYRirrlkDKLGTRSVATGEVEFDD----AEAyLIGDEGKGIYYILEMLNISRLDNAVAA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 349 AGTMKGIIAKAVDHAANRTQFGEKIHNFGLIQEKLARMAMLQYVTESMAYMVSANMDQGSTDFQIEA-------AISKIF 421
Cdd:cd01154 282 LGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKPVEAhmarlatPVAKLI 361
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 27806205 422 GSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRL 470
Cdd:cd01154 362 ACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQAL 410
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
213-313 |
1.95e-27 |
|
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: 106.21 E-value: 1.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 213 AFCLTEPSSGSDAASIRSSAVPSPcGKYYTLNGSKIWISNGGLADIFTVFAKTPVTDTATGavkekITAFVVERSFGGVT 292
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGD-GGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGG-----ISLFLVPKDAPGVS 74
|
90 100
....*....|....*....|.
gi 27806205 293 HGPPEKKMGIKASNTAEVYFD 313
Cdd:pfam02770 75 VRRIETKLGVRGLPTGELVFD 95
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
134-467 |
6.67e-27 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 115.74 E-value: 6.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 134 QGLKELGAFGLQVPNELGGVGLCNTQYARLVEIVGMYDLGVGIVLGahQSIG-FKGILLFGTKAQKEKYLPKLASGETIA 212
Cdd:PTZ00456 106 QALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPG--LSIGaANTLMAWGSEEQKEQYLTKLVSGEWSG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 213 AFCLTEPSSGSDAASIRSSAVPSPCGKyYTLNGSKIWISNG--GLAD--IFTVFAKTPVTDTATgavkEKITAFVVER-- 286
Cdd:PTZ00456 184 TMCLTEPQCGTDLGQVKTKAEPSADGS-YKITGTKIFISAGdhDLTEniVHIVLARLPNSLPTT----KGLSLFLVPRhv 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 287 --------SFGGVTHGPPEKKMGIKASNTAEVYFDGvrvPAENVLGEVGGGFKVAMHILNNGRFGMA------AALAgtM 352
Cdd:PTZ00456 259 vkpdgsleTAKNVKCIGLEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTARVGTAlegvchAELA--F 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 353 KGIIAKAVDHAANRTQFGEK---IHNFGLIQEKLARMAML--QYVTE---SMAYMVSANMD--QGSTDFQIEAA------ 416
Cdd:PTZ00456 334 QNALRYARERRSMRALSGTKepeKPADRIICHANVRQNILfaKAVAEggrALLLDVGRLLDihAAAKDAATREAldheig 413
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 27806205 417 ----ISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDI 467
Cdd:PTZ00456 414 fytpIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGI 468
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
72-615 |
1.17e-23 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 105.35 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 72 SFAVGTFKGQLTTDQVFPYPS-VLNEDQTQFLKELVgpvtrffeevNDAAKNDmlerveettmqglKELG-AFGLQVPNE 149
Cdd:PTZ00457 17 SYAAGLFNFKIVPEEMFPYPCrKLDGDEAENLQSLL----------EQIRSND-------------KILGnLYGARIATE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 150 LGGVGLCNTQYARLVEIVGMYdlGVGIVLGAHQSIGFKGILL--FGTKAQKEKYLPKLASGeTIAAFCLTEPSSGSDAAS 227
Cdd:PTZ00457 74 YGGLGLGHTAHALIYEEVGTN--CDSKLLSTIQHSGFCTYLLstVGSKELKGKYLTAMSDG-TIMMGWATEEGCGSDISM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 228 IRSSAVPSPCGKYyTLNGSKiWISNGGLADIFTVFAKTpVTDTATGA---VKEKITAFVVERSFGGVThgppekkmgika 304
Cdd:PTZ00457 151 NTTKASLTDDGSY-VLTGQK-RCEFAASATHFLVLAKT-LTQTAAEEgatEVSRNSFFICAKDAKGVS------------ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 305 SNTAEVYFDgvRVPAENVLGEVGGGFKVAMHILNNGRFGMAAALAGTMKGIIAKAVDHAANRTqfgekihnfglIQEKLA 384
Cdd:PTZ00457 216 VNGDSVVFE--NTPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVVQELRGSNAEEG-----------ATDTVA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 385 RMAMLQYVTESMAYMVSANMDQGSTDFQIEAAISKIFGSEAawkvTDECIQIMGGMGFMKEPgVERVLRDLRIFRIFEGT 464
Cdd:PTZ00457 283 SFACAMYAMESTLYALTANLDLPTEDSLLECTLVSAFVQST----TNQLLSILETATPPSTT-LEKCFANARLFLSMMES 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 465 NDIlrLFVALQGCmdkGKELSGLgnalknPFGNAGLLLGEAGKQLRrraglgSGLSLSGIVHQELsRSGELAVQALEQFA 544
Cdd:PTZ00457 358 RDF--LYSSAVCC---GVEDYGL------FFQRASTLQMMQARTLR------SLGVRDRVPIKNL-PDCSLIDEAVVAFG 419
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27806205 545 TVVEAKLIKHKKDIINEQFLLQRLADSAIDLYAMVVVLSRASRSLSEGHPTAQHEKMLCDSWCIEAAARIR 615
Cdd:PTZ00457 420 NAVEATFVRSGSQVPYQQLLLNRLGEAASLLYAASAVASRASMCVSKGLPSAKVEGELASAFIAMAVSRAR 490
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
95-209 |
2.00e-23 |
|
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain.
Pssm-ID: 460686 [Multi-domain] Cd Length: 113 Bit Score: 95.61 E-value: 2.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 95 NEDQTQFLKElvgpVTRFFEEV--NDAAKNDMLERVEETTMQGLKELGAFGLQVPNELGGVGLCNTQYARLVEIVGMYDL 172
Cdd:pfam02771 1 TEEQEALRDT----VREFAEEEiaPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADA 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 27806205 173 GVGIVLGAHQSIGFKGILLFGTKAQKEKYLPKLASGE 209
Cdd:pfam02771 77 SVALALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
136-441 |
1.77e-20 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 96.18 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 136 LKELGAFGLQVPNELGGVGLcnTQYA--RLVEIVGMYDLGVGIVLGAHQSIGfKGILL--FGTKAQKEKYLPKLASGETI 211
Cdd:PRK13026 117 LKKEGFFALIIPKEYGGKGF--SAYAnsTIVSKIATRSVSAAVTVMVPNSLG-PGELLthYGTQEQKDYWLPRLADGTEI 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 212 AAFCLTEPSSGSDAASIRSSAVpsPC-GKY-------YTLNGSKIWISnggLADIFTVF-----AKTPvtDTATGAVKE- 277
Cdd:PRK13026 194 PCFALTGPEAGSDAGAIPDTGI--VCrGEFegeevlgLRLTWDKRYIT---LAPVATVLglafkLRDP--DGLLGDKKEl 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 278 KITAFVVERSFGGVTHGPPEKKMGIKASNtAEVYFDGVRVPAENVLG---EVGGGFKVAMHILNNGRFGMAAALAGTMKG 354
Cdd:PRK13026 267 GITCALIPTDHPGVEIGRRHNPLGMAFMN-GTTRGKDVFIPLDWIIGgpdYAGRGWRMLVECLSAGRGISLPALGTASGH 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 355 IIAKAVD-HAANRTQFGEKIHNFGLIQEKLARMAMLQYVTESMAYMVSANMDQGSTDfQIEAAISKIFGSEAAWKVTDEC 433
Cdd:PRK13026 346 MATRTTGaYAYVRRQFGMPIGQFEGVQEALARIAGNTYLLEAARRLTTTGLDLGVKP-SVVTAIAKYHMTELARDVVNDA 424
|
....*...
gi 27806205 434 IQIMGGMG 441
Cdd:PRK13026 425 MDIHAGKG 432
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
109-578 |
5.61e-20 |
|
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: 94.32 E-value: 5.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 109 VTRFFE--EVNDAAKNDMLERVEETTMQGLKELGAFGLQVPNELGGVGLCNTQYAR--------------LVEIVGMYDL 172
Cdd:cd01150 17 LTHILEggEENLRRKREVERELESDPLFQRELPSKHLSREELYEELKRKAKTDVERmgelmaddpekmlaLTNSLGGYDL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 173 GVGIVLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETIAAFCLTEPSSGSDAASIRSSAVPSPCGKYYTLN-----GSK 247
Cdd:cd01150 97 SLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDPLTQEFVINtpdftATK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 248 IWIsnGGLADIFT---VFAKtpvtdTATGAVKEKITAFVVE-------RSFGGVTHGPPEKKMGIKASNTAEVYFDGVRV 317
Cdd:cd01150 177 WWP--GNLGKTAThavVFAQ-----LITPGKNHGLHAFIVPirdpkthQPLPGVTVGDIGPKMGLNGVDNGFLQFRNVRI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 318 PAENVL---GEV-------------GGGFKVAMHILNNGRFGMAAALAGTMKGIIAKAVDHAANRTQFGEK-------IH 374
Cdd:cd01150 250 PRENLLnrfGDVspdgtyvspfkdpNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPKpsdpevqIL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 375 NFGLIQEK----LARMAMLQYVTESMAYM---VSANMDQGSTDFQIE----AAISKIFGSEAAWKVTDECIQIMGGMGFM 443
Cdd:cd01150 330 DYQLQQYRlfpqLAAAYAFHFAAKSLVEMyheIIKELLQGNSELLAElhalSAGLKAVATWTAAQGIQECREACGGHGYL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 444 KEPGVERVLRDLRIFRIFEGTNDILRLFVAlQGCMDKGKELSGLGNALKNPFGNAGLLLGEAGKQLRRRAGLGSGLSLSG 523
Cdd:cd01150 410 AMNRLPTLRDDNDPFCTYEGDNTVLLQQTA-NYLLKKYAQAFSLADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGSFEAR 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 27806205 524 IVHQelsrsgELAVQALEQFA-TVVEAKLIKHKKDIINE--QFLLQRLAdsaiDLYAM 578
Cdd:cd01150 489 NNSQ------VHLRCAAKAHTeYTVLQRFHESVEEIVDPsvRAVLKRLC----DLYAL 536
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
88-446 |
4.79e-19 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 91.80 E-value: 4.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 88 FPYPSVLNEDQTqFLKelvGPVTRFFEEVNDAAKNDMLERVEETTMQGLKELGAFGLQVPNELGGVGLCNTQYARLVEIV 167
Cdd:PRK09463 74 YPKPTLTAEEQA-FLD---GPVEELCRMVNDWQITHELADLPPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 168 GMYDLGVGIVLGAHQSIGfKGILL--FGTKAQKEKYLPKLASGETIAAFCLTEPSSGSDAASIRSSAVpsPC-----GK- 239
Cdd:PRK09463 150 ASRSGTLAVTVMVPNSLG-PGELLlhYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGV--VCkgewqGEe 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 240 --YYTLNGSKIWISnggLADIFTVF-----AKTPvtDTATGAVKE-KITAFVVERSFGGVTHGPPEKKMGIkasntaeVY 311
Cdd:PRK09463 227 vlGMRLTWNKRYIT---LAPIATVLglafkLYDP--DGLLGDKEDlGITCALIPTDTPGVEIGRRHFPLNV-------PF 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 312 FDG------VRVPAENVLGE---VGGGFKVAMHILNNGRFGMAAALAGTMKGIIAKAV-DHAANRTQFGEKIHNFGLIQE 381
Cdd:PRK09463 295 QNGptrgkdVFIPLDYIIGGpkmAGQGWRMLMECLSVGRGISLPSNSTGGAKLAALATgAYARIRRQFKLPIGKFEGIEE 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27806205 382 KLARMAMLQYVTESMAYMVSANMDQGSTDFQIeAAISKIFGSEAAWKVTDECIQIMGGMGFMKEP 446
Cdd:PRK09463 375 PLARIAGNAYLMDAARTLTTAAVDLGEKPSVL-SAIAKYHLTERGRQVINDAMDIHGGKGICLGP 438
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
159-473 |
2.19e-18 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 89.53 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 159 QYARLVEIVGMYDLGVGIVLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETIAAFCLTEPSSGSDAASIRSSAVPSPCG 238
Cdd:PLN02636 122 KYFAITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLT 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 239 KYYTLN-----GSKIWISNGGLADIF-TVFAK--TPVTDtATGAVKEKITAFVV-------ERSFGGVTHGPPEKKMGIK 303
Cdd:PLN02636 202 DEFVINtpndgAIKWWIGNAAVHGKFaTVFARlkLPTHD-SKGVSDMGVHAFIVpirdmktHQVLPGVEIRDCGHKVGLN 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 304 ASNTAEVYFDGVRVPAENVLGEVG-----GGFKVAMHILNN-----------GRFGMAAALAGTMKGIIAKAVDHAANRT 367
Cdd:PLN02636 281 GVDNGALRFRSVRIPRDNLLNRFGdvsrdGKYTSSLPTINKrfaatlgelvgGRVGLAYGSVGVLKASNTIAIRYSLLRQ 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 368 QFGE------KIHNFGLIQEKLarMAML----------QYVTESMAYMVSANMDQGSTDFQIEAAISKIFGSEAAWKVTD 431
Cdd:PLN02636 361 QFGPpkqpeiSILDYQSQQHKL--MPMLastyafhfatEYLVERYSEMKKTHDDQLVADVHALSAGLKAYITSYTAKALS 438
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 27806205 432 ECIQIMGGMGFmkePGVER--VLR-DLRIFRIFEGTNDILRLFVA 473
Cdd:PLN02636 439 TCREACGGHGY---AAVNRfgSLRnDHDIFQTFEGDNTVLLQQVA 480
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
148-467 |
1.04e-17 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 87.54 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 148 NELGGVGLCNTQYARLVEIVGMYDLGVGIV-LGAHQSIGFKGILLFGTKAQKEKYLPKLASGETIAAFCLTEPS-SGSDA 225
Cdd:PLN02876 487 DQLLGAGLSNLEYGYLCEIMGRSVWAPQVFnCGAPDTGNMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDA 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 226 ASIRSSAVPSpcGKYYTLNGSKIWISngGLAD----IFTVFAKTPVT------------DTATGAVKEKITAFVVerSFG 289
Cdd:PLN02876 567 TNIECSIRRQ--GDSYVINGTKWWTS--GAMDprcrVLIVMGKTDFNapkhkqqsmilvDIQTPGVQIKRPLLVF--GFD 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 290 GVTHGppekkmgikasnTAEVYFDGVRVPAENVLGEVGGGFKVAMHILNNGRFGMAAALAGTMKGIIAKAVDHAANRTQF 369
Cdd:PLN02876 641 DAPHG------------HAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAF 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 370 GEKIHNFGLIQEKLARmamLQYVTESMAYMVSANMDQ----GSTDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKE 445
Cdd:PLN02876 709 GKLIAQHGSFLSDLAK---CRVELEQTRLLVLEAADQldrlGNKKARGIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSD 785
|
330 340
....*....|....*....|..
gi 27806205 446 PGVERVLRDLRIFRIFEGTNDI 467
Cdd:PLN02876 786 TVLAHLWATARTLRIADGPDEV 807
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
136-456 |
4.99e-09 |
|
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, which catalyzes the first two steps of DBT desulfurization in mesophilic bacteria. DszC converts DBT to DBT-sulfoxide, which is then converted to DBT-sulfone. Bacteria with this enzyme are candidates for the removal of organic sulfur compounds from fossil fuels, which pollute the environment. An equivalent enzyme tdsC, is found in thermophilic bacteria. This alignment also contains a closely related uncharacterized subgroup.
Pssm-ID: 173852 [Multi-domain] Cd Length: 377 Bit Score: 58.49 E-value: 4.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 136 LKELGAFGLQVPNELGGVGLCNTQYARLVEIVGMYDLGVGIVLGAHqsIGF-KGILLFGTKAQKEKYLPKLASGETIAAf 214
Cdd:cd01163 31 LRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAH--FGFvEALLLAGPEQFRKRWFGRVLNGWIFGN- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 215 clTEPSSGSDAASIRSSAVPSPCGKYYtLNGSKiWISNGGL-ADIFTVFAKTPVtdtatgavkEKITAFVVERSFGGVTH 293
Cdd:cd01163 108 --AVSERGSVRPGTFLTATVRDGGGYV-LNGKK-FYSTGALfSDWVTVSALDEE---------GKLVFAAVPTDRPGITV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 294 GPPEKKMGIK--ASNTAEvyFDGVRVPAENVLGEvGGGFKVAMHILNNGRFGMAAALAGTMKGIIAKAVDHAANRTQF-- 369
Cdd:cd01163 175 VDDWDGFGQRltASGTVT--FDNVRVEPDEVLPR-PNAPDRGTLLTAIYQLVLAAVLAGIARAALDDAVAYVRSRTRPwi 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 370 ---GEKIHNFGLIQEKLARMAMLQYVTESMAYMVSANMDQGSTDFQ-------IEAAIS----KIFGSEAAWKVTDECIQ 435
Cdd:cd01163 252 hsgAESARDDPYVQQVVGDLAARLHAAEALVLQAARALDAAAAAGTaltaearGEAALAvaaaKVVVTRLALDATSRLFE 331
|
330 340
....*....|....*....|.
gi 27806205 436 IMGGMGFMKEPGVERVLRDLR 456
Cdd:cd01163 332 VGGASATAREHNLDRHWRNAR 352
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
122-488 |
1.64e-08 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 57.86 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 122 NDMLERVEETTM---QGLKELGAF-----GLQVPNELggvglcntQYARLVEIVGMYDLGVGIVLGAHQSIGFKGILLFG 193
Cdd:PLN02312 97 NQTMEQQREITMkriLYLLERGVFrgwltETGPEAEL--------RKLALLEVIGIYDHSLAIKLGVHFFLWGGAIKFLG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 194 TKAQKEKYLPKLASGETIAAFCLTEPSSGSDAASIRSSAVPSPCGKYYTLN-----GSKIWIsnGGLADIFT---VFAKT 265
Cdd:PLN02312 169 TKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFVINtpcesAQKYWI--GGAANHAThtiVFSQL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 266 PVTdtatgAVKEKITAFVVE------RSFGGVTHGPPEKKMGIKASNTAEVYFDGVRVPAENVLGEV-----GGGFKVA- 333
Cdd:PLN02312 247 HIN-----GKNEGVHAFIAQirdqdgNICPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNSVadvspDGKYVSAi 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 334 ----------MHILNNGRFGMAAALAGTMKGIIAKAVDHAANRTQF-----GEKI-------HNFGLIqEKLARMAMLQY 391
Cdd:PLN02312 322 kdpdqrfgafLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAFsvtpnGPEVllldypsHQRRLL-PLLAKTYAMSF 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 392 VTESMAYMVSANMDQGSTDFQIeaaISKIFGSEAAW---KVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDIL 468
Cdd:PLN02312 401 AANDLKMIYVKRTPESNKAIHV---VSSGFKAVLTWhnmRTLQECREACGGQGLKTENRVGQLKAEYDVQSTFEGDNNVL 477
|
410 420
....*....|....*....|....*.
gi 27806205 469 R------LFVALQGCMDKGKELSGLG 488
Cdd:PLN02312 478 MqqvskaLLAEYVSAKKRNKPFKGLG 503
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
343-465 |
1.14e-07 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 51.19 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 343 GMAAALAGTMKGIIAKAVDHAANRTQ--FGEKIHNFGLIQEKLARMA-------MLQYVTESMAYMVSANMDQGSTDFQI 413
Cdd:pfam08028 1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAaridaarLLLERAAARIEAAAAAGKPVTPALRA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 27806205 414 EAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTN 465
Cdd:pfam08028 81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVN 132
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
216-479 |
1.52e-07 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 54.37 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 216 LTEPSSGSDAASIRSSAVPSPcGKYYTLNGSKiWISNGGLADIFTVFAKTpvtdtatgavKEKITAFVVERSFGGVTHGP 295
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAERLA-DGSYRLVGHK-WFFSVPQSDAHLVLAQA----------KGGLSCFFVPRFLPDGQRNA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 296 P-----EKKMGIKASNTAEVYFDGVrvpAENVLGEVGGGFKvamHILNNG---RFGMAAALAGTMKGIIAKAVDHAANRT 367
Cdd:PRK11561 252 IrlerlKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIR---LILKMGgmtRFDCALGSHGLMRRAFSVAIYHAHQRQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 368 QFGEKIHNFGLIQEKLARMAM-LQYVTESMAYMVSANMDQGSTDfqiEAAISKIFGSEAAWKVTD-------ECIQIMGG 439
Cdd:PRK11561 326 VFGKPLIEQPLMRQVLSRMALqLEGQTALLFRLARAWDRRADAK---EALWARLFTPAAKFVICKrgipfvaEAMEVLGG 402
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 27806205 440 MGFMKEPGVERVLRDLRIFRIFEGTN-----DILRLFVALQGCMD 479
Cdd:PRK11561 403 IGYCEESELPRLYREMPVNSIWEGSGnimclDVLRVLNKQPGVYD 447
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
119-456 |
1.90e-05 |
|
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, which is active against Gram-positive bacteria. Polyketides are secondary metabolites, which have important biological functions such as antitumor, immunosupressive or antibiotic activities. NcnH is a hydroxylase involved in the biosynthesis of naphthocyclinone and possibly other polyketides.
Pssm-ID: 173848 [Multi-domain] Cd Length: 370 Bit Score: 47.34 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 119 AAKNDMLERVEETTMQGLKELGAFGLQVPNELGGVGLCNTQYARLVEIVGMYDLGVGIV---LGAHQSIGfkgiLLFGTK 195
Cdd:cd01159 14 APEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVasiVATHSRML----AAFPPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 196 AQKEKYlpklasgetiaafcltepSSGSDAASIRSSAV---PSPCGKYYTLNGSKIWISNGGLADIftVFAKTPVTDTAT 272
Cdd:cd01159 90 AQEEVW------------------GDGPDTLLAGSYAPggrAERVDGGYRVSGTWPFASGCDHADW--ILVGAIVEDDDG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 273 GavkEKITAFVVERSfgGVTHGPPEKKMGIKASNTAEVYFDGVRVPAENVLgEVGGGFKVAMHILNNGRF---------- 342
Cdd:cd01159 150 G---PLPRAFVVPRA--EYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTL-TAGDMMAGDGPGGSTPVYrmplrqvfpl 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 343 GMAAALAGTMKGIIAKAVDHAANRTQ---FGEKIHNFGLIQEKLARMAMLQYVTESMAY-MVSANMDQGSTDFQIEAAIS 418
Cdd:cd01159 224 SFAAVSLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAELDAARAFLErATRDLWAHALAGGPIDVEER 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 27806205 419 KIFGSEAAWkVTDECIQI-------MGGMGFMKEPGVERVLRDLR 456
Cdd:cd01159 304 ARIRRDAAY-AAKLSAEAvdrlfhaAGGSALYTASPLQRIWRDIH 347
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
193-501 |
2.46e-05 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 47.52 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 193 GTKAQKEKYLPKLASGETIAAFCLTEPSSGSDAASIRSSAVPSPCGKYY-----TLNGSKIWisNGGLADIFT---VFAK 264
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFvihspTLTSSKWW--PGGLGKVSThavVYAR 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 265 tpvtdTATGAVKEKITAFVVE-RSFG------GVTHGPPEKKMGIKASNTAE---VYFDGVRVPAENVLGEVgggfkvaM 334
Cdd:PLN02443 192 -----LITNGKDHGIHGFIVQlRSLDdhsplpGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQMLMRL-------S 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 335 HILNNGRFGMAAA----LAGTM----KGIIAK-----------AVDHAANRTQFGEK-------IHNFGLIQEK----LA 384
Cdd:PLN02443 260 KVTREGKYVQSDVprqlVYGTMvyvrQTIVADastalsravciATRYSAVRRQFGSQdggpetqVIDYKTQQSRlfplLA 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 385 RMAMLQYVTESMAYMVSANMDQ-GSTDF----QIEAAIS--KIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRI 457
Cdd:PLN02443 340 SAYAFRFVGEWLKWLYTDVTQRlEANDFstlpEAHACTAglKSLTTSATADGIEECRKLCGGHGYLCSSGLPELFAVYVP 419
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 27806205 458 FRIFEGTNDILRLFVAlQGCMdkgKELSGLGNAlKNPFGNAGLL 501
Cdd:PLN02443 420 ACTYEGDNVVLLLQVA-RFLM---KTVSQLGSG-KKPVGTTAYM 458
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
193-473 |
3.43e-04 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 43.68 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 193 GTKAQKEKYLPKLASGETIAAFCLTEPSSGSDAASIRSSAVPSPCGKYYTLN-----GSKIWISN-GGLADIFTVFAKTP 266
Cdd:PTZ00460 110 GTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHtpsveAVKFWPGElGFLCNFALVYAKLI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 267 VTDTATG--AVKEKITAFVVERSFGGVTHGPPEKKMGIKASNTAEVYFDGVRVPAENVLG---EVGGGFKVAMHilNNGR 341
Cdd:PTZ00460 190 VNGKNKGvhPFMVRIRDKETHKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLAryiKVSEDGQVERQ--GNPK 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 342 FGMAAALagTMKGIIAK------------AVDHAANRTQFGE------KIHNFGLIQEKL-ARMAMLQ---YVTESMAYM 399
Cdd:PTZ00460 268 VSYASMM--YMRNLIIDqyprfaaqaltvAIRYSIYRQQFTNdnkqenSVLEYQTQQQKLlPLLAEFYaciFGGLKIKEL 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806205 400 VSANMDQ-GSTDFQIEAAISKIFGSEAAW------KVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFV 472
Cdd:PTZ00460 346 VDDNFNRvQKNDFSLLQLTHAILSAAKANytyfvsNCAEWCRLSCGGHGYAHYSGLPAIYFDMSPNITLEGENQIMYLQL 425
|
.
gi 27806205 473 A 473
Cdd:PTZ00460 426 A 426
|
|
| |
