|
Name |
Accession |
Description |
Interval |
E-value |
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
50-459 |
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: 747.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 50 SFAVGMFKGQLTTDQVFPYPSVLNEEQTQFLKELVEPVSRFFEEVNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELG 129
Cdd:cd01161 1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 130 GVGLCNTQYARLVEIVGMhDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTS 209
Cdd:cd01161 81 GLGLNNTQYARLAEIVGM-DLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 210 AVPSPCGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPaTGAVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVF 289
Cdd:cd01161 160 AVLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDA-TGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 290 FDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQY 369
Cdd:cd01161 239 FEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 370 VTESMAYMVSANMDQGAT-DFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRL 448
Cdd:cd01161 319 ATESMAYMTSGNMDRGLKaEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRL 398
|
410
....*....|.
gi 76496475 449 FVALQGCMDKG 459
Cdd:cd01161 399 FIALTGLQHAG 409
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
72-451 |
1.66e-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: 401.14 E-value: 1.66e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 72 LNEEQTQFLKElvepVSRFFEEVNDP--AKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHD 149
Cdd:COG1960 5 LTEEQRALRDE----VREFAEEEIAPeaREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 150 LGVGITLGAHQSIGfKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWIS 229
Cdd:COG1960 81 ASLALPVGVHNGAA-EALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRD--GDGYVLNGQKTFIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 230 NGGLADIFTVFAKTpvtDPATGAvkEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFK 309
Cdd:COG1960 158 NAPVADVILVLART---DPAAGH--RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 310 VAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGAtDF 389
Cdd:COG1960 233 IAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGE-DA 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 76496475 390 QIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 451
Cdd:COG1960 312 ALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIA 373
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
74-451 |
1.52e-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: 362.74 E-value: 1.52e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 74 EEQTQFLKElvepVSRFFEEVNDP--AKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLG 151
Cdd:cd01158 1 EEHQMIRKT----VRDFAEKEIAPlaAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 152 VGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNG 231
Cdd:cd01158 77 VAVIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKD--GDDYVLNGSKMWITNG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 232 GLADIFTVFAktpVTDPATGavKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVA 311
Cdd:cd01158 155 GEADFYIVFA---VTDPSKG--YRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 312 MHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGaTDFQI 391
Cdd:cd01158 230 MQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNG-EPFIK 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 392 EAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 451
Cdd:cd01158 309 EAAMAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIA 368
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
167-451 |
1.88e-103 |
|
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: 316.92 E-value: 1.88e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 167 ILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNGGLADIFTVFAKTPVT 246
Cdd:cd00567 48 LLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKD--GDGYVLNGRKIFISNGGDADLFIVLARTDEE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 247 DPATGAvkekITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAAL 326
Cdd:cd00567 126 GPGHRG----ISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLLAAVA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 327 AGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQIEAAISKIFGSEAAWK 406
Cdd:cd00567 202 LGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFATEAARE 281
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 76496475 407 VTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 451
Cdd:cd00567 282 VADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
72-451 |
1.14e-90 |
|
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: 285.84 E-value: 1.14e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 72 LNEEQTQflkeLVEPVSRFFEEVNDP--AKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHD 149
Cdd:cd01156 2 LDDEIEM----LRQSVREFAQKEIAPlaAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRAS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 150 LGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAvpSPCGKYYTLNGSKLWIS 229
Cdd:cd01156 78 GSVALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRA--EKKGDRYVLNGSKMWIT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 230 NGGLADIFTVFAKTpvtDPATGAvkEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFK 309
Cdd:cd01156 156 NGPDADTLVVYAKT---DPSAGA--HGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 310 VAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDf 389
Cdd:cd01156 231 VLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMD- 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 76496475 390 QIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 451
Cdd:cd01156 310 PKDAAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIG 371
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
116-451 |
5.91e-78 |
|
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: 252.36 E-value: 5.91e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 116 ELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGAHQSIGFKgILLFGTKAQKEKYLPKLASGETVAAFCLT 195
Cdd:cd01162 43 ELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAAYISIHNMCAWM-IDSFGNDEQRERFLPDLCTMEKLASYCLT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 196 EPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNGGLADIFTVFAKTpvtdpaTGAVKEKITAFVVERGFGGITHGPPE 275
Cdd:cd01162 122 EPGSGSDAAALRTRAVRE--GDHYVLNGSKAFISGAGDSDVYVVMART------GGEGPKGISCFVVEKGTPGLSFGANE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 276 KKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFG 355
Cdd:cd01162 194 KKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQ 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 356 LIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRI 435
Cdd:cd01162 274 ALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRV 353
|
330
....*....|....*.
gi 76496475 436 FRIFEGTNDILRLFVA 451
Cdd:cd01162 354 HQILEGTNEIMRLIIA 369
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
87-453 |
1.14e-73 |
|
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: 241.25 E-value: 1.14e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 87 VSRFFEEVNDP--AKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLcNTQYARLVEIVGMHDLGVGITLGAHQSIGF 164
Cdd:cd01160 10 VRRFFAKEVAPfhHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGG-DLLSAAVLWEELARAGGSGPGLSLHTDIVS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 165 KGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNGGLADIFTVFAKTp 244
Cdd:cd01160 89 PYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKD--GDHYVLNGSKTFITNGMLADVVIVVART- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 245 vTDPATGAvkEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAA 324
Cdd:cd01160 166 -GGEARGA--GGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 325 ALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDfQIEAAISKIFGSEAA 404
Cdd:cd01160 243 GALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLD-VAEASMAKYWATELQ 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 76496475 405 WKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVALQ 453
Cdd:cd01160 322 NRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQ 370
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
74-450 |
1.42e-65 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 220.90 E-value: 1.42e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 74 EEQTQFLKELVEPVSRFFEEVNDPAKNDALemveettWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVG 153
Cdd:PLN02519 35 ESVQQFAQENIAPHAAAIDATNSFPKDVNL-------WKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 154 ITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGkyYTLNGSKLWISNGGL 233
Cdd:PLN02519 108 LSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGG--YVLNGNKMWCTNGPV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 234 ADIFTVFAKTpvtDPATGAvkEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMH 313
Cdd:PLN02519 186 AQTLVVYAKT---DVAAGS--KGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 314 ILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQiEA 393
Cdd:PLN02519 261 GLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRK-DC 339
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 76496475 394 AISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFV 450
Cdd:PLN02519 340 AGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLI 396
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
56-465 |
8.69e-64 |
|
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: 215.30 E-value: 8.69e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 56 FKGQLTTDQVfpypsVLNEEQTQFLKELVEP--VSRFFEEVNDPakndalEMVEEttwqgLKELGAFGLQvPSELGGVGL 133
Cdd:cd01151 9 LDDLLTEEER-----AIRDTAREFCQEELAPrvLEAYREEKFDR------KIIEE-----MGELGLLGAT-IKGYGCAGL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 134 CNTQY---ARLVEIVgmhDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSA 210
Cdd:cd01151 72 SSVAYgliAREVERV---DSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 211 vpSPCGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDpatgavkeKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFF 290
Cdd:cd01151 149 --RKDGGGYKLNGSKTWITNSPIADVFVVWARNDETG--------KIRGFILERGMKGLSAPKIQGKFSLRASITGEIVM 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 291 DGVRVPSENVLGEVgSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARM-VMLQY 369
Cdd:cd01151 219 DNVFVPEENLLPGA-EGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMlTEIAL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 370 VTEsMAYMVSANMDQG-ATDFQIeaAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRL 448
Cdd:cd01151 298 GLL-ACLRVGRLKDQGkATPEQI--SLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHAL 374
|
410
....*....|....*..
gi 76496475 449 FValqgcmdkGKELSGL 465
Cdd:cd01151 375 IL--------GRAITGI 383
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
72-451 |
1.09e-63 |
|
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: 214.76 E-value: 1.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 72 LNEEQtqflKELVEPVSRFFEEVNDPAKNDaLEMVEETTWQGLK---ELGAFGLQVPSELGGVGLCNTQYARLVEIVGMH 148
Cdd:cd01157 1 LTEQQ----KEFQETARKFAREEIIPVAAE-YDKSGEYPWPLIKrawELGLMNTHIPEDCGGLGLGTFDTCLITEELAYG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 149 DLGVGITLGAHqSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWI 228
Cdd:cd01157 76 CTGVQTAIEAN-SLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKK--GDEYIINGQKMWI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 229 SNGGLADIFTVFAKTPvTDPATGAVKeKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGF 308
Cdd:cd01157 153 TNGGKANWYFLLARSD-PDPKCPASK-AFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 309 KVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMlQYVTESMAYMVSAN-MDQGAT 387
Cdd:cd01157 231 KIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAM-KVELARLAYQRAAWeVDSGRR 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 76496475 388 DfQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 451
Cdd:cd01157 310 N-TYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIIS 372
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
81-442 |
8.47e-63 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 213.65 E-value: 8.47e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 81 KELVEPVSRFFEEVNDP-AKNDALEM-VEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGA 158
Cdd:PTZ00461 42 AALRETVAKFSREVVDKhAREDDINMhFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 159 HQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYyTLNGSKLWISNGGLADIFT 238
Cdd:PTZ00461 122 HSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGNY-VLNGSKIWITNGTVADVFL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 239 VFAKtpvtdpatgaVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNG 318
Cdd:PTZ00461 201 IYAK----------VDGKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 319 RFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDfQIEAAISKI 398
Cdd:PTZ00461 271 RVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKN-RLGSDAAKL 349
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 76496475 399 FGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGT 442
Cdd:PTZ00461 350 FATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGT 393
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
116-445 |
1.80e-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: 188.37 E-value: 1.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 116 ELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGAHQsiGFKGILLFGTKAQKEKYLPKLASGETVAAFCLT 195
Cdd:cd01153 47 EAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMYASGTQG--AAATLLAHGTEAQREKWIPRLAEGEWTGTMCLT 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 196 EPSSGSDAASIRTSAVPSPCGKYYtLNGSKLWISNG--GLAD--IFTVFAKTPvtDPATGAvkEKITAFVV-------ER 264
Cdd:cd01153 125 EPDAGSDLGALRTKAVYQADGSWR-INGVKRFISAGehDMSEniVHLVLARSE--GAPPGV--KGLSLFLVpkflddgER 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 265 GfgGITHGPPEKKMGIKASNTAEVFFDGVRVPsenVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNR 344
Cdd:cd01153 200 N--GVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKER 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 345 TQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMD-----------QGATDFQIEAA----------ISKIFGSEA 403
Cdd:cd01153 275 KQGGDLIKAAPAVTIIHHPDVRRSLMTQKAYAEGSRALDlytatvqdlaeRKATEGEDRKAlsaladlltpVVKGFGSEA 354
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 76496475 404 AWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDI 445
Cdd:cd01153 355 ALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGI 396
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
72-446 |
1.09e-49 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 177.23 E-value: 1.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 72 LNEEQTQFLKELVEPVSRFFEEvNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEivGMHDLG 151
Cdd:PRK12341 5 LTEEQELLLASIRELITRNFPE-EYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLE--EVSKCG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 152 VGITLgAHQSIGFKGILLFGTKAQKEKYLpKLASGETVAAFCL--TEPSSGSDAASIRTSAVPSPcGKYYtLNGSKLWIS 229
Cdd:PRK12341 82 APAFL-ITNGQCIHSMRRFGSAEQLRKTA-ESTLETGDPAYALalTEPGAGSDNNSATTTYTRKN-GKVY-LNGQKTFIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 230 NGGLADIFTVFAKtpvtDPATGAVKEKITAFVVERGFGGITHGPPEKkMGIKASNTAEVFFDGVRVPSENVLGEVGSGFK 309
Cdd:PRK12341 158 GAKEYPYMLVLAR----DPQPKDPKKAFTLWWVDSSKPGIKINPLHK-IGWHMLSTCEVYLDNVEVEESDLVGEEGMGFL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 310 VAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATdF 389
Cdd:PRK12341 233 NVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQS-L 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 76496475 390 QIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDIL 446
Cdd:PRK12341 312 RTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIM 368
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
112-448 |
6.25e-42 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 156.14 E-value: 6.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 112 QGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMhdLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAA 191
Cdd:PRK03354 44 KALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGR--LGAPTYVLYQLPGGFNTFLREGTQEQIDKIMAFRGTGKQMWN 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 192 FCLTEPSSGSDAASIRTSAVPSPcGKYYtLNGSKLWISNGGLADIFTVFAKTPVTDPatgavKEKITAFVVERGFGGITH 271
Cdd:PRK03354 122 SAITEPGAGSDVGSLKTTYTRRN-GKVY-LNGSKCFITSSAYTPYIVVMARDGASPD-----KPVYTEWFVDMSKPGIKV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 272 GPPEKkMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKI 351
Cdd:PRK03354 195 TKLEK-LGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAI 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 352 HNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDfQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLR 431
Cdd:PRK03354 274 GRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTIT-SGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWR 352
|
330
....*....|....*..
gi 76496475 432 DLRIFRIFEGTNDILRL 448
Cdd:PRK03354 353 DLRVDRVSGGSDEMQIL 369
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
305-451 |
8.17e-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: 142.78 E-value: 8.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 305 GSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQ 384
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 76496475 385 GATDfQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 451
Cdd:pfam00441 81 GGPD-GAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
110-451 |
4.93e-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: 145.18 E-value: 4.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 110 TWQG-LKELGAFGLQVPSELGGVGLCNTQYARLVE---IVGM--HDLGVGITLGAHQsigfkgILLFGTKAQKEKYLPKL 183
Cdd:cd01152 39 RWQRaLAAAGWAAPGWPKEYGGRGASLMEQLIFREemaAAGApvPFNQIGIDLAGPT------ILAYGTDEQKRRFLPPI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 184 ASGETVaaFCL--TEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNGGLADIFTVFAKTpvtDPAtgAVKEK-ITAF 260
Cdd:cd01152 113 LSGEEI--WCQgfSEPGAGSDLAGLRTRAVRD--GDDWVVNGQKIWTSGAHYADWAWLLVRT---DPE--APKHRgISIL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 261 VVERGFGGITHGPPEKKMGikASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAvdH 340
Cdd:cd01152 184 LVDMDSPGVTVRPIRSING--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIGGSAATFFELLLARL--L 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 341 ATNRTQFGEkiHNFGLIQEKLARMVM----LQYVTESMAYMVSANMDQGAtdfqiEAAISKIFGSEAAWKVTDECIQIMG 416
Cdd:cd01152 260 LLTRDGRPL--IDDPLVRQRLARLEAeaeaLRLLVFRLASALAAGKPPGA-----EASIAKLFGSELAQELAELALELLG 332
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 76496475 417 GMGFMKEPG--------VERVLRDLRIFRIFEGTNDILRLFVA 451
Cdd:cd01152 333 TAALLRDPApgaelagrWEADYLRSRATTIYGGTSEIQRNIIA 375
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
80-441 |
2.45e-35 |
|
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: 137.52 E-value: 2.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 80 LKELVEPVSRFFEEVNDPAKNDALEMVEE---TTWQ------GLKE----LGAFGLQVPSELGGVGLCNTQYARLVEIVG 146
Cdd:cd01155 3 AQELRARVKAFMEEHVYPAEQEFLEYYAEggdRWWTpppiieKLKAkakaEGLWNLFLPEVSGLSGLTNLEYAYLAEETG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 147 MHDLGVGITLGAHQSIGFKGIL-LFGTKAQKEKYLPKLASGETVAAFCLTEPS-SGSDAASIRTSAVPSpcGKYYTLNGS 224
Cdd:cd01155 83 RSFFAPEVFNCQAPDTGNMEVLhRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERD--GDDYVINGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 225 KLWISNGGLAD--IFTVFAKTpvtDPATGAVKEKITAFVVERGFGGITHGPPEKKMGIKAS--NTAEVFFDGVRVPSENV 300
Cdd:cd01155 161 KWWSSGAGDPRckIAIVMGRT---DPDGAPRHRQQSMILVPMDTPGVTIIRPLSVFGYDDAphGHAEITFDNVRVPASNL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 301 LGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLA--RMV--MLQYVTESMAY 376
Cdd:cd01155 238 ILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAksRIEieQARLLVLKAAH 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 76496475 377 MvsanMDQ-GATDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEG 441
Cdd:cd01155 318 M----IDTvGNKAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADG 379
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
59-467 |
9.87e-34 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 133.44 E-value: 9.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 59 QLTTDQVFPyPSVLN----------EEQT------QFLKELVEPV-SRFFEEVNDPakndalemveettWQGLKELGAFG 121
Cdd:PLN02526 8 QATPASIFP-PSVSDyyqfddlltpEEQAlrkrvrECMEKEVAPImTEYWEKAEFP-------------FHIIPKLGSLG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 122 LqvpseLGGV-------GLCNTQYARLVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCL 194
Cdd:PLN02526 74 I-----AGGTikgygcpGLSITASAIATAEVARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 195 TEPSSGSDAASIRTSAVPSPCGkyYTLNGSKLWISNGGLADIFTVFAKTPVTDpatgavkeKITAFVVERGFGGITHGPP 274
Cdd:PLN02526 149 TEPDYGSDASSLNTTATKVEGG--WILNGQKRWIGNSTFADVLVIFARNTTTN--------QINGFIVKKGAPGLKATKI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 275 EKKMGIKASNTAEVFFDGVRVPSENVLGEVGSgFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNF 354
Cdd:PLN02526 219 ENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNS-FQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAF 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 355 GLIQEKLARmvMLQYVtESMAYM--------VSANMDQGatdfqiEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGV 426
Cdd:PLN02526 298 QINQEKLVR--MLGNI-QAMFLVgwrlcklyESGKMTPG------HASLGKAWITKKARETVALGRELLGGNGILADFLV 368
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 76496475 427 ERVLRDLRIFRIFEGTNDILRLFValqgcmdkGKELSGLGS 467
Cdd:PLN02526 369 AKAFCDLEPIYTYEGTYDINALVT--------GREITGIAS 401
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
177-448 |
2.06e-31 |
|
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: 126.72 E-value: 2.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 177 EKYLPKLASGET----VAAFCLTEPSSGSDAASIRTSAVPSPcGKYYTLNGSKlWISNGGLADIFTVFAKTPVTDPATGA 252
Cdd:cd01154 132 KQYLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERSG-GGVYRLNGHK-WFASAPLADAALVLARPEGAPAGARG 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 253 vkekITAFVVER-----GFGGITHGPPEKKMGIKASNTAEVFFDGvrvpSEN-VLGEVGSGFKVAMHILNNGRFGMAAAL 326
Cdd:cd01154 210 ----LSLFLVPRlledgTRNGYRIRRLKDKLGTRSVATGEVEFDD----AEAyLIGDEGKGIYYILEMLNISRLDNAVAA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 327 AGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQIEA-------AISKIF 399
Cdd:cd01154 282 LGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKPVEAhmarlatPVAKLI 361
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 76496475 400 GSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRL 448
Cdd:cd01154 362 ACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQAL 410
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
108-445 |
2.09e-28 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 120.36 E-value: 2.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 108 ETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGahQSIG-FKGILLFGTKAQKEKYLPKLASG 186
Cdd:PTZ00456 102 KEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPG--LSIGaANTLMAWGSEEQKEQYLTKLVSG 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 187 ETVAAFCLTEPSSGSDAASIRTSAVPSPCGKyYTLNGSKLWISNG--GLAD--IFTVFAKTPVTDPATgavkEKITAFVV 262
Cdd:PTZ00456 180 EWSGTMCLTEPQCGTDLGQVKTKAEPSADGS-YKITGTKIFISAGdhDLTEniVHIVLARLPNSLPTT----KGLSLFLV 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 263 ERGF----------GGITHGPPEKKMGIKASNTAEVFFDGvrvPSENVLGEVGSGFKVAMHILNNGRfgMAAALAGTMRG 332
Cdd:PTZ00456 255 PRHVvkpdgsletaKNVKCIGLEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTAR--VGTALEGVCHA 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 333 IIA--KAVDHATNR--------TQFGEKIHNFGLIQEKLARMVML-QYVTE---SMAYMVSANMD--QGATDFQIEAA-- 394
Cdd:PTZ00456 330 ELAfqNALRYARERrsmralsgTKEPEKPADRIICHANVRQNILFaKAVAEggrALLLDVGRLLDihAAAKDAATREAld 409
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 76496475 395 --------ISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDI 445
Cdd:PTZ00456 410 heigfytpIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGI 468
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
191-291 |
7.26e-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: 104.67 E-value: 7.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 191 AFCLTEPSSGSDAASIRTSAVPSPcGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPATGavkekITAFVVERGFGGIT 270
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGD-GGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGG-----ISLFLVPKDAPGVS 74
|
90 100
....*....|....*....|.
gi 76496475 271 HGPPEKKMGIKASNTAEVFFD 291
Cdd:pfam02770 75 VRRIETKLGVRGLPTGELVFD 95
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
73-187 |
2.58e-24 |
|
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: 97.92 E-value: 2.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 73 NEEQTQFLKElvepVSRFFEEVNDP--AKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDL 150
Cdd:pfam02771 1 TEEQEALRDT----VREFAEEEIAPhaAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADA 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 76496475 151 GVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGE 187
Cdd:pfam02771 77 SVALALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
50-593 |
1.46e-22 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 101.50 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 50 SFAVGMFKGQLTTDQVFPYPS-VLNEEQTQFLKELVEPVSrffeevndpaKNDalemveettwqglKELG-AFGLQVPSE 127
Cdd:PTZ00457 17 SYAAGLFNFKIVPEEMFPYPCrKLDGDEAENLQSLLEQIR----------SND-------------KILGnLYGARIATE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 128 LGGVGLCNTQYARLVEIVGMHdlGVGITLGAHQSIGFKGILL--FGTKAQKEKYLPKLASGETVAAFClTEPSSGSDAAS 205
Cdd:PTZ00457 74 YGGLGLGHTAHALIYEEVGTN--CDSKLLSTIQHSGFCTYLLstVGSKELKGKYLTAMSDGTIMMGWA-TEEGCGSDISM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 206 IRTSAVPSPCGKYyTLNGSKLWIsNGGLADIFTVFAKTpVTDPATGA---VKEKITAFVVERgfggithgppeKKMGIKA 282
Cdd:PTZ00457 151 NTTKASLTDDGSY-VLTGQKRCE-FAASATHFLVLAKT-LTQTAAEEgatEVSRNSFFICAK-----------DAKGVSV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 283 SNTAEVFFDgvrVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDhaTNRTQFgekihnfglIQEKLA 362
Cdd:PTZ00457 217 NGDSVVFEN---TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVVQELRG--SNAEEG---------ATDTVA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 363 RMVMLQYVTESMAYMVSANMDQGATDFQIEAAISKIFGSEAawkvTDECIQIMGGMGFMKEPgVERVLRDLRIFRIFEGT 442
Cdd:PTZ00457 283 SFACAMYAMESTLYALTANLDLPTEDSLLECTLVSAFVQST----TNQLLSILETATPPSTT-LEKCFANARLFLSMMES 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 443 NDIlrLFVALQGCmdkGKELSGLgsalknPFGNAGLLLGEAGKQLRrraglgsGLSLSGLVHPELSRSGELAVRALEQFA 522
Cdd:PTZ00457 358 RDF--LYSSAVCC---GVEDYGL------FFQRASTLQMMQARTLR-------SLGVRDRVPIKNLPDCSLIDEAVVAFG 419
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 76496475 523 TVVEAKLIKHKKGIVNEQFLLQRLADGAIDLYAMVVVLSRASRSLSEGHPTAQHEKMLCDTWCIEAAARIR 593
Cdd:PTZ00457 420 NAVEATFVRSGSQVPYQQLLLNRLGEAASLLYAASAVASRASMCVSKGLPSAKVEGELASAFIAMAVSRAR 490
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
66-424 |
1.09e-20 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 96.81 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 66 FPYPSVLNEEQTqFLKELVEPVSRFfeeVNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIV 145
Cdd:PRK09463 74 YPKPTLTAEEQA-FLDGPVEELCRM---VNDWQITHELADLPPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 146 GMHDLGVGITLGAHQSIGfKGILL--FGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVpsPC-----GK- 217
Cdd:PRK09463 150 ASRSGTLAVTVMVPNSLG-PGELLlhYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGV--VCkgewqGEe 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 218 --YYTLNGSKLWISnggLADIFTVFA---KtpVTDPaTGAVKEK----ITAFVVERGFGGITHGPPEKKMGIkasntaeV 288
Cdd:PRK09463 227 vlGMRLTWNKRYIT---LAPIATVLGlafK--LYDP-DGLLGDKedlgITCALIPTDTPGVEIGRRHFPLNV-------P 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 289 FFDG------VRVPSENVLGE---VGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAV-DHATNRTQFGEKIHNFGLIQ 358
Cdd:PRK09463 294 FQNGptrgkdVFIPLDYIIGGpkmAGQGWRMLMECLSVGRGISLPSNSTGGAKLAALATgAYARIRRQFKLPIGKFEGIE 373
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 76496475 359 EKLARMVMLQYVTESMAYMVSANMDQGATDFQIeAAISKIFGSEAAWKVTDECIQIMGGMGFMKEP 424
Cdd:PRK09463 374 EPLARIAGNAYLMDAARTLTTAAVDLGEKPSVL-SAIAKYHLTERGRQVINDAMDIHGGKGICLGP 438
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
111-419 |
2.42e-20 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 95.79 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 111 WQGLKELGAFGLQVPSELGGVGLcnTQYA--RLVEIVGMHDLGVGITLGAHQSIGfKGILL--FGTKAQKEKYLPKLASG 186
Cdd:PRK13026 114 WDYLKKEGFFALIIPKEYGGKGF--SAYAnsTIVSKIATRSVSAAVTVMVPNSLG-PGELLthYGTQEQKDYWLPRLADG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 187 ETVAAFCLTEPSSGSDAASIRTSAVpsPC-GKY-------YTLNGSKLWISnggLADIFTVF-----AKTPvtDPATGAV 253
Cdd:PRK13026 191 TEIPCFALTGPEAGSDAGAIPDTGI--VCrGEFegeevlgLRLTWDKRYIT---LAPVATVLglafkLRDP--DGLLGDK 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 254 KE-KITAFVVERGFGGITHGPPEKKMGIkasntaeVFFDG------VRVPSENVLG---EVGSGFKVAMHILNNGRFGMA 323
Cdd:PRK13026 264 KElGITCALIPTDHPGVEIGRRHNPLGM-------AFMNGttrgkdVFIPLDWIIGgpdYAGRGWRMLVECLSAGRGISL 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 324 AALAGTMRGIIAKAVD-HATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDfQIEAAISKIFGSE 402
Cdd:PRK13026 337 PALGTASGHMATRTTGaYAYVRRQFGMPIGQFEGVQEALARIAGNTYLLEAARRLTTTGLDLGVKP-SVVTAIAKYHMTE 415
|
330
....*....|....*..
gi 76496475 403 AAWKVTDECIQIMGGMG 419
Cdd:PRK13026 416 LARDVVNDAMDIHAGKG 432
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
141-491 |
1.46e-18 |
|
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: 89.70 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 141 LVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYYT 220
Cdd:cd01150 87 LTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDPLTQEFV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 221 LN-----GSKLWIsnGGLADIFT---VFAKTpvtdpATGAVKEKITAFVVE-------RGFGGITHGPPEKKMGIKASNT 285
Cdd:cd01150 167 INtpdftATKWWP--GNLGKTAThavVFAQL-----ITPGKNHGLHAFIVPirdpkthQPLPGVTVGDIGPKMGLNGVDN 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 286 AEVFFDGVRVPSENVL---GEV-------------GSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGE 349
Cdd:cd01150 240 GFLQFRNVRIPRENLLnrfGDVspdgtyvspfkdpNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGP 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 350 K-------IHNFGLIQEK----LARMVMLQYVTESMAYM---VSANMDQGATDFQIE----AAISKIFGSEAAWKVTDEC 411
Cdd:cd01150 320 KpsdpevqILDYQLQQYRlfpqLAAAYAFHFAAKSLVEMyheIIKELLQGNSELLAElhalSAGLKAVATWTAAQGIQEC 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 412 IQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVAlQGCMDKGKELSGLGSALKNPFGNAGLLLGEAGKQLRRRA 491
Cdd:cd01150 400 REACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTA-NYLLKKYAQAFSLADYLEAYEWLAAHLLRHAAAQLEKLK 478
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
137-451 |
2.09e-18 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 89.15 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 137 QYARLVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCG 216
Cdd:PLN02636 122 KYFAITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLT 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 217 KYYTLN-----GSKLWISNGGLADIF-TVFAKTPVTDPATGAVKEK-ITAFVV-------ERGFGGITHGPPEKKMGIKA 282
Cdd:PLN02636 202 DEFVINtpndgAIKWWIGNAAVHGKFaTVFARLKLPTHDSKGVSDMgVHAFIVpirdmktHQVLPGVEIRDCGHKVGLNG 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 283 SNTAEVFFDGVRVPSENVLGEVG----------------SGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQ 346
Cdd:PLN02636 282 VDNGALRFRSVRIPRDNLLNRFGdvsrdgkytsslptinKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQ 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 347 FGE------KIHNFGLIQEKLarMVML----------QYVTESMAYMVSANMDQGATDFQIEAAISKIFGSEAAWKVTDE 410
Cdd:PLN02636 362 FGPpkqpeiSILDYQSQQHKL--MPMLastyafhfatEYLVERYSEMKKTHDDQLVADVHALSAGLKAYITSYTAKALST 439
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 76496475 411 CIQIMGGMGFmkePGVER--VLR-DLRIFRIFEGTNDILRLFVA 451
Cdd:PLN02636 440 CREACGGHGY---AAVNRfgSLRnDHDIFQTFEGDNTVLLQQVA 480
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
126-445 |
5.00e-18 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 88.31 E-value: 5.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 126 SELGGVGLCNTQYARLVEIVGMHDLGVGI-TLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPS-SGSDA 203
Cdd:PLN02876 487 DQLLGAGLSNLEYGYLCEIMGRSVWAPQVfNCGAPDTGNMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDA 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 204 ASIRTSAVPSpcGKYYTLNGSKLWISngGLAD----IFTVFAKTPVTDPA------------TGAVKEKITAFVVerGFG 267
Cdd:PLN02876 567 TNIECSIRRQ--GDSYVINGTKWWTS--GAMDprcrVLIVMGKTDFNAPKhkqqsmilvdiqTPGVQIKRPLLVF--GFD 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 268 GITHGppekkmgikasnTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQF 347
Cdd:PLN02876 641 DAPHG------------HAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAF 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 348 GEKIHNFGLIQEKLARmvmLQYVTESMAYMVSANMDQ----GATDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKE 423
Cdd:PLN02876 709 GKLIAQHGSFLSDLAK---CRVELEQTRLLVLEAADQldrlGNKKARGIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSD 785
|
330 340
....*....|....*....|..
gi 76496475 424 PGVERVLRDLRIFRIFEGTNDI 445
Cdd:PLN02876 786 TVLAHLWATARTLRIADGPDEV 807
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
106-345 |
9.38e-11 |
|
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: 63.88 E-value: 9.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 106 VEETTWqgLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGAHqsIGF-KGILLFGTKAQKEKYLPKLA 184
Cdd:cd01163 25 YEEVAL--LRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAH--FGFvEALLLAGPEQFRKRWFGRVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 185 SGETVAAfclTEPSSGSDAASIRTSAVPSPCGKYYtLNGSKlWISNGGL-ADIFTVFAktpvTDPAtgavkEKITAFVVE 263
Cdd:cd01163 101 NGWIFGN---AVSERGSVRPGTFLTATVRDGGGYV-LNGKK-FYSTGALfSDWVTVSA----LDEE-----GKLVFAAVP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 264 RGFGGITHGPPEKKMGIK--ASNTAEvfFDGVRVPSENVLGEvGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHA 341
Cdd:cd01163 167 TDRPGITVVDDWDGFGQRltASGTVT--FDNVRVEPDEVLPR-PNAPDRGTLLTAIYQLVLAAVLAGIARAALDDAVAYV 243
|
....
gi 76496475 342 TNRT 345
Cdd:cd01163 244 RSRT 247
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
194-457 |
5.17e-08 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 55.91 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 194 LTEPSSGSDAASIRTSAVPSPcGKYYTLNGSKlWISNGGLADIFTVFAKTpvtdpatgavKEKITAFVVERGFGGITHGP 273
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAERLA-DGSYRLVGHK-WFFSVPQSDAHLVLAQA----------KGGLSCFFVPRFLPDGQRNA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 274 P-----EKKMGIKASNTAEVFFDGVrvpSENVLGEVGSGFKvamHILNNG---RFGMAAALAGTMRGIIAKAVDHATNRT 345
Cdd:PRK11561 252 IrlerlKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIR---LILKMGgmtRFDCALGSHGLMRRAFSVAIYHAHQRQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 346 QFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATdfQIEAAISKIFGSEAAWKVTD-------ECIQIMGGM 418
Cdd:PRK11561 326 VFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDRRAD--AKEALWARLFTPAAKFVICKrgipfvaEAMEVLGGI 403
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 76496475 419 GFMKEPGVERVLRDLRIFRIFEGTN-----DILRLFVALQGCMD 457
Cdd:PRK11561 404 GYCEESELPRLYREMPVNSIWEGSGnimclDVLRVLNKQPGVYD 447
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
139-466 |
1.75e-07 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 54.39 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 139 ARLVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKY 218
Cdd:PLN02312 136 LALLEVIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEE 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 219 YTLN-----GSKLWIsnGGLADIFT---VFAKTPVTdpatgAVKEKITAFVVE------RGFGGITHGPPEKKMGIKASN 284
Cdd:PLN02312 216 FVINtpcesAQKYWI--GGAANHAThtiVFSQLHIN-----GKNEGVHAFIAQirdqdgNICPNIRIADCGHKIGLNGVD 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 285 TAEVFFDGVRVPSENVLGEVG----------------SGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQF- 347
Cdd:PLN02312 289 NGRIWFDNLRIPRENLLNSVAdvspdgkyvsaikdpdQRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAFs 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 348 ----GEKI-------HNFGLIqEKLARMVMLQYVTESMAYMVSANMDQGATDFQIeaaISKIFGSEAAW---KVTDECIQ 413
Cdd:PLN02312 369 vtpnGPEVllldypsHQRRLL-PLLAKTYAMSFAANDLKMIYVKRTPESNKAIHV---VSSGFKAVLTWhnmRTLQECRE 444
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 76496475 414 IMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILR------LFVALQGCMDKGKELSGLG 466
Cdd:PLN02312 445 ACGGQGLKTENRVGQLKAEYDVQSTFEGDNNVLMqqvskaLLAEYVSAKKRNKPFKGLG 503
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
321-443 |
3.35e-07 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 49.65 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 321 GMAAALAGTMRGIIAKAVDHATNRTQ--FGEKIHNFGLIQEKLARMV-------MLQYVTESMAYMVSANMDQGATDFQI 391
Cdd:pfam08028 1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAaridaarLLLERAAARIEAAAAAGKPVTPALRA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 76496475 392 EAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTN 443
Cdd:pfam08028 81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVN 132
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
171-451 |
5.93e-06 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 49.46 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 171 GTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYYTLN-----GSKLWISN-GGLADIFTVFAKTP 244
Cdd:PTZ00460 110 GTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHtpsveAVKFWPGElGFLCNFALVYAKLI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 245 VTDPATG--AVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLG---EVGSGFKVAMHilNNGR 319
Cdd:PTZ00460 190 VNGKNKGvhPFMVRIRDKETHKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLAryiKVSEDGQVERQ--GNPK 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 320 FGMAAALagTMRGIIAK------------AVDHATNRTQFGE------KIHNFGLIQEK----LARMVMLQYVTESMAYM 377
Cdd:PTZ00460 268 VSYASMM--YMRNLIIDqyprfaaqaltvAIRYSIYRQQFTNdnkqenSVLEYQTQQQKllplLAEFYACIFGGLKIKEL 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 378 VSANMDQ-GATDFQIEAAISKIFGSEAAW------KVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFV 450
Cdd:PTZ00460 346 VDDNFNRvQKNDFSLLQLTHAILSAAKANytyfvsNCAEWCRLSCGGHGYAHYSGLPAIYFDMSPNITLEGENQIMYLQL 425
|
.
gi 76496475 451 A 451
Cdd:PTZ00460 426 A 426
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
171-479 |
2.13e-05 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 47.52 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 171 GTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYY-----TLNGSKLWisNGGLADIFT---VFAK 242
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFvihspTLTSSKWW--PGGLGKVSThavVYAR 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 243 TpvtdpATGAVKEKITAFVVE-------RGFGGITHGPPEKKMGIKASNTAE---VFFDGVRVPSENVLGEVGSGFKVAM 312
Cdd:PLN02443 192 L-----ITNGKDHGIHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQMLMRLSKVTREGK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 313 HILNNgrfgMAAALA-GTM----RGIIAK-----------AVDHATNRTQFGEK-------IHNFGLIQEK----LARMV 365
Cdd:PLN02443 267 YVQSD----VPRQLVyGTMvyvrQTIVADastalsravciATRYSAVRRQFGSQdggpetqVIDYKTQQSRlfplLASAY 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76496475 366 MLQYVTESMAYMVSANMDQ-GATDF----QIEAAIS--KIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRI 438
Cdd:PLN02443 343 AFRFVGEWLKWLYTDVTQRlEANDFstlpEAHACTAglKSLTTSATADGIEECRKLCGGHGYLCSSGLPELFAVYVPACT 422
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 76496475 439 FEGTNDILRLFVAlQGCMdkgKELSGLGSAlKNPFGNAGLL 479
Cdd:PLN02443 423 YEGDNVVLLLQVA-RFLM---KTVSQLGSG-KKPVGTTAYM 458
|
|
| |
