|
Name |
Accession |
Description |
Interval |
E-value |
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
4-408 |
2.23e-128 |
|
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: 374.95 E-value: 2.23e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 4 DLKLTEEQISAQKWAHDFARKEMReatvdgvPAHRHYDEVEEFPWPIVQKAAEVGLYGL----EYyqmAGQDPTGLTQAL 79
Cdd:COG1960 2 DFELTEEQRALRDEVREFAEEEIA-------PEAREWDREGEFPRELWRKLAELGLLGLtipeEY---GGLGLSLVELAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 80 IIEELFWGCAGIGLAIFGSGLALAGLASSGTGDQIAEWAPRIFgtpDDVKVGAYAVSEPGAGSDVSKIRTKATKVEGGWL 159
Cdd:COG1960 72 VLEELARADASLALPVGVHNGAAEALLRFGTEEQKERYLPRLA---SGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 160 LNGEKIWITNGGIADVHIVVATVDPTIGHRGQASFIVTSDAEGFQETKKTKKLGIRASHTAELSFTDCFVPDEQLLGGqd 239
Cdd:COG1960 149 LNGQKTFITNAPVADVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGE-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 240 kldakidaahnpdPNRKSSGALSTFEATRPIVGIQAVGVARAAFDASVQYAMERETFGVPIIRHQAIAFKLADMATEIDA 319
Cdd:COG1960 227 -------------EGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 320 ARLLCWRGINMgttwtpFKHG-----EGSMAKLHAGRTAVRVTDEAIQIHGGFGYSREFDVEKFHRDSKIYEIFEGTKEI 394
Cdd:COG1960 294 ARALVYRAAWL------LDAGedaalEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEI 367
|
410
....*....|....
gi 919108476 395 QQLVIGRAIARSHG 408
Cdd:COG1960 368 QRLIIARRLLGRPG 381
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
9-405 |
6.83e-121 |
|
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: 355.81 E-value: 6.83e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 9 EEQISAQKWAHDFARKEMreatvdgVPAHRHYDEVEEFPWPIVQKAAEVGLYGLEY---YQMAGQDptGLTQALIIEELF 85
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEI-------APLAAEMDEKGEFPREVIKEMAELGLMGIPIpeeYGGAGLD--FLAYAIAIEELA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 86 WGCAGIGLAIFG-SGLALAGLASSGTGDQIAEWAPRIFGtpdDVKVGAYAVSEPGAGSDVSKIRTKATKVEGGWLLNGEK 164
Cdd:cd01158 72 KVDASVAVIVSVhNSLGANPIIKFGTEEQKKKYLPPLAT---GEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 165 IWITNGGIADVHIVVATVDPTIGHRGQASFIVTSDAEGFQETKKTKKLGIRASHTAELSFTDCFVPDEQLLGgqdkldak 244
Cdd:cd01158 149 MWITNGGEADFYIVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILG-------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 245 idaahnpDPNRKSSGALSTFEATRPIVGIQAVGVARAAFDASVQYAMERETFGVPIIRHQAIAFKLADMATEIDAARLLC 324
Cdd:cd01158 221 -------EEGEGFKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLT 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 325 WRGINMGTTWTPFKHgEGSMAKLHAGRTAVRVTDEAIQIHGGFGYSREFDVEKFHRDSKIYEIFEGTKEIQQLVIGRAIA 404
Cdd:cd01158 294 YKAARLKDNGEPFIK-EAAMAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLL 372
|
.
gi 919108476 405 R 405
Cdd:cd01158 373 K 373
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
93-401 |
4.40e-97 |
|
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: 293.04 E-value: 4.40e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 93 LAIFGSGLALAGLASSGTGDQIAEWAPRIfgtPDDVKVGAYAVSEPGAGSDVSKIRTKATKVEGGWLLNGEKIWITNGGI 172
Cdd:cd00567 36 LAELGLLLGAALLLAYGTEEQKERYLPPL---ASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 173 ADVHIVVATVDP-TIGHRGQASFIVTSDAEGFQETKKTKKLGIRASHTAELSFTDCFVPDEQLLGGqdkldakidaahnp 251
Cdd:cd00567 113 ADLFIVLARTDEeGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGE-------------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 252 dPNRKSSGALSTFEATRPIVGIQAVGVARAAFDASVQYAMERETFGVPIIRHQAIAFKLADMATEIDAARLLCWRGINMG 331
Cdd:cd00567 179 -EGGGFELAMKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLL 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 332 TTWTPFKHGEGSMAKLHAGRTAVRVTDEAIQIHGGFGYSREFDVEKFHRDSKIYEIFEGTKEIQQLVIGR 401
Cdd:cd00567 258 DQGPDEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
7-401 |
9.18e-93 |
|
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: 284.09 E-value: 9.18e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 7 LTEEQISAQKWAHDFARKEMreatvdgVPAHRHYDEVEEFPWPIVQKAAEVGLYGLEYYQ-MAGQDPTGLTQALIIEELF 85
Cdd:cd01157 1 LTEQQKEFQETARKFAREEI-------IPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEdCGGLGLGTFDTCLITEELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 86 WGCAGIGLAIFGSGLALAGLASSGTGDQIAEWAPRIFGTPddvKVGAYAVSEPGAGSDVSKIRTKATKVEGGWLLNGEKI 165
Cdd:cd01157 74 YGCTGVQTAIEANSLGQMPVIISGNDEQKKKYLGRMTEEP---LMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 166 WITNGGIADVHIVVATVDP---TIGHRGQASFIVTSDAEGFQETKKTKKLGIRASHTAELSFTDCFVPDEQLLGGqDKLD 242
Cdd:cd01157 151 WITNGGKANWYFLLARSDPdpkCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIG-EGAG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 243 AKIdaahnpdpnrkssgALSTFEATRPIVGIQAVGVARAAFDASVQYAMERETFGVPIIRHQAIAFKLADMATEIDAARL 322
Cdd:cd01157 230 FKI--------------AMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 323 LCWRG---INMGTTWTPFkhgeGSMAKLHAGRTAVRVTDEAIQIHGGFGYSREFDVEKFHRDSKIYEIFEGTKEIQQLVI 399
Cdd:cd01157 296 AYQRAaweVDSGRRNTYY----ASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLII 371
|
..
gi 919108476 400 GR 401
Cdd:cd01157 372 SR 373
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
19-403 |
1.63e-77 |
|
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: 244.72 E-value: 1.63e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 19 HDFARKEMREATVDGV-PAHRHYDEVEEFPWPIVQKAAEVGLYGL---EYYQMAGQDPtgLTQALIIEEL-FWGCAGIGL 93
Cdd:cd01160 3 HDAFRDVVRRFFAKEVaPFHHEWEKAGEVPREVWRKAGEQGLLGVgfpEEYGGIGGDL--LSAAVLWEELaRAGGSGPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 94 AIFgSGLALAGLASSGTGDQIAEWAPRIFGTPddvKVGAYAVSEPGAGSDVSKIRTKATKVEGGWLLNGEKIWITNGGIA 173
Cdd:cd01160 81 SLH-TDIVSPYITRAGSPEQKERVLPQMVAGK---KIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 174 DVHIVVA-TVDPTIGHRGQASFIVTSDAEGFQETKKTKKLGIRASHTAELSFTDCFVPDEQLLGgqdkldakidaahnpD 252
Cdd:cd01160 157 DVVIVVArTGGEARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLG---------------E 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 253 PNRKSSGALSTFEATRPIVGIQAVGVARAAFDASVQYAMERETFGVPIIRHQAIAFKLADMATEIDAARLLCWRginmgT 332
Cdd:cd01160 222 ENKGFYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDN-----C 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919108476 333 TWtpfKHGEG-------SMAKLHAGRTAVRVTDEAIQIHGGFGYSREFDVEKFHRDSKIYEIFEGTKEIQQLVIGRAI 403
Cdd:cd01160 297 AW---RHEQGrldvaeaSMAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQM 371
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
7-403 |
5.51e-76 |
|
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: 240.78 E-value: 5.51e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 7 LTEEQISAQKWAHDFARKEMreatvdgVPAHRHYDEVEEFPWPIVQKAAEVGLYGL----EYyqmAGQDPTGLTQALIIE 82
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEI-------APLAAKIDRDNEFPRDLWRKMGKLGLLGItapeEY---GGSGMGYLAHVIIME 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 83 ELFWGCAGIGLAiFG--SGLALAGLASSGTGDQIAEWAPR-IFGTpddvKVGAYAVSEPGAGSDVSKIRTKATKVEGGWL 159
Cdd:cd01156 72 EISRASGSVALS-YGahSNLCINQIYRNGSAAQKEKYLPKlISGE----HIGALAMSEPNAGSDVVSMKLRAEKKGDRYV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 160 LNGEKIWITNGGIADVHIVVATVDPTIGHRGQASFIVTSDAEGFQETKKTKKLGIRASHTAELSFTDCFVPDEQLLGGQd 239
Cdd:cd01156 147 LNGSKMWITNGPDADTLVVYAKTDPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGE- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 240 kldakidaahnpdpNRKSSGALSTFEATRPIVGIQAVGVARAAFDASVQYAMERETFGVPIIRHQAIAFKLADMATEIDA 319
Cdd:cd01156 226 --------------NKGVYVLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 320 ARLLCW---RGINMGTTwTPfKHGEGSMakLHAGRTAVRVTDEAIQIHGGFGYSREFDVEKFHRDSKIYEIFEGTKEIQQ 396
Cdd:cd01156 292 SRSYLYtvaKACDRGNM-DP-KDAAGVI--LYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRR 367
|
....*..
gi 919108476 397 LVIGRAI 403
Cdd:cd01156 368 MVIGREL 374
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
7-405 |
2.29e-74 |
|
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: 236.57 E-value: 2.29e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 7 LTEEQISAQKWAHDFARKEMREATVDgvpahrhYDEVEEFPWPIVQKAAEVGLYGLeYYQ--MAGQDPTGLTQALIIEEL 84
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAAD-------WDQKKHFPVDVLRKAAELGFGGI-YIRddVGGSGLSRLDASIIFEAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 85 FWGCAGIGLAIFGSGLALAGLASSGTGDQIAEWAPRIFGTPddvKVGAYAVSEPGAGSDVSKIRTKATKVEGGWLLNGEK 164
Cdd:cd01162 73 STGCVSTAAYISIHNMCAWMIDSFGNDEQRERFLPDLCTME---KLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 165 IWITNGGIADVHIVVATVDPTiGHRGQASFIVTSDAEGFQETKKTKKLGIRASHTAELSFTDCFVPDEQLLGGQdkldak 244
Cdd:cd01162 150 AFISGAGDSDVYVVMARTGGE-GPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGE------ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 245 idaahnpdpNRKSSGALSTFEATRPIVGIQAVGVARAAFDASVQYAMERETFGVPIIRHQAIAFKLADMATEIDAARLLC 324
Cdd:cd01162 223 ---------GQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 325 WRGINMGTTWTPFKHGEGSMAKLHAGRTAVRVTDEAIQIHGGFGYSREFDVEKFHRDSKIYEIFEGTKEIQQLVIGRAIA 404
Cdd:cd01162 294 RRAASALDRGDPDAVKLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALL 373
|
.
gi 919108476 405 R 405
Cdd:cd01162 374 T 374
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
2-403 |
8.91e-68 |
|
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: 219.92 E-value: 8.91e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 2 PFDLK--LTEEQISAQKWAHDFARKEMreatvdgVPAHRHYDEVEEFPWPIVQKAAEVGLYG--LEYYQMAGQDPTGLtq 77
Cdd:cd01151 6 PLNLDdlLTEEERAIRDTAREFCQEEL-------APRVLEAYREEKFDRKIIEEMGELGLLGatIKGYGCAGLSSVAY-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 78 ALIIEELFWGCAGIGLAI-FGSGLALAGLASSGTGDQIAEWAPrifGTPDDVKVGAYAVSEPGAGSDVSKIRTKATKVEG 156
Cdd:cd01151 77 GLIAREVERVDSGYRSFMsVQSSLVMLPIYDFGSEEQKQKYLP---KLASGELIGCFGLTEPNHGSDPGGMETRARKDGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 157 GWLLNGEKIWITNGGIADVHIVVATVDPTIGHRGqasFIVTSDAEGFQETKKTKKLGIRASHTAELSFTDCFVPDEQLLG 236
Cdd:cd01151 154 GYKLNGSKTWITNSPIADVFVVWARNDETGKIRG---FILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 237 GQDKLdakidaahnpdpnrksSGALSTFEATRPIVGIQAVGVARAAFDASVQYAMERETFGVPIIRHQAIAFKLADMATE 316
Cdd:cd01151 231 GAEGL----------------RGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 317 IDAARLLCWRginMGTTWTPFKH--GEGSMAKLHAGRTAVRVTDEAIQIHGGFGYSREFDVEKFHRDSKIYEIFEGTKEI 394
Cdd:cd01151 295 IALGLLACLR---VGRLKDQGKAtpEQISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDI 371
|
....*....
gi 919108476 395 QQLVIGRAI 403
Cdd:cd01151 372 HALILGRAI 380
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
41-408 |
1.69e-64 |
|
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: 211.94 E-value: 1.69e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 41 DEVEEFPWPIVQKAAEVGLYGLEYYQMAGQDPTGLTQALIIEELFWGCAGIGLAIFG-SGLALAGLASSGTGDQIAEWAP 119
Cdd:cd01161 52 DQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMDLGFSVTLGAhQSIGFKGILLFGTEAQKEKYLP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 120 RIfgtPDDVKVGAYAVSEPGAGSDVSKIRTKATKVEGG--WLLNGEKIWITNGGIADVHIVVA---TVDPTiGHRGQ--A 192
Cdd:cd01161 132 KL---ASGEWIAAFALTEPSSGSDAASIRTTAVLSEDGkhYVLNGSKIWITNGGIADIFTVFAkteVKDAT-GSVKDkiT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 193 SFIVTSDAEGFQETKKTKKLGIRASHTAELSFTDCFVPDEQLLGgqdkldaKIDAAHNPDPNRKSSGALStfeatrpiVG 272
Cdd:cd01161 208 AFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLG-------EVGDGFKVAMNILNNGRFG--------MG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 273 IQAVGVARAAFDASVQYAMERETFGVPIIRHQAIAFKLADMATEIDAARLLCWR-GINMGTTWTPFKHGEGSMAKLHAGR 351
Cdd:cd01161 273 AALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMtSGNMDRGLKAEYQIEAAISKVFASE 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 919108476 352 TAVRVTDEAIQIHGGFGYSREFDVEKFHRDSKIYEIFEGTKEIQQLVIGRAIARSHG 408
Cdd:cd01161 353 AAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQHAG 409
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
75-401 |
1.13e-57 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 193.94 E-value: 1.13e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 75 LTQALIIEELFWGCAGIGLAiFG--SGLALAGLASSGTGDQIAEWAPRIFGTPddvKVGAYAVSEPGAGSDVSKIRTKAT 152
Cdd:PLN02519 90 LYHCIAMEEISRASGSVGLS-YGahSNLCINQLVRNGTPAQKEKYLPKLISGE---HVGALAMSEPNSGSDVVSMKCKAE 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 153 KVEGGWLLNGEKIWITNGGIADVHIVVATVDPTIGHRGQASFIVTSDAEGFQETKKTKKLGIRASHTAELSFTDCFVPDE 232
Cdd:PLN02519 166 RVDGGYVLNGNKMWCTNGPVAQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 233 QLLGGQDKLDAKIdaahnpdpnrkssgaLSTFEATRPIVGIQAVGVARAAFDASVQYAMERETFGVPIIRHQAIAFKLAD 312
Cdd:PLN02519 246 NVLGQEGKGVYVM---------------MSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLAD 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 313 MATEIDAARLLCW---RGINMGTTwtpfKHGEGSMAKLHAGRTAVRVTDEAIQIHGGFGYSREFDVEKFHRDSKIYEIFE 389
Cdd:PLN02519 311 MYTSLQSSRSYVYsvaRDCDNGKV----DRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGA 386
|
330
....*....|..
gi 919108476 390 GTKEIQQLVIGR 401
Cdd:PLN02519 387 GTSEIRRMLIGR 398
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
19-406 |
8.73e-48 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 168.19 E-value: 8.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 19 HDFARKEMREATVDGVPAHRHYDEVE-EFPWPIVQKAAEVGLYGLEYYQMAGQDPTGLTQALIIEELFWGC-AGIGLAIF 96
Cdd:PTZ00461 41 HAALRETVAKFSREVVDKHAREDDINmHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYdPGFCLAYL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 97 G-SGLALAGLASSGTGDQIAEWAPRIFGTPddvKVGAYAVSEPGAGSDVSKIRTKATKV-EGGWLLNGEKIWITNGGIAD 174
Cdd:PTZ00461 121 AhSMLFVNNFYYSASPAQRARWLPKVLTGE---HVGAMGMSEPGAGTDVLGMRTTAKKDsNGNYVLNGSKIWITNGTVAD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 175 VHIVVATVDPTIghrgqASFIVTSDAEGFQETKKTKKLGIRASHTAELSFTDCFVPDEQLLGGQDKldakidaahnpdpn 254
Cdd:PTZ00461 198 VFLIYAKVDGKI-----TAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGK-------------- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 255 rKSSGALSTFEATRPIVGIQAVGVARAAFDASVQYAMERETFGVPIIRHQAIAFKLADMATEIDAARLLCW---RGINMG 331
Cdd:PTZ00461 259 -GMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYsvsHNVHPG 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919108476 332 TtwtpfKHGEGS-MAKLHAGRTAVRVTDEAIQIHGGFGYSREFDVEKFHRDSKIYEIFEGTKEIQQLVIGRAIARS 406
Cdd:PTZ00461 338 N-----KNRLGSdAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLKG 408
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
260-403 |
2.01e-47 |
|
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: 158.96 E-value: 2.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 260 ALSTFEATRPIVGIQAVGVARAAFDASVQYAMERETFGVPIIRHQAIAFKLADMATEIDAARLLCWRGINMGTTWTPFKh 339
Cdd:pfam00441 7 AMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAGGPDG- 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919108476 340 GEGSMAKLHAGRTAVRVTDEAIQIHGGFGYSREFDVEKFHRDSKIYEIFEGTKEIQQLVIGRAI 403
Cdd:pfam00441 86 AEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
29-403 |
1.46e-44 |
|
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: 159.48 E-value: 1.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 29 ATVDGVPAHRHyDEVEEFPWPI---VQKAAEVGLYGLEYYQMAGQDPTGLTQALIIEELFWGCAGIGLAIFGSGLALAGL 105
Cdd:cd01153 18 ADGDREGPVFD-DGRVVVPPPFkeaLDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMYASGTQGAAATL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 106 ASSGTGDQIAEWAPRIFgtpDDVKVGAYAVSEPGAGSDVSKIRTKATKVEGG-WLLNGEKIWITNG--GIAD--VHIVVA 180
Cdd:cd01153 97 LAHGTEAQREKWIPRLA---EGEWTGTMCLTEPDAGSDLGALRTKAVYQADGsWRINGVKRFISAGehDMSEniVHLVLA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 181 -TVDPTIGHRGQASFIVTS---DAE--GFQETKKTKKLGIRASHTAELSFTDCFVPdeqLLGgqdkldakidaahnpDPN 254
Cdd:cd01153 174 rSEGAPPGVKGLSLFLVPKfldDGErnGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIG---------------EEG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 255 RKSSGALSTFEATRPIVGIQAVGVARAAFDASVQYAMERETFG--------VPIIRHQAIAFKLADMATEIDAARLL--- 323
Cdd:cd01153 236 MGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGdlikaapaVTIIHHPDVRRSLMTQKAYAEGSRALdly 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 324 CWRGINMGTTwtPFKHGEGS------------MAKLHAGRTAVRVTDEAIQIHGGFGYSREFDVEKFHRDSKIYEIFEGT 391
Cdd:cd01153 316 TATVQDLAER--KATEGEDRkalsaladlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGT 393
|
410
....*....|...
gi 919108476 392 KEIQ-QLVIGRAI 403
Cdd:cd01153 394 TGIQaLDLIGRKI 406
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
4-403 |
4.43e-44 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 157.58 E-value: 4.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 4 DLKLTEEQisaqKWAHDFARKEM-REATVDGVpahRHYDEVEEFPWPIVQKAAEVGLYGLEYYQMAGQDPTG-LTQALII 81
Cdd:PRK12341 2 DFSLTEEQ----ELLLASIRELItRNFPEEYF---RTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADyVTQMLVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 82 EELFWGCAGIglAIFGSGLALAGLASSGTGDQIAEWAPRIFGTPDDvkvgAY--AVSEPGAGSDVSKIRTKATKVEGGWL 159
Cdd:PRK12341 75 EEVSKCGAPA--FLITNGQCIHSMRRFGSAEQLRKTAESTLETGDP----AYalALTEPGAGSDNNSATTTYTRKNGKVY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 160 LNGEKIWITNGGIADVHIVVA-TVDPTIGHRGQASFIVTSDAEGFQeTKKTKKLGIRASHTAELSFTDCFVPDEQLLGgq 238
Cdd:PRK12341 149 LNGQKTFITGAKEYPYMLVLArDPQPKDPKKAFTLWWVDSSKPGIK-INPLHKIGWHMLSTCEVYLDNVEVEESDLVG-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 239 dkldakidaahnpdpnRKSSG---ALSTFEATRPIVGIQAVGVARAAFDASVQYAMERETFGVPIIRHQAIAFKLADMAT 315
Cdd:PRK12341 226 ----------------EEGMGflnVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAI 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 316 EIDAARLL----CWR---GINMGTTwtpfkhgeGSMAKLHAGRTAVRVTDEAIQIHGGFGYSREFDVEKFHRDSKIYEIF 388
Cdd:PRK12341 290 KIENMRNMvykvAWQadnGQSLRTS--------AALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIG 361
|
410
....*....|....*
gi 919108476 389 EGTKEIQQLVIGRAI 403
Cdd:PRK12341 362 GGTDEIMIYIAGRQI 376
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
3-403 |
4.45e-44 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 158.09 E-value: 4.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 3 FDLKLTEEQISAQKWAHDFARKEMreatvdgVPAHRHYDEVEEFPWPIVQKAAEVGLYG--LEYYQMAGQDPTGltQALI 80
Cdd:PLN02526 25 FDDLLTPEEQALRKRVRECMEKEV-------APIMTEYWEKAEFPFHIIPKLGSLGIAGgtIKGYGCPGLSITA--SAIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 81 IEELFWGCAGIGLAIF-GSGLALAGLASSGTGDQIAEWAPRIfgtPDDVKVGAYAVSEPGAGSDVSKIRTKATKVEGGWL 159
Cdd:PLN02526 96 TAEVARVDASCSTFILvHSSLAMLTIALCGSEAQKQKYLPSL---AQLDTVACWALTEPDYGSDASSLNTTATKVEGGWI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 160 LNGEKIWITNGGIADVHIVVATVDPTIGHRGqasFIVTSDAEGFQETKKTKKLGIRASHTAELSFTDCFVPDEQLLGGQD 239
Cdd:PLN02526 173 LNGQKRWIGNSTFADVLVIFARNTTTNQING---FIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVN 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 240 KLDakidaahnpDPNRkssgalsTFEATRPIVGIQAVGVARAAFDASVQYAMERETFGVPIIRHQAIAFKLADMATEIDA 319
Cdd:PLN02526 250 SFQ---------DTNK-------VLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 320 ARLLCWR--GINMGTTWTPfkhGEGSMAKLHAGRTAVRVTDEAIQIHGGFGYSREFDVEKFHRDSKIYEIFEGTKEIQQL 397
Cdd:PLN02526 314 MFLVGWRlcKLYESGKMTP---GHASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINAL 390
|
....*.
gi 919108476 398 VIGRAI 403
Cdd:PLN02526 391 VTGREI 396
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
84-405 |
9.39e-38 |
|
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: 141.35 E-value: 9.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 84 LFWG-CAGIGLAIFGSGLALAGLASSGtGDQIAEWAPRIFGtpDDVK---VGAYAVSEPGAGSDVSKIRTKATKVEGG-W 158
Cdd:cd01154 101 LLSDaAAGLLCPLTMTDAAVYALRKYG-PEELKQYLPGLLS--DRYKtglLGGTWMTEKQGGSDLGANETTAERSGGGvY 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 159 LLNGEKiWITNGGIADVHIVVA-TVDPTIGHRGQASFIVT---SDAE--GFQETKKTKKLGIRASHTAELSFTDCfvpDE 232
Cdd:cd01154 178 RLNGHK-WFASAPLADAALVLArPEGAPAGARGLSLFLVPrllEDGTrnGYRIRRLKDKLGTRSVATGEVEFDDA---EA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 233 QLLGGQDKldakidaahnpdpnrKSSGALSTFEATRPIVGIQAVGVARAAFDASVQYAMERETFGVPIIRHQAIAFKLAD 312
Cdd:cd01154 254 YLIGDEGK---------------GIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAE 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 313 MATEIDAARLLCWRGINMGTTWTPFKHGEGSMA-------KLHAGRTAVRVTDEAIQIHGGFGYSREFDVEKFHRDSKIY 385
Cdd:cd01154 319 MEVDVEAATALTFRAARAFDRAAADKPVEAHMArlatpvaKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVT 398
|
330 340
....*....|....*....|
gi 919108476 386 EIFEGTKEIQQLVIGRAIAR 405
Cdd:cd01154 399 PIWEGTGNIQALDVLRVLVK 418
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
35-403 |
1.12e-32 |
|
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: 126.69 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 35 PAHRHYDEVEEFPWPIVQKAAEVGLYGLEYYQMAGQDPTGLTQALII-EELFWGCAGIGLAIFGSGLALAGLASSGTGDQ 113
Cdd:cd01152 25 ESALGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFrEEMAAAGAPVPFNQIGIDLAGPTILAYGTDEQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 114 IAEWAPRIFgTPDDVKVGAYavSEPGAGSDVSKIRTKATKVEGGWLLNGEKIWITNGGIADVHIVVATVDPTI-GHRGQA 192
Cdd:cd01152 105 KRRFLPPIL-SGEEIWCQGF--SEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDPEApKHRGIS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 193 SFIVTSDAEGFQETKKTKKLGirASHTAELSFTDCFVPDEQLLGgqdkldakidaahnpDPNRKSSGALSTFEATRPIVG 272
Cdd:cd01152 182 ILLVDMDSPGVTVRPIRSING--GEFFNEVFLDDVRVPDANRVG---------------EVNDGWKVAMTTLNFERVSIG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 273 iqavGVARAAFDASVQYAMERETFGVPIIRHQAIAFKLADMATEIDAARLLCWRGINMGTTWTPfKHGEGSMAKLHAGRT 352
Cdd:cd01152 245 ----GSAATFFELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKP-PGAEASIAKLFGSEL 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 919108476 353 AVRVTDEAIQIHGGFGYSREF--------DVEKFHRDSKIYEIFEGTKEIQQLVIGRAI 403
Cdd:cd01152 320 AQELAELALELLGTAALLRDPapgaelagRWEADYLRSRATTIYGGTSEIQRNIIAERL 378
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
7-402 |
8.81e-30 |
|
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: 119.03 E-value: 8.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 7 LTEEQISAQKWAHDFARKEMReatvdgvPAHRHYDEVEEFPwpivQKAAEVGLYGLeyYQMAGQDPTGLTQ---ALIIEE 83
Cdd:cd01155 14 MEEHVYPAEQEFLEYYAEGGD-------RWWTPPPIIEKLK----AKAKAEGLWNL--FLPEVSGLSGLTNleyAYLAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 84 LfwGCAGIGLAIFGSGLALAG----LASSGTGDQIAEW-APRIFGtpdDVKvGAYAVSEPG-AGSDVSKIRTKATKVEGG 157
Cdd:cd01155 81 T--GRSFFAPEVFNCQAPDTGnmevLHRYGSEEQKKQWlEPLLDG---KIR-SAFAMTEPDvASSDATNIECSIERDGDD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 158 WLLNGEKIWITNGGIAD--VHIVVATVDPTIG--HRGQASFIVTSDAEGFQETKKTKKLGIRASHT--AELSFTDCFVPD 231
Cdd:cd01155 155 YVINGRKWWSSGAGDPRckIAIVMGRTDPDGAprHRQQSMILVPMDTPGVTIIRPLSVFGYDDAPHghAEITFDNVRVPA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 232 EQLLGGQDKldakidaahnpdpnrkssgalsTFEATRPIVG-------IQAVGVARAAFDASVQYAMERETFGVPIIRHQ 304
Cdd:cd01155 235 SNLILGEGR----------------------GFEIAQGRLGpgrihhcMRLIGAAERALELMCQRAVSREAFGKKLAQHG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 305 AIAFKLADMATEIDAARLLCWRGINMGTTWTPFK-HGEGSMAKLHAGRTAVRVTDEAIQIHGGFGYSREFDVEKFHRDSK 383
Cdd:cd01155 293 VVAHWIAKSRIEIEQARLLVLKAAHMIDTVGNKAaRKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWAR 372
|
410
....*....|....*....
gi 919108476 384 IYEIFEGTKEIQQLVIGRA 402
Cdd:cd01155 373 TLRIADGPDEVHLRSIARM 391
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
4-407 |
1.78e-29 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 118.01 E-value: 1.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 4 DLKLTEEQISAQKWAHDFARKEMREATVdgvpahRHYDEVEEFPWPIVQKAAEVGLYGL----EYyqmAGQDPTGLTQAL 79
Cdd:PRK03354 2 DFNLNDEQELFVAGIRELMASENWEAYF------AECDRDSVYPERFVKALADMGIDSLlipeEH---GGLDAGFVTLAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 80 IIEELfwGCAGI-GLAIFGSGLALAGLASSGTGDQIaEWAPRIFGTPDdvKVGAYAVSEPGAGSDVSKIRTKATKVEGGW 158
Cdd:PRK03354 73 VWMEL--GRLGApTYVLYQLPGGFNTFLREGTQEQI-DKIMAFRGTGK--QMWNSAITEPGAGSDVGSLKTTYTRRNGKV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 159 LLNGEKIWITNGGIADVHIVVA--TVDPTIGHRGQasFIVTSDAEGFQETKKTKkLGIRASHTAELSFTDCFVPDEQLLG 236
Cdd:PRK03354 148 YLNGSKCFITSSAYTPYIVVMArdGASPDKPVYTE--WFVDMSKPGIKVTKLEK-LGLRMDSCCEITFDDVELDEKDMFG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 237 gqdkldakidaahnpdpnRKSSG---ALSTFEATRPIVGIQAVGVARAAFDASVQYAMERETFGVPIIRHQAIAFKLADM 313
Cdd:PRK03354 225 ------------------REGNGfnrVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHM 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 314 ATEIDAARLL----CWRGINmGTtwtpFKHGEGSMAKLHAGRTAVRVTDEAIQIHGGFGYSREFDVEKFHRDSKIYEIFE 389
Cdd:PRK03354 287 AIKLNSMKNMlyeaAWKADN-GT----ITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSG 361
|
410
....*....|....*...
gi 919108476 390 GTKEIQQLVIGRAIARSH 407
Cdd:PRK03354 362 GSDEMQILTLGRAVLKQY 379
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
132-224 |
2.00e-25 |
|
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: 98.89 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 132 AYAVSEPGAGSDVSKIRTKA-TKVEGGWLLNGEKIWITNGGIADVHIVVATVDPTIGHRGQASFIVTSDAEGFQETKKTK 210
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....
gi 919108476 211 KLGIRASHTAELSF 224
Cdd:pfam02770 81 KLGVRGLPTGELVF 94
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
8-121 |
6.12e-17 |
|
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: 75.96 E-value: 6.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 8 TEEQISAQKWAHDFARKEMReatvdgvPAHRHYDEVEEFPWPIVQKAAEVGLYGL----EYyqmAGQDPTGLTQALIIEE 83
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIA-------PHAAEWDEEGEFPRELWKKLGELGLLGItipeEY---GGAGLDYLAYALVAEE 70
|
90 100 110
....*....|....*....|....*....|....*....
gi 919108476 84 LFWGCAGIGLAIF-GSGLALAGLASSGTGDQIAEWAPRI 121
Cdd:pfam02771 71 LARADASVALALSvHSSLGAPPILRFGTEEQKERYLPKL 109
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
270-393 |
2.26e-16 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 75.07 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 270 IVGIQAVGVARAAFDASVQYAMERET--FGVPIIRHQAIAFKLADMATEIDAARLL-------CWRGINMGTTWTPFKHG 340
Cdd:pfam08028 1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLleraaarIEAAAAAGKPVTPALRA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 919108476 341 EGSMAKLHAGRTAVRVTDEAIQIHGGFGYSREFDVEKFHRDSKIYEIFEGTKE 393
Cdd:pfam08028 81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
131-409 |
4.25e-16 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 80.30 E-value: 4.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 131 GAYAVSEPGAGSDVSKIRTKATKV-EGGWLLNGEKIWITNG--GIAD--VHIVVA-TVDPTIGHRGQASFIV---TSDAE 201
Cdd:PTZ00456 183 GTMCLTEPQCGTDLGQVKTKAEPSaDGSYKITGTKIFISAGdhDLTEniVHIVLArLPNSLPTTKGLSLFLVprhVVKPD 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 202 GFQETKKT-------KKLGIRASHTAELSFTDCFvpdEQLLGgqdkldakidaahnpDPNRKSSGALSTFEATRPIVGIQ 274
Cdd:PTZ00456 263 GSLETAKNvkcigleKKMGIKGSSTCQLSFENSV---GYLIG---------------EPNAGMKQMFTFMNTARVGTALE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 275 AVGVARAAFDASVQYAMER------------ETFGVPIIRHQ--------AIAFKLADMATEIDAARLLCWrginMGTTW 334
Cdd:PTZ00456 325 GVCHAELAFQNALRYARERrsmralsgtkepEKPADRIICHAnvrqnilfAKAVAEGGRALLLDVGRLLDI----HAAAK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 335 TPFKHGE--------GSMAKLHAGRTAVRVTDEAIQIHGGFGYSREFDVEKFHRDSKIYEIFEGTKEIQQL-VIGRAIAR 405
Cdd:PTZ00456 401 DAATREAldheigfyTPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALdFIGRKVLS 480
|
....
gi 919108476 406 SHGG 409
Cdd:PTZ00456 481 LKGG 484
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
109-401 |
3.30e-12 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 68.28 E-value: 3.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 109 GTGDQIAEW-APRIFGTpddVKVGaYAVSEPG-AGSDVSKIRTKATKVEGGWLLNGEKIWiTNGGI---ADVHIVVATVD 183
Cdd:PLN02876 533 GNKEQQLEWlIPLLEGK---IRSG-FAMTEPQvASSDATNIECSIRRQGDSYVINGTKWW-TSGAMdprCRVLIVMGKTD 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 184 PTIG-HRGQASFIVTSDAEGFQETKKTKKLGIR-ASHT-AELSFTDCFVPDEQLLGGQDKldakidaahnpdpnrkssga 260
Cdd:PLN02876 608 FNAPkHKQQSMILVDIQTPGVQIKRPLLVFGFDdAPHGhAEISFENVRVPAKNILLGEGR-------------------- 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 261 lsTFEATRPIVG-------IQAVGVARAAFDASVQYAMERETFGVPIIRHQAIAFKLADMATEIDAARLLCWRGINMGTT 333
Cdd:PLN02876 668 --GFEIAQGRLGpgrlhhcMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDR 745
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919108476 334 WTPFK-HGEGSMAKLHAGRTAVRVTDEAIQIHGGFGYSREFDVEKFHRDSKIYEIFEGTKEIQQLVIGR 401
Cdd:PLN02876 746 LGNKKaRGIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAK 814
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
274-368 |
1.23e-06 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 50.59 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 274 QAVGVARAAFDASVQYAMERETFGVPIIRHQAIAFKLADMATE---IDAARLLCWRGINmgttwtpfkHGE-----GSMA 345
Cdd:PRK09463 340 NSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNaylMDAARTLTTAAVD---------LGEkpsvlSAIA 410
|
90 100
....*....|....*....|...
gi 919108476 346 KLHAGRTAVRVTDEAIQIHGGFG 368
Cdd:PRK09463 411 KYHLTERGRQVINDAMDIHGGKG 433
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
109-368 |
2.50e-06 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 49.57 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 109 GTGDQIAEWAPRIfgtPDDVKVGAYAVSEPGAGSDVSKIRTKAT----KVEG----GWLLNGEKIWITNGGIADV-HIVV 179
Cdd:PRK13026 175 GTQEQKDYWLPRL---ADGTEIPCFALTGPEAGSDAGAIPDTGIvcrgEFEGeevlGLRLTWDKRYITLAPVATVlGLAF 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 180 ATVDP-----TIGHRGQASFIVTSDAEGFQETKKTKKLGIrASHTAELSFTDCFVPDEQLLGGQDKLdakidaahnpdpn 254
Cdd:PRK13026 252 KLRDPdgllgDKKELGITCALIPTDHPGVEIGRRHNPLGM-AFMNGTTRGKDVFIPLDWIIGGPDYA------------- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 255 rkSSG------ALStfeATRPIvGIQAVGVARA--AFDASVQYAMERETFGVPIIRHQAIAFKLADMAT---EIDAARLL 323
Cdd:PRK13026 318 --GRGwrmlveCLS---AGRGI-SLPALGTASGhmATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGntyLLEAARRL 391
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 919108476 324 CWRGINMGTtwtpfKHGEGS-MAKLHAGRTAVRVTDEAIQIHGGFG 368
Cdd:PRK13026 392 TTTGLDLGV-----KPSVVTaIAKYHMTELARDVVNDAMDIHAGKG 432
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
76-382 |
8.36e-06 |
|
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: 8.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 76 TQALIIEELFWGCAGIG--LAIFG-SGLALAGLassgtGDQIAEwapRIFGT-PDDVKVGAYAvsePGAgsdvskirtKA 151
Cdd:cd01159 54 EFAEAIATLAEACGSAAwvASIVAtHSRMLAAF-----PPEAQE---EVWGDgPDTLLAGSYA---PGG---------RA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 152 TKVEGGWLLNGEKIWITNGGIADVHIVVATVDPTIGHRGQASFIVTsdAEGFQETKKTKKLGIRASHTAELSFTDCFVPD 231
Cdd:cd01159 114 ERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDDGGPLPRAFVVP--RAEYEIVDTWHVVGLRGTGSNTVVVDDVFVPE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 232 EQLlggqdkLDAKIDAAHNPDPNRKSSGALSTFEATRPIVGIQAVGVARAAFDASVQYAMER---ETFGVPIIRHQAIAF 308
Cdd:cd01159 192 HRT------LTAGDMMAGDGPGGSTPVYRMPLRQVFPLSFAAVSLGAAEGALAEFLELAGKRvrqYGAAVKMAEAPITQL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 309 KLADMATEIDAARLL-------CWRGINMGTTWTPFKHGEGSMAKLHAGRTAVRVTDEAIQIHGGFGYSREFDVEKFHRD 381
Cdd:cd01159 266 RLAEAAAELDAARAFleratrdLWAHALAGGPIDVEERARIRRDAAYAAKLSAEAVDRLFHAAGGSALYTASPLQRIWRD 345
|
.
gi 919108476 382 S 382
Cdd:cd01159 346 I 346
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
136-408 |
1.07e-05 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 47.44 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 136 SEPGAGSDVSKIRTKATKVEGG-WLLNGEKiWITNGGIADVHIVVATVDptighRGQASFIV-------TSDAEGFQETK 207
Cdd:PRK11561 185 TEKQGGSDVLSNTTRAERLADGsYRLVGHK-WFFSVPQSDAHLVLAQAK-----GGLSCFFVprflpdgQRNAIRLERLK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 208 KtkKLGIRASHTAELSFTDC---FVPDE-----QLL--GGQDKLDAKIdAAHnpdpnrkssgalstfeatrpivgiqavG 277
Cdd:PRK11561 259 D--KLGNRSNASSEVEFQDAigwLLGEEgegirLILkmGGMTRFDCAL-GSH---------------------------G 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 278 VARAAFDASVQYAMERETFGVPIIRHQAIAFKLADMATEIDA--------ARLLCWRGINMGTTW----TPfkhgegsMA 345
Cdd:PRK11561 309 LMRRAFSVAIYHAHQRQVFGKPLIEQPLMRQVLSRMALQLEGqtallfrlARAWDRRADAKEALWarlfTP-------AA 381
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919108476 346 KLHAGRTAVRVTDEAIQIHGGFGYSREFDVEKFHRDSKIYEIFEGTKEIQQLVIGRAIARSHG 408
Cdd:PRK11561 382 KFVICKRGIPFVAEAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLNKQPG 444
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
51-390 |
1.09e-05 |
|
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: 47.71 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 51 VQKAAEVGLYGLEYYQMAGQDPTGLTQALIIEELFWGcAGIGLaifGSGLALAGLASSGTGDQIAEWAP-----RIFGTp 125
Cdd:cd01150 63 KRKAKTDVERMGELMADDPEKMLALTNSLGGYDLSLG-AKLGL---HLGLFGNAIKNLGTDEHQDYWLQgannlEIIGC- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 126 ddvkvgaYAVSEPGAGSDVSKIRTKAT--KVEGGWLLN-----GEKIWITNGGIADVHIVVATVDPTIGHR-GQASFIV- 196
Cdd:cd01150 138 -------FAQTELGHGSNLQGLETTATydPLTQEFVINtpdftATKWWPGNLGKTATHAVVFAQLITPGKNhGLHAFIVp 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 197 TSDAEGFQETKKT------KKLGIRASHTAELSFTDCFVPDEQLL--GGQDKLDAKIDAAhNPDPNRKSSGALSTFEATR 268
Cdd:cd01150 211 IRDPKTHQPLPGVtvgdigPKMGLNGVDNGFLQFRNVRIPRENLLnrFGDVSPDGTYVSP-FKDPNKRYGAMLGTRSGGR 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919108476 269 P-IVGIQAVGVARAAFDAsVQYAMERETFG-------VPIIRHQ------------AIAFKLAdmATEIDAARLLCWRGI 328
Cdd:cd01150 290 VgLIYDAAMSLKKAATIA-IRYSAVRRQFGpkpsdpeVQILDYQlqqyrlfpqlaaAYAFHFA--AKSLVEMYHEIIKEL 366
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 919108476 329 NMGTT-WTPFKHGEGSMAKLHAGRTAVRVTDEAIQIHGGFGYSREFDVEKFHRDSKIYEIFEG 390
Cdd:cd01150 367 LQGNSeLLAELHALSAGLKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEG 429
|
|
| |
