|
Name |
Accession |
Description |
Interval |
E-value |
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
1-355 |
0e+00 |
|
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: 716.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 1 MAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHNMCAWMIDSFGNE 80
Cdd:cd01162 20 MAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAAYISIHNMCAWMIDSFGND 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 81 EQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKQQGDHYILNGSKAFISGGGESDIYVVMCRTGESGAKGISCIV 160
Cdd:cd01162 100 EQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDVYVVMARTGGEGPKGISCFV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 161 VEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASCSLGAAHASVILTQEHL 240
Cdd:cd01162 180 VEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 241 KVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDAVALCSMAKLFATEECFAICNQALQMHGGYGYL 320
Cdd:cd01162 260 EERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATDECFDVANQALQLHGGYGYL 339
|
330 340 350
....*....|....*....|....*....|....*
gi 1720432362 321 KDYAVQQYMRDSRVHQILEGSNEVMRMLISRNLLQ 355
Cdd:cd01162 340 KDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLT 374
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
2-354 |
3.30e-147 |
|
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: 420.40 E-value: 3.30e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 2 APNMAEWDQKELFPVDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHNMCAWMIDSFGNEE 81
Cdd:COG1960 25 APEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASLALPVGVHNGAAEALLRFGTEE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 82 QRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKQQGDHYILNGSKAFISGGGESDIYVVMCRT-GESGAKGISCIV 160
Cdd:COG1960 105 QKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVADVILVLARTdPAAGHRGISLFL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 161 VEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASCSLGAAHASVILTQEHL 240
Cdd:COG1960 185 VPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 241 KVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEErEDAVALCSMAKLFATEECFAICNQALQMHGGYGYL 320
Cdd:COG1960 265 REREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAG-EDAALEAAMAKLFATEAALEVADEALQIHGGYGYT 343
|
330 340 350
....*....|....*....|....*....|....
gi 1720432362 321 KDYAVQQYMRDSRVHQILEGSNEVMRMLISRNLL 354
Cdd:COG1960 344 REYPLERLYRDARILTIYEGTNEIQRLIIARRLL 377
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
2-354 |
2.15e-142 |
|
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: 408.19 E-value: 2.15e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 2 APNMAEWDQKELFPVDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHN-MCAWMIDSFGNE 80
Cdd:cd01158 19 APLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVIVSVHNsLGANPIIKFGTE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 81 EQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKQQGDHYILNGSKAFISGGGESDIYVVMCRTGES-GAKGISCI 159
Cdd:cd01158 99 EQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFYIVFAVTDPSkGYRGITAF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 160 VVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASCSLGAAHASVILTQEH 239
Cdd:cd01158 179 IVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGIAAQALGIAQAALDAAVDY 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 240 LKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAvALQEEREDAVALCSMAKLFATEECFAICNQALQMHGGYGY 319
Cdd:cd01158 259 AKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAA-RLKDNGEPFIKEAAMAKLFASEVAMRVTTDAVQIFGGYGY 337
|
330 340 350
....*....|....*....|....*....|....*
gi 1720432362 320 LKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNLL 354
Cdd:cd01158 338 TKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLL 372
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
69-351 |
5.27e-119 |
|
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: 346.96 E-value: 5.27e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 69 MCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKQQGDHYILNGSKAFISGGGESDIYVVMCRT 148
Cdd:cd00567 43 LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLART 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 149 GESGA--KGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASCSL 226
Cdd:cd00567 123 DEEGPghRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLLAAVAL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 227 GAAHASVILTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDAVALCSMAKLFATEECFAI 306
Cdd:cd00567 203 GAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFATEAAREV 282
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1720432362 307 CNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISR 351
Cdd:cd00567 283 ADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
1-354 |
2.07e-96 |
|
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: 290.94 E-value: 2.07e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 1 MAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALA-TGCTSTTayISIHN-MCAWMIDSFG 78
Cdd:cd01160 18 VAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELArAGGSGPG--LSLHTdIVSPYITRAG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 79 NEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKQQGDHYILNGSKAFISGGGESDIYVVMCRTG--ESGAKGI 156
Cdd:cd01160 96 SPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVIVVARTGgeARGAGGI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 157 SCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASCSLGAAHASVILT 236
Cdd:cd01160 176 SLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAAGALAAAEFMLEET 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 237 QEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDaVALCSMAKLFATEECFAICNQALQMHGG 316
Cdd:cd01160 256 RNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLD-VAEASMAKYWATELQNRVAYECVQLHGG 334
|
330 340 350
....*....|....*....|....*....|....*...
gi 1720432362 317 YGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNLL 354
Cdd:cd01160 335 WGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
1-355 |
1.06e-94 |
|
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: 286.61 E-value: 1.06e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 1 MAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIH-NMCAWMIDSFGN 79
Cdd:cd01156 21 IAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVALSYGAHsNLCINQIYRNGS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 80 EEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKQQGDHYILNGSKAFISGGGESDIYVVMCRTG-ESGAKGISC 158
Cdd:cd01156 101 AAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDADTLVVYAKTDpSAGAHGITA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 159 IVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASCSLGAAHASVILTQE 238
Cdd:cd01156 181 FIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYERLVLAGGPIGIMQAALDVAIP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 239 HLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDAVAlCSMAKLFATEECFAICNQALQMHGGYG 318
Cdd:cd01156 261 YAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKD-AAGVILYAAEKATQVALDAIQILGGNG 339
|
330 340 350
....*....|....*....|....*....|....*..
gi 1720432362 319 YLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNLLQ 355
Cdd:cd01156 340 YINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
9-356 |
1.12e-87 |
|
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: 270.11 E-value: 1.12e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 9 DQKELFPVDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTSTTAYiSIHNMCAWM-IDSFGNEEQRHKFC 87
Cdd:cd01161 52 DQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMDLGFSVTL-GAHQSIGFKgILLFGTEAQKEKYL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 88 PPLCTMEKFASYCLTEPGSGSDAASLLTSAK--QQGDHYILNGSKAFISGGGESDIYVVMCRTGESGAKG-----ISCIV 160
Cdd:cd01161 131 PKLASGEWIAAFALTEPSSGSDAASIRTTAVlsEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDATGsvkdkITAFI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 161 VEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASCSLGAAHASVILTQEHL 240
Cdd:cd01161 211 VERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 241 KVRKQFGAPLARSQYLQFQLADMATKLVASRLMI-RTAAVALQEEREDAVALCSMAKLFATEECFAICNQALQMHGGYGY 319
Cdd:cd01161 291 NNRKQFGKKIHEFGLIQEKLANMAILQYATESMAyMTSGNMDRGLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGF 370
|
330 340 350
....*....|....*....|....*....|....*..
gi 1720432362 320 LKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNLLQD 356
Cdd:cd01161 371 MREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQH 407
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
3-354 |
6.17e-81 |
|
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: 251.74 E-value: 6.17e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 3 PNMAEWDQKELFPVDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHNMCAWMIDSFGNEEQ 82
Cdd:cd01157 22 PVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQTAIEANSLGQMPVIISGNDEQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 83 RHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKQQGDHYILNGSKAFISGGGESDIYVVMCRTGES----GAKGISC 158
Cdd:cd01157 102 KKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDpkcpASKAFTG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 159 IVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASCSLGAAHASVILTQE 238
Cdd:cd01157 182 FIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 239 HLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDAVaLCSMAKLFATEECFAICNQALQMHGGYG 318
Cdd:cd01157 262 YALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTY-YASIAKAFAADIANQLATDAVQIFGGNG 340
|
330 340 350
....*....|....*....|....*....|....*.
gi 1720432362 319 YLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNLL 354
Cdd:cd01157 341 FNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
1-356 |
1.24e-58 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 194.71 E-value: 1.24e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 1 MAPNMAEWDQKELFP--VDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIH-NMCAWMIDSF 77
Cdd:PLN02519 45 IAPHAAAIDATNSFPkdVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHsNLCINQLVRN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 78 GNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKQQGDHYILNGSKAFISGGGESDIYVVMCRTG-ESGAKGI 156
Cdd:PLN02519 125 GTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTDvAAGSKGI 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 157 SCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASCSLGAAHASVILT 236
Cdd:PLN02519 205 TAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 237 QEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDAVAlCSMAKLFATEECFAICNQALQMHGG 316
Cdd:PLN02519 285 LPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKD-CAGVILCAAERATQVALQAIQCLGG 363
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1720432362 317 YGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNLLQD 356
Cdd:PLN02519 364 NGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
1-351 |
7.20e-57 |
|
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: 189.49 E-value: 7.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 1 MAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVRtDVGGSGLSRLDTSVI---FEALATGCTSTtayISIH-NMCAWMIDS 76
Cdd:cd01151 32 LAPRVLEAYREEKFDRKIIEEMGELGLLGATIK-GYGCAGLSSVAYGLIareVERVDSGYRSF---MSVQsSLVMLPIYD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 77 FGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKQQGDHYILNGSKAFISGGGESDIYVVMCRTGESGakGI 156
Cdd:cd01151 108 FGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIADVFVVWARNDETG--KI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 157 SCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIgTEGQGFLIAMKGLNGGRINVASCSLGAAHASVILT 236
Cdd:cd01151 186 RGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL-PGAEGLRGPFKCLNNARYGIAWGALGAAEDCYHTA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 237 QEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLM-IRTAavALQEEREDAVALCSMAKLFATEECFAICNQALQMHG 315
Cdd:cd01151 265 RQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLAcLRVG--RLKDQGKATPEQISLLKRNNCGKALEIARTAREMLG 342
|
330 340 350
....*....|....*....|....*....|....*.
gi 1720432362 316 GYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISR 351
Cdd:cd01151 343 GNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGR 378
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
5-356 |
1.79e-52 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 178.00 E-value: 1.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 5 MAEWDQKELFPVDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTstTAYISIHNMCAWMIDSFGNEEQRH 84
Cdd:PRK12341 29 FRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCGA--PAFLITNGQCIHSMRRFGSAEQLR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 85 KfcpplcTMEKFA-----SYCL--TEPGSGSDAASLLTSAKQQGDHYILNGSKAFISGGGESDIYVVMCRTGESGA--KG 155
Cdd:PRK12341 107 K------TAESTLetgdpAYALalTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAKEYPYMLVLARDPQPKDpkKA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 156 ISCIVVEKGTPGLSFGKKEKkVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASCSLGAAHASVIL 235
Cdd:PRK12341 181 FTLWWVDSSKPGIKINPLHK-IGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFEMERLINAARSLGFAECAFED 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 236 TQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAValqeEREDAVAL---CSMAKLFATEECFAICNQALQ 312
Cdd:PRK12341 260 AARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAW----QADNGQSLrtsAALAKLYCARTAMEVIDDAIQ 335
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1720432362 313 MHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNLLQD 356
Cdd:PRK12341 336 IMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKD 379
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
204-353 |
7.60e-51 |
|
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: 166.28 E-value: 7.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 204 GQGFLIAMKGLNGGRINVASCSLGAAHASVILTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQE 283
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 284 EREDAVAlCSMAKLFATEECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNL 353
Cdd:pfam00441 81 GGPDGAE-ASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
1-342 |
1.17e-48 |
|
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: 168.72 E-value: 1.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 1 MAPNMAEWDQKEL--------FP---VDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTsTTAYISIHNM 69
Cdd:cd01153 13 LAPLNADGDREGPvfddgrvvVPppfKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDA-PLMYASGTQG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 70 CAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKQQGD-HYILNGSKAFISGG----GESDIYVV 144
Cdd:cd01153 92 AAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGehdmSENIVHLV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 145 MCRTGE--SGAKGISCIVVEK----GTP-GLSFGKKEKKVGWNSQPTRAVIFEDCAVPVanrIGTEGQGFLIAMKGLNGG 217
Cdd:cd01153 172 LARSEGapPGVKGLSLFLVPKflddGERnGVTVARIEEKMGLHGSPTCELVFDNAKGEL---IGEEGMGLAQMFAMMNGA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 218 RINVASCSLGAAHASVILTQEHLKVRKQFGAPL--------ARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDAV 289
Cdd:cd01153 249 RLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIkaapavtiIHHPDVRRSLMTQKAYAEGSRALDLYTATVQDLAERKAT 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720432362 290 -------------ALCSMAKLFATEECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSN 342
Cdd:cd01153 329 egedrkalsaladLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTT 394
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
14-355 |
1.45e-42 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 152.78 E-value: 1.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 14 FPVDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALATG----CTsttAYISiHNMCawMIDSFGNE---EQRHKF 86
Cdd:PTZ00461 69 FNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYdpgfCL---AYLA-HSML--FVNNFYYSaspAQRARW 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 87 CPPLCTMEKFASYCLTEPGSGSDAASLLTSAKQQGD-HYILNGSKAFISGGGESDIYVVMCRTGESgakgISCIVVEKGT 165
Cdd:PTZ00461 143 LPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGTVADVFLIYAKVDGK----ITAFVVERGT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 166 PGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASCSLGAAHASVILTQEHLKVRKQ 245
Cdd:PTZ00461 219 KGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 246 FGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDAVAlCSMAKLFATEECFAICNQALQMHGGYGYLKDYAV 325
Cdd:PTZ00461 299 FGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLG-SDAAKLFATPIAKKVADSAIQVMGGMGYSRDMPV 377
|
330 340 350
....*....|....*....|....*....|
gi 1720432362 326 QQYMRDSRVHQILEGSNEVMRMLISRNLLQ 355
Cdd:PTZ00461 378 ERLWRDAKLLEIGGGTIEAHHKNITKDLLK 407
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
6-356 |
4.19e-41 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 148.06 E-value: 4.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 6 AEWDQKELFPVDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALatGCTSTTAYISIHNMCAW-MIDSFGNEEQRH 84
Cdd:PRK03354 30 AECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMEL--GRLGAPTYVLYQLPGGFnTFLREGTQEQID 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 85 KFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKQQGDHYILNGSKAFISGGGESDIYVVMCRTGESGAKGI-SCIVVEK 163
Cdd:PRK03354 108 KIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASPDKPVyTEWFVDM 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 164 GTPGLSFGKKEkKVGWNSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASCSLGAAHASVILTQEHLKVR 243
Cdd:PRK03354 188 SKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 244 KQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVAlQEEREDAVALCSMAKLFATEECFAICNQALQMHGGYGYLKDY 323
Cdd:PRK03354 267 VQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWK-ADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNH 345
|
330 340 350
....*....|....*....|....*....|...
gi 1720432362 324 AVQQYMRDSRVHQILEGSNEVMRMLISRNLLQD 356
Cdd:PRK03354 346 RISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQ 378
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
20-355 |
1.24e-39 |
|
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 144.03 E-value: 1.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 20 RKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASY 99
Cdd:cd01152 42 RALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 100 CLTEPGSGSDAASLLTSAKQQGDHYILNGSKAFISGGGESDIYVVMCRTGESGAK--GISCIVVEKGTPGLSFGKKEKKV 177
Cdd:cd01152 122 GFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDPEAPKhrGISILLVDMDSPGVTVRPIRSIN 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 178 GwnSQPTRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVascslgAAHASVILTQ--EHLKVRKQFGAPLARSQY 255
Cdd:cd01152 202 G--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSI------GGSAATFFELllARLLLLTRDGRPLIDDPL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 256 LQFQLADMATKLVASRLMIRTAAVALQE-EREDAVAlcSMAKLFATEECFAICNQALQMHGGYGYLKDYA--------VQ 326
Cdd:cd01152 274 VRQRLARLEAEAEALRLLVFRLASALAAgKPPGAEA--SIAKLFGSELAQELAELALELLGTAALLRDPApgaelagrWE 351
|
330 340
....*....|....*....|....*....
gi 1720432362 327 QYMRDSRVHQILEGSNEVMRMLISRNLLQ 355
Cdd:cd01152 352 ADYLRSRATTIYGGTSEIQRNIIAERLLG 380
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
77-355 |
7.88e-39 |
|
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: 142.14 E-value: 7.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 77 FGNEEQRHKFCPPLCTMEKFASYCLTEPG-SGSDAASLLTSAKQQGDHYILNGSKAFISGGGESD--IYVVMCRTGESGA 153
Cdd:cd01155 107 YGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRKWWSSGAGDPRckIAIVMGRTDPDGA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 154 ---KGISCIVVEKGTPGLSFGKKEKKVGWNSQPT--RAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASCSLGA 228
Cdd:cd01155 187 prhRQQSMILVPMDTPGVTIIRPLSVFGYDDAPHghAEITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIHHCMRLIGA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 229 AHASVILTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVAL-QEEREDAVALCSMAKLFATEECFAIC 307
Cdd:cd01155 267 AERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIdTVGNKAARKEIAMIKVAAPRMALKII 346
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1720432362 308 NQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNLLQ 355
Cdd:cd01155 347 DRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMELK 394
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
1-353 |
4.08e-37 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 138.06 E-value: 4.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 1 MAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVRtDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHN-MCAWMIDSFGN 79
Cdd:PLN02526 48 VAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIK-GYGCPGLSITASAIATAEVARVDASCSTFILVHSsLAMLTIALCGS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 80 EEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKQQGDHYILNGSKAFISGGGESDIYVVMCRTGESgaKGISCI 159
Cdd:PLN02526 127 EAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFADVLVIFARNTTT--NQINGF 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 160 VVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIgTEGQGFLIAMKGLNGGRINVASCSLGAAHASVILTQEH 239
Cdd:PLN02526 205 IVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRL-PGVNSFQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRY 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 240 LKVRKQFGAPLARSQYLQFQLADM-----ATKLVASRLmirtaaVALQEEREDAVALCSMAKLFATEECFAICNQALQMH 314
Cdd:PLN02526 284 LKERKQFGAPLAAFQINQEKLVRMlgniqAMFLVGWRL------CKLYESGKMTPGHASLGKAWITKKARETVALGRELL 357
|
330 340 350
....*....|....*....|....*....|....*....
gi 1720432362 315 GGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNL 353
Cdd:PLN02526 358 GGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREI 396
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
64-345 |
1.20e-32 |
|
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: 125.95 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 64 ISIHNMCAWMIDSFGNEEQRHkFCPPLCTMEK----FASYCLTEPGSGSDAASLLTSA-KQQGDHYILNGSKAFISGGgE 138
Cdd:cd01154 113 LTMTDAAVYALRKYGPEELKQ-YLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAeRSGGGVYRLNGHKWFASAP-L 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 139 SDIYVVMCRT--GESGAKGISCIVV----EKGT-PGLSFGKKEKKVGWNSQPTRAVIFEDCavpVANRIGTEGQGFLIAM 211
Cdd:cd01154 191 ADAALVLARPegAPAGARGLSLFLVprllEDGTrNGYRIRRLKDKLGTRSVATGEVEFDDA---EAYLIGDEGKGIYYIL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 212 KGLNGGRINVASCSLGAAHASVILTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQ-------EE 284
Cdd:cd01154 268 EMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDraaadkpVE 347
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720432362 285 REDAVALCSMAKLFATEECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVM 345
Cdd:cd01154 348 AHMARLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQ 408
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
1-94 |
3.72e-31 |
|
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: 113.71 E-value: 3.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 1 MAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHN-MCAWMIDSFGN 79
Cdd:pfam02771 19 IAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVALALSVHSsLGAPPILRFGT 98
|
90
....*....|....*
gi 1720432362 80 EEQRHKFCPPLCTME 94
Cdd:pfam02771 99 EEQKERYLPKLASGE 113
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
98-190 |
2.49e-29 |
|
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: 108.52 E-value: 2.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 98 SYCLTEPGSGSDAASLLTSA-KQQGDHYILNGSKAFISGGGESDIYVVMCRTG-ESGAKGISCIVVEKGTPGLSFGKKEK 175
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGgDDRHGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 1720432362 176 KVGWNSQPTRAVIFE 190
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
77-355 |
2.22e-24 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 104.49 E-value: 2.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 77 FGNEEQRHKFCPPLCTMEKFASYCLTEPG-SGSDAASLLTSAKQQGDHYILNGSKAFISGGGES--DIYVVMCRTGESGA 153
Cdd:PLN02876 532 YGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPrcRVLIVMGKTDFNAP 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 154 --KGISCIVVEKGTPGLSFGKKEKKVGWNSQPT--RAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASCSLGAA 229
Cdd:PLN02876 612 khKQQSMILVDIQTPGVQIKRPLLVFGFDDAPHghAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAA 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 230 HASVILTQEHLKVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEE-REDAVALCSMAKLFATEECFAICN 308
Cdd:PLN02876 692 ERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDRLgNKKARGIIAMAKVAAPNMALKVLD 771
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1720432362 309 QALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNLLQ 355
Cdd:PLN02876 772 MAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAKLELQ 818
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
26-354 |
1.54e-21 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 95.71 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 26 GFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTSTTAY--ISIHNMCAWMidSFGNEEQRHKFCPPLCTMEKFASYCLTE 103
Cdd:PTZ00456 112 GWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYpgLSIGAANTLM--AWGSEEQKEQYLTKLVSGEWSGTMCLTE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 104 PGSGSDAASLLTSAKQQGD-HYILNGSKAFISGGG----ESDIYVVMCRTGES--GAKGISCIVVEKGTP---------- 166
Cdd:PTZ00456 190 PQCGTDLGQVKTKAEPSADgSYKITGTKIFISAGDhdltENIVHIVLARLPNSlpTTKGLSLFLVPRHVVkpdgsletak 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 167 GLSFGKKEKKVGWNSQPTRAVIFEDcavPVANRIGTEGQGFLIAMKGLNGGRInvaSCSL-GAAHASVILtQEHLKVRKQ 245
Cdd:PTZ00456 270 NVKCIGLEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTARV---GTALeGVCHAELAF-QNALRYARE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 246 FGAPLARSQYLQFQLAdmATKLVAS---RLMIRTA-AVA---------------LQEEREDAVA----------LCSMAK 296
Cdd:PTZ00456 343 RRSMRALSGTKEPEKP--ADRIICHanvRQNILFAkAVAeggrallldvgrlldIHAAAKDAATrealdheigfYTPIAK 420
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720432362 297 LFATEECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRM-LISRNLL 354
Cdd:PTZ00456 421 GCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALdFIGRKVL 479
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
221-343 |
1.40e-19 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 83.55 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 221 VASCSLGAAHASVILTQEHL--KVRKQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDA-------VAL 291
Cdd:pfam08028 2 IAAAALGAARAALAEFTERArgRVRAYFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAAAGkpvtpalRAE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1720432362 292 CSMAKLFATEECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNE 343
Cdd:pfam08028 82 ARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
17-354 |
1.11e-12 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 69.22 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 17 DVMRKAaqlGFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHNMC--AWMIDSFGNEEQRHKFCPPLCTME 94
Cdd:PRK13026 115 DYLKKE---GFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPNSLgpGELLTHYGTQEQKDYWLPRLADGT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 95 KFASYCLTEPGSGSDAASL-----LTSAKQQGDHYI---LNGSKAFIS--------G------------GGESDIyvvmc 146
Cdd:PRK13026 192 EIPCFALTGPEAGSDAGAIpdtgiVCRGEFEGEEVLglrLTWDKRYITlapvatvlGlafklrdpdgllGDKKEL----- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 147 rtgesgakGISCIVVEKGTPGLSFGKKEKKVGWNSQ--PTRAvifEDCAVPVANRIGTE---GQGFLIAMKGLNGGR-IN 220
Cdd:PRK13026 267 --------GITCALIPTDHPGVEIGRRHNPLGMAFMngTTRG---KDVFIPLDWIIGGPdyaGRGWRMLVECLSAGRgIS 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 221 VASCSLGAAHASVILTQEHLKVRKQFGAPLARSQYLQFQLADMATK---LVASRLMIrTAAVALQEEREDAVAlcsMAKL 297
Cdd:PRK13026 336 LPALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGNtylLEAARRLT-TTGLDLGVKPSVVTA---IAKY 411
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 298 FATEECFAICNQALQMHGGYGYL---KDYAVQQYMRdSRVHQILEGSNevmrmLISRNLL 354
Cdd:PRK13026 412 HMTELARDVVNDAMDIHAGKGIQlgpKNYLGHAYMA-VPIAITVEGAN-----ILTRNLM 465
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
77-318 |
1.28e-12 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 69.07 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 77 FGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASL-----LTSAKQQGDHYI---LNGSKAFIS--------G----- 135
Cdd:PRK09463 175 YGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIpdtgvVCKGEWQGEEVLgmrLTWNKRYITlapiatvlGlafkl 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 136 -------GGESDIyvvmcrtgesgakGISCIVVEKGTPGLSFGKKEKKVGWNSQ--PTRAvifEDCAVPVANRIGTE--- 203
Cdd:PRK09463 255 ydpdgllGDKEDL-------------GITCALIPTDTPGVEIGRRHFPLNVPFQngPTRG---KDVFIPLDYIIGGPkma 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 204 GQGFLIAMKGLNGGR-INVASCSLGAAHASVILTQEHLKVRKQFGAPLARSQYLQFQLADMATK---LVASRLMIrTAAV 279
Cdd:PRK09463 319 GQGWRMLMECLSVGRgISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNaylMDAARTLT-TAAV 397
|
250 260 270
....*....|....*....|....*....|....*....
gi 1720432362 280 ALQEerEDAVaLCSMAKLFATEECFAICNQALQMHGGYG 318
Cdd:PRK09463 398 DLGE--KPSV-LSAIAKYHLTERGRQVINDAMDIHGGKG 433
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
101-345 |
1.68e-10 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 62.08 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 101 LTEPGSGSDAASLLTSA-KQQGDHYILNGSKAFISGGgESDIYVVMCRTgesgAKGISCIVVEKGTP-----GLSFGKKE 174
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAeRLADGSYRLVGHKWFFSVP-QSDAHLVLAQA----KGGLSCFFVPRFLPdgqrnAIRLERLK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 175 KKVGWNSQPTRAVIFEDCavpVANRIGTEGQGF--LIAMKGLNggRINvasCSLGAaHA------SVILTQEHLkvRKQF 246
Cdd:PRK11561 259 DKLGNRSNASSEVEFQDA---IGWLLGEEGEGIrlILKMGGMT--RFD---CALGS-HGlmrrafSVAIYHAHQ--RQVF 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 247 GAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDAVALcsMAKLFATEECFAICNQ-------ALQMHGGYGY 319
Cdd:PRK11561 328 GKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDRRADAKEAL--WARLFTPAAKFVICKRgipfvaeAMEVLGGIGY 405
|
250 260
....*....|....*....|....*.
gi 1720432362 320 LKDYAVQQYMRDSRVHQILEGSNEVM 345
Cdd:PRK11561 406 CEESELPRLYREMPVNSIWEGSGNIM 431
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
4-334 |
3.38e-10 |
|
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: 60.83 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 4 NMAEWDQKELFPVDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHNMCAWMIDSFGNEEQR 83
Cdd:cd01159 13 RAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIVATHSRMLAAFPPEAQE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 84 HKFcpplctmekfasycltepgsGSDAASLLTS-------AKQQGDHYILNGSKAFISGGGESDIYVVMCRTGESGAKGI 156
Cdd:cd01159 93 EVW--------------------GDGPDTLLAGsyapggrAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDDGGPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 157 SCIVVekgtpglsFGKKEKK-------VGWNSQPTRAVIFEDCAVPVANrigtegqgFLIAMKGLNGGR----------- 218
Cdd:cd01159 153 PRAFV--------VPRAEYEivdtwhvVGLRGTGSNTVVVDDVFVPEHR--------TLTAGDMMAGDGpggstpvyrmp 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 219 ------INVASCSLGAAHASVILTQEHLKVRKQ---FGAPLARSQYLQFQLADMATKLVASR-LMIRTAAV--ALQEERE 286
Cdd:cd01159 217 lrqvfpLSFAAVSLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAELDAARaFLERATRDlwAHALAGG 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1720432362 287 ----DAVALCSMAKLFATEECFAICNQALQMHGGYGYLKDYAVQQYMRDSRV 334
Cdd:cd01159 297 pidvEERARIRRDAAYAAKLSAEAVDRLFHAAGGSALYTASPLQRIWRDIHA 348
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
17-354 |
7.78e-09 |
|
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: 56.95 E-value: 7.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 17 DVMRKAAQLGF-GGVYVRTDVggsglsrLDTSVIFEALATGCTSTTAYISIH-NMCAWMIDSFGNEEQRHKFCPPLCTME 94
Cdd:cd01150 61 ELKRKAKTDVErMGELMADDP-------EKMLALTNSLGGYDLSLGAKLGLHlGLFGNAIKNLGTDEHQDYWLQGANNLE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 95 KFASYCLTEPGSGSDAASLLTSAK--QQGDHYILN-----GSKAFISGGGESDIYVV----MCRTGES-GAKG----ISC 158
Cdd:cd01150 134 IIGCFAQTELGHGSNLQGLETTATydPLTQEFVINtpdftATKWWPGNLGKTATHAVvfaqLITPGKNhGLHAfivpIRD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 159 IVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVP---VANRIG-------------TEGQGFLIAMKGLNGGRINVA 222
Cdd:cd01150 214 PKTHQPLPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPrenLLNRFGdvspdgtyvspfkDPNKRYGAMLGTRSGGRVGLI 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 223 SCSLGAAHASVILTQEHLKVRKQFGAPLARS----------QYLQF-QLA-----DMATKLVASRL--MIRTAAVALQEE 284
Cdd:cd01150 294 YDAAMSLKKAATIAIRYSAVRRQFGPKPSDPevqildyqlqQYRLFpQLAaayafHFAAKSLVEMYheIIKELLQGNSEL 373
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 285 REDAVALCSMAKLFATEECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNLL 354
Cdd:cd01150 374 LAELHALSAGLKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLL 443
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
2-335 |
9.64e-09 |
|
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, which catalyzes the first two steps of DBT desulfurization in mesophilic bacteria. DszC converts DBT to DBT-sulfoxide, which is then converted to DBT-sulfone. Bacteria with this enzyme are candidates for the removal of organic sulfur compounds from fossil fuels, which pollute the environment. An equivalent enzyme tdsC, is found in thermophilic bacteria. This alignment also contains a closely related uncharacterized subgroup.
Pssm-ID: 173852 [Multi-domain] Cd Length: 377 Bit Score: 56.18 E-value: 9.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 2 APNMAEWDQKELFPVDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHNMCAWMIDSFGNEE 81
Cdd:cd01163 11 AEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGFVEALLLAGPEQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 82 QRhKFCPPLCTMEKFASYCLTEPGSgSDAASLLTSAKQQGDHYILNGSKAFISGGGESDiYVVMCRTGESGAKGIscIVV 161
Cdd:cd01163 91 FR-KRWFGRVLNGWIFGNAVSERGS-VRPGTFLTATVRDGGGYVLNGKKFYSTGALFSD-WVTVSALDEEGKLVF--AAV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 162 EKGTPGLS-------FGKKEKKVGwNSQPTRAVIFEDCAVPVANR------IGTEGQGFLIAmkglnggriNVASCSLGA 228
Cdd:cd01163 166 PTDRPGITvvddwdgFGQRLTASG-TVTFDNVRVEPDEVLPRPNApdrgtlLTAIYQLVLAA---------VLAGIARAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 229 AHASVILTQEHLKVRKQFGAPLARSQ-YLQFQLADMATKLVASRLMIRTAAVALQ-----------EEREDAVALCSMAK 296
Cdd:cd01163 236 LDDAVAYVRSRTRPWIHSGAESARDDpYVQQVVGDLAARLHAAEALVLQAARALDaaaaagtaltaEARGEAALAVAAAK 315
|
330 340 350
....*....|....*....|....*....|....*....
gi 1720432362 297 LFATEECFAICNQALQMHGGYGYLKDYAVQQYMRDSRVH 335
Cdd:cd01163 316 VVVTRLALDATSRLFEVGGASATAREHNLDRHWRNARTH 354
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
29-211 |
1.80e-04 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 43.33 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 29 GVYVRTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIH-NMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYClTEPGSG 107
Cdd:PTZ00457 67 GARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHsGFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWA-TEEGCG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 108 SDAASLLTSAKQQGD-HYILNGSKAFISGGGESDiYVVMCRT-----GESGAKGI---SCIVVEKGTPGLSfgkkekkVG 178
Cdd:PTZ00457 146 SDISMNTTKASLTDDgSYVLTGQKRCEFAASATH-FLVLAKTltqtaAEEGATEVsrnSFFICAKDAKGVS-------VN 217
|
170 180 190
....*....|....*....|....*....|...
gi 1720432362 179 WNSqptraVIFEDcaVPVANRIGTEGQGFLIAM 211
Cdd:PTZ00457 218 GDS-----VVFEN--TPAADVVGVVGEGFKDAM 243
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
57-126 |
3.38e-04 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 42.52 E-value: 3.38e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720432362 57 CTSTTAYISIH-NMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSA--KQQGDHYIL 126
Cdd:PTZ00460 88 CPQGTFISTVHfAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTAtyDKQTNEFVI 160
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
166-355 |
5.47e-03 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 38.69 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 166 PGLSFGKKEKKVGWNSQPTRAVIFEDCAVP---VANRIG-------------TEGQGFLIAMKGLNGGRINVASCSLGAA 229
Cdd:PLN02636 266 PGVEIRDCGHKVGLNGVDNGALRFRSVRIPrdnLLNRFGdvsrdgkytsslpTINKRFAATLGELVGGRVGLAYGSVGVL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432362 230 HASVILTQEHLKVRKQFGAP------LARSQYLQFQLADM-----ATKLVASRLMIRTAAVALQEERE---DAVALCSMA 295
Cdd:PLN02636 346 KASNTIAIRYSLLRQQFGPPkqpeisILDYQSQQHKLMPMlastyAFHFATEYLVERYSEMKKTHDDQlvaDVHALSAGL 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720432362 296 KLFATE---ECFAICNQALqmhGGYGYLkdyAVQQY--MR-DSRVHQILEGSNEVMRMLISRNLLQ 355
Cdd:PLN02636 426 KAYITSytaKALSTCREAC---GGHGYA---AVNRFgsLRnDHDIFQTFEGDNTVLLQQVAADLLK 485
|
|
| |
