|
Name |
Accession |
Description |
Interval |
E-value |
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
5-384 |
3.34e-120 |
|
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: 352.99 E-value: 3.34e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 5 SEELNAIREGVRALCAEFDAAYWRRIDEQRGFPEAFVKALTDAGWLSAMIPEEYGGSGLGLAEASVILEEVNR-CGGNSG 83
Cdd:COG1960 6 TEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARaDASLAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 84 TVHGQMYNMFTLLRNGSEAQKRFYLPKLASGELRLqSMGVTEPTTGTDTTKIKTTAVRKGDRYVINGQKVWISRIQHSDL 163
Cdd:COG1960 86 PVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIG-AFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVADV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 164 MILLARTTPlaevKRKSEGMSIFLVDLREAigkGLTVQPIAN---MVNHETNELFFDNLEIPADSLIGEEGKGFRYILDG 240
Cdd:COG1960 165 ILVLARTDP----AAGHRGISLFLVPKDTP---GVTVGRIEDkmgLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMST 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 241 LNAERTLIAAECIGDGRWFIDKASHYARDRVVFGRPIGQNQGVQFPIAEAHIEVEAADLMRWRACQEYDAGLNAGASANM 320
Cdd:COG1960 238 LNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAM 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489176391 321 AKYLAAKASWEAANACLQTHGGFGFACEYDVERKFRETRLYQVAPISTNLILSYVAEHLLELPR 384
Cdd:COG1960 318 AKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
6-381 |
1.46e-82 |
|
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: 256.81 E-value: 1.46e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 6 EELNAIREGVRALCAEFDAAYWRRIDEQRGFPEAFVKALTDAGWLSAMIPEEYGGSGLGLAEASVILEEVNRCGGNSGT- 84
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 85 --VHGQMYNMfTLLRNGSEAQKRFYLPKLASGElRLQSMGVTEPTTGTDTTKIKTTAVRKGDRYVINGQKVWISRIQHSD 162
Cdd:cd01158 81 vsVHNSLGAN-PIIKFGTEEQKKKYLPPLATGE-KIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 163 LMILLARTTPlaevKRKSEGMSIFLVDlREAigKGLTV-QPIANMVNH--ETNELFFDNLEIPADSLIGEEGKGFRYILD 239
Cdd:cd01158 159 FYIVFAVTDP----SKGYRGITAFIVE-RDT--PGLSVgKKEDKLGIRgsSTTELIFEDVRVPKENILGEEGEGFKIAMQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 240 GLNAERTLIAAECIGDGRWFIDKASHYARDRVVFGRPIGQNQGVQFPIAEAHIEVEAADLMRWRACQEYDAGLNAGASAN 319
Cdd:cd01158 232 TLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAA 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489176391 320 MAKYLAAKASWEAANACLQTHGGFGFACEYDVERKFRETRLYQVAPISTNLILSYVAEHLLE 381
Cdd:cd01158 312 MAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
6-377 |
2.41e-81 |
|
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: 251.82 E-value: 2.41e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 6 EELNAIREGVRALCAEFDAAYWRRIDEQRGFPEAFVKALtdaGWLSAMipeeyggsglglaeasvileevnrcggnsgtv 85
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAEL---GLLLGA-------------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 86 hgqmynmFTLLRNGSEAQKRFYLPKLASGELRLqSMGVTEPTTGTDTTKIKTTAVRKGDRYVINGQKVWISRIQHSDLMI 165
Cdd:cd00567 46 -------ALLLAYGTEEQKERYLPPLASGEAIA-AFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 166 LLARTTPLAEVKRkseGMSIFLVDLREaigKGLTVQPIANMVNHE---TNELFFDNLEIPADSLIGEEGKGFRYILDGLN 242
Cdd:cd00567 118 VLARTDEEGPGHR---GISAFLVPADT---PGVTVGRIWDKMGMRgsgTGELVFDDVRVPEDNLLGEEGGGFELAMKGLN 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 243 AERTLIAAECIGDGRWFIDKASHYARDRVVFGRPIGQNQGVQFPIAEAHIEVEAADLMRWRACQEYDAGL-NAGASANMA 321
Cdd:cd00567 192 VGRLLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPdEARLEAAMA 271
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 489176391 322 KYLAAKASWEAANACLQTHGGFGFACEYDVERKFRETRLYQVAPISTNLILSYVAE 377
Cdd:cd00567 272 KLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
6-380 |
1.31e-68 |
|
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: 220.83 E-value: 1.31e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 6 EELNAIREGVRALCAEFDAAYWRRIDEQRGFPEAFVKALTDAGWLSAMIPEEYGGSGLGLAEASVILEEVNRCGGNSGT- 84
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGSGPGl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 85 -VHGQMYnMFTLLRNGSEAQKRFYLPKLASGElRLQSMGVTEPTTGTDTTKIKTTAVRKGDRYVINGQKVWISRIQHSDL 163
Cdd:cd01160 81 sLHTDIV-SPYITRAGSPEQKERVLPQMVAGK-KIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 164 MILLARTTPLAevkRKSEGMSIFLVdlrEAIGKGLTV-QPIANM--VNHETNELFFDNLEIPADSLIGEEGKGFRYILDG 240
Cdd:cd01160 159 VIVVARTGGEA---RGAGGISLFLV---ERGTPGFSRgRKLKKMgwKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 241 LNAERTLIAAECIGDGRWFIDKASHYARDRVVFGRPIGQNQGVQFPIAEAHIEVEAADLMRWRACQEYDAGLNAGASANM 320
Cdd:cd01160 233 LPQERLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASM 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 321 AKYLAAKASWEAANACLQTHGGFGFACEYDVERKFRETRLYQVAPISTNLILSYVAEHLL 380
Cdd:cd01160 313 AKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
5-363 |
1.38e-66 |
|
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: 215.74 E-value: 1.38e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 5 SEELNAIREGVRALCAEFDAAYWRRIDEQRGFPEAFVKALTDAGWLSAMIPEEYGGSGLGLAEASVILEEVNRCGGNSGT 84
Cdd:cd01156 3 DDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 85 VHGQMYNMF--TLLRNGSEAQKRFYLPKLASGElRLQSMGVTEPTTGTDTTKIKTTAVRKGDRYVINGQKVWISRIQHSD 162
Cdd:cd01156 83 SYGAHSNLCinQIYRNGSAAQKEKYLPKLISGE-HIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDAD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 163 LMILLARTTPlaevKRKSEGMSIFLVdlrEAIGKGLTVQPIAN---MVNHETNELFFDNLEIPADSLIGEEGKGFRYILD 239
Cdd:cd01156 162 TLVVYAKTDP----SAGAHGITAFIV---EKGMPGFSRAQKLDklgMRGSNTCELVFEDCEVPEENILGGENKGVYVLMS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 240 GLNAERTLIAAECIGDGRWFIDKASHYARDRVVFGRPIGQNQGVQFPIAEAHIEVEAADLMRWRACQEYDAG-LNAGASA 318
Cdd:cd01156 235 GLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGnMDPKDAA 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 489176391 319 NMAKYLAAKASWEAANAcLQTHGGFGFACEYDVERKFRETRLYQV 363
Cdd:cd01156 315 GVILYAAEKATQVALDA-IQILGGNGYINDYPTGRLLRDAKLYEI 358
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
6-341 |
5.42e-58 |
|
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: 193.33 E-value: 5.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 6 EELNAIREGVRALCA--------EFDAAYWRRIDEQRgfpEAFVKALTDAGWLSAMIPEEYGGSGLGLAEASVILEEVNR 77
Cdd:cd01152 1 PSEEAFRAEVRAWLAahlppelrEESALGYREGREDR---RRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 78 CGG-NSGTVHGQMYNMFTLLRNGSEAQKRFYLPKLASGELRLqSMGVTEPTTGTDTTKIKTTAVRKGDRYVINGQKVWIS 156
Cdd:cd01152 78 AGApVPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIW-CQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 157 RIQHSDLMILLARTTPLAevkRKSEGMSIFLVDLREaigKGLTVQPIAN-MVNHETNELFFDNLEIPADSLIGEEGKGFR 235
Cdd:cd01152 157 GAHYADWAWLLVRTDPEA---PKHRGISILLVDMDS---PGVTVRPIRSiNGGEFFNEVFLDDVRVPDANRVGEVNDGWK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 236 YILDGLNAERTLIAAECIGDGRWFIDKASHYARDrvvfGRPIGQNQGVQFPIAEAHIEVEAADLMRWRACQEYDAGLNAG 315
Cdd:cd01152 231 VAMTTLNFERVSIGGSAATFFELLLARLLLLTRD----GRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPG 306
|
330 340
....*....|....*....|....*.
gi 489176391 316 ASANMAKYLAAKASWEAANACLQTHG 341
Cdd:cd01152 307 AEASIAKLFGSELAQELAELALELLG 332
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
28-372 |
1.69e-57 |
|
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: 193.07 E-value: 1.69e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 28 RRIDEQRGFPEAFVKALTDAGWLSAMIPEEYGGSGLGLAEASVILEEVNRCGGNSGTV--HgQMYNMFTLLRNGSEAQKR 105
Cdd:cd01161 49 AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMDLGFSVTLgaH-QSIGFKGILLFGTEAQKE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 106 FYLPKLASGElRLQSMGVTEPTTGTDTTKIKTTAVRK--GDRYVINGQKVWISRIQHSDLMILLARTTPLAEVKRKSEGM 183
Cdd:cd01161 128 KYLPKLASGE-WIAAFALTEPSSGSDAASIRTTAVLSedGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDATGSVKDKI 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 184 SIFLVdlrEAIGKGLTVQPIANMVN---HETNELFFDNLEIPADSLIGEEGKGFRYILDGLNAERTLIAAECIGDGRWFI 260
Cdd:cd01161 207 TAFIV---ERSFGGVTNGPPEKKMGikgSNTAEVYFEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCI 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 261 DKASHYARDRVVFGRPIGQNQGVQFPIAEAHIEVEAADLMRWRACQEYDAGLNAGAS--ANMAKYLAAKASWEAANACLQ 338
Cdd:cd01161 284 EKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLKAEYQieAAISKVFASEAAWLVVDEAIQ 363
|
330 340 350
....*....|....*....|....*....|....
gi 489176391 339 THGGFGFACEYDVERKFRETRLYQVAPiSTNLIL 372
Cdd:cd01161 364 IHGGMGFMREYGVERVLRDLRIFRIFE-GTNEIL 396
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
5-376 |
6.34e-57 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 190.71 E-value: 6.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 5 SEELNAIREGVRALCA-EFDAAYWRRIDEQRGFPEAFVKALTDAGWLSAMIPEEYGGSGLGLAEASVILEEVNRCGGnSG 83
Cdd:PRK12341 6 TEEQELLLASIRELITrNFPEEYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCGA-PA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 84 TVHGQMYNMFTLLRNGSEAQKRF-YLPKLASGELRLqSMGVTEPTTGTDTTKIKTTAVRKGDRYVINGQKVWISRIQHSD 162
Cdd:PRK12341 85 FLITNGQCIHSMRRFGSAEQLRKtAESTLETGDPAY-ALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAKEYP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 163 LMILLARTtPLAEVKRKSegMSIFLVDLREaigKGLTVQPIANMVNH--ETNELFFDNLEIPADSLIGEEGKGFRYILDG 240
Cdd:PRK12341 164 YMLVLARD-PQPKDPKKA--FTLWWVDSSK---PGIKINPLHKIGWHmlSTCEVYLDNVEVEESDLVGEEGMGFLNVMYN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 241 LNAERTLIAAECIGDGRWFIDKASHYARDRVVFGRPIGQNQGVQFPIAEAHIEVEAADLMRWRACQEYDAGLNAGASANM 320
Cdd:PRK12341 238 FEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAAL 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 489176391 321 AKYLAAKASWEAANACLQTHGGFGFACEYDVERKFRETRLYQVAPiSTNLILSYVA 376
Cdd:PRK12341 318 AKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGG-GTDEIMIYIA 372
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
5-363 |
5.00e-54 |
|
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: 183.03 E-value: 5.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 5 SEELNAIREGVRALCAEF---DAAYWrriDEQRGFPEAFVKALTDAGWLSAMIPEEYGGSGLGLAEASVILEEVNrCGGN 81
Cdd:cd01162 2 NEEQRAIQEVARAFAAKEmapHAADW---DQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALS-TGCV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 82 SGTVHGQMYNM--FTLLRNGSEAQKRFYLPKLASGELrLQSMGVTEPTTGTDTTKIKTTAVRKGDRYVINGQKVWISRIQ 159
Cdd:cd01162 78 STAAYISIHNMcaWMIDSFGNDEQRERFLPDLCTMEK-LASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 160 HSDLMILLARTTplaevKRKSEGMSIFLVdlrEAIGKGLTV-QPIANMVNHE--TNELFFDNLEIPADSLIGEEGKGFRY 236
Cdd:cd01162 157 DSDVYVVMARTG-----GEGPKGISCFVV---EKGTPGLSFgANEKKMGWNAqpTRAVIFEDCRVPVENRLGGEGQGFGI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 237 ILDGLNAERTLIAAECIGDGRWFIDKASHYARDRVVFGRPIGQNQGVQFPIAEAHIEVEAADLMRWRACQEYDAG-LNAG 315
Cdd:cd01162 229 AMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGdPDAV 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 489176391 316 ASANMAKYLAAKASWEAANACLQTHGGFGFACEYDVERKFRETRLYQV 363
Cdd:cd01162 309 KLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQI 356
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
31-363 |
1.70e-48 |
|
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: 168.53 E-value: 1.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 31 DEQRGFPEAFVKALTDAGWLSAMIPEEYGGSGLGLAEASVILEEVNR-CGGNSGTVHGQMYNMFTLLRNGSEAQKRFYLP 109
Cdd:cd01157 28 DKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYgCTGVQTAIEANSLGQMPVIISGNDEQKKKYLG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 110 KLASGELrLQSMGVTEPTTGTDTTKIKTTAVRKGDRYVINGQKVWISRIQHSDLMILLARTTPLAEVKrKSEGMSIFLVD 189
Cdd:cd01157 108 RMTEEPL-MCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKCP-ASKAFTGFIVE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 190 lREAIGkgltVQPIANMVN-----HETNELFFDNLEIPADSLIGEEGKGFRYILDGLNAERTLIAAECIGDGRWFIDKAS 264
Cdd:cd01157 186 -ADTPG----IQPGRKELNmgqrcSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKTRPPVAAGAVGLAQRALDEAT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 265 HYARDRVVFGRPIGQNQGVQFPIAEAHIEVEAADLMRWRACQEYDAGLNAGASANMAKYLAAKASWEAANACLQTHGGFG 344
Cdd:cd01157 261 KYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAFAADIANQLATDAVQIFGGNG 340
|
330
....*....|....*....
gi 489176391 345 FACEYDVERKFRETRLYQV 363
Cdd:cd01157 341 FNSEYPVEKLMRDAKIYQI 359
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
5-364 |
3.54e-45 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 159.61 E-value: 3.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 5 SEELNAIREGVRALCA-EFDAAYWRRIDEQRGFPEAFVKALTDAGWLSAMIPEEYGGSGLGLAEASVILEEVNRCGGNSG 83
Cdd:PRK03354 6 NDEQELFVAGIRELMAsENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPTY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 84 TVHGQMYNMFTLLRNGSEAQKRFYLPKLASGELRLQSmGVTEPTTGTDTTKIKTTAVRKGDRYVINGQKVWISRIQHSDL 163
Cdd:PRK03354 86 VLYQLPGGFNTFLREGTQEQIDKIMAFRGTGKQMWNS-AITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTPY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 164 MILLARTTPlaevkrkSEGMSIF---LVDLREAigkGLTVQPIANM--VNHETNELFFDNLEIPADSLIGEEGKGFRYIL 238
Cdd:PRK03354 165 IVVMARDGA-------SPDKPVYtewFVDMSKP---GIKVTKLEKLglRMDSCCEITFDDVELDEKDMFGREGNGFNRVK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 239 DGLNAERTLIAAECIGDGRWFIDKASHYARDRVVFGRPIGQNQGVQFPIAEAHIEVEAADLMRWRACQEYDAGLNAGASA 318
Cdd:PRK03354 235 EEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDA 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 489176391 319 NMAKYLAAKASWEAANACLQTHGGFGFACEYDVERKFRETRLYQVA 364
Cdd:PRK03354 315 AMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVS 360
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
12-363 |
1.48e-44 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 158.50 E-value: 1.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 12 REGVRALCAEFDAAYWRRIDEQRGFPEA--FVKALTDAGWLSAMIPEEYGGSGLGLAEASVILEEVNRCGGNSGTVHGQM 89
Cdd:PLN02519 34 KESVQQFAQENIAPHAAAIDATNSFPKDvnLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAH 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 90 YNMFT--LLRNGSEAQKRFYLPKLASGElRLQSMGVTEPTTGTDTTKIKTTAVRKGDRYVINGQKVWISRIQHSDLMILL 167
Cdd:PLN02519 114 SNLCInqLVRNGTPAQKEKYLPKLISGE-HVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVY 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 168 ARTTPLAevkrKSEGMSIFLVDlreaigKGL----TVQPI--ANMVNHETNELFFDNLEIPADSLIGEEGKGFRYILDGL 241
Cdd:PLN02519 193 AKTDVAA----GSKGITAFIIE------KGMpgfsTAQKLdkLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 242 NAERTLIAAECIGDGRWFIDKASHYARDRVVFGRPIGQNQGVQFPIAEAHIEVEAADLMRWRACQEYDAGLNAGASANMA 321
Cdd:PLN02519 263 DLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGV 342
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 489176391 322 KYLAAKASWEAANACLQTHGGFGFACEYDVERKFRETRLYQV 363
Cdd:PLN02519 343 ILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEI 384
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
5-355 |
2.56e-44 |
|
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: 157.52 E-value: 2.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 5 SEELNAIREGVRALCAE----FDAAYWRriDEQrgFPEAFVKALTDAGWLSAmIPEEYGGSGLGLAEASVILEEVNRCgg 80
Cdd:cd01151 14 TEEERAIRDTAREFCQEelapRVLEAYR--EEK--FDRKIIEEMGELGLLGA-TIKGYGCAGLSSVAYGLIAREVERV-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 81 NSG-----TVHGQMYnMFTLLRNGSEAQKRFYLPKLASGELrLQSMGVTEPTTGTDTTKIKTTAVRKGDRYVINGQKVWI 155
Cdd:cd01151 87 DSGyrsfmSVQSSLV-MLPIYDFGSEEQKQKYLPKLASGEL-IGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 156 SRIQHSDLMILLARTTPLAE-----VKRKSEGMSIflvdlrEAIGKGLTVQPIAnmvnheTNELFFDNLEIPADSLIgEE 230
Cdd:cd01151 165 TNSPIADVFVVWARNDETGKirgfiLERGMKGLSA------PKIQGKFSLRASI------TGEIVMDNVFVPEENLL-PG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 231 GKGFRYILDGLNAERTLIAAECIGDGRWFIDKASHYARDRVVFGRPIGQNQGVQFPIAEAHIEVEAADLMRWRACQEYDA 310
Cdd:cd01151 232 AEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQ 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 489176391 311 GLNAGASANMAKYLAAKASWEAANACLQTHGGFGFACEYDVERKF 355
Cdd:cd01151 312 GKATPEQISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHM 356
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
1-363 |
3.79e-38 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 141.61 E-value: 3.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 1 MNPNSEElNAIREGVRALCAEFDAAYWRRIDEQRGFPEAFVKALTDAGWLSAMIPEEYGGSGLGLAEASVILEEVNRC-- 78
Cdd:PTZ00461 35 YNPTPEH-AALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYdp 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 79 GGNSGTVHGQMYNMFTLLRNGSEAQKRFYLPKLASGElRLQSMGVTEPTTGTDTTKIKTTAVRKGD-RYVINGQKVWISR 157
Cdd:PTZ00461 114 GFCLAYLAHSMLFVNNFYYSASPAQRARWLPKVLTGE-HVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITN 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 158 IQHSDLMILLArttplaevkrKSEG-MSIFLVdlrEAIGKGLTVQPIAN---MVNHETNELFFDNLEIPADSLIGEEGKG 233
Cdd:PTZ00461 193 GTVADVFLIYA----------KVDGkITAFVV---ERGTKGFTQGPKIDkcgMRASHMCQLFFEDVVVPAENLLGEEGKG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 234 FRYILDGLNAERTLIAAECIGDGRWFIDKASHYARDRVVFGRPIGQNQGVQFPIAEAHIEVEAADLMRWRACQEYDAGLN 313
Cdd:PTZ00461 260 MVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNK 339
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 489176391 314 AGASANMAKYLAAKASWEAANACLQTHGGFGFACEYDVERKFRETRLYQV 363
Cdd:PTZ00461 340 NRLGSDAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEI 389
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
231-379 |
2.04e-34 |
|
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: 124.29 E-value: 2.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 231 GKGFRYILDGLNAERTLIAAECIGDGRWFIDKASHYARDRVVFGRPIGQNQGVQFPIAEAHIEVEAADLMRWRACQEYDA 310
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489176391 311 GLNAGASANMAKYLAAKASWEAANACLQTHGGFGFACEYDVERKFRETRLYQVAPISTNLILSYVAEHL 379
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
35-360 |
7.48e-34 |
|
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: 129.82 E-value: 7.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 35 GFPEAFvKALTDAGWLSAMIPEEYGGSGLGLAEASVILEEVNRCGGNSGTVHGQMYNMFTLLRNGSEAQKRFYLPKLASG 114
Cdd:cd01153 37 PFKEAL-DAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMYASGTQGAAATLLAHGTEAQREKWIPRLAEG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 115 ELrLQSMGVTEPTTGTDTTKIKTTAVRKGD-RYVINGQKVWISRIQH----SDLMILLARTtplAEVKRKSEGMSIFLVD 189
Cdd:cd01153 116 EW-TGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGEHdmseNIVHLVLARS---EGAPPGVKGLSLFLVP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 190 LREAIGKGLTVQpIANmVNHE-------TNELFFDNLEIPadsLIGEEGKGFRYILDGLNAERTLIAAECIGDGRWFIDK 262
Cdd:cd01153 192 KFLDDGERNGVT-VAR-IEEKmglhgspTCELVFDNAKGE---LIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLN 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 263 ASHYARDRVVFGRPIGQNQGVqfPIAEaHIEVEAADLMR--------------WRACQEYDAGLNAGASAN--------- 319
Cdd:cd01153 267 ALAYAKERKQGGDLIKAAPAV--TIIH-HPDVRRSLMTQkayaegsraldlytATVQDLAERKATEGEDRKalsaladll 343
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 489176391 320 --MAKYLAAKASWEAANACLQTHGGFGFACEYDVERKFRETRL 360
Cdd:cd01153 344 tpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARI 386
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
5-115 |
7.25e-32 |
|
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: 116.41 E-value: 7.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 5 SEELNAIREGVRALCAEFDAAYWRRIDEQRGFPEAFVKALTDAGWLSAMIPEEYGGSGLGLAEASVILEEVNRCGGNSGT 84
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|....
gi 489176391 85 ---VHGQMYnMFTLLRNGSEAQKRFYLPKLASGE 115
Cdd:pfam02771 81 alsVHSSLG-APPILRFGTEEQKERYLPKLASGE 113
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
54-344 |
5.15e-28 |
|
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: 113.64 E-value: 5.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 54 IPEEYGGSGLGLAEASVILEEVNRCGGNSGTVHGQ---MYNMFTLLRNGSEAQKRFYLPKLASGELRLQSMGVTEPTTGT 130
Cdd:cd01155 60 LPEVSGLSGLTNLEYAYLAEETGRSFFAPEVFNCQapdTGNMEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDVASS 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 131 DTTKIKTTAVRKGDRYVINGQKVWISRIQHSD--LMILLARTTPLAEVKRKSEGMsiFLVDLREaigKGLTVqpIANM-- 206
Cdd:cd01155 140 DATNIECSIERDGDDYVINGRKWWSSGAGDPRckIAIVMGRTDPDGAPRHRQQSM--ILVPMDT---PGVTI--IRPLsv 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 207 -----VNHETNELFFDNLEIPADSLIGEEGKGFRYILDGL------NAERTLIAAECIgdgrwfIDKASHYARDRVVFGR 275
Cdd:cd01155 213 fgyddAPHGHAEITFDNVRVPASNLILGEGRGFEIAQGRLgpgrihHCMRLIGAAERA------LELMCQRAVSREAFGK 286
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489176391 276 PIGQNQGVQFPIAEAHIEVEAADLMRWRACQEYDAGLNAGASAN--MAKYLAAKASWEAANACLQTHGGFG 344
Cdd:cd01155 287 KLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTVGNKAARKEiaMIKVAAPRMALKIIDRAIQVHGAAG 357
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
5-355 |
1.22e-21 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 95.69 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 5 SEELNAIREGVRAlCAEFDAA-----YWrridEQRGFPEAFVKALTDAGWLSAMIpEEYGGSGLGLAEASVILEEVNRCG 79
Cdd:PLN02526 30 TPEEQALRKRVRE-CMEKEVApimteYW----EKAEFPFHIIPKLGSLGIAGGTI-KGYGCPGLSITASAIATAEVARVD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 80 GNSGT---VHGQMyNMFTLLRNGSEAQKRFYLPKLAsgelRLQSMG---VTEPTTGTDTTKIKTTAVRKGDRYVINGQKV 153
Cdd:PLN02526 104 ASCSTfilVHSSL-AMLTIALCGSEAQKQKYLPSLA----QLDTVAcwaLTEPDYGSDASSLNTTATKVEGGWILNGQKR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 154 WISRIQHSDLMILLARTTplaevkrKSEGMSIFLVdlrEAIGKGLTVQPIAN-----MVnhETNELFFDNLEIP-ADSLI 227
Cdd:PLN02526 179 WIGNSTFADVLVIFARNT-------TTNQINGFIV---KKGAPGLKATKIENkiglrMV--QNGDIVLKDVFVPdEDRLP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 228 GEegKGFRYILDGLNAERTLIAAECIGDGRWFIDKASHYARDRVVFGRPIGQNQGVQFPIAEAHIEVEAADLMRWRACQE 307
Cdd:PLN02526 247 GV--NSFQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKL 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 489176391 308 YDAGLNAGASANMAKYLAAKASWEAANACLQTHGGFGFACEYDVERKF 355
Cdd:PLN02526 325 YESGKMTPGHASLGKAWITKKARETVALGRELLGGNGILADFLVAKAF 372
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
25-366 |
8.76e-19 |
|
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: 87.43 E-value: 8.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 25 AYWRRIDEQRgFPEAF---VKALTDAGwLSAMIPEEYGGSGLGLAEASVILeeVNR-CGGNSGTVHGQMYNMFTLLRNGS 100
Cdd:cd01154 53 RWGRRVDRVW-VHPAWhalMRRLIEEG-VINIEDGPAGEGRRHVHFAAGYL--LSDaAAGLLCPLTMTDAAVYALRKYGP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 101 EAQKRFYLPKLASG--ELRLQSMGVTEPTTGTDTTKIKTTAVR-KGDRYVINGQKVWISRIQhSDLMILLARTtplAEVK 177
Cdd:cd01154 129 EELKQYLPGLLSDRykTGLLGGTWMTEKQGGSDLGANETTAERsGGGVYRLNGHKWFASAPL-ADAALVLARP---EGAP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 178 RKSEGMSIFLVD--LREAIGKGLTVQPIANMVNHETN---ELFFDNLEipaDSLIGEEGKGFRYILDGLNAERTLIAAEC 252
Cdd:cd01154 205 AGARGLSLFLVPrlLEDGTRNGYRIRRLKDKLGTRSVatgEVEFDDAE---AYLIGDEGKGIYYILEMLNISRLDNAVAA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 253 IGDGRWFIDKASHYARDRVVFGRPIGQNQGVQFPIAEAHIEVEAADLMRWRACQEYDAG--------LNAGASANMAKYL 324
Cdd:cd01154 282 LGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAaadkpveaHMARLATPVAKLI 361
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 489176391 325 AAKASWEAANACLQTHGGFGFACEYDVERKFRETrlyQVAPI 366
Cdd:cd01154 362 ACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREA---QVTPI 400
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
34-360 |
3.13e-18 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 86.46 E-value: 3.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 34 RGFPEAFvKALTDAGWLSAMIPEEYGGSGLGLAEASVILEEVNRCGGNSGTVHGQ-MYNMFTLLRNGSEAQKRFYLPKLA 112
Cdd:PTZ00456 99 KGFKEAY-QALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPGLsIGAANTLMAWGSEEQKEQYLTKLV 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 113 SGELrLQSMGVTEPTTGTDTTKIKTTAVRKGD-RYVINGQKVWISRIQH----SDLMILLARtTPLAEVKRKseGMSIFL 187
Cdd:PTZ00456 178 SGEW-SGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISAGDHdlteNIVHIVLAR-LPNSLPTTK--GLSLFL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 188 VDlREAIGKGLTVQPIANMV-----------NHETNELFFDNleiPADSLIGEEGKGFRYILDGLNAERTLIAAECIGDG 256
Cdd:PTZ00456 254 VP-RHVVKPDGSLETAKNVKciglekkmgikGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHA 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 257 RWFIDKASHYAR------------------DRVVFGRPIGQNQGVQFPIAEA--HIEVEAADLMRWRACQEyDAGLNAGA 316
Cdd:PTZ00456 330 ELAFQNALRYARerrsmralsgtkepekpaDRIICHANVRQNILFAKAVAEGgrALLLDVGRLLDIHAAAK-DAATREAL 408
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 489176391 317 SANMAKYLA-AKA---SW--EAANACLQTHGGFGFACEYDVERKFRETRL 360
Cdd:PTZ00456 409 DHEIGFYTPiAKGcltEWgvEAASRCLQVWGGHGYIKGNGMEQILRDARI 458
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
91-344 |
1.29e-15 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 78.68 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 91 NMFTLLRNGSEAQKRFYLPKLASGELRLQSMGVTEPTTGTDTTKIKTTAVRKGDRYVINGQKVWIS-----RIQhsdLMI 165
Cdd:PLN02876 525 NMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQVASSDATNIECSIRRQGDSYVINGTKWWTSgamdpRCR---VLI 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 166 LLARTTPLAEVKRKSegmSIFLVDLRE---AIGKGLTVQPIANmVNHETNELFFDNLEIPADSLIGEEGKGFRYILDGLN 242
Cdd:PLN02876 602 VMGKTDFNAPKHKQQ---SMILVDIQTpgvQIKRPLLVFGFDD-APHGHAEISFENVRVPAKNILLGEGRGFEIAQGRLG 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 243 AERTLIAAECIGDGRWFIDKASHYARDRVVFGRPIGQNQGVQFPIAEAHIEVEAADLMRWRACQEYDAGLNAGASAN--M 320
Cdd:PLN02876 678 PGRLHHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDRLGNKKARGIiaM 757
|
250 260
....*....|....*....|....
gi 489176391 321 AKYLAAKASWEAANACLQTHGGFG 344
Cdd:PLN02876 758 AKVAAPNMALKVLDMAMQVHGAAG 781
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
16-326 |
2.34e-15 |
|
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: 76.59 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 16 RALCAEFDAAYWRRiDEQRGFPEAFVKALTDAGWLSAMIPEEYGGSGLGLAEASVILEEVNRCGGNSGTVHGQMYNM-FT 94
Cdd:cd01163 4 RPLAARIAEGAAER-DRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGFvEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 95 LLRNGSEAQKRFYLPKLASGELrlqSMGVTEPTTGTDTTKIKTTAVRKGDRYVINGQKVWISRIQHSDLMILLA---RTT 171
Cdd:cd01163 83 LLLAGPEQFRKRWFGRVLNGWI---FGNAVSERGSVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSAldeEGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 172 PL-AEVKRKSEGMSIflVDLREAIGKGLTvqpianmvnhETNELFFDNLEIPADSLIGEEGKGFRYILDGLNAERTLIAA 250
Cdd:cd01163 160 LVfAAVPTDRPGITV--VDDWDGFGQRLT----------ASGTVTFDNVRVEPDEVLPRPNAPDRGTLLTAIYQLVLAAV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 251 EcIGDGRWFIDKASHYARDRvvfGRPI---GQNQGVQFP-----IAEAHIEVEAADLMRWRACQEYDAGLNAGASANMAK 322
Cdd:cd01163 228 L-AGIARAALDDAVAYVRSR---TRPWihsGAESARDDPyvqqvVGDLAARLHAAEALVLQAARALDAAAAAGTALTAEA 303
|
....
gi 489176391 323 YLAA 326
Cdd:cd01163 304 RGEA 307
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
135-217 |
1.02e-13 |
|
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: 66.53 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 135 IKTTAV-RKGDRYVINGQKVWISRIQHSDLMILLARTTPLAevkrKSEGMSIFLVDLREaigKGLTVQPIAN---MVNHE 210
Cdd:pfam02770 16 LKTTAAdGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDD----RHGGISLFLVPKDA---PGVSVRRIETklgVRGLP 88
|
....*..
gi 489176391 211 TNELFFD 217
Cdd:pfam02770 89 TGELVFD 95
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
248-359 |
1.71e-09 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 55.43 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 248 IAAECIGDGRWFIDKASHYARDRV--VFGRPIGQNQGVQFPIAEAHIEVEAADLMRWRACQEYDAGLNAG--------AS 317
Cdd:pfam08028 2 IAAAALGAARAALAEFTERARGRVraYFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAAAGkpvtpalrAE 81
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 489176391 318 ANMAKYLAAKASWEAANACLQTHGGFGFACEYDVERKFRETR 359
Cdd:pfam08028 82 ARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIH 123
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
13-356 |
2.08e-09 |
|
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: 58.51 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 13 EGVRALCAEFdAAYWRRIDEQRGFPEAFVKALTDAGWLSAMIPEEYGGSGLGLAEASVILEEVNRCGGNSG------TVH 86
Cdd:cd01159 1 ARAEDLAPLI-RERAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAwvasivATH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 87 GQMYNMFtllrnGSEAQKRFY---LPKLASGELrlQSMGvtepttgtdttkiktTAVRKGDRYVINGQKVWISRIQHSDL 163
Cdd:cd01159 80 SRMLAAF-----PPEAQEEVWgdgPDTLLAGSY--APGG---------------RAERVDGGYRVSGTWPFASGCDHADW 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 164 MILLARTTPLAEVKRksegMSIFLVDLREaigkgLTVQPI---ANMVNHETNELFFDNLEIPADSLI-----------GE 229
Cdd:cd01159 138 ILVGAIVEDDDGGPL----PRAFVVPRAE-----YEIVDTwhvVGLRGTGSNTVVVDDVFVPEHRTLtagdmmagdgpGG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 230 EGKGFRYILDGLNAerTLIAAECIGDGRWFIDKASHYARDRV-VFGRPIGQNQ--GVQFPIAEAHIEVEAADLMRWRACQ 306
Cdd:cd01159 209 STPVYRMPLRQVFP--LSFAAVSLGAAEGALAEFLELAGKRVrQYGAAVKMAEapITQLRLAEAAAELDAARAFLERATR 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 489176391 307 EYDAGLNAGASANM--------AKYLAAKASWEAANACLQTHGGFGFACEYDVERKFR 356
Cdd:cd01159 287 DLWAHALAGGPIDVeerarirrDAAYAAKLSAEAVDRLFHAAGGSALYTASPLQRIWR 344
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
37-115 |
2.44e-05 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 46.35 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 37 PEA--FVKaltDAGWLSAMIPEEYGGSGL-GLAEASVILEEVNRCGGNSGTVhgqmynMFT--------LLRNGSEAQKR 105
Cdd:PRK09463 112 PEVwqFIK---EHGFFGMIIPKEYGGLEFsAYAHSRVLQKLASRSGTLAVTV------MVPnslgpgelLLHYGTDEQKD 182
|
90
....*....|
gi 489176391 106 FYLPKLASGE 115
Cdd:PRK09463 183 HYLPRLARGE 192
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
5-115 |
1.29e-03 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 40.71 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176391 5 SEELNAIREGVRALCAEFDAayWRRIDEQRGFPEAFVKALTDAGWLSAMIPEEYGGSGLG-LAEASVILEEVNRCGGNSG 83
Cdd:PRK13026 80 AEEQAFIDNEVETLLTMLDD--WDIVQNRKDLPPEVWDYLKKEGFFALIIPKEYGGKGFSaYANSTIVSKIATRSVSAAV 157
|
90 100 110
....*....|....*....|....*....|....*....
gi 489176391 84 TVH-------GQMynmftLLRNGSEAQKRFYLPKLASGE 115
Cdd:PRK13026 158 TVMvpnslgpGEL-----LTHYGTQEQKDYWLPRLADGT 191
|
|
| |
