|
Name |
Accession |
Description |
Interval |
E-value |
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
7-383 |
0e+00 |
|
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: 588.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 7 DIQQDFLKLAHDFGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDggdVLSYILAVEELAKYDAGV 86
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLD---FLAYAIAIEELAKVDASV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 87 AITLSATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDgTYTLNGSKIFITNGGA 166
Cdd:cd01158 78 AVIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGD-DYVLNGSKMWITNGGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 167 ADIYIVFAMTDKSKGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIAMMTLDGG 246
Cdd:cd01158 157 ADFYIVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 247 RIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVDAAIAKRV 326
Cdd:cd01158 237 RIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLF 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
1BUC_A 327 ASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGALLR 383
Cdd:cd01158 317 ASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
1-383 |
1.46e-171 |
|
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: 483.57 E-value: 1.46e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 1 MDFNLTDIQQDFLKLAHDFGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDggdVLSYILAVEELA 80
Cdd:COG1960 1 MDFELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLS---LVELALVLEELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 81 KYDAGVAITLSATVSlCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGtYTLNGSKIF 160
Cdd:COG1960 78 RADASLALPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDG-YVLNGQKTF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 161 ITNGGAADIYIVFAMTDKSKGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIAM 240
Cdd:COG1960 156 ITNAPVADVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 241 MTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVDA 320
Cdd:COG1960 236 STLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEA 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
1BUC_A 321 AIAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGALLR 383
Cdd:COG1960 316 AMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLG 378
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
96-378 |
5.54e-132 |
|
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: 380.86 E-value: 5.54e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 96 LCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGtYTLNGSKIFITNGGAADIYIVFAM 175
Cdd:cd00567 43 LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDG-YVLNGRKIFISNGGDADLFIVLAR 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 176 TDKS-KGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIAMMTLDGGRIGVAAQA 254
Cdd:cd00567 122 TDEEgPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLLAAVA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 255 LGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPF-TVDAAIAKRVASDVAMR 333
Cdd:cd00567 202 LGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEaRLEAAMAKLFATEAARE 281
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
1BUC_A 334 VTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTG 378
Cdd:cd00567 282 VADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
5-383 |
2.87e-112 |
|
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: 332.49 E-value: 2.87e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 5 LTDIQQDFLKLAHDFGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDGgdvLSYILAVEELAKYDA 84
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSR---LDASIIFEALSTGCV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 85 GVAITLSATvSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDgTYTLNGSKIFITNG 164
Cdd:cd01162 78 STAAYISIH-NMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGD-HYVLNGSKAFISGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 165 GAADIYIVFAMTDkSKGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIAMMTLD 244
Cdd:cd01162 156 GDSDVYVVMARTG-GEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 245 GGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVD-AAIA 323
Cdd:cd01162 235 GGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKlCAMA 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 324 KRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGALLR 383
Cdd:cd01162 315 KRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLT 374
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
5-381 |
9.71e-111 |
|
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: 328.60 E-value: 9.71e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 5 LTDIQQDFLKLAHDFGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDGgdvLSYILAVEELAKYDA 84
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGY---LAHVIIMEEISRASG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 85 GVAITLSATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGtYTLNGSKIFITNG 164
Cdd:cd01156 79 SVALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDR-YVLNGSKMWITNG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 165 GAADIYIVFAMTDKSKGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIAMMTLD 244
Cdd:cd01156 158 PDADTLVVYAKTDPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 245 GGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVDAAIAK 324
Cdd:cd01156 238 YERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVI 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
1BUC_A 325 RVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGAL 381
Cdd:cd01156 318 LYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGREL 374
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
2-383 |
2.25e-102 |
|
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: 308.63 E-value: 2.25e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 2 DFNLTDIQQDFLKL----AHDFGEKKLAPTVTerDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDGgdVLSYILAve 77
Cdd:cd01161 20 PSVLTEEQTEELNMlvgpVEKFFEEVNDPAKN--DQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNN--TQYARLA-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 78 ELAKYDAGVAITLSATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGT-YTLNG 156
Cdd:cd01161 94 EIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSEDGKhYVLNG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 157 SKIFITNGGAADIYIVFAMT-----DKSKGNHgITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGE 231
Cdd:cd01161 174 SKIWITNGGIADIFTVFAKTevkdaTGSVKDK-ITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 232 EGKGFKIAMMTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYK-AACKK 310
Cdd:cd01161 253 VGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMtSGNMD 332
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1BUC_A 311 QEGKP-FTVDAAIAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGALLR 383
Cdd:cd01161 333 RGLKAeYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQ 406
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
19-372 |
3.90e-98 |
|
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: 296.33 E-value: 3.90e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 19 FGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDggdVLSYILAVEELAkYDAGVAITLSATVSLCA 98
Cdd:cd01160 13 FFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGD---LLSAAVLWEELA-RAGGSGPGLSLHTDIVS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 99 NPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKndDGT-YTLNGSKIFITNGGAADIYIVFAMTD 177
Cdd:cd01160 89 PYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARK--DGDhYVLNGSKTFITNGMLADVVIVVARTG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 178 -KSKGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIAMMTLDGGRIGVAAQALG 256
Cdd:cd01160 167 gEARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAAGALA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 257 IAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVDAAIAKRVASDVAMRVTT 336
Cdd:cd01160 247 AAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATELQNRVAY 326
|
330 340 350
....*....|....*....|....*....|....*.
1BUC_A 337 EAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEV 372
Cdd:cd01160 327 ECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEI 362
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
5-376 |
1.08e-95 |
|
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: 290.64 E-value: 1.08e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 5 LTDIQQDFLKLAHDFGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDggdVLSYILAVEELAKYDA 84
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLG---TFDTCLITEELAYGCT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 85 GVAITLSATvSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDgTYTLNGSKIFITNG 164
Cdd:cd01157 78 GVQTAIEAN-SLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGD-EYIINGQKMWITNG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 165 GAADIYIVFAMTD---KSKGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIAMM 241
Cdd:cd01157 156 GKANWYFLLARSDpdpKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 242 TLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVDAA 321
Cdd:cd01157 236 AFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYAS 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
1BUC_A 322 IAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMV 376
Cdd:cd01157 316 IAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLI 370
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
5-380 |
9.93e-93 |
|
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: 283.10 E-value: 9.93e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 5 LTDIQQDFLKLAHDFGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEkYGGSGDDGgdvLSYILAVEELAKYDA 84
Cdd:cd01151 13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIKG-YGCAGLSS---VAYGLIAREVERVDS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 85 GVAITLSATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKnDDGTYTLNGSKIFITNG 164
Cdd:cd01151 89 GYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARK-DGGGYKLNGSKTWITNS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 165 GAADIYIVFAmtdKSKGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLgEEGKGFKIAMMTLD 244
Cdd:cd01151 168 PIADVFVVWA---RNDETGKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL-PGAEGLRGPFKCLN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 245 GGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVDAAIAK 324
Cdd:cd01151 244 NARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLK 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
1BUC_A 325 RVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGA 380
Cdd:cd01151 324 RNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRA 379
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
2-383 |
1.56e-88 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 272.91 E-value: 1.56e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 2 DFNLTDIQQDFLKLAHDFGEKKLAPTVTERDHKGIYDKE--LIDELLSLGITGAYFEEKYGGSGDDGgdvLSYILAVEEL 79
Cdd:PLN02519 23 SLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDvnLWKLMGDFNLHGITAPEEYGGLGLGY---LYHCIAMEEI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 80 AKYDAGVAITLSATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGtYTLNGSKI 159
Cdd:PLN02519 100 SRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGG-YVLNGNKM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 160 FITNGGAADIYIVFAMTDKSKGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIA 239
Cdd:PLN02519 179 WCTNGPVAQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 240 MMTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVD 319
Cdd:PLN02519 259 MSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKD 338
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
1BUC_A 320 AAIAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGALLR 383
Cdd:PLN02519 339 CAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFK 402
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
1-383 |
1.94e-77 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 243.87 E-value: 1.94e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 1 MDFNLTDIQQDFLK-----LAHDFGEKKLAptvtERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDggdVLSYILA 75
Cdd:PRK12341 1 MDFSLTEEQELLLAsirelITRNFPEEYFR----TCDENGTYPREFMRALADNGISMLGVPEEFGGTPAD---YVTQMLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 76 VEELAKydAGVAITLsATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLG-AFGLTEPNAGTDASGQQTIATKNDDGTYtL 154
Cdd:PRK12341 74 LEEVSK--CGAPAFL-ITNGQCIHSMRRFGSAEQLRKTAESTLETGDPAyALALTEPGAGSDNNSATTTYTRKNGKVY-L 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 155 NGSKIFITNGGAADIYIVFAMTDKSKGNH-GITAFILEDGTPGFTYGKKEdKMGIHTSQTMELVFQDVKVPAENMLGEEG 233
Cdd:PRK12341 150 NGQKTFITGAKEYPYMLVLARDPQPKDPKkAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEEG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 234 KGFKIAMMTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEG 313
Cdd:PRK12341 229 MGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNG 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 314 KPFTVDAAIAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGALLR 383
Cdd:PRK12341 309 QSLRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILK 378
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
19-371 |
6.04e-76 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 240.61 E-value: 6.04e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 19 FGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEkygGSGDDGGDVLSYILAVEELAKYDAGVAITLSATVSLCA 98
Cdd:PTZ00461 51 FSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPE---ADGGAGMDAVAAVIIHHELSKYDPGFCLAYLAHSMLFV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 99 NPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGTYTLNGSKIFITNGGAADIYIVFAMTDK 178
Cdd:PTZ00461 128 NNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGNYVLNGSKIWITNGTVADVFLIYAKVDG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 179 SkgnhgITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIAMMTLDGGRIGVAAQALGIA 258
Cdd:PTZ00461 208 K-----ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 259 EAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVDAAIAKRVASDVAMRVTTEA 338
Cdd:PTZ00461 283 ERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKLFATPIAKKVADSA 362
|
330 340 350
....*....|....*....|....*....|...
1BUC_A 339 VQIFGGYGYSEEYPVARHMRDAKITQIYEGTNE 371
Cdd:PTZ00461 363 IQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIE 395
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
13-373 |
6.68e-65 |
|
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: 211.86 E-value: 6.68e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 13 LKLAHDFGEKKLAPTVTERDHKG-IYD----------KELIDELLSLGITGAYFEEKYGGSGddggdvLSYIL--AVEEL 79
Cdd:cd01153 2 LEEVARLAENVLAPLNADGDREGpVFDdgrvvvpppfKEALDAFAEAGWMALGVPEEYGGQG------LPITVysALAEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 80 AKYDAGVAITLSATVSlCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGTYTLNGSKI 159
Cdd:cd01153 76 FSRGDAPLMYASGTQG-AAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSWRINGVKR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 160 FITNGGAAD----IYIVFAMT-DKSKGNHGITAFI----LEDGTP-GFTYGKKEDKMGIHTSQTMELVFQDVKVPaenML 229
Cdd:cd01153 155 FISAGEHDMseniVHLVLARSeGAPPGVKGLSLFLvpkfLDDGERnGVTVARIEEKMGLHGSPTCELVFDNAKGE---LI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 230 GEEGKGFKIAMMTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQS--------ISFKLADMKMQIEAARN 301
Cdd:cd01153 232 GEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAPAvtiihhpdVRRSLMTQKAYAEGSRA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 302 LV-YKA-ACKKQEGKPFTVDAA------------IAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYE 367
Cdd:cd01153 312 LDlYTAtVQDLAERKATEGEDRkalsaladlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYE 391
|
....*.
1BUC_A 368 GTNEVQ 373
Cdd:cd01153 392 GTTGIQ 397
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
233-376 |
7.50e-57 |
|
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: 182.84 E-value: 7.50e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 233 GKGFKIAMMTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQE 312
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
1BUC_A 313 GKPFTVDAAIAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMV 376
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNI 144
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
1-383 |
7.05e-56 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 187.73 E-value: 7.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 1 MDFNLTDIQQDFLKLAHDFGEKKLAPT-VTERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDGGDVLSyilAVEEL 79
Cdd:PRK03354 1 MDFNLNDEQELFVAGIRELMASENWEAyFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAA---VWMEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 80 AKYDAGVAITLSATVSLcaNPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGTYtLNGSKI 159
Cdd:PRK03354 78 GRLGAPTYVLYQLPGGF--NTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVY-LNGSKC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 160 FITNGgAADIYIVFAMTDKSKGNHGI-TAFILEDGTPGFTYGKKEdKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKI 238
Cdd:PRK03354 155 FITSS-AYTPYIVVMARDGASPDKPVyTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 239 AMMTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTV 318
Cdd:PRK03354 233 VKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSG 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
1BUC_A 319 DAAIAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGALLR 383
Cdd:PRK03354 313 DAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLK 377
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
83-373 |
5.09e-52 |
|
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: 178.72 E-value: 5.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 83 DAGVAITLSATvSLCANPIWQFGTEAQKEKFLVPLVEGTK---LGAFGLTEPNAGTDASGQQTIATKNDDGTYTLNGSKI 159
Cdd:cd01154 106 AAGLLCPLTMT-DAAVYALRKYGPEELKQYLPGLLSDRYKtglLGGTWMTEKQGGSDLGANETTAERSGGGVYRLNGHKW 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 160 FiTNGGAADIYIVFAMTDKSK-GNHGITAFI----LEDGT-PGFTYGKKEDKMGIHTSQTMELVFQDvkvpAEN-MLGEE 232
Cdd:cd01154 185 F-ASAPLADAALVLARPEGAPaGARGLSLFLvprlLEDGTrNGYRIRRLKDKLGTRSVATGEVEFDD----AEAyLIGDE 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 233 GKGFKIAMMTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAAC---K 309
Cdd:cd01154 260 GKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARafdR 339
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1BUC_A 310 KQEGKP--------FTvdaAIAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQ 373
Cdd:cd01154 340 AAADKPveahmarlAT---PVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQ 408
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
5-378 |
8.47e-50 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 172.73 E-value: 8.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 5 LTDIQQDFLKLAHDFGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEekygGSGDDGGDVLSYILAVEELAKYDA 84
Cdd:PLN02526 29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIK----GYGCPGLSITASAIATAEVARVDA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 85 GVAITLSATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGtYTLNGSKIFITNG 164
Cdd:PLN02526 105 SCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGG-WILNGQKRWIGNS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 165 GAADIYIVFAmtdKSKGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLgEEGKGFKIAMMTLD 244
Cdd:PLN02526 184 TFADVLVIFA---RNTTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRL-PGVNSFQDTNKVLA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 245 GGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARnLVYKAACKKQE-GKPFTVDAAIA 323
Cdd:PLN02526 260 VSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMF-LVGWRLCKLYEsGKMTPGHASLG 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
1BUC_A 324 KRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTG 378
Cdd:PLN02526 339 KAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTG 393
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
103-374 |
2.29e-49 |
|
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: 171.03 E-value: 2.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 103 QFGTEAQKEKFLVPLVEGTKLGAFGLTEPN-AGTDASGQQTIATKnDDGTYTLNGSKIFITngGAAD----IYIVFAMTD 177
Cdd:cd01155 106 RYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIER-DGDDYVINGRKWWSS--GAGDprckIAIVMGRTD 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 178 -KSKGNHGITAFILED-GTPGFT-------YGKkEDKMGIHtsqtMELVFQDVKVPAENMLGEEGKGFKIAMMTLDGGRI 248
Cdd:cd01155 183 pDGAPRHRQQSMILVPmDTPGVTiirplsvFGY-DDAPHGH----AEITFDNVRVPASNLILGEGRGFEIAQGRLGPGRI 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 249 GVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVDAAIA--KRV 326
Cdd:cd01155 258 HHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTVGNKAARKEIAmiKVA 337
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
1BUC_A 327 ASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQL 374
Cdd:cd01155 338 APRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHL 385
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
77-382 |
7.14e-42 |
|
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: 150.96 E-value: 7.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 77 EELAKYDAGVAITLSATvSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGtYTLNG 156
Cdd:cd01152 73 EEMAAAGAPVPFNQIGI-DLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDD-WVVNG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 157 SKIFITNGGAADIYIVFAMTDKSKGNH-GITAFILEDGTPGFTYGKKEDKMGiHTSqTMELVFQDVKVPAENMLGEEGKG 235
Cdd:cd01152 151 QKIWTSGAHYADWAWLLVRTDPEAPKHrGISILLVDMDSPGVTVRPIRSING-GEF-FNEVFLDDVRVPDANRVGEVNDG 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 236 FKIAMMTLDGGR---IGVAAQALGIAEAALADAVEYskqrvqfGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQE 312
Cdd:cd01152 229 WKVAMTTLNFERvsiGGSAATFFELLLARLLLLTRD-------GRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAA 301
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1BUC_A 313 GKPFTVDAAIAKRVASDVAMRVTTEAVQIFGGYGY-SEEYPVA-------RHMRDAKITQIYEGTNEVQLMVTGGALL 382
Cdd:cd01152 302 GKPPGAEASIAKLFGSELAQELAELALELLGTAALlRDPAPGAelagrweADYLRSRATTIYGGTSEIQRNIIAERLL 379
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
98-373 |
4.28e-31 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 124.60 E-value: 4.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 98 ANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGTYTLNGSKIFITNGG----AADIYIVF 173
Cdd:PTZ00456 157 ANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADGSYKITGTKIFISAGDhdltENIVHIVL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 174 AMTDKSK-GNHGITAFIL------EDGT----PGFTYGKKEDKMGIHTSQTMELVFQDVKvpaENMLGEEGKGFKIAMMT 242
Cdd:PTZ00456 237 ARLPNSLpTTKGLSLFLVprhvvkPDGSletaKNVKCIGLEKKMGIKGSSTCQLSFENSV---GYLIGEPNAGMKQMFTF 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 243 LDGGRIGVAAQALGIAEAALADAVEYSKQRVQF------------GKPLCKFQSISFKLADMKMQIEAARNLVYK----- 305
Cdd:PTZ00456 314 MNTARVGTALEGVCHAELAFQNALRYARERRSMralsgtkepekpADRIICHANVRQNILFAKAVAEGGRALLLDvgrll 393
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1BUC_A 306 --------AACKKQEGKPFTVDAAIAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQ 373
Cdd:PTZ00456 394 dihaaakdAATREALDHEIGFYTPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQ 469
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
103-374 |
3.97e-30 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 122.21 E-value: 3.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 103 QFGTEAQKEKFLVPLVEGTKLGAFGLTEPN-AGTDASGQQ-TIATKNDdgTYTLNGSKIFITngGAAD----IYIVFAMT 176
Cdd:PLN02876 531 RYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIEcSIRRQGD--SYVINGTKWWTS--GAMDprcrVLIVMGKT 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 177 DKSKGNHGITAFILED-GTPG-------FTYGKKEDKMGiHTsqtmELVFQDVKVPAENMLGEEGKGFKIAMMTLDGGRI 248
Cdd:PLN02876 607 DFNAPKHKQQSMILVDiQTPGvqikrplLVFGFDDAPHG-HA----EISFENVRVPAKNILLGEGRGFEIAQGRLGPGRL 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 249 GVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAA-------CKKQEGKpftvdAA 321
Cdd:PLN02876 682 HHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAAdqldrlgNKKARGI-----IA 756
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
1BUC_A 322 IAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQL 374
Cdd:PLN02876 757 MAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHL 809
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
125-218 |
7.82e-30 |
|
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: 110.45 E-value: 7.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 125 AFGLTEPNAGTDASGQQTIATKNDDGTYTLNGSKIFITNGGAADIYIVFAMTDKSKGNHGITAFILEDGTPGFTYGKKED 204
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....
1BUC_A 205 KMGIHTSQTMELVF 218
Cdd:pfam02770 81 KLGVRGLPTGELVF 94
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
249-371 |
8.68e-28 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 106.28 E-value: 8.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 249 GVAAQALGIAEAALADAVEYSKQRVQ--FGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQE----GKPFTV---- 318
Cdd:pfam08028 1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAaaaaGKPVTPalra 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
1BUC_A 319 DAAIAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNE 371
Cdd:pfam08028 81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
6-120 |
2.04e-27 |
|
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: 104.47 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 6 TDIQQDFLKLAHDFGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDGgdvLSYILAVEELAKYDAG 85
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDY---LAYALVAEELARADAS 77
|
90 100 110
....*....|....*....|....*....|....*
1BUC_A 86 VAITLSATVSLCANPIWQFGTEAQKEKFLVPLVEG 120
Cdd:pfam02771 78 VALALSVHSSLGAPPILRFGTEEQKERYLPKLASG 112
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
84-346 |
7.80e-19 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 88.33 E-value: 7.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 84 AGVAITLSATV----SLCANPIWQ-FGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDAS--------------GQQTIA 144
Cdd:PRK09463 150 ASRSGTLAVTVmvpnSLGPGELLLhYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGsipdtgvvckgewqGEEVLG 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 145 TKnddgtytLNGSKIFITNG------GAAdiyivFAMTDK-----SKGNHGITAFILEDGTPGFTYGKKEDKMGIhtsqt 213
Cdd:PRK09463 230 MR-------LTWNKRYITLApiatvlGLA-----FKLYDPdgllgDKEDLGITCALIPTDTPGVEIGRRHFPLNV----- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 214 melVFQ-------DVKVPAENMLGEE---GKGFKIAMMTLDGGR-IGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKF 282
Cdd:PRK09463 293 ---PFQngptrgkDVFIPLDYIIGGPkmaGQGWRMLMECLSVGRgISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKF 369
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1BUC_A 283 QSISFKLADM---KMQIEAARNLVykAACKKQEGKPfTVDAAIAKRVASDVAMRVTTEAVQIFGGYG 346
Cdd:PRK09463 370 EGIEEPLARIagnAYLMDAARTLT--TAAVDLGEKP-SVLSAIAKYHLTERGRQVINDAMDIHGGKG 433
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
103-346 |
9.80e-19 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 88.09 E-value: 9.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 103 QFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASG--QQTIATKND-DGTYTL----NGSKIFITNGGAADIY-IVFA 174
Cdd:PRK13026 173 HYGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAipDTGIVCRGEfEGEEVLglrlTWDKRYITLAPVATVLgLAFK 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 175 MTDK-----SKGNHGIT-AFILEDgTPGFTYGKKEDKMGihtsqtmeLVFQ-------DVKVPAENMLG---EEGKGFKI 238
Cdd:PRK13026 253 LRDPdgllgDKKELGITcALIPTD-HPGVEIGRRHNPLG--------MAFMngttrgkDVFIPLDWIIGgpdYAGRGWRM 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 239 AMMTLDGGRiGVAAQALGIAEAALA--DAVEYSKQRVQFGKPLCKFQSISFKLADM---KMQIEAARNLVYKAACKKQeg 313
Cdd:PRK13026 324 LVECLSAGR-GISLPALGTASGHMAtrTTGAYAYVRRQFGMPIGQFEGVQEALARIagnTYLLEAARRLTTTGLDLGV-- 400
|
250 260 270
....*....|....*....|....*....|...
1BUC_A 314 KPfTVDAAIAKRVASDVAMRVTTEAVQIFGGYG 346
Cdd:PRK13026 401 KP-SVVTAIAKYHMTELARDVVNDAMDIHAGKG 432
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
74-372 |
3.08e-15 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 77.10 E-value: 3.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 74 LAVEELAKYDAGVA----ITLSATV---SLC-------ANPIWQFGTEAQKEKFLVPLVE----------GTKLG---AF 126
Cdd:PRK11561 103 LAWEEDARSGAFVAraarFMLHAQVeagTLCpitmtfaATPLLLQMLPAPFQDWLTPLLSdrydshllpgGQKRGlliGM 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 127 GLTEPNAGTDASGQQTIATKNDDGTYTLNGSKIFITNGgAADIYIVFAMTdksKGnhGITAF----ILEDGT-PGFTYGK 201
Cdd:PRK11561 183 GMTEKQGGSDVLSNTTRAERLADGSYRLVGHKWFFSVP-QSDAHLVLAQA---KG--GLSCFfvprFLPDGQrNAIRLER 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 202 KEDKMGIHTSQTMELVFQDVkvpAENMLGEEGKG----FKIAMMTldggRIGVAAQALGIAEAALADAVEYSKQRVQFGK 277
Cdd:PRK11561 257 LKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGirliLKMGGMT----RFDCALGSHGLMRRAFSVAIYHAHQRQVFGK 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 278 PLCKFQSISFKLADMKMQIEAARNLVYK-AACKKQEGKP--------FTVDA--AIAKRVASDVAmrvttEAVQIFGGYG 346
Cdd:PRK11561 330 PLIEQPLMRQVLSRMALQLEGQTALLFRlARAWDRRADAkealwarlFTPAAkfVICKRGIPFVA-----EAMEVLGGIG 404
|
330 340
....*....|....*....|....*.
1BUC_A 347 YSEEYPVARHMRDAKITQIYEGTNEV 372
Cdd:PRK11561 405 YCEESELPRLYREMPVNSIWEGSGNI 430
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
82-383 |
6.81e-15 |
|
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: 76.21 E-value: 6.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 82 YDAGVAITLSATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIAT--KNDD----GTYTLN 155
Cdd:cd01150 94 YDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATydPLTQefviNTPDFT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 156 GSKIFITNGG-AADIYIVFAMTDKSKGNHGITAFIL---EDGT----PGFTYGKKEDKMGIHTSQTMELVFQDVKVPAEN 227
Cdd:cd01150 174 ATKWWPGNLGkTATHAVVFAQLITPGKNHGLHAFIVpirDPKThqplPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPREN 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 228 MLG----------------EEGKGFKIAMMTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGK-------PLCKFQS 284
Cdd:cd01150 254 LLNrfgdvspdgtyvspfkDPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPkpsdpevQILDYQL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 285 ISFKLADMkmqieAARNLVYKAACKK-----------------QEGKPFTVDAAIAKRVASDVAMRVTTEAVQIFGGYGY 347
Cdd:cd01150 334 QQYRLFPQ-----LAAAYAFHFAAKSlvemyheiikellqgnsELLAELHALSAGLKAVATWTAAQGIQECREACGGHGY 408
|
330 340 350
....*....|....*....|....*....|....*...
1BUC_A 348 SEE--YPVARHMRDAKITqiYEGTNEVQLMVTGGALLR 383
Cdd:cd01150 409 LAMnrLPTLRDDNDPFCT--YEGDNTVLLQQTANYLLK 444
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
23-361 |
1.16e-14 |
|
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: 74.67 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 23 KLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDggdVLSYILAVEELAKYDAGVAITLSATVSLCANpIW 102
Cdd:cd01163 9 RIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGAS---LPDLYEVVRELAAADSNIAQALRAHFGFVEA-LL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 103 QFGTEAQKEKFLVPLVEGTKLGAfGLTEpnAGTDASGQQTIATKNDDGTYTLNGSKIFITNGGAADIYIVFAMTDKSKgn 182
Cdd:cd01163 85 LAGPEQFRKRWFGRVLNGWIFGN-AVSE--RGSVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGK-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 183 hgITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIAMMTLdGGRIGVAAQALGIAEAAL 262
Cdd:cd01163 160 --LVFAAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPNAPDRGTLLTA-IYQLVLAAVLAGIARAAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 263 ADAVEYSKQRVQ------FGKPLCKFQSISfKLADMKMQIEAARNLVYKAA------------CKKQEGKPFTVDAAIAK 324
Cdd:cd01163 237 DDAVAYVRSRTRpwihsgAESARDDPYVQQ-VVGDLAARLHAAEALVLQAAraldaaaaagtaLTAEARGEAALAVAAAK 315
|
330 340 350
....*....|....*....|....*....|....*..
1BUC_A 325 RVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAK 361
Cdd:cd01163 316 VVVTRLALDATSRLFEVGGASATAREHNLDRHWRNAR 352
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
71-383 |
1.41e-14 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 75.28 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 71 SYILAVEELAKYDAGVAITLSATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKN--- 147
Cdd:PLN02636 122 KYFAITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDplt 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 148 --------DDGtytlnGSKIFITNGGA-ADIYIVFAM----TDKSKG--NHGITAFI-----LEDGT--PGFTYGKKEDK 205
Cdd:PLN02636 202 defvintpNDG-----AIKWWIGNAAVhGKFATVFARlklpTHDSKGvsDMGVHAFIvpirdMKTHQvlPGVEIRDCGHK 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 206 MGIHTSQTMELVFQDVKVPAENMLGEEG----------------KGFKIAMMTLDGGRIGVAAQALGIAEAALADAVEYS 269
Cdd:PLN02636 277 VGLNGVDNGALRFRSVRIPRDNLLNRFGdvsrdgkytsslptinKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYS 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 270 KQRVQFGKP------LCKFQSISFKLADMKMQIE----AARNLVYKAACKKQE------GKPFTVDAAIAKRVASDVAMR 333
Cdd:PLN02636 357 LLRQQFGPPkqpeisILDYQSQQHKLMPMLASTYafhfATEYLVERYSEMKKThddqlvADVHALSAGLKAYITSYTAKA 436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
1BUC_A 334 VTT--EAVqifGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGALLR 383
Cdd:PLN02636 437 LSTcrEAC---GGHGYAAVNRFGSLRNDHDIFQTFEGDNTVLLQQVAADLLK 485
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
75-383 |
1.65e-13 |
|
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: 71.23 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 75 AVEELAKYDAGVA--ITLSATVS--LCAnpiwqFGTEAQKEKFLVPlvEGTKLgafgltepnAGTDASGQQtiATKNDDG 150
Cdd:cd01159 58 AIATLAEACGSAAwvASIVATHSrmLAA-----FPPEAQEEVWGDG--PDTLL---------AGSYAPGGR--AERVDGG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 151 tYTLNGSKIFITNGGAADIYIVFAMTDKSKGNHGITAFILedgtPGFTYGKKED--KMGIHTSQTMELVFQDVKVPAENM 228
Cdd:cd01159 120 -YRVSGTWPFASGCDHADWILVGAIVEDDDGGPLPRAFVV----PRAEYEIVDTwhVVGLRGTGSNTVVVDDVFVPEHRT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 229 L-----------GEEGKGFKIAMMTLDGgrIGVAAQALGIAEAALADAVEYSKQRVQ---FGKPLCKFQSISFKLADMKM 294
Cdd:cd01159 195 LtagdmmagdgpGGSTPVYRMPLRQVFP--LSFAAVSLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 295 QIEAARNLVYKAA----CKKQEGKPFTVDAAIAKRVASDVAMRVTTEAVQIF----GGYGYSEEYPVARHMRDAKITQIY 366
Cdd:cd01159 273 ELDAARAFLERATrdlwAHALAGGPIDVEERARIRRDAAYAAKLSAEAVDRLfhaaGGSALYTASPLQRIWRDIHAAAQH 352
|
330
....*....|....*...
1BUC_A 367 EGTN-EVQLMVTGGALLR 383
Cdd:cd01159 353 AALNpETAAEAYGRALLG 370
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
77-382 |
2.01e-11 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 65.56 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 77 EELAKYDAGVAITLSATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKN-DDGTYTLN 155
Cdd:PLN02312 140 EVIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDpKTEEFVIN 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 156 -----GSKIFItnGGAAD---IYIVFAMTDKSKGNHGITAFIL----EDGT--PGFTYGKKEDKMGIHTSQTMELVFQDV 221
Cdd:PLN02312 220 tpcesAQKYWI--GGAANhatHTIVFSQLHINGKNEGVHAFIAqirdQDGNicPNIRIADCGHKIGLNGVDNGRIWFDNL 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 222 KVPAENMLGE------EGK----------GFKIAMMTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQF----GKP--- 278
Cdd:PLN02312 298 RIPRENLLNSvadvspDGKyvsaikdpdqRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAFsvtpNGPevl 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 279 --------------LCKFQSISFKLADMKMqieaarnLVYKAacKKQEGKPFTVDAAIAKRVASDVAMRVTTEAVQIFGG 344
Cdd:PLN02312 378 lldypshqrrllplLAKTYAMSFAANDLKM-------IYVKR--TPESNKAIHVVSSGFKAVLTWHNMRTLQECREACGG 448
|
330 340 350
....*....|....*....|....*....|....*...
1BUC_A 345 YGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGALL 382
Cdd:PLN02312 449 QGLKTENRVGQLKAEYDVQSTFEGDNNVLMQQVSKALL 486
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
105-276 |
3.28e-08 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 55.23 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 105 GTEAQKEKFLvPLVEGTK-LGAFGLTEPNAGTDASGQQTIAT---KNDD---GTYTLNGSKIFITNGGAADIY-IVFAMT 176
Cdd:PLN02443 114 GTEEQQKKWL-PLAYKMQiIGCYAQTELGHGSNVQGLETTATfdpKTDEfviHSPTLTSSKWWPGGLGKVSTHaVVYARL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 177 DKSKGNHGITAFI-----LEDGTP--GFTYGKKEDKMGIHTSQTME---LVFQDVKVPAENMLgeegkgFKIAMMTLDGG 246
Cdd:PLN02443 193 ITNGKDHGIHGFIvqlrsLDDHSPlpGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQML------MRLSKVTREGK 266
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
1BUC_A 247 ------------------RIGVAAQALGIAEAALADAVEYSKQRVQFG 276
Cdd:PLN02443 267 yvqsdvprqlvygtmvyvRQTIVADASTALSRAVCIATRYSAVRRQFG 314
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
105-257 |
7.72e-05 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 44.49 E-value: 7.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 105 GTEAQKEKFLVPLVEGTKLGAFGLTEPNaGTDASGQQTIATKNDDGTYTLNGSKiFITNGGAADIYIVFAMT-DKSKGNH 183
Cdd:PTZ00457 117 GSKELKGKYLTAMSDGTIMMGWATEEGC-GSDISMNTTKASLTDDGSYVLTGQK-RCEFAASATHFLVLAKTlTQTAAEE 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1BUC_A 184 GITA------FILEDGTPGFTYGKKedkmgihtsqtmELVFQDvkVPAENMLGEEGKGFKIAMMTLDGGRIGVAAQALGI 257
Cdd:PTZ00457 195 GATEvsrnsfFICAKDAKGVSVNGD------------SVVFEN--TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGI 260
|
|
|