|
Name |
Accession |
Description |
Interval |
E-value |
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
41-398 |
0e+00 |
|
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- dehydrogenation of short branched chain acyl-CoA intermediates in valine catabolism. It is predicted to be a homotetramer.
Pssm-ID: 173851 [Multi-domain] Cd Length: 375 Bit Score: 742.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 41 LNEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTT 120
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 121 AYISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDI 200
Cdd:cd01162 81 AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 201 YVVMCRTGGPGPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGGRINI 280
Cdd:cd01162 161 YVVMARTGGEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 281 ASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFTLADMATRLVAARLMVRNAAVALQEERKDAVALCSMAKLFATD 360
Cdd:cd01162 241 ASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATD 320
|
330 340 350
....*....|....*....|....*....|....*...
gi 767969970 361 ECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILE 398
Cdd:cd01162 321 ECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILE 358
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
41-398 |
2.69e-145 |
|
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: 419.63 E-value: 2.69e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 41 LNEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTT 120
Cdd:COG1960 5 LTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 121 AYISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDI 200
Cdd:COG1960 85 LPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVADV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 201 YVVMCRTGG-PGPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGGRIN 279
Cdd:COG1960 165 ILVLARTDPaAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGRLG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 280 IASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFTLADMATRLVAARLMVRNAAVALQEErKDAVALCSMAKLFAT 359
Cdd:COG1960 245 LAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAG-EDAALEAAMAKLFAT 323
|
330 340 350
....*....|....*....|....*....|....*....
gi 767969970 360 DECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILE 398
Cdd:COG1960 324 EAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYE 362
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
43-398 |
3.27e-141 |
|
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases; Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.
Pssm-ID: 173847 [Multi-domain] Cd Length: 373 Bit Score: 408.97 E-value: 3.27e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 43 EEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTTAY 122
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 123 ISIHN-MCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDIY 201
Cdd:cd01158 81 VSVHNsLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 202 VVMCRTGGP-GPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGGRINI 280
Cdd:cd01158 161 IVFAVTDPSkGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 281 ASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFTLADMATRLVAARLMVRNAAvALQEERKDAVALCSMAKLFATD 360
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAA-RLKDNGEPFIKEAAMAKLFASE 319
|
330 340 350
....*....|....*....|....*....|....*...
gi 767969970 361 ECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILE 398
Cdd:cd01158 320 VAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYE 357
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
43-398 |
5.00e-116 |
|
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: 343.11 E-value: 5.00e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 43 EEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLgfggvyiqtdvggsglsrldtsvifealatgctsttay 122
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLL-------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 123 isihnMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDIYV 202
Cdd:cd00567 43 -----LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 203 VMCRTGGPGP--KGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGGRINI 280
Cdd:cd00567 118 VLARTDEEGPghRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 281 ASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFTLADMATRLVAARLMVRNAAVALQEERKDAVALCSMAKLFATD 360
Cdd:cd00567 198 AAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFATE 277
|
330 340 350
....*....|....*....|....*....|....*...
gi 767969970 361 ECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILE 398
Cdd:cd00567 278 AAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAE 315
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
40-396 |
6.97e-94 |
|
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA dehydrogenase, which catalyzes the third step in leucine catabolism, the conversion of isovaleryl-CoA (3-methylbutyryl-CoA) into 3-methylcrotonyl-CoA. IVD is a homotetramer and has the greatest affinity for small branched chain substrates.
Pssm-ID: 173845 [Multi-domain] Cd Length: 376 Bit Score: 288.16 E-value: 6.97e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 40 GLNEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTST 119
Cdd:cd01156 1 GLDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 120 TAYISIH-NMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGES 198
Cdd:cd01156 81 ALSYGAHsNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 199 DIYVVMCRTGG-PGPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGGR 277
Cdd:cd01156 161 DTLVVYAKTDPsAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 278 INIASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFTLADMATRLVAARLMVRNAAVALQEERKDAVAlCSMAKLF 357
Cdd:cd01156 241 LVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKD-AAGVILY 319
|
330 340 350
....*....|....*....|....*....|....*....
gi 767969970 358 ATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQI 396
Cdd:cd01156 320 AAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEI 358
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
43-396 |
4.41e-93 |
|
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: 285.93 E-value: 4.41e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 43 EEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALA-TGCTSTTa 121
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELArAGGSGPG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 122 yISIHN-MCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDI 200
Cdd:cd01160 80 -LSLHTdIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 201 YVVMCRTGGP--GPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGGRI 278
Cdd:cd01160 159 VIVVARTGGEarGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 279 NIASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFTLADMATRLVAARLMVRNAAVALQEERKDaVALCSMAKLFA 358
Cdd:cd01160 239 LIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLD-VAEASMAKYWA 317
|
330 340 350
....*....|....*....|....*....|....*...
gi 767969970 359 TDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQI 396
Cdd:cd01160 318 TELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPI 355
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
41-398 |
4.30e-82 |
|
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: 257.90 E-value: 4.30e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 41 LNEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTT 120
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 121 AYISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDI 200
Cdd:cd01157 81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 201 YVVMCRTG----GPGPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGG 276
Cdd:cd01157 161 YFLLARSDpdpkCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 277 RINIASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFTLADMATRLVAARLMVRNAAVALQEERKDAVaLCSMAKL 356
Cdd:cd01157 241 RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTY-YASIAKA 319
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 767969970 357 FATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILE 398
Cdd:cd01157 320 FAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYE 361
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
40-398 |
3.42e-78 |
|
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: 248.92 E-value: 3.42e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 40 GLNEEQKEFQKVAFD----FAAREMAPnmAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFE--ALA 113
Cdd:cd01161 22 VLTEEQTEELNMLVGpvekFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEivGMD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 114 TGCTSTtayISIHNMCAWM-IDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQ--GDHYILNGSKA 190
Cdd:cd01161 100 LGFSVT---LGAHQSIGFKgILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSedGKHYVLNGSKI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 191 FISGAGESDIYVVMCRT-----GGPGPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGSEGQG 265
Cdd:cd01161 177 WITNGGIADIFTVFAKTevkdaTGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 266 FLIAVRGLNGGRINIASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFTLADMATRLVAARLMVRNAAVALQEERK 345
Cdd:cd01161 257 FKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLK 336
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 767969970 346 DAVAL-CSMAKLFATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILE 398
Cdd:cd01161 337 AEYQIeAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFE 390
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
41-384 |
1.76e-60 |
|
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: 202.20 E-value: 1.76e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 41 LNEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQtDVGGSGLSRLDTSVI---FEALATGCT 117
Cdd:cd01151 13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIK-GYGCAGLSSVAYGLIareVERVDSGYR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 118 STtayISIH-NMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAG 196
Cdd:cd01151 92 SF---MSVQsSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 197 ESDIYVVMCRTGGPGpkGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIgSEGQGFLIAVRGLNGG 276
Cdd:cd01151 169 IADVFVVWARNDETG--KIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL-PGAEGLRGPFKCLNNA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 277 RINIASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFTLADMATRLVAARLMVRNAAvALQEERKDAVALCSMAKL 356
Cdd:cd01151 246 RYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVG-RLKDQGKATPEQISLLKR 324
|
330 340
....*....|....*....|....*...
gi 767969970 357 FATDECFAICNQALQMHGGYGYLKDYAV 384
Cdd:cd01151 325 NNCGKALEIARTAREMLGGNGISDEYHI 352
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
37-396 |
5.67e-54 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 185.47 E-value: 5.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 37 PSMGLNEEQKEFQKVAFDFAAREMAPNMAEWDQKELFP--VDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALAT 114
Cdd:PLN02519 22 SSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPkdVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 115 GCTSTTAYISIH-NMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFIS 193
Cdd:PLN02519 102 ASGSVGLSYGAHsNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 194 GAGESDIYVVMCRTG-GPGPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGSEGQGFLIAVRG 272
Cdd:PLN02519 182 NGPVAQTLVVYAKTDvAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 273 LNGGRINIASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFTLADMATRLVAARLMVRNAAVALQE---ERKDava 349
Cdd:PLN02519 262 LDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNgkvDRKD--- 338
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 767969970 350 lCSMAKLFATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQI 396
Cdd:PLN02519 339 -CAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEI 384
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
64-396 |
6.78e-48 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 168.75 E-value: 6.78e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 64 MAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTstTAYISIHNMCAWMIDSFGNEEQRH 143
Cdd:PRK12341 29 FRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCGA--PAFLITNGQCIHSMRRFGSAEQLR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 144 KfcpplcTMEKFA-----SYCL--TEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDIYVVMCR-TGGPGP-KG 214
Cdd:PRK12341 107 K------TAESTLetgdpAYALalTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAKEYPYMLVLARdPQPKDPkKA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 215 ISCIVVEKGTPGLSFGKKEkKVGWNSQPTRAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGGRINIASCSLGAAHASVIL 294
Cdd:PRK12341 181 FTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFEMERLINAARSLGFAECAFED 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 295 TRDHLNVRKQFGEPLASNQYLQFTLADMATRLVAARLMVRNAavALQEERKDAVALCS-MAKLFATDECFAICNQALQMH 373
Cdd:PRK12341 260 AARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKV--AWQADNGQSLRTSAaLAKLYCARTAMEVIDDAIQIM 337
|
330 340
....*....|....*....|...
gi 767969970 374 GGYGYLKDYAVQQYVRDSRVHQI 396
Cdd:PRK12341 338 GGLGYTDEARVSRFWRDVRCERI 360
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
54-398 |
9.96e-47 |
|
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: 166.41 E-value: 9.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 54 DFAAREMAPNMAEWDQKEL--------FP---VDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTsTTAY 122
Cdd:cd01153 7 RLAENVLAPLNADGDREGPvfddgrvvVPppfKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDA-PLMY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 123 ISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGD-HYILNGSKAFISgAGESD-- 199
Cdd:cd01153 86 ASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFIS-AGEHDms 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 200 ---IYVVMCRTGGPGP--KGISCIVVEK----GTP-GLSFGKKEKKVGWNSQPTRAVIFEDCAVPVanrIGSEGQGFLIA 269
Cdd:cd01153 165 eniVHLVLARSEGAPPgvKGLSLFLVPKflddGERnGVTVARIEEKMGLHGSPTCELVFDNAKGEL---IGEEGMGLAQM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 270 VRGLNGGRINIASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFT--------LADMATRLVAARLMVRNAAVALQ 341
Cdd:cd01153 242 FAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAPAVTIIhhpdvrrsLMTQKAYAEGSRALDLYTATVQD 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 342 EERKDAV-------------ALCSMAKLFATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILE 398
Cdd:cd01153 322 LAERKATegedrkalsaladLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYE 391
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
44-405 |
1.25e-44 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 160.87 E-value: 1.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 44 EQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATG----CTst 119
Cdd:PTZ00461 40 EHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYdpgfCL-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 120 tAYISiHNMCawMIDSFGNE---EQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGD-HYILNGSKAFISGA 195
Cdd:PTZ00461 118 -AYLA-HSML--FVNNFYYSaspAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 196 GESDIYVVMCRTGGPgpkgISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGSEGQGFLIAVRGLNG 275
Cdd:PTZ00461 194 TVADVFLIYAKVDGK----ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLEL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 276 GRINIASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFTLADMATRLVAARLMVRNAAVALQEERKDAVAlCSMAK 355
Cdd:PTZ00461 270 ERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLG-SDAAK 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 767969970 356 LFATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQI----LEAPFSNLS 405
Cdd:PTZ00461 349 LFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIgggtIEAHHKNIT 402
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
263-398 |
2.88e-40 |
|
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.
Pssm-ID: 395354 [Multi-domain] Cd Length: 149 Bit Score: 141.24 E-value: 2.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 263 GQGFLIAVRGLNGGRINIASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFTLADMATRLVAARLMVRNAAvALQE 342
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAA-EALD 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 767969970 343 ERKDAVALCSMAKLFATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILE 398
Cdd:pfam00441 80 AGGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGE 135
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
56-382 |
7.06e-40 |
|
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: 147.54 E-value: 7.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 56 AAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEAL--------ATGCTSTtayiSIHN 127
Cdd:cd01155 25 FLEYYAEGGDRWWTPPPIIEKLKAKAKAEGLWNLFLPEVSGLSGLTNLEYAYLAEETgrsffapeVFNCQAP----DTGN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 128 McaWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPG-SGSDAASLLTSAKKQGDHYILNGSKAFISGAGESD--IYVVM 204
Cdd:cd01155 101 M--EVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRKWWSSGAGDPRckIAIVM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 205 CRTGGPGP---KGISCIVVEKGTPGLSFGKKEKKVGWNSQPT--RAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGGRIN 279
Cdd:cd01155 179 GRTDPDGAprhRQQSMILVPMDTPGVTIIRPLSVFGYDDAPHghAEITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIH 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 280 IASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFTLADMATRLVAARLMVRNAAVAL-QEERKDAVALCSMAKLFA 358
Cdd:cd01155 259 HCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIdTVGNKAARKEIAMIKVAA 338
|
330 340
....*....|....*....|....
gi 767969970 359 TDECFAICNQALQMHGGYGYLKDY 382
Cdd:cd01155 339 PRMALKIIDRAIQVHGAAGVSQDT 362
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
42-153 |
6.23e-39 |
|
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: 136.44 E-value: 6.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 42 NEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTTA 121
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|...
gi 767969970 122 YISIHN-MCAWMIDSFGNEEQRHKFCPPLCTME 153
Cdd:pfam02771 81 ALSVHSsLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
41-396 |
1.57e-37 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 140.74 E-value: 1.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 41 LNEEQKEFQKVAFDFAAREMAPN-MAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALatGCTST 119
Cdd:PRK03354 5 LNDEQELFVAGIRELMASENWEAyFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMEL--GRLGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 120 TAYISIHNMCAW-MIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGES 198
Cdd:PRK03354 83 PTYVLYQLPGGFnTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 199 DIYVVMCRTGGPGPKGI-SCIVVEKGTPGLSFGKKEkKVGWNSQPTRAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGGR 277
Cdd:PRK03354 163 PYIVVMARDGASPDKPVyTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHER 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 278 INIASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFTLADMATRLVAARLMVRNAAVALQEERKDAvALCSMAKLF 357
Cdd:PRK03354 242 FLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITS-GDAAMCKYF 320
|
330 340 350
....*....|....*....|....*....|....*....
gi 767969970 358 ATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQI 396
Cdd:PRK03354 321 CANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRV 359
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
41-384 |
1.89e-35 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 135.75 E-value: 1.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 41 LNEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQtDVGGSGLSRLDTSVIFEALATGCTSTT 120
Cdd:PLN02526 29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIK-GYGCPGLSITASAIATAEVARVDASCS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 121 AYISIHN-MCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESD 199
Cdd:PLN02526 108 TFILVHSsLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFAD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 200 IYVVMCRTggPGPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGSEgQGFLIAVRGLNGGRIN 279
Cdd:PLN02526 188 VLVIFARN--TTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGV-NSFQDTNKVLAVSRVM 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 280 IASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFTLADM-----ATRLVAARLmvrnaaVALQEERKDAVALCSMA 354
Cdd:PLN02526 265 VAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMlgniqAMFLVGWRL------CKLYESGKMTPGHASLG 338
|
330 340 350
....*....|....*....|....*....|
gi 767969970 355 KLFATDECFAICNQALQMHGGYGYLKDYAV 384
Cdd:PLN02526 339 KAWITKKARETVALGRELLGGNGILADFLV 368
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
79-360 |
1.46e-34 |
|
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: 132.47 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 79 RKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASY 158
Cdd:cd01152 42 RALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 159 CLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDIYVVMCRTGGPGPK--GISCIVVEKGTPGLSFGKKEKKV 236
Cdd:cd01152 122 GFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDPEAPKhrGISILLVDMDSPGVTVRPIRSIN 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 237 GwnSQPTRAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGGRINI---ASCSLGAAHASVILTRDHlnvrkqfGEPLASNQ 313
Cdd:cd01152 202 G--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIggsAATFFELLLARLLLLTRD-------GRPLIDDP 272
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767969970 314 YLQFTLADMATRLVAARLMVRNAAVALQEErKDAVALCSMAKLFATD 360
Cdd:cd01152 273 LVRQRLARLEAEAEALRLLVFRLASALAAG-KPPGAEASIAKLFGSE 318
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
123-416 |
4.09e-33 |
|
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: 129.41 E-value: 4.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 123 ISIHNMCAWMIDSFGNEEQRHkFCPPLCTMEK----FASYCLTEPGSGSDAASLLTSAKKQ-GDHYILNGSKAFISGAgE 197
Cdd:cd01154 113 LTMTDAAVYALRKYGPEELKQ-YLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERSgGGVYRLNGHKWFASAP-L 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 198 SDIYVVMCRTGG--PGPKGISCIVV----EKGT-PGLSFGKKEKKVGWNSQPTRAVIFEDCavpVANRIGSEGQGFLIAV 270
Cdd:cd01154 191 ADAALVLARPEGapAGARGLSLFLVprllEDGTrNGYRIRRLKDKLGTRSVATGEVEFDDA---EAYLIGDEGKGIYYIL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 271 RGLNGGRINIASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFTLADMATRLVAARLMVRNAAVALQEERKDAVAL 350
Cdd:cd01154 268 EMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKPVE 347
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767969970 351 CSMAKLFATDECFAICNQALQM-------HGGYGYLKDYAVQQYVRDSRVHQILEAPfSNLsLCWNRLEGMGA 416
Cdd:cd01154 348 AHMARLATPVAKLIACKRAAPVtseamevFGGNGYLEEWPVARLHREAQVTPIWEGT-GNI-QALDVLRVLVK 418
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
157-249 |
1.98e-29 |
|
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a beta-barrel fold.
Pssm-ID: 460685 [Multi-domain] Cd Length: 95 Bit Score: 110.45 E-value: 1.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 157 SYCLTEPGSGSDAASLLTSA-KKQGDHYILNGSKAFISGAGESDIYVVMCRTGGPGPK-GISCIVVEKGTPGLSFGKKEK 234
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHgGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 767969970 235 KVGWNSQPTRAVIFE 249
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
136-400 |
1.22e-24 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 107.19 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 136 FGNEEQRHKFCPPLCTMEKFASYCLTEPG-SGSDAASLLTSAKKQGDHYILNGSKAFISGAGES--DIYVVMCRT--GGP 210
Cdd:PLN02876 532 YGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPrcRVLIVMGKTdfNAP 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 211 GPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPT--RAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGGRINIASCSLGAA 288
Cdd:PLN02876 612 KHKQQSMILVDIQTPGVQIKRPLLVFGFDDAPHghAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAA 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 289 HASVILTRDHLNVRKQFGEPLASNQYLQFTLADMATRLVAARLMVRNAAVALQEE-RKDAVALCSMAKLFATDECFAICN 367
Cdd:PLN02876 692 ERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDRLgNKKARGIIAMAKVAAPNMALKVLD 771
|
250 260 270
....*....|....*....|....*....|...
gi 767969970 368 QALQMHGGYGYLKDYAVQQYVRDSRVHQILEAP 400
Cdd:PLN02876 772 MAMQVHGAAGVSSDTVLAHLWATARTLRIADGP 804
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
280-396 |
2.72e-20 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 86.63 E-value: 2.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 280 IASCSLGAAHASVILTRDHLNVRKQ--FGEPLASNQYLQFTLADMATRLVAARLMVRNAAVALQEERKDA-------VAL 350
Cdd:pfam08028 2 IAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAAAGkpvtpalRAE 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 767969970 351 CSMAKLFATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQI 396
Cdd:pfam08028 82 ARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQ 127
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
85-398 |
9.11e-20 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 91.85 E-value: 9.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 85 GFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTTAY--ISIHNMCAWMidSFGNEEQRHKFCPPLCTMEKFASYCLTE 162
Cdd:PTZ00456 112 GWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYpgLSIGAANTLM--AWGSEEQKEQYLTKLVSGEWSGTMCLTE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 163 PGSGSDAASLLTSAKKQGD-HYILNGSKAFISgAGESD-----IYVVMCRTGG--PGPKGISCIVVEKGTP--------- 225
Cdd:PTZ00456 190 PQCGTDLGQVKTKAEPSADgSYKITGTKIFIS-AGDHDlteniVHIVLARLPNslPTTKGLSLFLVPRHVVkpdgsleta 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 226 -GLSFGKKEKKVGWNSQPTRAVIFEDcavPVANRIGSEGQGFLIAVRGLNGGRIniaSCSL-GAAHASVIL------TRD 297
Cdd:PTZ00456 269 kNVKCIGLEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTARV---GTALeGVCHAELAFqnalryARE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 298 HLNVRKQFG--EPLASNQYLQFTlADMATRLVAARLMVRNAAVALQE---------ERKDAVA----------LCSMAKL 356
Cdd:PTZ00456 343 RRSMRALSGtkEPEKPADRIICH-ANVRQNILFAKAVAEGGRALLLDvgrlldihaAAKDAATrealdheigfYTPIAKG 421
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 767969970 357 FATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILE 398
Cdd:PTZ00456 422 CLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYE 463
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
76-377 |
2.67e-12 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 68.83 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 76 DVMRKAaqlGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHNMC--AWMIDSFGNEEQRHKFCPPLCTME 153
Cdd:PRK13026 115 DYLKKE---GFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPNSLgpGELLTHYGTQEQKDYWLPRLADGT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 154 KFASYCLTEPGSGSDAASL-----LTSAKKQGDHYI---LNGSKAFISGAGESDIYVVMCRT-------GGPGPKGISCI 218
Cdd:PRK13026 192 EIPCFALTGPEAGSDAGAIpdtgiVCRGEFEGEEVLglrLTWDKRYITLAPVATVLGLAFKLrdpdgllGDKKELGITCA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 219 VVEKGTPGLSFGKKEKKVGWNSQ--PTRAvifEDCAVPVANRIGSE---GQGFLIAVRGLNGGR-INIASCSLGAAHASV 292
Cdd:PRK13026 272 LIPTDHPGVEIGRRHNPLGMAFMngTTRG---KDVFIPLDWIIGGPdyaGRGWRMLVECLSAGRgISLPALGTASGHMAT 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 293 ILTRDHLNVRKQFGEPLASNQYLQFTLADMAT---RLVAARLMVrnaAVALQEERKDAVAlCSMAKLFATDECFAICNQA 369
Cdd:PRK13026 349 RTTGAYAYVRRQFGMPIGQFEGVQEALARIAGntyLLEAARRLT---TTGLDLGVKPSVV-TAIAKYHMTELARDVVNDA 424
|
....*...
gi 767969970 370 LQMHGGYG 377
Cdd:PRK13026 425 MDIHAGKG 432
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
56-393 |
1.97e-10 |
|
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, which is active against Gram-positive bacteria. Polyketides are secondary metabolites, which have important biological functions such as antitumor, immunosupressive or antibiotic activities. NcnH is a hydroxylase involved in the biosynthesis of naphthocyclinone and possibly other polyketides.
Pssm-ID: 173848 [Multi-domain] Cd Length: 370 Bit Score: 61.98 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 56 AAREMAP----NMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHNMCAW 131
Cdd:cd01159 2 RAEDLAPlireRAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIVATHSR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 132 MIDSFGNEEQRHKFcpplctmekfasycltepgsGSDAASLLTS-------AKKQGDHYILNGSKAFISGAGESDIYVVM 204
Cdd:cd01159 82 MLAAFPPEAQEEVW--------------------GDGPDTLLAGsyapggrAERVDGGYRVSGTWPFASGCDHADWILVG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 205 CRTGGPGPKGISCIVVekgtpglsFGKKEKK-------VGWNSQPTRAVIFEDCAVP--------VANRIGSEGQGFLI- 268
Cdd:cd01159 142 AIVEDDDGGPLPRAFV--------VPRAEYEivdtwhvVGLRGTGSNTVVVDDVFVPehrtltagDMMAGDGPGGSTPVy 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 269 --AVRGLNGgrINIASCSLGAAHASVILTRDHLNVRKQ---FGEPLASNQYLQFTLADMATRLVAARLMV-RNAAV--AL 340
Cdd:cd01159 214 rmPLRQVFP--LSFAAVSLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAELDAARAFLeRATRDlwAH 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 767969970 341 QEERK----DAVALCSMAKLFATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRV 393
Cdd:cd01159 292 ALAGGpidvEERARIRRDAAYAAKLSAEAVDRLFHAAGGSALYTASPLQRIWRDIHA 348
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
52-394 |
3.31e-10 |
|
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: 61.57 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 52 AFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYIQTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHNMCAW 131
Cdd:cd01163 2 RARPLAARIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGFVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 132 MIDSFGNEEQRhKFCPPLCTMEKFASYCLTEPGSgSDAASLLTSAKKQGDHYILNGSKAFISGAGESDiYVVMCRTGGPG 211
Cdd:cd01163 82 ALLLAGPEQFR-KRWFGRVLNGWIFGNAVSERGS-VRPGTFLTATVRDGGGYVLNGKKFYSTGALFSD-WVTVSALDEEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 212 PKGIscIVVEKGTPGLS-------FGKKEKKVGwNSQPTRAVIFEDCAVPVANRigSEGQGFLIAVRGLnggriNIASCS 284
Cdd:cd01163 159 KLVF--AAVPTDRPGITvvddwdgFGQRLTASG-TVTFDNVRVEPDEVLPRPNA--PDRGTLLTAIYQL-----VLAAVL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 285 LGAAHASVILTRDHlnVRKQ---FGEPLASNQ----YLQFTLADMATRLVAARLMVRNAAVALQ-----------EERKD 346
Cdd:cd01163 229 AGIARAALDDAVAY--VRSRtrpWIHSGAESArddpYVQQVVGDLAARLHAAEALVLQAARALDaaaaagtaltaEARGE 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 767969970 347 AVALCSMAKLFATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVH 394
Cdd:cd01163 307 AALAVAAAKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNARTH 354
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
136-377 |
3.31e-09 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 59.06 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 136 FGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASL-----LTSAKKQGDHYI---LNGSKAFISGA------------ 195
Cdd:PRK09463 175 YGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIpdtgvVCKGEWQGEEVLgmrLTWNKRYITLApiatvlglafkl 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 196 --------GESDIyvvmcrtggpgpkGISCIVVEKGTPGLSFGKKEKKVGWNSQ--PTRAvifEDCAVPVANRIGSE--- 262
Cdd:PRK09463 255 ydpdgllgDKEDL-------------GITCALIPTDTPGVEIGRRHFPLNVPFQngPTRG---KDVFIPLDYIIGGPkma 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 263 GQGFLIAVRGLNGGR-INIASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFTLADMA--TRLV-AARLMVrNAAV 338
Cdd:PRK09463 319 GQGWRMLMECLSVGRgISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAgnAYLMdAARTLT-TAAV 397
|
250 260 270
....*....|....*....|....*....|....*....
gi 767969970 339 ALQEerKDAVaLCSMAKLFATDECFAICNQALQMHGGYG 377
Cdd:PRK09463 398 DLGE--KPSV-LSAIAKYHLTERGRQVINDAMDIHGGKG 433
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
116-185 |
4.46e-04 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 42.52 E-value: 4.46e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767969970 116 CTSTTAYISIH-NMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSA--KKQGDHYIL 185
Cdd:PTZ00460 88 CPQGTFISTVHfAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTAtyDKQTNEFVI 160
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
88-266 |
5.27e-04 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 42.18 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 88 GVYIQTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIH-NMCAWMIDSFGNEEQRHKFcppLCTME--KFASYCLTEPG 164
Cdd:PTZ00457 67 GARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHsGFCTYLLSTVGSKELKGKY---LTAMSdgTIMMGWATEEG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767969970 165 SGSDAASLLTSAKKQGD-HYILNGSKAFISGAGESDiYVVMCRT-----GGPGPKGI---SCIVVEKGTPGLSfgkkekk 235
Cdd:PTZ00457 144 CGSDISMNTTKASLTDDgSYVLTGQKRCEFAASATH-FLVLAKTltqtaAEEGATEVsrnSFFICAKDAKGVS------- 215
|
170 180 190
....*....|....*....|....*....|.
gi 767969970 236 VGWNSqptraVIFEDcaVPVANRIGSEGQGF 266
Cdd:PTZ00457 216 VNGDS-----VVFEN--TPAADVVGVVGEGF 239
|
|
| |
