|
Name |
Accession |
Description |
Interval |
E-value |
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
41-415 |
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: 773.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 41 LNEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVQTDVGGSGLSRLDTSVIFEALATGCTSTT 120
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 121 AYISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDV 200
Cdd:cd01162 81 AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 201 YVVMCRTGGPGPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGGRINI 280
Cdd:cd01162 161 YVVMARTGGEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 281 ASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFKLADMATRLVAARLMVRNAAVALQEERKDAVALCSMAKLFATD 360
Cdd:cd01162 241 ASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATD 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 410210768 361 ECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILEGSNEVMRILISRSLLQE 415
Cdd:cd01162 321 ECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
41-413 |
7.15e-156 |
|
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: 445.05 E-value: 7.15e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 41 LNEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVQTDVGGSGLSRLDTSVIFEALATGCTSTT 120
Cdd:COG1960 5 LTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 121 AYISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDV 200
Cdd:COG1960 85 LPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVADV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 201 YVVMCRTGG-PGPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGGRIN 279
Cdd:COG1960 165 ILVLARTDPaAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGRLG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 280 IASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFKLADMATRLVAARLMVRNAAVALQEErKDAVALCSMAKLFAT 359
Cdd:COG1960 245 LAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAG-EDAALEAAMAKLFAT 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 410210768 360 DECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILEGSNEVMRILISRSLL 413
Cdd:COG1960 324 EAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLL 377
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
43-413 |
4.24e-149 |
|
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: 427.45 E-value: 4.24e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 43 EEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVQTDVGGSGLSRLDTSVIFEALATGCTSTTAY 122
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 123 ISIHN-MCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDVY 201
Cdd:cd01158 81 VSVHNsLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 202 VVMCRTGGP-GPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGGRINI 280
Cdd:cd01158 161 IVFAVTDPSkGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 281 ASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFKLADMATRLVAARLMVRNAAvALQEERKDAVALCSMAKLFATD 360
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAA-RLKDNGEPFIKEAAMAKLFASE 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 410210768 361 ECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILEGSNEVMRILISRSLL 413
Cdd:cd01158 320 VAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLL 372
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
43-410 |
5.99e-124 |
|
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: 361.99 E-value: 5.99e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 43 EEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLgfggvyvqtdvggsglsrldtsvifealatgctsttay 122
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLL-------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 123 isihnMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDVYV 202
Cdd:cd00567 43 -----LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 203 VMCRTGGPGP--KGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGGRINI 280
Cdd:cd00567 118 VLARTDEEGPghRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 281 ASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFKLADMATRLVAARLMVRNAAVALQEERKDAVALCSMAKLFATD 360
Cdd:cd00567 198 AAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFATE 277
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 410210768 361 ECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILEGSNEVMRILISR 410
Cdd:cd00567 278 AAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
40-414 |
1.15e-102 |
|
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: 309.34 E-value: 1.15e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 40 GLNEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVQTDVGGSGLSRLDTSVIFEALATGCTST 119
Cdd:cd01156 1 GLDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 120 TAYISIH-NMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGES 198
Cdd:cd01156 81 ALSYGAHsNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 199 DVYVVMCRTGG-PGPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGGR 277
Cdd:cd01156 161 DTLVVYAKTDPsAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 278 INIASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFKLADMATRLVAARLMVRNAAVALQEERKDAVAlCSMAKLF 357
Cdd:cd01156 241 LVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKD-AAGVILY 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 410210768 358 ATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILEGSNEVMRILISRSLLQ 414
Cdd:cd01156 320 AAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
43-413 |
2.35e-101 |
|
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: 305.96 E-value: 2.35e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 43 EEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVQTDVGGSGLSRLDTSVIFEALA-TGCTSTTa 121
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELArAGGSGPG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 122 yISIHN-MCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDV 200
Cdd:cd01160 80 -LSLHTdIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 201 YVVMCRTGGP--GPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGGRI 278
Cdd:cd01160 159 VIVVARTGGEarGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 279 NIASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFKLADMATRLVAARLMVRNAAVALQEERKDaVALCSMAKLFA 358
Cdd:cd01160 239 LIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLD-VAEASMAKYWA 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 410210768 359 TDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILEGSNEVMRILISRSLL 413
Cdd:cd01160 318 TELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
41-413 |
2.98e-88 |
|
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: 272.54 E-value: 2.98e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 41 LNEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVQTDVGGSGLSRLDTSVIFEALATGCTSTT 120
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 121 AYISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDV 200
Cdd:cd01157 81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 201 YVVMCRTG----GPGPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGG 276
Cdd:cd01157 161 YFLLARSDpdpkCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 277 RINIASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFKLADMATRLVAARLMVRNAAVALQEERKDAVaLCSMAKL 356
Cdd:cd01157 241 RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTY-YASIAKA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 410210768 357 FATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILEGSNEVMRILISRSLL 413
Cdd:cd01157 320 FAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
40-414 |
2.83e-87 |
|
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is found in the mitochondria of eukaryotes and in some bacteria. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. VLCAD acts as a homodimer.
Pssm-ID: 173850 [Multi-domain] Cd Length: 409 Bit Score: 270.88 E-value: 2.83e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 40 GLNEEQKEFQKVAFD----FAAREMAPnmAEWDQKELFPVDVMRKAAQLGFGGVYVQTDVGGSGLSRLDTSVIFE--ALA 113
Cdd:cd01161 22 VLTEEQTEELNMLVGpvekFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEivGMD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 114 TGCTSTtayISIHNMCAWM-IDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQ--GDHYILNGSKA 190
Cdd:cd01161 100 LGFSVT---LGAHQSIGFKgILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSedGKHYVLNGSKI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 191 FISGAGESDVYVVMCRT-----GGPGPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGSEGQG 265
Cdd:cd01161 177 WITNGGIADIFTVFAKTevkdaTGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 266 FLIAVRGLNGGRINIASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFKLADMATRLVAARLMVRNAAVALQEERK 345
Cdd:cd01161 257 FKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLK 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 346 DAVAL-CSMAKLFATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILEGSNEVMRILISRSLLQ 414
Cdd:cd01161 337 AEYQIeAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQ 406
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
41-410 |
6.13e-63 |
|
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: 207.21 E-value: 6.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 41 LNEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVQtDVGGSGLSRLDTSVI---FEALATGCT 117
Cdd:cd01151 13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIK-GYGCAGLSSVAYGLIareVERVDSGYR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 118 STtayISIH-NMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAG 196
Cdd:cd01151 92 SF---MSVQsSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 197 ESDVYVVMCRTGGPGpkGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIgSEGQGFLIAVRGLNGG 276
Cdd:cd01151 169 IADVFVVWARNDETG--KIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL-PGAEGLRGPFKCLNNA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 277 RINIASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFKLADMATRLVAARLMVRNAAvALQEERKDAVALCSMAKL 356
Cdd:cd01151 246 RYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVG-RLKDQGKATPEQISLLKR 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 410210768 357 FATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILEGSNEVMRILISR 410
Cdd:cd01151 325 NNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGR 378
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
37-415 |
1.19e-61 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 204.73 E-value: 1.19e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 37 PSMGLNEEQKEFQKVAFDFAAREMAPNMAEWDQKELFP--VDVMRKAAQLGFGGVYVQTDVGGSGLSRLDTSVIFEALAT 114
Cdd:PLN02519 22 SSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPkdVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 115 GCTSTTAYISIH-NMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFIS 193
Cdd:PLN02519 102 ASGSVGLSYGAHsNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 194 GAGESDVYVVMCRTG-GPGPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGSEGQGFLIAVRG 272
Cdd:PLN02519 182 NGPVAQTLVVYAKTDvAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 273 LNGGRINIASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFKLADMATRLVAARLMVRNAAVALQE---ERKDava 349
Cdd:PLN02519 262 LDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNgkvDRKD--- 338
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 410210768 350 lCSMAKLFATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILEGSNEVMRILISRSLLQE 415
Cdd:PLN02519 339 -CAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
64-415 |
6.10e-53 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 181.08 E-value: 6.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 64 MAEWDQKELFPVDVMRKAAQLGFGGVYVQTDVGGSGLSRLDTSVIFEALATGCTstTAYISIHNMCAWMIDSFGNEEQRH 143
Cdd:PRK12341 29 FRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCGA--PAFLITNGQCIHSMRRFGSAEQLR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 144 KfcpplcTMEKFA-----SYCL--TEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDVYVVMCR-TGGPGP-KG 214
Cdd:PRK12341 107 K------TAESTLetgdpAYALalTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAKEYPYMLVLARdPQPKDPkKA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 215 ISCIVVEKGTPGLSFGKKEkKVGWNSQPTRAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGGRINIASCSLGAAHASVIL 294
Cdd:PRK12341 181 FTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFEMERLINAARSLGFAECAFED 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 295 TRDHLNVRKQFGEPLASNQYLQFKLADMATRLVAARLMVRNAavALQEERKDAVALCS-MAKLFATDECFAICNQALQMH 373
Cdd:PRK12341 260 AARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKV--AWQADNGQSLRTSAaLAKLYCARTAMEVIDDAIQIM 337
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 410210768 374 GGYGYLKDYAVQQYVRDSRVHQILEGSNEVMRILISRSLLQE 415
Cdd:PRK12341 338 GGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKD 379
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
263-412 |
3.53e-49 |
|
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: 163.58 E-value: 3.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 263 GQGFLIAVRGLNGGRINIASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFKLADMATRLVAARLMVRNAAVALQE 342
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 343 ERKDAVAlCSMAKLFATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILEGSNEVMRILISRSL 412
Cdd:pfam00441 81 GGPDGAE-ASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
54-401 |
2.08e-48 |
|
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173842 [Multi-domain] Cd Length: 407 Bit Score: 169.88 E-value: 2.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 54 DFAAREMAPNMAEWDQKEL--------FP---VDVMRKAAQLGFGGVYVQTDVGGSGLSRLDTSVIFEALATGCTsTTAY 122
Cdd:cd01153 7 RLAENVLAPLNADGDREGPvfddgrvvVPppfKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDA-PLMY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 123 ISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGD-HYILNGSKAFISgAGESD-- 199
Cdd:cd01153 86 ASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFIS-AGEHDms 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 200 ---VYVVMCRTGGPGP--KGISCIVVEK----GTP-GLSFGKKEKKVGWNSQPTRAVIFEDCAVPVanrIGSEGQGFLIA 269
Cdd:cd01153 165 eniVHLVLARSEGAPPgvKGLSLFLVPKflddGERnGVTVARIEEKMGLHGSPTCELVFDNAKGEL---IGEEGMGLAQM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 270 VRGLNGGRINIASCSLGAAHASVILTRDHLNVRKQFGEPLAS--------NQYLQFKLADMATRLVAARLMVRNAAVALQ 341
Cdd:cd01153 242 FAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAapavtiihHPDVRRSLMTQKAYAEGSRALDLYTATVQD 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 410210768 342 EERKDAV-------------ALCSMAKLFATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILEGSN 401
Cdd:cd01153 322 LAERKATegedrkalsaladLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTT 394
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
44-415 |
1.80e-46 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 164.73 E-value: 1.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 44 EQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVQTDVGGSGLSRLDTSVIFEALATG----CTst 119
Cdd:PTZ00461 40 EHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYdpgfCL-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 120 tAYISiHNMCawMIDSFGNE---EQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGD-HYILNGSKAFISGA 195
Cdd:PTZ00461 118 -AYLA-HSML--FVNNFYYSaspAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 196 GESDVYVVMCRTGGPgpkgISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGSEGQGFLIAVRGLNG 275
Cdd:PTZ00461 194 TVADVFLIYAKVDGK----ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLEL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 276 GRINIASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFKLADMATRLVAARLMVRNAAVALQEERKDAVAlCSMAK 355
Cdd:PTZ00461 270 ERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLG-SDAAK 348
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 356 LFATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILEGSNEVMRILISRSLLQE 415
Cdd:PTZ00461 349 LFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLKG 408
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
41-415 |
3.62e-42 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 152.29 E-value: 3.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 41 LNEEQKEFQKVAFDFAAREMAPN-MAEWDQKELFPVDVMRKAAQLGFGGVYVQTDVGGSGLSRLDTSVIFEALatGCTST 119
Cdd:PRK03354 5 LNDEQELFVAGIRELMASENWEAyFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMEL--GRLGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 120 TAYISIHNMCAW-MIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGES 198
Cdd:PRK03354 83 PTYVLYQLPGGFnTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 199 DVYVVMCRTGGPGPKGI-SCIVVEKGTPGLSFGKKEkKVGWNSQPTRAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGGR 277
Cdd:PRK03354 163 PYIVVMARDGASPDKPVyTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHER 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 278 INIASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFKLADMATRLVAARLMVRNAAVALQEERKDAvALCSMAKLF 357
Cdd:PRK03354 242 FLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITS-GDAAMCKYF 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 410210768 358 ATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILEGSNEVMRILISRSLLQE 415
Cdd:PRK03354 321 CANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQ 378
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
56-414 |
7.62e-42 |
|
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: 151.77 E-value: 7.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 56 AAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVQTDVGGSGLSRLDTSVIFEAL--------ATGCTSTtayiSIHN 127
Cdd:cd01155 25 FLEYYAEGGDRWWTPPPIIEKLKAKAKAEGLWNLFLPEVSGLSGLTNLEYAYLAEETgrsffapeVFNCQAP----DTGN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 128 McaWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPG-SGSDAASLLTSAKKQGDHYILNGSKAFISGAGESD--VYVVM 204
Cdd:cd01155 101 M--EVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRKWWSSGAGDPRckIAIVM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 205 CRTGGPGP---KGISCIVVEKGTPGLSFGKKEKKVGWNSQPT--RAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGGRIN 279
Cdd:cd01155 179 GRTDPDGAprhRQQSMILVPMDTPGVTIIRPLSVFGYDDAPHghAEITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIH 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 280 IASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFKLADMATRLVAARLMVRNAAVAL-QEERKDAVALCSMAKLFA 358
Cdd:cd01155 259 HCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIdTVGNKAARKEIAMIKVAA 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 410210768 359 TDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILEGSNEVMRILISRSLLQ 414
Cdd:cd01155 339 PRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMELK 394
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
79-414 |
8.17e-40 |
|
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: 145.95 E-value: 8.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 79 RKAAQLGFGGVYVQTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASY 158
Cdd:cd01152 42 RALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 159 CLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESDVYVVMCRTGGPGPK--GISCIVVEKGTPGLSFGKKEKKV 236
Cdd:cd01152 122 GFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDPEAPKhrGISILLVDMDSPGVTVRPIRSIN 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 237 GwnSQPTRAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGGRINI---ASCSLGAAHASVILTRDHlnvrkqfGEPLASNQ 313
Cdd:cd01152 202 G--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIggsAATFFELLLARLLLLTRD-------GRPLIDDP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 314 YLQFKLADMATRLVAARLMVRNAAVALQEErKDAVALCSMAKLFATDECFAICNQALQMHGGYGYLKDYA--------VQ 385
Cdd:cd01152 273 LVRQRLARLEAEAEALRLLVFRLASALAAG-KPPGAEASIAKLFGSELAQELAELALELLGTAALLRDPApgaelagrWE 351
|
330 340
....*....|....*....|....*....
gi 410210768 386 QYVRDSRVHQILEGSNEVMRILISRSLLQ 414
Cdd:cd01152 352 ADYLRSRATTIYGGTSEIQRNIIAERLLG 380
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
42-153 |
3.03e-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: 3.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 42 NEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVQTDVGGSGLSRLDTSVIFEALATGCTSTTA 121
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|...
gi 410210768 122 YISIHN-MCAWMIDSFGNEEQRHKFCPPLCTME 153
Cdd:pfam02771 81 ALSVHSsLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
41-412 |
1.89e-37 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 140.37 E-value: 1.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 41 LNEEQKEFQKVAFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVQtDVGGSGLSRLDTSVIFEALATGCTSTT 120
Cdd:PLN02526 29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIK-GYGCPGLSITASAIATAEVARVDASCS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 121 AYISIHN-MCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKKQGDHYILNGSKAFISGAGESD 199
Cdd:PLN02526 108 TFILVHSsLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFAD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 200 VYVVMCRTggPGPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVANRIGSEgQGFLIAVRGLNGGRIN 279
Cdd:PLN02526 188 VLVIFARN--TTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGV-NSFQDTNKVLAVSRVM 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 280 IASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFKLADM-----ATRLVAARLmvrnaaVALQEERKDAVALCSMA 354
Cdd:PLN02526 265 VAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMlgniqAMFLVGWRL------CKLYESGKMTPGHASLG 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 410210768 355 KLFATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILEGSNEVMRILISRSL 412
Cdd:PLN02526 339 KAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREI 396
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
123-404 |
8.86e-35 |
|
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: 133.27 E-value: 8.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 123 ISIHNMCAWMIDSFGNEEQRHkFCPPLCTMEK----FASYCLTEPGSGSDAASLLTSAKKQ-GDHYILNGSKAFISGAgE 197
Cdd:cd01154 113 LTMTDAAVYALRKYGPEELKQ-YLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERSgGGVYRLNGHKWFASAP-L 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 198 SDVYVVMCRTGG--PGPKGISCIVV----EKGT-PGLSFGKKEKKVGWNSQPTRAVIFEDCavpVANRIGSEGQGFLIAV 270
Cdd:cd01154 191 ADAALVLARPEGapAGARGLSLFLVprllEDGTrNGYRIRRLKDKLGTRSVATGEVEFDDA---EAYLIGDEGKGIYYIL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 271 RGLNGGRINIASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFKLADMATRLVAARLMVRNAAVALQEERKDAVAL 350
Cdd:cd01154 268 EMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKPVE 347
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 410210768 351 CSMAKLFATDECFAICNQALQM-------HGGYGYLKDYAVQQYVRDSRVHQILEGSNEVM 404
Cdd:cd01154 348 AHMARLATPVAKLIACKRAAPVtseamevFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQ 408
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
157-249 |
1.39e-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: 110.06 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 157 SYCLTEPGSGSDAASLLTSA-KKQGDHYILNGSKAFISGAGESDVYVVMCRTGGPGPK-GISCIVVEKGTPGLSFGKKEK 234
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHgGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 410210768 235 KVGWNSQPTRAVIFE 249
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
136-414 |
2.41e-26 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 111.81 E-value: 2.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 136 FGNEEQRHKFCPPLCTMEKFASYCLTEPG-SGSDAASLLTSAKKQGDHYILNGSKAFISGAGES--DVYVVMCRT--GGP 210
Cdd:PLN02876 532 YGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPrcRVLIVMGKTdfNAP 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 211 GPKGISCIVVEKGTPGLSFGKKEKKVGWNSQPT--RAVIFEDCAVPVANRIGSEGQGFLIAVRGLNGGRINIASCSLGAA 288
Cdd:PLN02876 612 KHKQQSMILVDIQTPGVQIKRPLLVFGFDDAPHghAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAA 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 289 HASVILTRDHLNVRKQFGEPLASNQYLQFKLADMATRLVAARLMVRNAAVALQEE-RKDAVALCSMAKLFATDECFAICN 367
Cdd:PLN02876 692 ERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDRLgNKKARGIIAMAKVAAPNMALKVLD 771
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 410210768 368 QALQMHGGYGYLKDYAVQQYVRDSRVHQILEGSNEVMRILISRSLLQ 414
Cdd:PLN02876 772 MAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAKLELQ 818
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
280-402 |
1.22e-21 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 90.10 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 280 IASCSLGAAHASVILTRDHLNVRKQ--FGEPLASNQYLQFKLADMATRLVAARLMVRNAAVALQEERKDA-------VAL 350
Cdd:pfam08028 2 IAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAAAGkpvtpalRAE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 410210768 351 CSMAKLFATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILEGSNE 402
Cdd:pfam08028 82 ARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
85-413 |
1.24e-21 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 97.25 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 85 GFGGVYVQTDVGGSGLSRLDTSVIFEALATGCTSTTAY--ISIHNMCAWMidSFGNEEQRHKFCPPLCTMEKFASYCLTE 162
Cdd:PTZ00456 112 GWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYpgLSIGAANTLM--AWGSEEQKEQYLTKLVSGEWSGTMCLTE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 163 PGSGSDAASLLTSAKKQGD-HYILNGSKAFISgAGESD-----VYVVMCRTGG--PGPKGISCIVVEKGTP--------- 225
Cdd:PTZ00456 190 PQCGTDLGQVKTKAEPSADgSYKITGTKIFIS-AGDHDlteniVHIVLARLPNslPTTKGLSLFLVPRHVVkpdgsleta 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 226 -GLSFGKKEKKVGWNSQPTRAVIFEDcavPVANRIGSEGQGFLIAVRGLNGGRIniaSCSL-GAAHASVIL------TRD 297
Cdd:PTZ00456 269 kNVKCIGLEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTARV---GTALeGVCHAELAFqnalryARE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 298 HLNVRKQFG--EPLASNQYLQFKlADMATRLVAARLMVRNAAVALQE---------ERKDAVA----------LCSMAKL 356
Cdd:PTZ00456 343 RRSMRALSGtkEPEKPADRIICH-ANVRQNILFAKAVAEGGRALLLDvgrlldihaAAKDAATrealdheigfYTPIAKG 421
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 410210768 357 FATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILEGSNEVMRI-LISRSLL 413
Cdd:PTZ00456 422 CLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALdFIGRKVL 479
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
76-377 |
3.86e-13 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 71.14 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 76 DVMRKAaqlGFGGVYVQTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHNMC--AWMIDSFGNEEQRHKFCPPLCTME 153
Cdd:PRK13026 115 DYLKKE---GFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPNSLgpGELLTHYGTQEQKDYWLPRLADGT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 154 KFASYCLTEPGSGSDAASL-----LTSAKKQGDHYI---LNGSKAFISGAGESDVYVVMCRT-------GGPGPKGISCI 218
Cdd:PRK13026 192 EIPCFALTGPEAGSDAGAIpdtgiVCRGEFEGEEVLglrLTWDKRYITLAPVATVLGLAFKLrdpdgllGDKKELGITCA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 219 VVEKGTPGLSFGKKEKKVGWNSQ--PTRAvifEDCAVPVANRIGSE---GQGFLIAVRGLNGGR-INIASCSLGAAHASV 292
Cdd:PRK13026 272 LIPTDHPGVEIGRRHNPLGMAFMngTTRG---KDVFIPLDWIIGGPdyaGRGWRMLVECLSAGRgISLPALGTASGHMAT 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 293 ILTRDHLNVRKQFGEPLASNQYLQFKLADMAT---RLVAARLMVrnaAVALQEERKDAVAlCSMAKLFATDECFAICNQA 369
Cdd:PRK13026 349 RTTGAYAYVRRQFGMPIGQFEGVQEALARIAGntyLLEAARRLT---TTGLDLGVKPSVV-TAIAKYHMTELARDVVNDA 424
|
....*...
gi 410210768 370 LQMHGGYG 377
Cdd:PRK13026 425 MDIHAGKG 432
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
160-412 |
3.09e-12 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 68.24 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 160 LTEPGSGSDAASLLTSAKK-QGDHYILNGSKAFISgAGESDVYVVMCRTGGpgpkGISCIVVEKGTP-----GLSFGKKE 233
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAERlADGSYRLVGHKWFFS-VPQSDAHLVLAQAKG----GLSCFFVPRFLPdgqrnAIRLERLK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 234 KKVGWNSQPTRAVIFEDCavpVANRIGSEGQGfliaVRG-LNGGRINIASCSLGAaHA------SVILTrdHLNVRKQFG 306
Cdd:PRK11561 259 DKLGNRSNASSEVEFQDA---IGWLLGEEGEG----IRLiLKMGGMTRFDCALGS-HGlmrrafSVAIY--HAHQRQVFG 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 307 EPLASNQYLQFKLADMATRLVAARLMVRNAAVALqeERKDAVALCSMAKLFATDECFAICNQ-------ALQMHGGYGYL 379
Cdd:PRK11561 329 KPLIEQPLMRQVLSRMALQLEGQTALLFRLARAW--DRRADAKEALWARLFTPAAKFVICKRgipfvaeAMEVLGGIGYC 406
|
250 260 270
....*....|....*....|....*....|...
gi 410210768 380 KDYAVQQYVRDSRVHQILEGSNEVMRILISRSL 412
Cdd:PRK11561 407 EESELPRLYREMPVNSIWEGSGNIMCLDVLRVL 439
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
56-393 |
2.36e-11 |
|
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: 64.68 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 56 AAREMAP----NMAEWDQKELFPVDVMRKAAQLGFGGVYVQTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHNMCAW 131
Cdd:cd01159 2 RAEDLAPlireRAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIVATHSR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 132 MIDSFGNEEQRHKFcpplctmekfasycltepgsGSDAASLLTS-------AKKQGDHYILNGSKAFISGAGESDVYVVM 204
Cdd:cd01159 82 MLAAFPPEAQEEVW--------------------GDGPDTLLAGsyapggrAERVDGGYRVSGTWPFASGCDHADWILVG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 205 CRTGGPGPKGISCIVVekgtpglsFGKKEKK-------VGWNSQPTRAVIFEDCAVP--------VANRIGSEGQGFLI- 268
Cdd:cd01159 142 AIVEDDDGGPLPRAFV--------VPRAEYEivdtwhvVGLRGTGSNTVVVDDVFVPehrtltagDMMAGDGPGGSTPVy 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 269 --AVRGLNGgrINIASCSLGAAHASVILTRDHLNVRKQ---FGEPLASNQYLQFKLADMATRLVAARLMV-RNAAV--AL 340
Cdd:cd01159 214 rmPLRQVFP--LSFAAVSLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAELDAARAFLeRATRDlwAH 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 410210768 341 QEERK----DAVALCSMAKLFATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRV 393
Cdd:cd01159 292 ALAGGpidvEERARIRRDAAYAAKLSAEAVDRLFHAAGGSALYTASPLQRIWRDIHA 348
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
76-413 |
3.33e-11 |
|
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: 65.04 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 76 DVMRKAAQLGF-GGVYVQTDVggsglsrLDTSVIFEALATGCTSTTAYISIH-NMCAWMIDSFGNEEQRHKFCPPLCTME 153
Cdd:cd01150 61 ELKRKAKTDVErMGELMADDP-------EKMLALTNSLGGYDLSLGAKLGLHlGLFGNAIKNLGTDEHQDYWLQGANNLE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 154 KFASYCLTEPGSGSDAASLLTSAK--KQGDHYILN-----GSKAFISGAGES-DVYVVMCRTGGPGPK-GISCIVV---E 221
Cdd:cd01150 134 IIGCFAQTELGHGSNLQGLETTATydPLTQEFVINtpdftATKWWPGNLGKTaTHAVVFAQLITPGKNhGLHAFIVpirD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 222 KGT----PGLSFGKKEKKVGWNSQPTRAVIFEDCAVP---VANRIG-------------SEGQGFLIAVRGLNGGRINIA 281
Cdd:cd01150 214 PKThqplPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPrenLLNRFGdvspdgtyvspfkDPNKRYGAMLGTRSGGRVGLI 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 282 SCSLGA-AHASVILTRDHLnVRKQFGEPLASN-------QYLQFKL-----ADMATRLVAARLM------VRNAAVALQE 342
Cdd:cd01150 294 YDAAMSlKKAATIAIRYSA-VRRQFGPKPSDPevqildyQLQQYRLfpqlaAAYAFHFAAKSLVemyheiIKELLQGNSE 372
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 410210768 343 ERKDAVALCSMAKLFATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVHQILEGSNEVMRILISRSLL 413
Cdd:cd01150 373 LLAELHALSAGLKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLL 443
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
52-394 |
1.81e-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: 61.96 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 52 AFDFAAREMAPNMAEWDQKELFPVDVMRKAAQLGFGGVYVQTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIHNMCAW 131
Cdd:cd01163 2 RARPLAARIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGFVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 132 MIDSFGNEEQRhKFCPPLCTMEKFASYCLTEPGSgSDAASLLTSAKKQGDHYILNGSKAFISGAGESDvYVVMCRTGGPG 211
Cdd:cd01163 82 ALLLAGPEQFR-KRWFGRVLNGWIFGNAVSERGS-VRPGTFLTATVRDGGGYVLNGKKFYSTGALFSD-WVTVSALDEEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 212 PKGIscIVVEKGTPGLS-------FGKKEKKVGwNSQPTRAVIFEDCAVPVANRigSEGQGFLIAVRGLnggriNIASCS 284
Cdd:cd01163 159 KLVF--AAVPTDRPGITvvddwdgFGQRLTASG-TVTFDNVRVEPDEVLPRPNA--PDRGTLLTAIYQL-----VLAAVL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 285 LGAAHASVILTRDHlnVRKQ---FGEPLASNQ----YLQFKLADMATRLVAARLMVRNAAVALQ-----------EERKD 346
Cdd:cd01163 229 AGIARAALDDAVAY--VRSRtrpWIHSGAESArddpYVQQVVGDLAARLHAAEALVLQAARALDaaaaagtaltaEARGE 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 410210768 347 AVALCSMAKLFATDECFAICNQALQMHGGYGYLKDYAVQQYVRDSRVH 394
Cdd:cd01163 307 AALAVAAAKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNARTH 354
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
136-377 |
9.53e-10 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 60.60 E-value: 9.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 136 FGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASL-----LTSAKKQGDHYI---LNGSKAFISGA------------ 195
Cdd:PRK09463 175 YGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIpdtgvVCKGEWQGEEVLgmrLTWNKRYITLApiatvlglafkl 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 196 --------GESDVyvvmcrtggpgpkGISCIVVEKGTPGLSFGKKEKKVGWNSQ--PTRAvifEDCAVPVANRIGSE--- 262
Cdd:PRK09463 255 ydpdgllgDKEDL-------------GITCALIPTDTPGVEIGRRHFPLNVPFQngPTRG---KDVFIPLDYIIGGPkma 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 263 GQGFLIAVRGLNGGR-INIASCSLGAAHASVILTRDHLNVRKQFGEPLASNQYLQFKLADMA--TRLV-AARLMVrNAAV 338
Cdd:PRK09463 319 GQGWRMLMECLSVGRgISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAgnAYLMdAARTLT-TAAV 397
|
250 260 270
....*....|....*....|....*....|....*....
gi 410210768 339 ALQEerKDAVaLCSMAKLFATDECFAICNQALQMHGGYG 377
Cdd:PRK09463 398 DLGE--KPSV-LSAIAKYHLTERGRQVINDAMDIHGGKG 433
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
116-185 |
3.91e-04 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 42.52 E-value: 3.91e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 410210768 116 CTSTTAYISIH-NMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSA--KKQGDHYIL 185
Cdd:PTZ00460 88 CPQGTFISTVHfAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTAtyDKQTNEFVI 160
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
121-414 |
5.15e-04 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 42.13 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 121 AYISIH-NMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAK--KQGDHYILN-----GSKAFI 192
Cdd:PLN02443 97 GYTDLHwGMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATfdPKTDEFVIHsptltSSKWWP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 193 SGAGESDVY-VVMCRTGGPGPK-GISCIVVE-------KGTPGLSFGKKEKKVG---WNSQPTRAVIFEDCAVPVAN--- 257
Cdd:PLN02443 177 GGLGKVSTHaVVYARLITNGKDhGIHGFIVQlrslddhSPLPGVTVGDIGMKFGngaYNTMDNGFLRFDHVRIPRDQmlm 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 258 ---RIGSEGQ------------GFLIAVRglnggRINIASCSLGAAHASVILTRdHLNVRKQFGE--------------- 307
Cdd:PLN02443 257 rlsKVTREGKyvqsdvprqlvyGTMVYVR-----QTIVADASTALSRAVCIATR-YSAVRRQFGSqdggpetqvidyktq 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 308 -----PLASNQY--------LQFKLADMATRLVAarlmvrNAAVALQEERKDAVALCSMAKLFATD---ECFAICnqalq 371
Cdd:PLN02443 331 qsrlfPLLASAYafrfvgewLKWLYTDVTQRLEA------NDFSTLPEAHACTAGLKSLTTSATADgieECRKLC----- 399
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 410210768 372 mhGGYGYL------KDYAVqqYVRDSrvhqILEGSNEVMRILISRSLLQ 414
Cdd:PLN02443 400 --GGHGYLcssglpELFAV--YVPAC----TYEGDNVVLLLQVARFLMK 440
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
88-266 |
1.54e-03 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 40.63 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 88 GVYVQTDVGGSGLSRLDTSVIFEALATGCTSTTAYISIH-NMCAWMIDSFGNEEQRHKFcppLCTME--KFASYCLTEPG 164
Cdd:PTZ00457 67 GARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHsGFCTYLLSTVGSKELKGKY---LTAMSdgTIMMGWATEEG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410210768 165 SGSDAASLLTSAKKQGD-HYILNGSKAFISGAGESDvYVVMCRT-----GGPGPKGI---SCIVVEKGTPGLSfgkkekk 235
Cdd:PTZ00457 144 CGSDISMNTTKASLTDDgSYVLTGQKRCEFAASATH-FLVLAKTltqtaAEEGATEVsrnSFFICAKDAKGVS------- 215
|
170 180 190
....*....|....*....|....*....|.
gi 410210768 236 VGWNSqptraVIFEDcaVPVANRIGSEGQGF 266
Cdd:PTZ00457 216 VNGDS-----VVFEN--TPAADVVGVVGEGF 239
|
|
| |
