|
Name |
Accession |
Description |
Interval |
E-value |
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
43-417 |
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: 778.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 43 LTDEQKEFQKVAFDFAANEMAPHMAEWDQKEIFPVEAMRKAAELGFGGIYVNPDVGGSGLSRLDTSIIFEALSTGCVSTT 122
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 123 AYVSIHNMCAWMIDTFGNNEQRERFCPDLCSMQKFASYCLTEPGSGSDAASLLTSATLKGDHYILNGSKAFISGGGDTDV 202
Cdd:cd01162 81 AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 203 YVVMCRTGGKGPKGISCLVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVTNRLGTEGQGFSIAMKGLNGGRINI 282
Cdd:cd01162 161 YVVMARTGGEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 283 ASCSLGAAHASVLLARDHMCVRKQFGETLANSQFLQFKLAEMATKLVASRLLVRQAALALQDGRPDAVSLCSMAKLFVTD 362
Cdd:cd01162 241 ASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATD 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 41055941 363 ECFSICNQALQIHGGYGYLKDYAVQQYVRDIRVHQILEGTNEVMRMIIARSLLTE 417
Cdd:cd01162 321 ECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
43-415 |
2.98e-159 |
|
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: 453.53 E-value: 2.98e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 43 LTDEQKEFQKVAFDFAANEMAPHMAEWDQKEIFPVEAMRKAAELGFGGIYVNPDVGGSGLSRLDTSIIFEALSTGCVSTT 122
Cdd:COG1960 5 LTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 123 AYVSIHNMCAWMIDTFGNNEQRERFCPDLCSMQKFASYCLTEPGSGSDAASLLTSATLKGDHYILNGSKAFISGGGDTDV 202
Cdd:COG1960 85 LPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVADV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 203 YVVMCRTGG-KGPKGISCLVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVTNRLGTEGQGFSIAMKGLNGGRIN 281
Cdd:COG1960 165 ILVLARTDPaAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGRLG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 282 IASCSLGAAHASVLLARDHMCVRKQFGETLANSQFLQFKLAEMATKLVASRLLVRQAALALQDGRPDAVsLCSMAKLFVT 361
Cdd:COG1960 245 LAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAAL-EAAMAKLFAT 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 41055941 362 DECFSICNQALQIHGGYGYLKDYAVQQYVRDIRVHQILEGTNEVMRMIIARSLL 415
Cdd:COG1960 324 EAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLL 377
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
45-415 |
1.66e-145 |
|
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: 418.60 E-value: 1.66e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 45 DEQKEFQKVAFDFAANEMAPHMAEWDQKEIFPVEAMRKAAELGFGGIYVNPDVGGSGLSRLDTSIIFEALSTGCVSTTAY 124
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 125 VSIHN-MCAWMIDTFGNNEQRERFCPDLCSMQKFASYCLTEPGSGSDAASLLTSATLKGDHYILNGSKAFISGGGDTDVY 203
Cdd:cd01158 81 VSVHNsLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 204 VVMCRTG-GKGPKGISCLVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVTNRLGTEGQGFSIAMKGLNGGRINI 282
Cdd:cd01158 161 IVFAVTDpSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 283 ASCSLGAAHASVLLARDHMCVRKQFGETLANSQFLQFKLAEMATKLVASRLLVRQAALALQDGRP---DAvslcSMAKLF 359
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPfikEA----AMAKLF 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 41055941 360 VTDECFSICNQALQIHGGYGYLKDYAVQQYVRDIRVHQILEGTNEVMRMIIARSLL 415
Cdd:cd01158 317 ASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLL 372
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
45-412 |
2.31e-131 |
|
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. In contrast, AXO catalyzes a different oxidative half-reaction, in which the reduced FAD is reoxidized by molecular oxygen. The ACAD family includes the eukaryotic beta-oxidation enzymes, short (SCAD), medium (MCAD), long (LCAD) and very-long (VLCAD) chain acyl-CoA dehydrogenases. These enzymes all share high sequence similarity, but differ in their substrate specificities. The ACAD family also includes amino acid catabolism enzymes such as Isovaleryl-CoA dehydrogenase (IVD), short/branched chain acyl-CoA dehydrogenases(SBCAD), Isobutyryl-CoA dehydrogenase (IBDH), glutaryl-CoA deydrogenase (GCD) and Crotonobetainyl-CoA dehydrogenase. The mitochondrial ACAD's are generally homotetramers, except for VLCAD, which is a homodimer. Related enzymes include the SOS adaptive reponse proten aidB, Naphthocyclinone hydroxylase (NcnH), and and Dibenzothiophene (DBT) desulfurization enzyme C (DszC)
Pssm-ID: 173838 [Multi-domain] Cd Length: 327 Bit Score: 380.86 E-value: 2.31e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 45 DEQKEFQKVAFDFAANEMAPHMAEWDQKEIFPVEAMRKAAELgfggiyvnpdvggsglsrldtsiifealstgcvsttay 124
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLL-------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 125 vsihnMCAWMIDTFGNNEQRERFCPDLCSMQKFASYCLTEPGSGSDAASLLTSATLKGDHYILNGSKAFISGGGDTDVYV 204
Cdd:cd00567 43 -----LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 205 VMCRTGGKGP--KGISCLVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVTNRLGTEGQGFSIAMKGLNGGRINI 282
Cdd:cd00567 118 VLARTDEEGPghRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 283 ASCSLGAAHASVLLARDHMCVRKQFGETLANSQFLQFKLAEMATKLVASRLLVRQAALALQDGRPDAVSLCSMAKLFVTD 362
Cdd:cd00567 198 AAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFATE 277
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 41055941 363 ECFSICNQALQIHGGYGYLKDYAVQQYVRDIRVHQILEGTNEVMRMIIAR 412
Cdd:cd00567 278 AAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
42-414 |
4.16e-106 |
|
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: 318.20 E-value: 4.16e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 42 GLTDEQKEFQKVAFDFAANEMAPHMAEWDQKEIFPVEAMRKAAELGFGGIYVNPDVGGSGLSRLDTSIIFEALSTGCVST 121
Cdd:cd01156 1 GLDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 122 TAYVSIH-NMCAWMIDTFGNNEQRERFCPDLCSMQKFASYCLTEPGSGSDAASLLTSATLKGDHYILNGSKAFISGGGDT 200
Cdd:cd01156 81 ALSYGAHsNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 201 DVYVVMCRTGGK-GPKGISCLVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVTNRLGTEGQGFSIAMKGLNGGR 279
Cdd:cd01156 161 DTLVVYAKTDPSaGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 280 INIASCSLGAAHASVLLARDHMCVRKQFGETLANSQFLQFKLAEMATKLVASRLLVRQAALALQDGRPDAVSlCSMAKLF 359
Cdd:cd01156 241 LVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKD-AAGVILY 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 41055941 360 VTDECFSICNQALQIHGGYGYLKDYAVQQYVRDIRVHQILEGTNEVMRMIIARSL 414
Cdd:cd01156 320 AAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGREL 374
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
46-415 |
1.43e-104 |
|
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: 314.05 E-value: 1.43e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 46 EQKEFQKVAFDFAANEMAPHMAEWDQKEIFPVEAMRKAAELGFGGIYVNPDVGGSGLSRLDTSIIFEALS-TGCVSTTay 124
Cdd:cd01160 2 EHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELArAGGSGPG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 125 VSIHN-MCAWMIDTFGNNEQRERFCPDLCSMQKFASYCLTEPGSGSDAASLLTSATLKGDHYILNGSKAFISGGGDTDVY 203
Cdd:cd01160 80 LSLHTdIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 204 VVMCRTGG--KGPKGISCLVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVTNRLGTEGQGFSIAMKGLNGGRIN 281
Cdd:cd01160 160 IVVARTGGeaRGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 282 IASCSLGAAHASVLLARDHMCVRKQFGETLANSQFLQFKLAEMATKLVASRLLVRQAALALQDGRPDAVSLCsMAKLFVT 361
Cdd:cd01160 240 IAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEAS-MAKYWAT 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 41055941 362 DECFSICNQALQIHGGYGYLKDYAVQQYVRDIRVHQILEGTNEVMRMIIARSLL 415
Cdd:cd01160 319 ELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
42-415 |
1.23e-94 |
|
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: 290.14 E-value: 1.23e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 42 GLTDEQKEFQKVAFD----FAANEMAPhmAEWDQKEIFPVEAMRKAAELGFGGIYVNPDVGGSGLSRLDTSIIFE----A 113
Cdd:cd01161 22 VLTEEQTEELNMLVGpvekFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEivgmD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 114 LSTGcVSTTAYVSIHNMCawmIDTFGNNEQRERFCPDLCSMQKFASYCLTEPGSGSDAASLLTSATLK--GDHYILNGSK 191
Cdd:cd01161 100 LGFS-VTLGAHQSIGFKG---ILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSedGKHYVLNGSK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 192 AFISGGGDTDVYVVMCRTGGKGPKG-----ISCLVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVTNRLGTEGQ 266
Cdd:cd01161 176 IWITNGGIADIFTVFAKTEVKDATGsvkdkITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 267 GFSIAMKGLNGGRINIASCSLGAAHASVLLARDHMCVRKQFGETLANSQFLQFKLAEMATKLVASRLLV-RQAALALQDG 345
Cdd:cd01161 256 GFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAyMTSGNMDRGL 335
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 346 RPDAVSLCSMAKLFVTDECFSICNQALQIHGGYGYLKDYAVQQYVRDIRVHQILEGTNEVMRMIIARSLL 415
Cdd:cd01161 336 KAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGL 405
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
43-415 |
8.16e-89 |
|
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: 274.08 E-value: 8.16e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 43 LTDEQKEFQKVAFDFAANEMAPHMAEWDQKEIFPVEAMRKAAELGFGGIYVNPDVGGSGLSRLDTSIIFEALSTGCVSTT 122
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 123 AYVSIHNMCAWMIDTFGNNEQRERFCPDLCSMQKFASYCLTEPGSGSDAASLLTSATLKGDHYILNGSKAFISGGGDTDV 202
Cdd:cd01157 81 TAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 203 YVVMCRTGG--KGP--KGISCLVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVTNRLGTEGQGFSIAMKGLNGG 278
Cdd:cd01157 161 YFLLARSDPdpKCPasKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 279 RINIASCSLGAAHASVLLARDHMCVRKQFGETLANSQFLQFKLAEMATKLVASRLLVRQAALALQDGRPDAVSlCSMAKL 358
Cdd:cd01157 241 RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYY-ASIAKA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 41055941 359 FVTDECFSICNQALQIHGGYGYLKDYAVQQYVRDIRVHQILEGTNEVMRMIIARSLL 415
Cdd:cd01157 320 FAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
39-418 |
2.99e-65 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 213.97 E-value: 2.99e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 39 PSIGLTDEQKEFQKVAFDFAANEMAPHMAEWDQKEIFP--VEAMRKAAELGFGGIYVNPDVGGSGLSRLDTSIIFEALS- 115
Cdd:PLN02519 22 SSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPkdVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 116 -TGCVSTTaYVSIHNMCAWMIDTFGNNEQRERFCPDLCSMQKFASYCLTEPGSGSDAASLLTSATLKGDHYILNGSKAFI 194
Cdd:PLN02519 102 aSGSVGLS-YGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWC 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 195 SGGGDTDVYVVMCRTGGK-GPKGISCLVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVTNRLGTEGQGFSIAMK 273
Cdd:PLN02519 181 TNGPVAQTLVVYAKTDVAaGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 274 GLNGGRINIASCSLGAAHASVLLARDHMCVRKQFGETLANSQFLQFKLAEMATKLVASRLLVRQAALALQDGRPDAVSlC 353
Cdd:PLN02519 261 GLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKD-C 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41055941 354 SMAKLFVTDECFSICNQALQIHGGYGYLKDYAVQQYVRDIRVHQILEGTNEVMRMIIARSLLTES 418
Cdd:PLN02519 340 AGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKEE 404
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
43-412 |
4.01e-64 |
|
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: 210.68 E-value: 4.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 43 LTDEQKEFQKVAFDFAANEMAPHMAEWDQKEIFPVEAMRKAAELGFGGIYVNpDVGGSGLSRLDTSII---FEALSTGCV 119
Cdd:cd01151 13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIK-GYGCAGLSSVAYGLIareVERVDSGYR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 120 STtayVSIH-NMCAWMIDTFGNNEQRERFCPDLCSMQKFASYCLTEPGSGSDAASLLTSATLKGDHYILNGSKAFISGGG 198
Cdd:cd01151 92 SF---MSVQsSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 199 DTDVYVVMCRTGGKGpkGISCLVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVTNRLgTEGQGFSIAMKGLNGG 278
Cdd:cd01151 169 IADVFVVWARNDETG--KIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL-PGAEGLRGPFKCLNNA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 279 RINIASCSLGAAHASVLLARDHMCVRKQFGETLANSQFLQFKLAEMATKLVASRLLVRQAALALQDGR--PDAVslcSMA 356
Cdd:cd01151 246 RYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKatPEQI---SLL 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 41055941 357 KLFVTDECFSICNQALQIHGGYGYLKDYAVQQYVRDIRVHQILEGTNEVMRMIIAR 412
Cdd:cd01151 323 KRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGR 378
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
43-415 |
3.14e-58 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 194.95 E-value: 3.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 43 LTDEQKEFQKVAFDFAANEmAPH--MAEWDQKEIFPVEAMRKAAELGFGGIYVNPDVGGSGLSRLDTSIIFEALSTGCVs 120
Cdd:PRK12341 5 LTEEQELLLASIRELITRN-FPEeyFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCGA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 121 tTAYVSIHNMCAWMIDTFGNNEQReRFCPDLCSMQKFASYCL--TEPGSGSDAASLLTSATLKGDHYILNGSKAFISGGG 198
Cdd:PRK12341 83 -PAFLITNGQCIHSMRRFGSAEQL-RKTAESTLETGDPAYALalTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 199 DTDVYVVMCR-TGGKGP-KGISCLVVEKGTPGLSFGKKEKkVGWNSQPTRAVIFEDCAVPVTNRLGTEGQGFSIAMKGLN 276
Cdd:PRK12341 161 EYPYMLVLARdPQPKDPkKAFTLWWVDSSKPGIKINPLHK-IGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 277 GGRINIASCSLGAAHASVLLARDHMCVRKQFGETLANSQFLQFKLAEMATKLVASRLLVRQAALALQDGRPDAVSlCSMA 356
Cdd:PRK12341 240 MERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTS-AALA 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 41055941 357 KLFVTDECFSICNQALQIHGGYGYLKDYAVQQYVRDIRVHQILEGTNEVMRMIIARSLL 415
Cdd:PRK12341 319 KLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQIL 377
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
56-403 |
1.89e-51 |
|
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: 177.97 E-value: 1.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 56 DFAANEMAPHMAEWDQKE--------IFP---VEAMRKAAELGFGGIYVNPDVGGSGLSRLDTSIIFEALSTGCVSTT-A 123
Cdd:cd01153 7 RLAENVLAPLNADGDREGpvfddgrvVVPppfKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMyA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 124 YVSIHNMCAwmIDTFGNNEQRERFCPDLCSMQKFASYCLTEPGSGSDAASLLTSATLKGD-HYILNGSKAFISGG----G 198
Cdd:cd01153 87 SGTQGAAAT--LLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGehdmS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 199 DTDVYVVMCRTGGKGP--KGISCLVVEK----GTP-GLSFGKKEKKVGWNSQPTRAVIFEDCAVPVtnrLGTEGQGFSIA 271
Cdd:cd01153 165 ENIVHLVLARSEGAPPgvKGLSLFLVPKflddGERnGVTVARIEEKMGLHGSPTCELVFDNAKGEL---IGEEGMGLAQM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 272 MKGLNGGRINIASCSLGAAHASVLLARDHMCVRKQFGETL--------ANSQFLQFKLAEMATKLVASRLLVRQAALALQ 343
Cdd:cd01153 242 FAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIkaapavtiIHHPDVRRSLMTQKAYAEGSRALDLYTATVQD 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41055941 344 DGRPDAVS-------------LCSMAKLFVTDECFSICNQALQIHGGYGYLKDYAVQQYVRDIRVHQILEGTN 403
Cdd:cd01153 322 LAERKATEgedrkalsaladlLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTT 394
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
265-414 |
9.98e-51 |
|
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.
Pssm-ID: 395354 [Multi-domain] Cd Length: 149 Bit Score: 167.82 E-value: 9.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 265 GQGFSIAMKGLNGGRINIASCSLGAAHASVLLARDHMCVRKQFGETLANSQFLQFKLAEMATKLVASRLLVRQAALALQD 344
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 345 GRPDAVsLCSMAKLFVTDECFSICNQALQIHGGYGYLKDYAVQQYVRDIRVHQILEGTNEVMRMIIARSL 414
Cdd:pfam00441 81 GGPDGA-EASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
44-417 |
4.37e-49 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 171.66 E-value: 4.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 44 TDEQKEFQKVAFDFAANEMAPHMAEWDQKEIFPVEAMRKAAELGFGGIYVNPDVGGSGLSRLDTSIIFEALSTG----CV 119
Cdd:PTZ00461 38 TPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYdpgfCL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 120 sttAYVSiHNMCawMIDTFGNN---EQRERFCPDLCSMQKFASYCLTEPGSGSDAASLLTSATLKGD-HYILNGSKAFIS 195
Cdd:PTZ00461 118 ---AYLA-HSML--FVNNFYYSaspAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWIT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 196 GGGDTDVYVVMCRTGGKgpkgISCLVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVTNRLGTEGQGFSIAMKGL 275
Cdd:PTZ00461 192 NGTVADVFLIYAKVDGK----ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 276 NGGRINIASCSLGAAHASVLLARDHMCVRKQFGETLANSQFLQFKLAEMATKLVASRLLVRQAALALQDGRPDAVSlCSM 355
Cdd:PTZ00461 268 ELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLG-SDA 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41055941 356 AKLFVTDECFSICNQALQIHGGYGYLKDYAVQQYVRDIRVHQILEGTNEVMRMIIARSLLTE 417
Cdd:PTZ00461 347 AKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLKG 408
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
43-415 |
2.08e-45 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 161.15 E-value: 2.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 43 LTDEQKEFQKVAFDFAANE-MAPHMAEWDQKEIFPVEAMRKAAELGFGGIYVNPDVGGSGLSRLDTSIIFEALstGCVST 121
Cdd:PRK03354 5 LNDEQELFVAGIRELMASEnWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMEL--GRLGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 122 TAYVSIHNMCAWmiDTF---GNNEQRERFCPDLCSMQKFASYCLTEPGSGSDAASLLTSATLKGDHYILNGSKAFISGGG 198
Cdd:PRK03354 83 PTYVLYQLPGGF--NTFlreGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 199 DTDVYVVMCRTGGKGPKGI-SCLVVEKGTPGLSFGKKEkKVGWNSQPTRAVIFEDCAVPVTNRLGTEGQGFSIAMKGLNG 277
Cdd:PRK03354 161 YTPYIVVMARDGASPDKPVyTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 278 GRINIASCSLGAAHASVLLARDHMCVRKQFGETLANSQFLQFKLAEMATKLVASRLLVRQAALALQDGRPDAVSlCSMAK 357
Cdd:PRK03354 240 ERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGD-AAMCK 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 41055941 358 LFVTDECFSICNQALQIHGGYGYLKDYAVQQYVRDIRVHQILEGTNEVMRMIIARSLL 415
Cdd:PRK03354 319 YFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVL 376
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
81-415 |
2.20e-42 |
|
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 153.27 E-value: 2.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 81 RKAAELGFGGIYVNPDVGGSGLSRLDTSIIFEALSTGCVSTTAYVSIHNMCAWMIDTFGNNEQRERFCPDLCSMQKFASY 160
Cdd:cd01152 42 RALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 161 CLTEPGSGSDAASLLTSATLKGDHYILNGSKAFISGGGDTDVYVVMCRTGGKGPK--GISCLVVEKGTPGLSFGKKEKKV 238
Cdd:cd01152 122 GFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDPEAPKhrGISILLVDMDSPGVTVRPIRSIN 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 239 GwnSQPTRAVIFEDCAVPVTNRLGTEGQGFSIAMKGLNGGRINIascslgAAHASVLL--ARDHMCVRKQFGETLANSQF 316
Cdd:cd01152 202 G--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSI------GGSAATFFelLLARLLLLTRDGRPLIDDPL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 317 LQFKLAEMATKLVASRLLVRQAALALQDG-RPDAVSlcSMAKLFVTDECFSICNQALQIHGGYGYLKDYA--------VQ 387
Cdd:cd01152 274 VRQRLARLEAEAEALRLLVFRLASALAAGkPPGAEA--SIAKLFGSELAQELAELALELLGTAALLRDPApgaelagrWE 351
|
330 340
....*....|....*....|....*...
gi 41055941 388 QYVRDIRVHQILEGTNEVMRMIIARSLL 415
Cdd:cd01152 352 ADYLRSRATTIYGGTSEIQRNIIAERLL 379
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
44-154 |
3.19e-40 |
|
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: 139.14 E-value: 3.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 44 TDEQKEFQKVAFDFAANEMAPHMAEWDQKEIFPVEAMRKAAELGFGGIYVNPDVGGSGLSRLDTSIIFEALSTGCVSTTA 123
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|..
gi 41055941 124 YVSIHN-MCAWMIDTFGNNEQRERFCPDLCSM 154
Cdd:pfam02771 81 ALSVHSsLGAPPILRFGTEEQKERYLPKLASG 112
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
43-414 |
1.73e-36 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 138.06 E-value: 1.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 43 LTDEQKEFQKVAFDFAANEMAPHMAEWDQKEIFPVEAMRKAAELGFGGIYVNpDVGGSGLSRLDTSIIFEALSTGCVSTT 122
Cdd:PLN02526 29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIK-GYGCPGLSITASAIATAEVARVDASCS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 123 AYVSIHN-MCAWMIDTFGNNEQRERFCPDLCSMQKFASYCLTEPGSGSDAASLLTSATLKGDHYILNGSKAFISGGGDTD 201
Cdd:PLN02526 108 TFILVHSsLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFAD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 202 VYVVMCRTggKGPKGISCLVVEKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVTNRLgTEGQGFSIAMKGLNGGRIN 281
Cdd:PLN02526 188 VLVIFARN--TTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRL-PGVNSFQDTNKVLAVSRVM 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 282 IASCSLGAAHASVLLARDHMCVRKQFGETLANSQFLQFKLAEM-----ATKLVASRLLVRQAALALQDGRpdavslCSMA 356
Cdd:PLN02526 265 VAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMlgniqAMFLVGWRLCKLYESGKMTPGH------ASLG 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 41055941 357 KLFVTDECFSICNQALQIHGGYGYLKDYAVQQYVRDIRVHQILEGTNEVMRMIIARSL 414
Cdd:PLN02526 339 KAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREI 396
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
69-412 |
5.94e-36 |
|
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: 135.98 E-value: 5.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 69 WDQKEIfpVEAMR-KAAELGFGGIYVNPDVGGSGLSRLDTSIIFEALSTGCVSTTAYvsihNmCAwMIDT--------FG 139
Cdd:cd01155 37 WTPPPI--IEKLKaKAKAEGLWNLFLPEVSGLSGLTNLEYAYLAEETGRSFFAPEVF----N-CQ-APDTgnmevlhrYG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 140 NNEQRERFCPDLCSMQKFASYCLTEPG-SGSDAASLLTSATLKGDHYILNGSKAFISGGGDTD--VYVVMCRTGGKGP-- 214
Cdd:cd01155 109 SEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRKWWSSGAGDPRckIAIVMGRTDPDGApr 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 215 -KGISCLVVEKGTPGLSFGKKEKKVGWNSQPT--RAVIFEDCAVPVTNRLGTEGQGFSIAMKGLNGGRINIASCSLGAAH 291
Cdd:cd01155 189 hRQQSMILVPMDTPGVTIIRPLSVFGYDDAPHghAEITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIHHCMRLIGAAE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 292 ASVLLARDHMCVRKQFGETLANSQFLQFKLAEMATKLVASRLLVRQAALAL-QDGRPDAVSLCSMAKLFVTDECFSICNQ 370
Cdd:cd01155 269 RALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIdTVGNKAARKEIAMIKVAAPRMALKIIDR 348
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 41055941 371 ALQIHGGYGYLKDYAVQQYVRDIRVHQILEGTNEVMRMIIAR 412
Cdd:cd01155 349 AIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIAR 390
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
162-406 |
1.35e-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: 130.18 E-value: 1.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 162 LTEPGSGSDAASLLTSAT-LKGDHYILNGSKAFISGGgDTDVYVVMCRTGG--KGPKGISCLVV----EKGT-PGLSFGK 233
Cdd:cd01154 153 MTEKQGGSDLGANETTAErSGGGVYRLNGHKWFASAP-LADAALVLARPEGapAGARGLSLFLVprllEDGTrNGYRIRR 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 234 KEKKVGWNSQPTRAVIFEDCavpVTNRLGTEGQGFSIAMKGLNGGRINIASCSLGAAHASVLLARDHMCVRKQFGETLAN 313
Cdd:cd01154 232 LKDKLGTRSVATGEVEFDDA---EAYLIGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLID 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 314 SQFLQFKLAEMATKLVASRLLVRQAALALQDGRPDAVSLCSMAKLFVTDECFSICNQ-------ALQIHGGYGYLKDYAV 386
Cdd:cd01154 309 HPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKPVEAHMARLATPVAKLIACKRaapvtseAMEVFGGNGYLEEWPV 388
|
250 260
....*....|....*....|
gi 41055941 387 QQYVRDIRVHQILEGTNEVM 406
Cdd:cd01154 389 ARLHREAQVTPIWEGTGNIQ 408
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
159-251 |
3.21e-28 |
|
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: 106.60 E-value: 3.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 159 SYCLTEPGSGSDAASLLTSA-TLKGDHYILNGSKAFISGGGDTDVYVVMCRTGGKGPK-GISCLVVEKGTPGLSFGKKEK 236
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHgGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 41055941 237 KVGWNSQPTRAVIFE 251
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
138-412 |
1.92e-23 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 102.95 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 138 FGNNEQRERFCPDLCSMQKFASYCLTEPG-SGSDAASLLTSATLKGDHYILNGSKAFISGGGD--TDVYVVMCRTGGKGP 214
Cdd:PLN02876 532 YGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAMDprCRVLIVMGKTDFNAP 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 215 --KGISCLVVEKGTPGLSFGKKEKKVGWNSQPT--RAVIFEDCAVPVTNRLGTEGQGFSIAMKGLNGGRINIASCSLGAA 290
Cdd:PLN02876 612 khKQQSMILVDIQTPGVQIKRPLLVFGFDDAPHghAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAA 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 291 HASVLLARDHMCVRKQFGETLANSQFLQFKLAEMATKLVASRLLVRQAALALQD-GRPDAVSLCSMAKLFVTDECFSICN 369
Cdd:PLN02876 692 ERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDRlGNKKARGIIAMAKVAAPNMALKVLD 771
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 41055941 370 QALQIHGGYGYLKDYAVQQYVRDIRVHQILEGTNEVMRMIIAR 412
Cdd:PLN02876 772 MAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAK 814
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
78-415 |
2.27e-19 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 90.31 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 78 EAMRKAAELGFGGIYVNPDVGGSGLSRLDTSIIFEALSTGCVSTTAY--VSIHNMCAWMidTFGNNEQRERFCPDLCSMQ 155
Cdd:PTZ00456 103 EAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYpgLSIGAANTLM--AWGSEEQKEQYLTKLVSGE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 156 KFASYCLTEPGSGSDAASLLTSATLKGD-HYILNGSKAFISgGGDTD-----VYVVMCRTGGKGP--KGISCLVVEKGTP 227
Cdd:PTZ00456 181 WSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFIS-AGDHDlteniVHIVLARLPNSLPttKGLSLFLVPRHVV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 228 ----------GLSFGKKEKKVGWNSQPTRAVIFEDcavPVTNRLGTEGQGFSIAMKGLNGGRIniaSCSL-GAAHASVLL 296
Cdd:PTZ00456 260 kpdgsletakNVKCIGLEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTARV---GTALeGVCHAELAF 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 297 ------ARDHMCVRKQFGETLANS------------QFLQF--KLAEMATKLV--ASRLLVRQAAL---ALQDGRPDAVS 351
Cdd:PTZ00456 334 qnalryARERRSMRALSGTKEPEKpadriichanvrQNILFakAVAEGGRALLldVGRLLDIHAAAkdaATREALDHEIG 413
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41055941 352 LCS-MAKLFVTDECFSICNQALQIHGGYGYLKDYAVQQYVRDIRVHQILEGTNEVMRM-IIARSLL 415
Cdd:PTZ00456 414 FYTpIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALdFIGRKVL 479
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
282-404 |
5.59e-19 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 82.39 E-value: 5.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 282 IASCSLGAAHASVLLARDHMCVRKQ--FGETLANSQFLQFKLAEMATKLVASRLLVRQAALALQDGR-------PDAVSL 352
Cdd:pfam08028 2 IAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAaagkpvtPALRAE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 41055941 353 CSMAKLFVTDECFSICNQALQIHGGYGYLKDYAVQQYVRDIRVHQILEGTNE 404
Cdd:pfam08028 82 ARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
18-415 |
1.31e-14 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 75.76 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 18 GRPRsliFNSLHRRGIAAcidpsigLTDEQKefqkvafDFAANEMAPHMAEWDQKEIF------PVEAMRKAAELGFGGI 91
Cdd:PRK13026 63 GKPD---WQKLHSYPKPT-------LTAEEQ-------AFIDNEVETLLTMLDDWDIVqnrkdlPPEVWDYLKKEGFFAL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 92 YVNPDVGGSGLSRLDTSIIFEALSTGCVSTTAYVSIHNMC--AWMIDTFGNNEQRERFCPDLCSMQKFASYCLTEPGSGS 169
Cdd:PRK13026 126 IIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPNSLgpGELLTHYGTQEQKDYWLPRLADGTEIPCFALTGPEAGS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 170 DAASLLTSATL-KGDH-------YILNGSKAFISGGGDTDVYVVMCRT-------GGKGPKGISCLVVEKGTPGLSFGKK 234
Cdd:PRK13026 206 DAGAIPDTGIVcRGEFegeevlgLRLTWDKRYITLAPVATVLGLAFKLrdpdgllGDKKELGITCALIPTDHPGVEIGRR 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 235 EKKVGWNSQ--PTRAvifEDCAVPVTNRLGTE---GQGFSIAMKGLNGGR-INIASCSLGAAHASVLLARDHMCVRKQFG 308
Cdd:PRK13026 286 HNPLGMAFMngTTRG---KDVFIPLDWIIGGPdyaGRGWRMLVECLSAGRgISLPALGTASGHMATRTTGAYAYVRRQFG 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 309 ETLANSQFLQFKLAEMATK---LVASRLLVrqaALALQDG-RPDAVSlcSMAKLFVTDECFSICNQALQIHGGYG----- 379
Cdd:PRK13026 363 MPIGQFEGVQEALARIAGNtylLEAARRLT---TTGLDLGvKPSVVT--AIAKYHMTELARDVVNDAMDIHAGKGiqlgp 437
|
410 420 430
....*....|....*....|....*....|....*...
gi 41055941 380 --YLKdYAVQQYVRDIRVhqilEGTNevmrmIIARSLL 415
Cdd:PRK13026 438 knYLG-HAYMAVPIAITV----EGAN-----ILTRNLM 465
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
162-414 |
4.14e-12 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 67.85 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 162 LTEPGSGSDAASLLTSAT-LKGDHYILNGSKAFISGGgDTDVYVVMCRTGGkgpkGISCLVVEKGTP-----GLSFGKKE 235
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAErLADGSYRLVGHKWFFSVP-QSDAHLVLAQAKG----GLSCFFVPRFLPdgqrnAIRLERLK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 236 KKVGWNSQPTRAVIFEDCavpVTNRLGTEGQGFS--IAMKGLNggRINIASCSLGAAHASVLLARDHMCVRKQFGETLAN 313
Cdd:PRK11561 259 DKLGNRSNASSEVEFQDA---IGWLLGEEGEGIRliLKMGGMT--RFDCALGSHGLMRRAFSVAIYHAHQRQVFGKPLIE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 314 SQFLQFKLAEMATKLVA-SRLLVRqaaLALQDGRPDAVSLCSMAKLFVTDECFSICNQ-------ALQIHGGYGYLKDYA 385
Cdd:PRK11561 334 QPLMRQVLSRMALQLEGqTALLFR---LARAWDRRADAKEALWARLFTPAAKFVICKRgipfvaeAMEVLGGIGYCEESE 410
|
250 260
....*....|....*....|....*....
gi 41055941 386 VQQYVRDIRVHQILEGTNEVMRMIIARSL 414
Cdd:PRK11561 411 LPRLYREMPVNSIWEGSGNIMCLDVLRVL 439
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
139-416 |
2.15e-10 |
|
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: 62.35 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 139 GNNEQRERFCPDLCSMQKFASYCLTEPGSGSDAASLLTSATL--KGDHYILN-----GSKAFISGGGDT-DVYVVMCR-- 208
Cdd:cd01150 117 GTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYdpLTQEFVINtpdftATKWWPGNLGKTaTHAVVFAQli 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 209 TGGKGpKGISCLVV---EKGT----PGLSFGKKEKKVGWNSQPTRAVIFEDCAVPVTNRL---------GT-------EG 265
Cdd:cd01150 197 TPGKN-HGLHAFIVpirDPKThqplPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLnrfgdvspdGTyvspfkdPN 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 266 QGFSIAMKGLNGGRINIASCSLGAAHASVLLARDHMCVRKQFGETLANS-------QFLQFKLAEM---------ATKLV 329
Cdd:cd01150 276 KRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPKPSDPevqildyQLQQYRLFPQlaaayafhfAAKSL 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 330 ASRLLVRQAALALQDGR--PDAVSLCSMAKLFVTDEC---FSICNQALqihGGYGYLKDYAVQQYVRDIRVHQILEGTNE 404
Cdd:cd01150 356 VEMYHEIIKELLQGNSEllAELHALSAGLKAVATWTAaqgIQECREAC---GGHGYLAMNRLPTLRDDNDPFCTYEGDNT 432
|
330
....*....|..
gi 41055941 405 VMRMIIARSLLT 416
Cdd:cd01150 433 VLLQQTANYLLK 444
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
58-395 |
1.76e-09 |
|
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, which is active against Gram-positive bacteria. Polyketides are secondary metabolites, which have important biological functions such as antitumor, immunosupressive or antibiotic activities. NcnH is a hydroxylase involved in the biosynthesis of naphthocyclinone and possibly other polyketides.
Pssm-ID: 173848 [Multi-domain] Cd Length: 370 Bit Score: 58.90 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 58 AANEMAP----HMAEWDQKEIFPVEAMRKAAELGFGGIYVNPDVGGSGLSRLDTSIIFEALSTGCVSTTAYVSIHNMCAW 133
Cdd:cd01159 2 RAEDLAPlireRAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIVATHSR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 134 MIDTFGNNEQRERFcpdlcsmqkfasycltepGSGSDAASLLTSATLK-----GDHYILNGSKAFISGGGDTDVYVVMCR 208
Cdd:cd01159 82 MLAAFPPEAQEEVW------------------GDGPDTLLAGSYAPGGraervDGGYRVSGTWPFASGCDHADWILVGAI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 209 TGGKGPKGISCLVVekgtpglsFGKKEKK-------VGWNSQPTRAVIFEDCAVP--------VTNRLGTEGQG---FSI 270
Cdd:cd01159 144 VEDDDGGPLPRAFV--------VPRAEYEivdtwhvVGLRGTGSNTVVVDDVFVPehrtltagDMMAGDGPGGStpvYRM 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 271 AMKGLNGgrINIASCSLGAAHASVLLARDHMCVRKQ---FGETLANSQFLQFKLAEMATKLVASRLLVRQA-----ALAL 342
Cdd:cd01159 216 PLRQVFP--LSFAAVSLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAELDAARAFLERAtrdlwAHAL 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 41055941 343 QDGRPDAVSL--CSMAKLFVTDECFSICNQALQIHGGYGYLKDYAVQQYVRDIRV 395
Cdd:cd01159 294 AGGPIDVEERarIRRDAAYAAKLSAEAVDRLFHAAGGSALYTASPLQRIWRDIHA 348
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
138-379 |
1.76e-08 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 56.75 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 138 FGNNEQRERFCPDLCSMQKFASYCLTEPGSGSDAASLLTSATL-KGDH------YI-LNGSKAFISGG------------ 197
Cdd:PRK09463 175 YGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGVVcKGEWqgeevlGMrLTWNKRYITLApiatvlglafkl 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 198 -------GDTDVYvvmcrtggkgpkGISCLVVEKGTPGLSFGKKEKKVGWNSQ--PTRAvifEDCAVPVTNRLGTE---G 265
Cdd:PRK09463 255 ydpdgllGDKEDL------------GITCALIPTDTPGVEIGRRHFPLNVPFQngPTRG---KDVFIPLDYIIGGPkmaG 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 266 QGFSIAMKGLNGGR-INIASCSLGAAHASVLLARDHMCVRKQFGetLANSQF--LQFKLAEMATK---LVASRLLVrqaA 339
Cdd:PRK09463 320 QGWRMLMECLSVGRgISLPSNSTGGAKLAALATGAYARIRRQFK--LPIGKFegIEEPLARIAGNaylMDAARTLT---T 394
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 41055941 340 LALQDG-RPDAVSlcSMAKLFVTDECFSICNQALQIHGGYG 379
Cdd:PRK09463 395 AAVDLGeKPSVLS--AIAKYHLTERGRQVINDAMDIHGGKG 433
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
54-396 |
6.12e-08 |
|
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: 54.25 E-value: 6.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 54 AFDFAANEMAPHMAEWDQKEIFPVEAMRKAAELGFGGIYVNPDVGGSGLSRLDTSIIFEALSTGCVSTTAYVSIHNMCAW 133
Cdd:cd01163 2 RARPLAARIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGFVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 134 MIDTFGNNEQRERfCPDLCSMQKFASYCLTEPGSGSDAASLLTSATlKGDHYILNGSKAFISGGGDTDvYVVMCRTGGKG 213
Cdd:cd01163 82 ALLLAGPEQFRKR-WFGRVLNGWIFGNAVSERGSVRPGTFLTATVR-DGGGYVLNGKKFYSTGALFSD-WVTVSALDEEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 214 PKGIscLVVEKGTPGLS-------FGKKEKKVGwNSQPTRAVIFEDCAVPVTNRLGTEGQGFSIAmkglnggRINIASCS 286
Cdd:cd01163 159 KLVF--AAVPTDRPGITvvddwdgFGQRLTASG-TVTFDNVRVEPDEVLPRPNAPDRGTLLTAIY-------QLVLAAVL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 287 LGAAHASVLLARDHmcVRKQF-------GETLANSQFLQFKLAEMATKLVASRLLVRQAALALQDG--RPDAVS------ 351
Cdd:cd01163 229 AGIARAALDDAVAY--VRSRTrpwihsgAESARDDPYVQQVVGDLAARLHAAEALVLQAARALDAAaaAGTALTaearge 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 41055941 352 ---LCSMAKLFVTDECFSICNQALQIHGGYGYLKDYAVQQYVRDIRVH 396
Cdd:cd01163 307 aalAVAAAKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNARTH 354
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
118-179 |
2.06e-04 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 43.68 E-value: 2.06e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41055941 118 CVSTTAYVSIH-NMCAWMIDTFGNNEQRERFCPDLCSMQKFASYCLTEPGSGSDAASLLTSAT 179
Cdd:PTZ00460 88 CPQGTFISTVHfAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTAT 150
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
90-272 |
4.61e-04 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 42.18 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 90 GIYVNPDVGGSGLSRLDTSIIFEALSTGCVSTTAYVSIH-NMCAWMIDTFGNNEQRERFC---PDLCSMQKFAsyclTEP 165
Cdd:PTZ00457 67 GARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHsGFCTYLLSTVGSKELKGKYLtamSDGTIMMGWA----TEE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 166 GSGSDAASLLTSATLKGD-HYILNGSKAFISGGGDTDvYVVMCRT-----GGKGPKGI---SCLVVEKGTPGLSfgkkek 236
Cdd:PTZ00457 143 GCGSDISMNTTKASLTDDgSYVLTGQKRCEFAASATH-FLVLAKTltqtaAEEGATEVsrnSFFICAKDAKGVS------ 215
|
170 180 190
....*....|....*....|....*....|....*.
gi 41055941 237 kVGWNSqptraVIFEDcaVPVTNRLGTEGQGFSIAM 272
Cdd:PTZ00457 216 -VNGDS-----VVFEN--TPAADVVGVVGEGFKDAM 243
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
138-417 |
4.79e-04 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 42.54 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 138 FGNNEQRERFCPDLCSMQKFASYCLTEPGSGSDAASLLTSATLK--GDHYILN-----GSKAFIsggGDTDVY----VVM 206
Cdd:PLN02636 155 LGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDplTDEFVINtpndgAIKWWI---GNAAVHgkfaTVF 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 207 CR-------TGGKGPKGISCLVV-------EKGTPGLSFGKKEKKVGWNSQPTRAVIFEDCAVP---VTNRLG------- 262
Cdd:PLN02636 232 ARlklpthdSKGVSDMGVHAFIVpirdmktHQVLPGVEIRDCGHKVGLNGVDNGALRFRSVRIPrdnLLNRFGdvsrdgk 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 263 ------TEGQGFSIAMKGLNGGRINIASCSLGAAHASVLLARDHMCVRKQFGE------TLANSQFLQFKLAEM-----A 325
Cdd:PLN02636 312 ytsslpTINKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPpkqpeiSILDYQSQQHKLMPMlastyA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 326 TKLVASRLLVRQAALAL---QDGRPDAVSLCSMAKLFVTD---ECFSICNQALqihGGYGYLkdyAVQQY--VR-DIRVH 396
Cdd:PLN02636 392 FHFATEYLVERYSEMKKthdDQLVADVHALSAGLKAYITSytaKALSTCREAC---GGHGYA---AVNRFgsLRnDHDIF 465
|
330 340
....*....|....*....|.
gi 41055941 397 QILEGTNEVMRMIIARSLLTE 417
Cdd:PLN02636 466 QTFEGDNTVLLQQVAADLLKQ 486
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
119-415 |
4.99e-04 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 42.52 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 119 VSTTAYVSIH-NMCAWMIDTFGNNEQRERFCPDLCSMQKFASYCLTEPGSGSDAASLLTSATL--KGDHYILN-----GS 190
Cdd:PLN02443 93 VDEPGYTDLHwGMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFdpKTDEFVIHsptltSS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 191 KAFISGGGDTDVY-VVMCR--TGGKgPKGISCLVVE-------KGTPGLSFGKKEKKVG---WNSQPTRAVIFEDCAVPV 257
Cdd:PLN02443 173 KWWPGGLGKVSTHaVVYARliTNGK-DHGIHGFIVQlrslddhSPLPGVTVGDIGMKFGngaYNTMDNGFLRFDHVRIPR 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 258 TN---RLGT---EGQGF-SIAMKGLNGG-----RINIASCSLGAAHASVLLARDHMCVRKQFG------ET--------- 310
Cdd:PLN02443 252 DQmlmRLSKvtrEGKYVqSDVPRQLVYGtmvyvRQTIVADASTALSRAVCIATRYSAVRRQFGsqdggpETqvidyktqq 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055941 311 ------LANS-------QFLQFKLAEMATKLVASRLLVRQAALALQDGRPdavSLCSMAKLFVTDECFSICnqalqihGG 377
Cdd:PLN02443 332 srlfplLASAyafrfvgEWLKWLYTDVTQRLEANDFSTLPEAHACTAGLK---SLTTSATADGIEECRKLC-------GG 401
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 41055941 378 YGYL------KDYAVqqYVRDIrvhqILEGTNEVMRMIIARSLL 415
Cdd:PLN02443 402 HGYLcssglpELFAV--YVPAC----TYEGDNVVLLLQVARFLM 439
|
|
| |
