|
Name |
Accession |
Description |
Interval |
E-value |
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
3-392 |
0e+00 |
|
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: 721.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 3 AKAIDYRTRLSDFMTEHVFGAEADYDDYRRAAGPADHTAPPIIEELKTKAKDRGLWNLFLSAES---GLTNLEYAPLAEM 79
Cdd:cd01155 1 RKAQELRARVKAFMEEHVYPAEQEFLEYYAEGGDRWWTPPPIIEKLKAKAKAEGLWNLFLPEVSglsGLTNLEYAYLAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 80 TGWSmEIAPEALNCAAPDTGNMEILHMFGTEQQRAQWLRPLLDGKIRSAFSMTEPAVASSDARNIETTISRDGADYVING 159
Cdd:cd01155 81 TGRS-FFAPEVFNCQAPDTGNMEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDVASSDATNIECSIERDGDDYVING 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 160 RKWWTSGAADPRCKILIVMGRTNPD-AAAHQQQSMVLVPIDTPGVTIVRSTPVFGWQD-RHGHCEIDYHNVRVPATNLLG 237
Cdd:cd01155 160 RKWWSSGAGDPRCKIAIVMGRTDPDgAPRHRQQSMILVPMDTPGVTIIRPLSVFGYDDaPHGHAEITFDNVRVPASNLIL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 238 EEGSGFAIAQARLGPGRIHHCMRALGAAERALALMVNRVRNRVAFGRPLAEQGVVQQAIAQSRNEIDQARLLCEKAAWTI 317
Cdd:cd01155 240 GEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMI 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15607296 318 DQHGNKEARHLVAMIKAVAPRVACDVIDRAIQVHGAAGVSDDTPLARLYGWHRAMRIFDGPDEVHLRSIARAELS 392
Cdd:cd01155 320 DTVGNKAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMELK 394
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
2-395 |
1.70e-170 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 497.40 E-value: 1.70e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 2 SAKAIDYRTRLSDFMTEHVFGAEADYddYRRAAGPADHTAPPIIEELKTKAKDRGLWNLFLSAES--------------- 66
Cdd:PLN02876 403 SEKVLELRKKLIKFMEDHIYPMENEF--YKLAQSSSRWTVHPEEERLKELAKKEGLWNLWIPLDSaararkllfednkhm 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 67 ------------GLTNLEYAPLAEMTGWSMeIAPEALNCAAPDTGNMEILHMFGTEQQRAQWLRPLLDGKIRSAFSMTEP 134
Cdd:PLN02876 481 vsgdsadqllgaGLSNLEYGYLCEIMGRSV-WAPQVFNCGAPDTGNMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEP 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 135 AVASSDARNIETTISRDGADYVINGRKWWTSGAADPRCKILIVMGRTNPDAAAHQQQSMVLVPIDTPGVTIVRSTPVFGW 214
Cdd:PLN02876 560 QVASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPRCRVLIVMGKTDFNAPKHKQQSMILVDIQTPGVQIKRPLLVFGF 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 215 QDR-HGHCEIDYHNVRVPATNLLGEEGSGFAIAQARLGPGRIHHCMRALGAAERALALMVNRVRNRVAFGRPLAEQGVVQ 293
Cdd:PLN02876 640 DDApHGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFL 719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 294 QAIAQSRNEIDQARLLCEKAAWTIDQHGNKEARHLVAMIKAVAPRVACDVIDRAIQVHGAAGVSDDTPLARLYGWHRAMR 373
Cdd:PLN02876 720 SDLAKCRVELEQTRLLVLEAADQLDRLGNKKARGIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLR 799
|
410 420
....*....|....*....|..
gi 15607296 374 IFDGPDEVHLRSIARAELSREK 395
Cdd:PLN02876 800 IADGPDEVHLGTIAKLELQRAK 821
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
7-393 |
1.08e-117 |
|
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: 347.60 E-value: 1.08e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 7 DYRTRLSDFMTEHVFGAEADYDDYRRaagpadhtappIIEELKTKAKDRGLWNLFLSAE---SGLTNLEYAPLAEMTGWS 83
Cdd:COG1960 11 ALRDEVREFAEEEIAPEAREWDREGE-----------FPRELWRKLAELGLLGLTIPEEyggLGLSLVELALVLEELARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 84 MeiAPEALNCAAPDtGNMEILHMFGTEQQRAQWLRPLLDGKIRSAFSMTEPAvASSDARNIETTISRDGADYVINGRKWW 163
Cdd:COG1960 80 D--ASLALPVGVHN-GAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPG-AGSDAAALRTTAVRDGDGYVLNGQKTF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 164 TSGAadPRCKILIVMGRTNPDAAaHQQQSMVLVPIDTPGVTIVRSTPVFGWQDrHGHCEIDYHNVRVPATNLLGEEGSGF 243
Cdd:COG1960 156 ITNA--PVADVILVLARTDPAAG-HRGISLFLVPKDTPGVTVGRIEDKMGLRG-SDTGELFFDDVRVPAENLLGEEGKGF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 244 AIAQARLGPGRIHHCMRALGAAERALALMVNRVRNRVAFGRPLAEQGVVQQAIAQSRNEIDQARLLCEKAAWTIDQhgNK 323
Cdd:COG1960 232 KIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDA--GE 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 324 EARHLVAMIKAVAPRVACDVIDRAIQVHGAAGVSDDTPLARLYGWHRAMRIFDGPDEVHLRSIARAELSR 393
Cdd:COG1960 310 DAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGR 379
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
72-388 |
1.00e-97 |
|
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: 294.58 E-value: 1.00e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 72 EYAPLAEMTGWSMEIAPEALNcAAPDTGNMEILHMFGTEQQRAQWLRPLLDGKIRSAFSMTEPAvASSDARNIETTISRD 151
Cdd:cd00567 17 ELEPYARERRETPEEPWELLA-ELGLLLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPG-AGSDLAGIRTTARKD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 152 GADYVINGRKWWTSGAadPRCKILIVMGRTNPDAAAHQQQSMVLVPIDTPGVTIVRSTPVFGWqDRHGHCEIDYHNVRVP 231
Cdd:cd00567 95 GDGYVLNGRKIFISNG--GDADLFIVLARTDEEGPGHRGISAFLVPADTPGVTVGRIWDKMGM-RGSGTGELVFDDVRVP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 232 ATNLLGEEGSGFAIAQARLGPGRIHHCMRALGAAERALALMVNRVRNRVAFGRPLAEQGVVQQAIAQSRNEIDQARLLCE 311
Cdd:cd00567 172 EDNLLGEEGGGFELAMKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLY 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15607296 312 KAAWTIDQhGNKEARHLVAMIKAVAPRVACDVIDRAIQVHGAAGVSDDTPLARLYGWHRAMRIFDGPDEVHLRSIAR 388
Cdd:cd00567 252 RAAWLLDQ-GPDEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
102-389 |
1.09e-59 |
|
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: 198.26 E-value: 1.09e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 102 EILHMFGTEQQRAQWLRPLLDGKIRSAFSMTEPAvASSDARNIETTISRDGADYVINGRKWWTS--GAADprckILIVMG 179
Cdd:cd01158 90 NPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPG-AGSDAAALKTTAKKDGDDYVLNGSKMWITngGEAD----FYIVFA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 180 RTNPDAAaHQQQSMVLVPIDTPGVTIVRSTPVFGwqdRHGH--CEIDYHNVRVPATNLLGEEGSGFAIAQARLGPGRIHH 257
Cdd:cd01158 165 VTDPSKG-YRGITAFIVERDTPGLSVGKKEDKLG---IRGSstTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 258 CMRALGAAERALALMVNRVRNRVAFGRPLAEQGVVQQAIAQSRNEIDQARLLCEKAAWTIDQHGN--KEArhlvAMIKAV 335
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPfiKEA----AMAKLF 316
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 15607296 336 APRVACDVIDRAIQVHGAAGVSDDTPLARLYGWHRAMRIFDGPDEVHLRSIARA 389
Cdd:cd01158 317 ASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKH 370
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
108-388 |
5.11e-49 |
|
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: 169.99 E-value: 5.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 108 GTEQQRAQWLRPLLDGKIRSAFSMTEPAvASSDARNIETTISRDGADYVINGRKWW-TSGAadpRCKILIVMGRTNPDAA 186
Cdd:cd01160 95 GSPEQKERVLPQMVAGKKIGAIAMTEPG-AGSDLQGIRTTARKDGDHYVLNGSKTFiTNGM---LADVVIVVARTGGEAR 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 187 AHQQQSMVLVPIDTPGVTIVRSTPVFGWQDRHGhCEIDYHNVRVPATNLLGEEGSGFAIAQARLGPGRIHHCMRALGAAE 266
Cdd:cd01160 171 GAGGISLFLVERGTPGFSRGRKLKKMGWKAQDT-AELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAAGALAAAE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 267 RALALMVNRVRNRVAFGRPLAEQGVVQQAIAQSRNEIDQARLLCEKAAWTIDQhGNKEARHlVAMIKAVAPRVACDVIDR 346
Cdd:cd01160 250 FMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQ-GRLDVAE-ASMAKYWATELQNRVAYE 327
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 15607296 347 AIQVHGAAGVSDDTPLARLYGWHRAMRIFDGPDEVHLRSIAR 388
Cdd:cd01160 328 CVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISR 369
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
89-393 |
2.56e-48 |
|
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: 168.39 E-value: 2.56e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 89 EALNCAAPDTG------NM--EILHMFGTEQQRAQWLRPLLDGKIRSAFSMTEPAvASSDARNIETTISRDGADYVINGR 160
Cdd:cd01162 70 EALSTGCVSTAayisihNMcaWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPG-SGSDAAALRTRAVREGDHYVLNGS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 161 KWWTSGAADPrcKILIVMGRTNPDAAahQQQSMVLVPIDTPGVTIVRSTPVFGWQDRHGHcEIDYHNVRVPATNLLGEEG 240
Cdd:cd01162 149 KAFISGAGDS--DVYVVMARTGGEGP--KGISCFVVEKGTPGLSFGANEKKMGWNAQPTR-AVIFEDCRVPVENRLGGEG 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 241 SGFAIAQARLGPGRIHHCMRALGAAERALALMVNRVRNRVAFGRPLAEQGVVQQAIAQSRNEIDQARLLCEKAAWTIDQh 320
Cdd:cd01162 224 QGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDR- 302
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15607296 321 GNKEARHLVAMIKAVAPRVACDVIDRAIQVHGAAGVSDDTPLARLYGWHRAMRIFDGPDEVHLRSIARAELSR 393
Cdd:cd01162 303 GDPDAVKLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
240-389 |
1.38e-42 |
|
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: 146.25 E-value: 1.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 240 GSGFAIAQARLGPGRIHHCMRALGAAERALALMVNRVRNRVAFGRPLAEQGVVQQAIAQSRNEIDQARLLCEKAAWTIDQ 319
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 320 HGNKEARhlVAMIKAVAPRVACDVIDRAIQVHGAAGVSDDTPLARLYGWHRAMRIFDGPDEVHLRSIARA 389
Cdd:pfam00441 81 GGPDGAE--ASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARR 148
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
44-381 |
8.82e-42 |
|
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: 151.85 E-value: 8.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 44 IIEELKTKAKDRGLWNLFLSAE---SGLTNLEYAPLAEMTGWSMEIAPeALNcAAPDTGNMEILhMFGTEQQRAQWLRPL 120
Cdd:cd01161 57 IPRKTLTQLKELGLFGLQVPEEyggLGLNNTQYARLAEIVGMDLGFSV-TLG-AHQSIGFKGIL-LFGTEAQKEKYLPKL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 121 LDGKIRSAFSMTEPAvASSDARNIETT--ISRDGADYVINGRKWWTS--GAADprckILIVMGRT---NPDAAAHQQQSM 193
Cdd:cd01161 134 ASGEWIAAFALTEPS-SGSDAASIRTTavLSEDGKHYVLNGSKIWITngGIAD----IFTVFAKTevkDATGSVKDKITA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 194 VLVPIDTPGVTIVRSTPVFGWQDRHGhCEIDYHNVRVPATNLLGEEGSGFAIAQARLGPGRIHHCMRALGAAERALALMV 273
Cdd:cd01161 209 FIVERSFGGVTNGPPEKKMGIKGSNT-AEVYFEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 274 NRVRNRVAFGRPLAEQGVVQQAIAQsrneIDQARLLCEKAAWTI----DQHGNKEARHLVAMIKAVAPRVACDVIDRAIQ 349
Cdd:cd01161 288 DYANNRKQFGKKIHEFGLIQEKLAN----MAILQYATESMAYMTsgnmDRGLKAEYQIEAAISKVFASEAAWLVVDEAIQ 363
|
330 340 350
....*....|....*....|....*....|..
gi 15607296 350 VHGAAGVSDDTPLARLYGWHRAMRIFDGPDEV 381
Cdd:cd01161 364 IHGGMGFMREYGVERVLRDLRIFRIFEGTNEI 395
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
80-391 |
1.67e-41 |
|
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 150.19 E-value: 1.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 80 TGWS-ME---IAPEALNCAAPDTGNMEILHM-------FGTEQQRAQWLRPLLDGKIRSAFSMTEPAvASSDARNIETTI 148
Cdd:cd01152 61 RGASlMEqliFREEMAAAGAPVPFNQIGIDLagptilaYGTDEQKRRFLPPILSGEEIWCQGFSEPG-AGSDLAGLRTRA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 149 SRDGADYVINGRKWWTSGAADPRCKILIVmgRTNPDAAAHQQQSMVLVPIDTPGVTIvrsTPVFGWQDRHGHCEIDYHNV 228
Cdd:cd01152 140 VRDGDDWVVNGQKIWTSGAHYADWAWLLV--RTDPEAPKHRGISILLVDMDSPGVTV---RPIRSINGGEFFNEVFLDDV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 229 RVPATNLLGEEGSGFAIAQARLGPGRihhcMRALGAAERALALMVNRVRNRVAFGRPLAEQGVVQQAIAQSRNEIDQARL 308
Cdd:cd01152 215 RVPDANRVGEVNDGWKVAMTTLNFER----VSIGGSAATFFELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 309 LCEKAAWTIDQHGNKEARhlVAMIKAVAPRVACDVIDRAIQVHGAAGV----SDDTPLARLYGWH----RAMRIFDGPDE 380
Cdd:cd01152 291 LVFRLASALAAGKPPGAE--ASIAKLFGSELAQELAELALELLGTAALlrdpAPGAELAGRWEADylrsRATTIYGGTSE 368
|
330
....*....|.
gi 15607296 381 VHLRSIARAEL 391
Cdd:cd01152 369 IQRNIIAERLL 379
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
83-391 |
1.09e-35 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 134.86 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 83 SMEIAPealNCA-APDTGNMEILH---MFGTEQQRAQWLRPLLdGKIRSAFSM--TEPAvASSDARNIETTISRDGADYV 156
Cdd:PRK12341 74 LEEVSK---CGApAFLITNGQCIHsmrRFGSAEQLRKTAESTL-ETGDPAYALalTEPG-AGSDNNSATTTYTRKNGKVY 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 157 INGRKWWTSGAADprCKILIVMGRTNPDAAAHQQQSMVLVPIDTPGVTIvrsTPV--FGWQdRHGHCEIDYHNVRVPATN 234
Cdd:PRK12341 149 LNGQKTFITGAKE--YPYMLVLARDPQPKDPKKAFTLWWVDSSKPGIKI---NPLhkIGWH-MLSTCEVYLDNVEVEESD 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 235 LLGEEGSGFAIAQARLGPGRIHHCMRALGAAERALALMVNRVRNRVAFGRPLAEQGVVQQAIAQSRNEIDQARLLCEKAA 314
Cdd:PRK12341 223 LVGEEGMGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVA 302
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15607296 315 WTIDQHgnKEARHLVAMIKAVAPRVACDVIDRAIQVHGAAGVSDDTPLARLYGWHRAMRIFDGPDEVHLRSIARAEL 391
Cdd:PRK12341 303 WQADNG--QSLRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQIL 377
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
95-393 |
5.04e-35 |
|
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: 132.71 E-value: 5.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 95 APDTGNMEILhMFGTEQQRAQWLRPLLDGKIRSAFSMTEPAvASSDARNIETTISRDGADYVINGRKWWTSGAAdpRCKI 174
Cdd:cd01157 85 ANSLGQMPVI-ISGNDEQKKKYLGRMTEEPLMCAYCVTEPG-AGSDVAGIKTKAEKKGDEYIINGQKMWITNGG--KANW 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 175 LIVMGRTNPD--AAAHQQQSMVLVPIDTPGVTIVRSTPVFGWQ--DRHGhceIDYHNVRVPATNLLGEEGSGFAIAQARL 250
Cdd:cd01157 161 YFLLARSDPDpkCPASKAFTGFIVEADTPGIQPGRKELNMGQRcsDTRG---ITFEDVRVPKENVLIGEGAGFKIAMGAF 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 251 GPGRIHHCMRALGAAERALALMVNRVRNRVAFGRPLAEQGVVQQAIAQSRNEIDQARLLCEKAAWTIDQhgNKEARHLVA 330
Cdd:cd01157 238 DKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDS--GRRNTYYAS 315
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15607296 331 MIKAVAPRVACDVIDRAIQVHGAAGVSDDTPLARLYGWHRAMRIFDGPDEVHLRSIARAELSR 393
Cdd:cd01157 316 IAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
101-389 |
1.79e-32 |
|
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: 125.93 E-value: 1.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 101 MEILHMFGTEQQRAQWLRPLLDGKIRSAFSMTEPAvASSDARNIETTISRDGADYVINGRKWWTSGAadPRCKILIVMGR 180
Cdd:cd01151 102 MLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPN-HGSDPGGMETRARKDGGGYKLNGSKTWITNS--PIADVFVVWAR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 181 TNPDAAAHQqqsmVLVPIDTPGVTIVRSTPVFGWQ-DRHGHCEIDyhNVRVPATNLL----GEEGSGFAIAQARLGPGRI 255
Cdd:cd01151 179 NDETGKIRG----FILERGMKGLSAPKIQGKFSLRaSITGEIVMD--NVFVPEENLLpgaeGLRGPFKCLNNARYGIAWG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 256 hhcmrALGAAERALALMVNRVRNRVAFGRPLAEQGVVQQAIAQSRNEIDQARLLCEKAAWTIDQhgNKEARHLVAMIKAV 335
Cdd:cd01151 253 -----ALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQ--GKATPEQISLLKRN 325
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 15607296 336 APRVACDVIDRAIQVHGAAGVSDDTPLARLYGWHRAMRIFDGPDEVHLRSIARA 389
Cdd:cd01151 326 NCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRA 379
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
47-389 |
3.84e-29 |
|
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: 116.74 E-value: 3.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 47 ELKTKAKDRGLWNLFLSAESGLTNLEYapLAEMtgwsmeIAPEALNCAAPDTG-------NMEI--LHMFGTEQQRAQWL 117
Cdd:cd01156 37 DLWRKMGKLGLLGITAPEEYGGSGMGY--LAHV------IIMEEISRASGSVAlsygahsNLCInqIYRNGSAAQKEKYL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 118 RPLLDGKIRSAFSMTEPAvASSDARNIETTISRDGADYVINGRKWWTSGAadPRCKILIVMGRTNPDAAAHQQQSmVLVP 197
Cdd:cd01156 109 PKLISGEHIGALAMSEPN-AGSDVVSMKLRAEKKGDRYVLNGSKMWITNG--PDADTLVVYAKTDPSAGAHGITA-FIVE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 198 IDTPGVTIVRSTPVFGWQDRHGhCEIDYHNVRVPATNLLGEEGSGFAIAQARLGPGRIHHCMRALGAAERALALMVNRVR 277
Cdd:cd01156 185 KGMPGFSRAQKLDKLGMRGSNT-CELVFEDCEVPEENILGGENKGVYVLMSGLDYERLVLAGGPIGIMQAALDVAIPYAH 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 278 NRVAFGRPLAEQGVVQQAIAQSRNEIDQARLLCEKAAWTIDQHG--NKEARHLVAMIKAVAPRVACDvidrAIQVHGAAG 355
Cdd:cd01156 264 QRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNmdPKDAAGVILYAAEKATQVALD----AIQILGGNG 339
|
330 340 350
....*....|....*....|....*....|....
gi 15607296 356 VSDDTPLARLYGWHRAMRIFDGPDEVHLRSIARA 389
Cdd:cd01156 340 YINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRE 373
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
109-388 |
6.81e-29 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 116.58 E-value: 6.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 109 TEQQRAQWLRPLLDGKIRSAFSMTEPAvASSDARNIETTISRDG-ADYVINGRKWW-TSGA-ADprckILIVMGRTNPDA 185
Cdd:PTZ00461 135 SPAQRARWLPKVLTGEHVGAMGMSEPG-AGTDVLGMRTTAKKDSnGNYVLNGSKIWiTNGTvAD----VFLIYAKVDGKI 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 186 AAhqqqsmVLVPIDTPGVTIVRSTPVFGWQDRHgHCEIDYHNVRVPATNLLGEEGSGFAIAQARLGPGRIHHCMRALGAA 265
Cdd:PTZ00461 210 TA------FVVERGTKGFTQGPKIDKCGMRASH-MCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIA 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 266 ERALALMVNRVRNRVAFGRPLAEQGVVQQAIAQSRNEIDQARLLCEKAAWTIdqHGNKEARHLVAMIKAVAPRVACDVID 345
Cdd:PTZ00461 283 ERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNV--HPGNKNRLGSDAAKLFATPIAKKVAD 360
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15607296 346 RAIQVHGAAGVSDDTPLARLYGWHRAMRIFDGPDEVHLRSIAR 388
Cdd:PTZ00461 361 SAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITK 403
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
39-377 |
1.49e-22 |
|
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: 98.62 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 39 HTAPPIIEELKTKAKDrGLWNLFLSAESGLTNLEYAP---LAEMtgwsMEIAPEALNCAAPDTGNMEILHMFGTEQQRAQ 115
Cdd:cd01153 33 VVPPPFKEALDAFAEA-GWMALGVPEEYGGQGLPITVysaLAEI----FSRGDAPLMYASGTQGAAATLLAHGTEAQREK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 116 WLRPLLDGKIRSAFSMTEPAvASSDARNIET--TISRDGAdYVINGRKWW-TSGAADPRCKIL-IVMGRTNPDAAAHQQQ 191
Cdd:cd01153 108 WIPRLAEGEWTGTMCLTEPD-AGSDLGALRTkaVYQADGS-WRINGVKRFiSAGEHDMSENIVhLVLARSEGAPPGVKGL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 192 SMVLVP-----IDTPGVTIVRSTPVFGWqdrHGH--CEIDYHNVRVPatnLLGEEGSGFA-----IAQARLGPGrihhcM 259
Cdd:cd01153 186 SLFLVPkflddGERNGVTVARIEEKMGL---HGSptCELVFDNAKGE---LIGEEGMGLAqmfamMNGARLGVG-----T 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 260 RALGAAERALALMVNRVRNRVAFGRPLAEQGVVqqAIAQSRneiDQARLLCEKAA------------WTIDQHGNKEARH 327
Cdd:cd01153 255 QGTGLAEAAYLNALAYAKERKQGGDLIKAAPAV--TIIHHP---DVRRSLMTQKAyaegsraldlytATVQDLAERKATE 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15607296 328 -------------LVAMIKAVAPRVACDVIDRAIQVHGAAGVSDDTPLARLYGWHRAMRIFDG 377
Cdd:cd01153 330 gedrkalsaladlLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEG 392
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
115-366 |
1.56e-21 |
|
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: 95.52 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 115 QWLRPLLDGKIR----SAFSMTEPAvASSDARNIETTISRDGAD-YVINGRKWWTSGAAdprCKILIVMGRTNPDAAAHQ 189
Cdd:cd01154 133 QYLPGLLSDRYKtgllGGTWMTEKQ-GGSDLGANETTAERSGGGvYRLNGHKWFASAPL---ADAALVLARPEGAPAGAR 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 190 QQSMVLVPIDTP-----GVTIVRstpvfgWQDRHGH-----CEIDYHNVrvpATNLLGEEGSGFAIAQARLGPGRIHHCM 259
Cdd:cd01154 209 GLSLFLVPRLLEdgtrnGYRIRR------LKDKLGTrsvatGEVEFDDA---EAYLIGDEGKGIYYILEMLNISRLDNAV 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 260 RALGAAERALALMVNRVRNRVAFGRPLAEQGVVQQAIAQSRNEIDQARLLCEKAAWTID--QHGNKE----ARHLVAMIK 333
Cdd:cd01154 280 AALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDraAADKPVeahmARLATPVAK 359
|
250 260 270
....*....|....*....|....*....|...
gi 15607296 334 AVAPRVACDVIDRAIQVHGAAGVSDDTPLARLY 366
Cdd:cd01154 360 LIACKRAAPVTSEAMEVFGGNGYLEEWPVARLH 392
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
128-223 |
8.63e-21 |
|
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: 86.18 E-value: 8.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 128 AFSMTEPAvASSDARNIETT-ISRDGADYVINGRKWWTSGAADprCKILIVMGRTNPDaAAHQQQSMVLVPIDTPGVTIV 206
Cdd:pfam02770 1 AFALTEPG-AGSDVASLKTTaADGDGGGWVLNGTKWWITNAGI--ADLFLVLARTGGD-DRHGGISLFLVPKDAPGVSVR 76
|
90
....*....|....*..
gi 15607296 207 RSTPVFGwQDRHGHCEI 223
Cdd:pfam02770 77 RIETKLG-VRGLPTGEL 92
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
108-394 |
1.79e-20 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 92.25 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 108 GTEQQRAQWLRPLLDGKIRSAFSMTEPAvASSDARNIETTISRDGADYVINGRKWW-TSGaadPRCKILIVMGRTNPDAA 186
Cdd:PLN02519 125 GTPAQKEKYLPKLISGEHVGALAMSEPN-SGSDVVSMKCKAERVDGGYVLNGNKMWcTNG---PVAQTLVVYAKTDVAAG 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 187 AHQQQSMvLVPIDTPGVTIVRSTPVFGWQDRHGhCEIDYHNVRVPATNLLGEEGSGFAIAQARLGPGRIHHCMRALGAAE 266
Cdd:PLN02519 201 SKGITAF-IIEKGMPGFSTAQKLDKLGMRGSDT-CELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQ 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 267 RALALMVNRVRNRVAFGRPLAEQGVVQQAIAQSRNEIDQARLLCEKAAWTIDQhGNKEARHLVAMIKAVAPRvACDVIDR 346
Cdd:PLN02519 279 ACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDN-GKVDRKDCAGVILCAAER-ATQVALQ 356
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 15607296 347 AIQVHGAAGVSDDTPLARLYGWHRAMRIFDGPDEVHLRSIARaELSRE 394
Cdd:PLN02519 357 AIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGR-ELFKE 403
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
108-395 |
3.51e-20 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 91.43 E-value: 3.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 108 GTEQQRAQWLRPLLDGKIRSAFSMTEPAvASSDARNIETTISRDGADYVINGRKWW-TSGAADPrckILIVMGRtNPDAA 186
Cdd:PRK03354 101 GTQEQIDKIMAFRGTGKQMWNSAITEPG-AGSDVGSLKTTYTRRNGKVYLNGSKCFiTSSAYTP---YIVVMAR-DGASP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 187 AHQQQSMVLVPIDTPGVTIVRSTPVFGWQDrhGHCEIDYHNVRVPATNLLGEEGSGFAIAQARLGPGRIHHCMRALGAAE 266
Cdd:PRK03354 176 DKPVYTEWFVDMSKPGIKVTKLEKLGLRMD--SCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAM 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 267 RALALMVNRVRNRVAFGRPLAEQGVVQQAIAQSRNEIDQARLLCEKAAWTID--QHGNKEArhlvAMIKAVAPRVACDVI 344
Cdd:PRK03354 254 CAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADngTITSGDA----AMCKYFCANAAFEVV 329
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 15607296 345 DRAIQVHGAAGVSDDTPLARLYGWHRAMRIFDGPDEVHLRSIARAELSREK 395
Cdd:PRK03354 330 DSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQYR 380
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
257-366 |
2.65e-15 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 71.99 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 257 HCMRALGAAERALALMVNRVRNRV--AFGRPLAEQGVVQQAIAQSRNEIDQARLLCEKAAWTI------DQHGNKEARHL 328
Cdd:pfam08028 2 IAAAALGAARAALAEFTERARGRVraYFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIeaaaaaGKPVTPALRAE 81
|
90 100 110
....*....|....*....|....*....|....*...
gi 15607296 329 VAMIKAVAPRVACDVIDRAIQVHGAAGVSDDTPLARLY 366
Cdd:pfam08028 82 ARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIW 119
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
102-357 |
3.16e-14 |
|
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, which catalyzes the first two steps of DBT desulfurization in mesophilic bacteria. DszC converts DBT to DBT-sulfoxide, which is then converted to DBT-sulfone. Bacteria with this enzyme are candidates for the removal of organic sulfur compounds from fossil fuels, which pollute the environment. An equivalent enzyme tdsC, is found in thermophilic bacteria. This alignment also contains a closely related uncharacterized subgroup.
Pssm-ID: 173852 [Multi-domain] Cd Length: 377 Bit Score: 73.51 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 102 EILHMFGTEQQRAQWLRPLLDGKIrsaFSMTEPAVASSDARNIETTISRDGADYVINGRKWWTSGAADprCKILIVMGRT 181
Cdd:cd01163 81 EALLLAGPEQFRKRWFGRVLNGWI---FGNAVSERGSVRPGTFLTATVRDGGGYVLNGKKFYSTGALF--SDWVTVSALD 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 182 NPDAAAHqqqsmVLVPIDTPGVTIVRSTPVFGwQDRHGHCEIDYHNVRVPATNLLGEEGSGF------AIAQarlgpgrI 255
Cdd:cd01163 156 EEGKLVF-----AAVPTDRPGITVVDDWDGFG-QRLTASGTVTFDNVRVEPDEVLPRPNAPDrgtlltAIYQ-------L 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 256 HHCMRALGAAERALALMVNRVRNRV-AFGRPLAEQGV----VQQAIAQSRNEIDQARLLCEKAAWTIDQHGNK------- 323
Cdd:cd01163 223 VLAAVLAGIARAALDDAVAYVRSRTrPWIHSGAESARddpyVQQVVGDLAARLHAAEALVLQAARALDAAAAAgtaltae 302
|
250 260 270
....*....|....*....|....*....|....*..
gi 15607296 324 ---EARHLVAMIKAVAPRVACDVIDRAIQVHGAAGVS 357
Cdd:cd01163 303 argEAALAVAAAKVVVTRLALDATSRLFEVGGASATA 339
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
46-402 |
3.46e-08 |
|
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: 55.41 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 46 EELKTKAKDRGLWNLFLSAESgltNLEYAPLAE--MTGWSMEIAPEALNcaapdtGNM---EILHMfGTEQQRAQWLRPL 120
Cdd:cd01150 60 EELKRKAKTDVERMGELMADD---PEKMLALTNslGGYDLSLGAKLGLH------LGLfgnAIKNL-GTDEHQDYWLQGA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 121 LDGKIRSAFSMTEPAvASSDARNIETTISRDGA--DYVIN-----GRKWWTSGAADpRCKILIVMGRTNPDAAAHQQQSM 193
Cdd:cd01150 130 NNLEIIGCFAQTELG-HGSNLQGLETTATYDPLtqEFVINtpdftATKWWPGNLGK-TATHAVVFAQLITPGKNHGLHAF 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 194 VlVPI---DT----PGVTIVRSTPVFGWQdrhghcEID-----YHNVRVPATNLLGEEG---------SGFAIAQARLG- 251
Cdd:cd01150 208 I-VPIrdpKThqplPGVTVGDIGPKMGLN------GVDngflqFRNVRIPRENLLNRFGdvspdgtyvSPFKDPNKRYGa 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 252 ------PGRIHHCMRALGAAERALALMVNRVRNRVAFGRPLAEQGV------VQQ---------AIAQSRneidQARLLC 310
Cdd:cd01150 281 mlgtrsGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPKPSDPEVqildyqLQQyrlfpqlaaAYAFHF----AAKSLV 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 311 EKAAWTIDQHGNKEAR-----H-LVAMIKAVAPRVACDVIDRAIQVHGAAGVSDDTPLARLYGWHRAMRIFDGPDEVHLR 384
Cdd:cd01150 357 EMYHEIIKELLQGNSEllaelHaLSAGLKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQ 436
|
410
....*....|....*...
gi 15607296 385 SIARAELSREKSTFAAAV 402
Cdd:cd01150 437 QTANYLLKKYAQAFSLAD 454
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
101-309 |
1.76e-06 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 49.85 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 101 MEILHMFGTEQQRAQWLRPLLDGKIRSAFSMTEPAVASsDARNIETTISRDGADYVINGRKWW--TSGAADprckILIVM 178
Cdd:PLN02526 118 MLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGS-DASSLNTTATKVEGGWILNGQKRWigNSTFAD----VLVIF 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 179 GRTnpdaAAHQQQSMVLVPIDTPGVTIVRSTPVFGWQDRHgHCEIDYHNVRVPATNLLGEEGSgFAIAQARLGPGRIHHC 258
Cdd:PLN02526 193 ARN----TTTNQINGFIVKKGAPGLKATKIENKIGLRMVQ-NGDIVLKDVFVPDEDRLPGVNS-FQDTNKVLAVSRVMVA 266
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15607296 259 MRALGAAERALALMVNRVRNRVAFGRPLAEQGVVQQAIAQSRNEIdQARLL 309
Cdd:PLN02526 267 WQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNI-QAMFL 316
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
14-124 |
5.27e-06 |
|
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: 45.15 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 14 DFMTEHVFGAEADYDdyRRAAGPAdhtappiieELKTKAKDRGLWNLFLSAE---SGLTNLEYAPLAEmtgwsmEIA--- 87
Cdd:pfam02771 13 EFAEEEIAPHAAEWD--EEGEFPR---------ELWKKLGELGLLGITIPEEyggAGLDYLAYALVAE------ELArad 75
|
90 100 110
....*....|....*....|....*....|....*...
gi 15607296 88 -PEALNCAAPDTGNMEILHMFGTEQQRAQWLRPLLDGK 124
Cdd:pfam02771 76 aSVALALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
257-365 |
6.45e-06 |
|
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: 47.73 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 257 HCMRALGAAERALALMVNRVRNRV---AFGRPLAEQGVVQQAIAQSRNEIDQARLLCEKAAWTIDQHG------NKEARH 327
Cdd:cd01159 225 FAAVSLGAAEGALAEFLELAGKRVrqyGAAVKMAEAPITQLRLAEAAAELDAARAFLERATRDLWAHAlaggpiDVEERA 304
|
90 100 110
....*....|....*....|....*....|....*...
gi 15607296 328 LVAMIKAVAPRVACDVIDRAIQVHGAAGVSDDTPLARL 365
Cdd:cd01159 305 RIRRDAAYAAKLSAEAVDRLFHAAGGSALYTASPLQRI 342
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
107-168 |
1.89e-04 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 43.61 E-value: 1.89e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15607296 107 FGTEQQRAQWLRPLLDGKIRSAFSMTEPAvASSDARNIETTISRDGA--DYVIN-----GRKWWTSGAA 168
Cdd:PLN02312 167 LGTKRHHDKWLKDTEDYVVKGCFAMTELG-HGSNVRGIETVTTYDPKteEFVINtpcesAQKYWIGGAA 234
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
40-336 |
2.21e-03 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 40.24 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 40 TAPPIIEELKTKAKDRGLWNLFLSAESGLTNLEYApLAEMTGWSMEIA-PEALNCAAPDTGNMEILHMFGTEQQRAQWLR 118
Cdd:PTZ00456 96 TTPKGFKEAYQALKAGGWTGISEPEEYGGQALPLS-VGFITRELMATAnWGFSMYPGLSIGAANTLMAWGSEEQKEQYLT 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 119 PLLDGKIRSAFSMTEPAvASSDARNIETTISR--DGAdYVINGRKWWTS-GAADPRCKIL-IVMGRTNPDAAAHQQQSMV 194
Cdd:PTZ00456 175 KLVSGEWSGTMCLTEPQ-CGTDLGQVKTKAEPsaDGS-YKITGTKIFISaGDHDLTENIVhIVLARLPNSLPTTKGLSLF 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 195 LVPIDTP----GVTIVRSTPVFGWQDRHG-----HCEIDYHNvrvPATNLLGEEGSGFAIAQARLGPGRIHHCMRALGAA 265
Cdd:PTZ00456 253 LVPRHVVkpdgSLETAKNVKCIGLEKKMGikgssTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHA 329
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15607296 266 ERALALMVNRVRNRVAfgrplaeqgvvQQAIAQSRNEidqarllcEKAAWTIDQHGNkeARHLVAMIKAVA 336
Cdd:PTZ00456 330 ELAFQNALRYARERRS-----------MRALSGTKEP--------EKPADRIICHAN--VRQNILFAKAVA 379
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
235-366 |
5.77e-03 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 38.96 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607296 235 LLGEEGSGFAIAQARLGPGRIHHCMRALGAAERALALMVNRVRNRVAFGRPLAEQGVVQQAIAQSRNEID-QARLLCEKA 313
Cdd:PRK11561 280 LLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQRQVFGKPLIEQPLMRQVLSRMALQLEgQTALLFRLA 359
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 15607296 314 -AWtiDQHGN-KE---ARHLVAMIKAVAPRVACDVIDRAIQVHGAAGVSDDTPLARLY 366
Cdd:PRK11561 360 rAW--DRRADaKEalwARLFTPAAKFVICKRGIPFVAEAMEVLGGIGYCEESELPRLY 415
|
|
| |
