|
Name |
Accession |
Description |
Interval |
E-value |
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
10-402 |
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: 644.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 10 PRGAQLRDELQDLLDTRILPNEATYHEQIEASGDRHH-HPAILEELKAEARERGLWNLFLPDETHGAGLTNLDYAHLAEL 88
Cdd:cd01155 1 RKAQELRARVKAFMEEHVYPAEQEFLEYYAEGGDRWWtPPPIIEKLKAKAKAEGLWNLFLPEVSGLSGLTNLEYAYLAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 89 TGRSVLmAPEALNCAAPDTGNMEVLHMFGTPAQQEEWLTPLLEGEIRSAFFMTEPDVASSDARNIGSRIERDGDEYVING 168
Cdd:cd01155 81 TGRSFF-APEVFNCQAPDTGNMEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDVASSDATNIECSIERDGDDYVING 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 169 RKWWSSGAASPRCKVGIFMGITDPD-ESPYRQQSQILVPMDTPGVRVVRELPVYGRYDGHGGHPEVEFVDVRVPAGNLIG 247
Cdd:cd01155 160 RKWWSSGAGDPRCKIAIVMGRTDPDgAPRHRQQSMILVPMDTPGVTIIRPLSVFGYDDAPHGHAEITFDNVRVPASNLIL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 248 NEGDGFAIAQARLGPGRIHHCMRLIGMAERAFDLMCERALTREPFGRPIADQGVFQHWLAQARVRIEQARLLTLKAARLM 327
Cdd:cd01155 240 GEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMI 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919112682 328 DTVGNKGARMEISAIKIVAPSMAEWVLDKAIQTHGGGGFSDDFVLAQMWAHARTLRMADGPDEVHEMALARRELK 402
Cdd:cd01155 320 DTVGNKAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMELK 394
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
9-405 |
1.02e-163 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 480.06 E-value: 1.02e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 9 SPRGAQLRDELQDLLDTRILPNEATYHEQIEASGDRHHHPAiLEELKAEARERGLWNLFLP------------------- 69
Cdd:PLN02876 403 SEKVLELRKKLIKFMEDHIYPMENEFYKLAQSSSRWTVHPE-EERLKELAKKEGLWNLWIPldsaararkllfednkhmv 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 70 -----DETHGAGLTNLDYAHLAELTGRSVlMAPEALNCAAPDTGNMEVLHMFGTPAQQEEWLTPLLEGEIRSAFFMTEPD 144
Cdd:PLN02876 482 sgdsaDQLLGAGLSNLEYGYLCEIMGRSV-WAPQVFNCGAPDTGNMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQ 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 145 VASSDARNIGSRIERDGDEYVINGRKWWSSGAASPRCKVGIFMGITDPDESPYRQQSQILVPMDTPGVRVVRELPVYGRY 224
Cdd:PLN02876 561 VASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPRCRVLIVMGKTDFNAPKHKQQSMILVDIQTPGVQIKRPLLVFGFD 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 225 DGHGGHPEVEFVDVRVPAGNLIGNEGDGFAIAQARLGPGRIHHCMRLIGMAERAFDLMCERALTREPFGRPIADQGVFQH 304
Cdd:PLN02876 641 DAPHGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLS 720
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 305 WLAQARVRIEQARLLTLKAARLMDTVGNKGARMEISAIKIVAPSMAEWVLDKAIQTHGGGGFSDDFVLAQMWAHARTLRM 384
Cdd:PLN02876 721 DLAKCRVELEQTRLLVLEAADQLDRLGNKKARGIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRI 800
|
410 420
....*....|....*....|.
gi 919112682 385 ADGPDEVHEMALARRELKRYR 405
Cdd:PLN02876 801 ADGPDEVHLGTIAKLELQRAK 821
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
5-405 |
1.30e-121 |
|
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: 357.61 E-value: 1.30e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 5 DLSLSPRGAQLRDELQDLLDTRILPNEAtyheqieasgDRHHHPAILEELKAEARERGLWNLFLPDETHGAGLTNLDYAH 84
Cdd:COG1960 2 DFELTEEQRALRDEVREFAEEEIAPEAR----------EWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 85 LAELTGRSVlmAPEALNCAAPDtGNMEVLHMFGTPAQQEEWLTPLLEGEIRSAFFMTEPDvASSDARNIGSRIERDGDEY 164
Cdd:COG1960 72 VLEELARAD--ASLALPVGVHN-GAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPG-AGSDAAALRTTAVRDGDGY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 165 VINGRKWWSSGAasPRCKVGIFMGITDPDEsPYRQQSQILVPMDTPGVRVVRELPVYG-RYDGHGghpEVEFVDVRVPAG 243
Cdd:COG1960 148 VLNGQKTFITNA--PVADVILVLARTDPAA-GHRGISLFLVPKDTPGVTVGRIEDKMGlRGSDTG---ELFFDDVRVPAE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 244 NLIGNEGDGFAIAQARLGPGRIHHCMRLIGMAERAFDLMCERALTREPFGRPIADQGVFQHWLAQARVRIEQARLLTLKA 323
Cdd:COG1960 222 NLLGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 324 ARLMDTvgNKGARMEISAIKIVAPSMAEWVLDKAIQTHGGGGFSDDFVLAQMWAHARTLRMADGPDEVHEMALARRELKR 403
Cdd:COG1960 302 AWLLDA--GEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGR 379
|
..
gi 919112682 404 YR 405
Cdd:COG1960 380 PG 381
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
106-398 |
7.08e-91 |
|
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: 277.24 E-value: 7.08e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 106 DTGNMEVLHMFGTPAQQEEWLTPLLEGEIRSAFFMTEPDvASSDARNIGSRIERDGDEYVINGRKWWSSGAasPRCKVGI 185
Cdd:cd00567 41 LLLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPG-AGSDLAGIRTTARKDGDGYVLNGRKIFISNG--GDADLFI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 186 FMGITDPDESPYRQQSQILVPMDTPGVRVVRELPVYGryDGHGGHPEVEFVDVRVPAGNLIGNEGDGFAIAQARLGPGRI 265
Cdd:cd00567 118 VLARTDEEGPGHRGISAFLVPADTPGVTVGRIWDKMG--MRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 266 HHCMRLIGMAERAFDLMCERALTREPFGRPIADQGVFQHWLAQARVRIEQARLLTLKAARLMDTvGNKGARMEISAIKIV 345
Cdd:cd00567 196 LLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQ-GPDEARLEAAMAKLF 274
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 919112682 346 APSMAEWVLDKAIQTHGGGGFSDDFVLAQMWAHARTLRMADGPDEVHEMALAR 398
Cdd:cd00567 275 ATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
14-402 |
2.74e-58 |
|
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: 194.41 E-value: 2.74e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 14 QLRDELQDLLDTRILPNEATYheqieasgDRHH--HPAILEELKaearERGLWNLFLPDETHGAGLTNLDYAHLAELTGR 91
Cdd:cd01158 5 MIRKTVRDFAEKEIAPLAAEM--------DEKGefPREVIKEMA----ELGLMGIPIPEEYGGAGLDFLAYAIAIEELAK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 92 ---SVLMAPEALN--CAAPdtgnmevLHMFGTPAQQEEWLTPLLEGEIRSAFFMTEPdVASSDARNIGSRIERDGDEYVI 166
Cdd:cd01158 73 vdaSVAVIVSVHNslGANP-------IIKFGTEEQKKKYLPPLATGEKIGAFALSEP-GAGSDAAALKTTAKKDGDDYVL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 167 NGRKWW--SSGAASprckVGIFMGITDPDESpYRQQSQILVPMDTPGVRVVRELPVYGRydgHG-GHPEVEFVDVRVPAG 243
Cdd:cd01158 145 NGSKMWitNGGEAD----FYIVFAVTDPSKG-YRGITAFIVERDTPGLSVGKKEDKLGI---RGsSTTELIFEDVRVPKE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 244 NLIGNEGDGFAIAQARLGPGRIHHCMRLIGMAERAFDLMCERALTREPFGRPIADQGVFQHWLAQARVRIEQARLLTLKA 323
Cdd:cd01158 217 NILGEEGEGFKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 324 ARLMDtvgNKGARMEISAI-KIVAPSMAEWVLDKAIQTHGGGGFSDDFVLAQMWAHARTLRMADGPDEVHEMALARRELK 402
Cdd:cd01158 297 ARLKD---NGEPFIKEAAMaKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
15-403 |
4.01e-43 |
|
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: 154.52 E-value: 4.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 15 LRDELQDLLDTRILPNEATYHEQieasgdrHHHPAileELKAEARERGLWNLFLPDETHGAGLTNLDYAhlaeltgrsvl 94
Cdd:cd01162 8 IQEVARAFAAKEMAPHAADWDQK-------KHFPV---DVLRKAAELGFGGIYIRDDVGGSGLSRLDAS----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 95 MAPEALNCAAPDTG------NMEV--LHMFGTPAQQEEWLTPLLEGEIRSAFFMTEPDvASSDARNIGSRIERDGDEYVI 166
Cdd:cd01162 67 IIFEALSTGCVSTAayisihNMCAwmIDSFGNDEQRERFLPDLCTMEKLASYCLTEPG-SGSDAAALRTRAVREGDHYVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 167 NGRKWWSSGAASPrcKVGIFMGITDPDESpyRQQSQILVPMDTPGVRvvrelpvYGRYD---GHGGHP--EVEFVDVRVP 241
Cdd:cd01162 146 NGSKAFISGAGDS--DVYVVMARTGGEGP--KGISCFVVEKGTPGLS-------FGANEkkmGWNAQPtrAVIFEDCRVP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 242 AGNLIGNEGDGFAIAQARLGPGRIHHCMRLIGMAERAFDLMCERALTREPFGRPIADQGVFQHWLAQARVRIEQARLLTL 321
Cdd:cd01162 215 VENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 322 KAARLMDTvGNKGARMEISAIKIVAPSMAEWVLDKAIQTHGGGGFSDDFVLAQMWAHARTLRMADGPDEVHEMALARREL 401
Cdd:cd01162 295 RAASALDR-GDPDAVKLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALL 373
|
..
gi 919112682 402 KR 403
Cdd:cd01162 374 TR 375
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
50-404 |
6.02e-41 |
|
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: 149.54 E-value: 6.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 50 ILEELKAEARERGLWNLFLPDETHGAGLTNLDYAHLAELTGR----SVLMApealncAAPDTGNMEVLhMFGTPAQQEEW 125
Cdd:cd01161 57 IPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMdlgfSVTLG------AHQSIGFKGIL-LFGTEAQKEKY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 126 LTPLLEGEIRSAFFMTEPDvASSDARNIGSRIER--DGDEYVINGRKWW-SSGAASPRCKVGIFMGITDPDESPYRQQSQ 202
Cdd:cd01161 130 LPKLASGEWIAAFALTEPS-SGSDAASIRTTAVLseDGKHYVLNGSKIWiTNGGIADIFTVFAKTEVKDATGSVKDKITA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 203 ILVPMDTPGVRVVRE---LPVYGrydghGGHPEVEFVDVRVPAGNLIGNEGDGFAIAQARLGPGRIHHCMRLIGMAERAF 279
Cdd:cd01161 209 FIVERSFGGVTNGPPekkMGIKG-----SNTAEVYFEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCI 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 280 DLMCERALTREPFGRPIADQGVFQHWLAQARVRIEQARLLTLKAARLMDTVGNKGARMEISAIKIVAPSMAEWVLDKAIQ 359
Cdd:cd01161 284 EKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLKAEYQIEAAISKVFASEAAWLVVDEAIQ 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 919112682 360 THGGGGFSDDFVLAQMWAHARTLRMADGPDEVHEMALARRELKRY 404
Cdd:cd01161 364 IHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQHA 408
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
10-401 |
7.27e-40 |
|
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 145.95 E-value: 7.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 10 PRGAQLRDELQDLLDTRILPneatyhEQIEASGDrhHHPAILEELKAEAR---ERGLWNLFLPDETHGAGLTNLDYAHLA 86
Cdd:cd01152 1 PSEEAFRAEVRAWLAAHLPP------ELREESAL--GYREGREDRRRWQRalaAAGWAAPGWPKEYGGRGASLMEQLIFR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 87 ELTGRSvlmapealncAAPDTGNMEVLHM-------FGTPAQQEEWLTPLLEGEIRSAFFMTEPDvASSDARNIGSRIER 159
Cdd:cd01152 73 EEMAAA----------GAPVPFNQIGIDLagptilaYGTDEQKRRFLPPILSGEEIWCQGFSEPG-AGSDLAGLRTRAVR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 160 DGDEYVINGRKWWSSGAASPRCKVGIFMgiTDPDESPYRQQSQILVPMDTPGVRV--VRELpvygryDGHGGHPEVEFVD 237
Cdd:cd01152 142 DGDDWVVNGQKIWTSGAHYADWAWLLVR--TDPEAPKHRGISILLVDMDSPGVTVrpIRSI------NGGEFFNEVFLDD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 238 VRVPAGNLIGNEGDGFAIAQARLGPGRihhcMRLIGMAERAFDLMCERALTREPFGRPIADQGVFQHWLAQARVRIEQAR 317
Cdd:cd01152 214 VRVPDANRVGEVNDGWKVAMTTLNFER----VSIGGSAATFFELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 318 LLTLKAARLMDTVGNKGArmEISAIKIVAPSMAEWVLDKAIQTHG----GGGFSDDFVLAQMWA----HARTLRMADGPD 389
Cdd:cd01152 290 LLVFRLASALAAGKPPGA--EASIAKLFGSELAQELAELALELLGtaalLRDPAPGAELAGRWEadylRSRATTIYGGTS 367
|
410
....*....|..
gi 919112682 390 EVHEMALARREL 401
Cdd:cd01152 368 EIQRNIIAERLL 379
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
15-399 |
2.95e-39 |
|
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: 144.18 E-value: 2.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 15 LRDELQDLLDTRILPneatYHEQIEASGDrhhhpaILEELKAEARERGLWNLFLPDETHGAGLTNLDYAHLAELTGRSvl 94
Cdd:cd01160 6 FRDVVRRFFAKEVAP----FHHEWEKAGE------VPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 95 mapealNCAAP------DTGnMEVLHMFGTPAQQEEWLTPLLEGEIRSAFFMTEPDvASSDARNIGSRIERDGDEYVING 168
Cdd:cd01160 74 ------GGSGPglslhtDIV-SPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPG-AGSDLQGIRTTARKDGDHYVLNG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 169 RKWW-SSGAaspRCKVGIFMGITDPDESPYRQQSQILVPMDTPGVRVVRELPVYGRYDGHGGhpEVEFVDVRVPAGNLIG 247
Cdd:cd01160 146 SKTFiTNGM---LADVVIVVARTGGEARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTA--ELFFDDCRVPAENLLG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 248 NEGDGFAIAQARLGPGRIHHCMRLIGMAERAFDLMCERALTREPFGRPIADQGVFQHWLAQARVRIEQAR-----LLTLK 322
Cdd:cd01160 221 EENKGFYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRafldnCAWRH 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919112682 323 AARLMDTVgnkgarmEISAIKIVAPSMAEWVLDKAIQTHGGGGFSDDFVLAQMWAHARTLRMADGPDEVHEMALARR 399
Cdd:cd01160 301 EQGRLDVA-------EASMAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQ 370
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
250-399 |
2.24e-38 |
|
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: 135.46 E-value: 2.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 250 GDGFAIAQARLGPGRIHHCMRLIGMAERAFDLMCERALTREPFGRPIADQGVFQHWLAQARVRIEQARLLTLKAARLMDT 329
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 330 vgNKGARMEISAIKIVAPSMAEWVLDKAIQTHGGGGFSDDFVLAQMWAHARTLRMADGPDEVHEMALARR 399
Cdd:pfam00441 81 --GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARR 148
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
27-403 |
1.08e-37 |
|
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: 140.03 E-value: 1.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 27 ILPNEATYHEqieaSGDrhhHPAileELKAEARERGLWNLFLPDETHGAGLTNLDYAHLAE-----LTGrsVLMAPEAln 101
Cdd:cd01157 20 IIPVAAEYDK----SGE---YPW---PLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEelaygCTG--VQTAIEA-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 102 caaPDTGNMEVLhMFGTPAQQEEWLTPLLEGEIRSAFFMTEPDvASSDARNIGSRIERDGDEYVINGRKWWSSGAAspRC 181
Cdd:cd01157 86 ---NSLGQMPVI-ISGNDEQKKKYLGRMTEEPLMCAYCVTEPG-AGSDVAGIKTKAEKKGDEYIINGQKMWITNGG--KA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 182 KVGIFMGITDPDES--PYRQQSQILVPMDTPGVRVVR-ELPVYGRYDGHGGhpeVEFVDVRVPAGNLIGNEGDGFAIAQA 258
Cdd:cd01157 159 NWYFLLARSDPDPKcpASKAFTGFIVEADTPGIQPGRkELNMGQRCSDTRG---ITFEDVRVPKENVLIGEGAGFKIAMG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 259 RLGPGRIHHCMRLIGMAERAFDLMCERALTREPFGRPIADQGVFQHWLAQARVRIEQARLLTLKAARLMDTvgnkGARME 338
Cdd:cd01157 236 AFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDS----GRRNT 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919112682 339 ISA--IKIVAPSMAEWVLDKAIQTHGGGGFSDDFVLAQMWAHARTLRMADGPDEVHEMALARRELKR 403
Cdd:cd01157 312 YYAsiAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
14-398 |
5.01e-33 |
|
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: 127.53 E-value: 5.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 14 QLRDELQDLLDTRILPneatYHEQIeasgDRHHHpaILEELKAEARERGLWNLFLPDETHGAGLTNLDYAHLAELTGRSV 93
Cdd:cd01156 8 MLRQSVREFAQKEIAP----LAAKI----DRDNE--FPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRAS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 94 lmAPEALNCAAPDTGNMEVLHMFGTPAQQEEWLTPLLEGEIRSAFFMTEPDvASSDARNIGSRIERDGDEYVINGRKWWS 173
Cdd:cd01156 78 --GSVALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPN-AGSDVVSMKLRAEKKGDRYVLNGSKMWI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 174 SGAasPRCKVGIFMGITDPDESPyRQQSQILVPMDTPGVRVVRELPVYGRYDGHGGhpEVEFVDVRVPAGNLIGNEGDGF 253
Cdd:cd01156 155 TNG--PDADTLVVYAKTDPSAGA-HGITAFIVEKGMPGFSRAQKLDKLGMRGSNTC--ELVFEDCEVPEENILGGENKGV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 254 AIAQARLGPGRIHHCMRLIGMAERAFDLMCERALTREPFGRPIADQGVFQHWLAQARVRIEQARLLTLKAARLMDTvGNK 333
Cdd:cd01156 230 YVLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDR-GNM 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919112682 334 GARMEISAIKIVAPSmAEWVLDKAIQTHGGGGFSDDFVLAQMWAHARTLRMADGPDEVHEMALAR 398
Cdd:cd01156 309 DPKDAAGVILYAAEK-ATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGR 372
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
3-398 |
1.23e-27 |
|
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: 112.84 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 3 DLDLSLSPRGAQLRDELQDLLDTRILPNEATYHEqieasgDRHHHPAILEELKaearERGLwnLFLPDETHG-AGLTNLD 81
Cdd:cd01151 8 NLDDLLTEEERAIRDTAREFCQEELAPRVLEAYR------EEKFDRKIIEEMG----ELGL--LGATIKGYGcAGLSSVA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 82 YAhlaeLTGRSVLMAPEALNCAAPDTGN--MEVLHMFGTPAQQEEWLTPLLEGEIRSAFFMTEPDvASSDARNIGSRIER 159
Cdd:cd01151 76 YG----LIAREVERVDSGYRSFMSVQSSlvMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPN-HGSDPGGMETRARK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 160 DGDEYVINGRKWWSSGaaSPRCKVGIFMGITDPDespyrqqSQI---LVPMDTPGVRVVRELPVYGRYDGHGGHpeVEFV 236
Cdd:cd01151 151 DGGGYKLNGSKTWITN--SPIADVFVVWARNDET-------GKIrgfILERGMKGLSAPKIQGKFSLRASITGE--IVMD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 237 DVRVPAGNLI----GNEGDGFAIAQARLGPGRIhhcmrLIGMAERAFDLMCERALTREPFGRPIADQGVFQHWLAQARVR 312
Cdd:cd01151 220 NVFVPEENLLpgaeGLRGPFKCLNNARYGIAWG-----ALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 313 IEQARLLTLKAARLMDTVgnKGARMEISAIKIVAPSMAEWVLDKAIQTHGGGGFSDDFVLAQMWAHARTLRMADGPDEVH 392
Cdd:cd01151 295 IALGLLACLRVGRLKDQG--KATPEQISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIH 372
|
....*.
gi 919112682 393 EMALAR 398
Cdd:cd01151 373 ALILGR 378
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
118-402 |
1.44e-26 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 110.03 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 118 TPAQQEEWLTPLLEGEIRSAFFMTEPDvASSDARNIGSRIERDGDE-YVINGRKWW-SSGAASprckvGIFMGITDPDEs 195
Cdd:PTZ00461 135 SPAQRARWLPKVLTGEHVGAMGMSEPG-AGTDVLGMRTTAKKDSNGnYVLNGSKIWiTNGTVA-----DVFLIYAKVDG- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 196 pyrQQSQILVPMDTPGVRVVRELPVYGRYDGHggHPEVEFVDVRVPAGNLIGNEGDGFAIAQARLGPGRIHHCMRLIGMA 275
Cdd:PTZ00461 208 ---KITAFVVERGTKGFTQGPKIDKCGMRASH--MCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIA 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 276 ERAFDLMCERALTREPFGRPIADQGVFQHWLAQARVRIEQARLLTLKAARLMDTvGNKGaRMEISAIKIVAPSMAEWVLD 355
Cdd:PTZ00461 283 ERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHP-GNKN-RLGSDAAKLFATPIAKKVAD 360
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 919112682 356 KAIQTHGGGGFSDDFVLAQMWAHARTLRMADGPDEVHEMALARRELK 402
Cdd:PTZ00461 361 SAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLK 407
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
15-405 |
4.94e-26 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 107.89 E-value: 4.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 15 LRDELQDLLDT--RILPNEATyHEQIEASGDRHHHPailEELKAEARERGLWNLFLPDETHGaglTNLDYAHLaeltgrs 92
Cdd:PRK12341 5 LTEEQELLLASirELITRNFP-EEYFRTCDENGTYP---REFMRALADNGISMLGVPEEFGG---TPADYVTQ------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 93 VLMAPEALNCAAPD--TGNMEVLH---MFGTPAQQEEWLTPLLE-GEIRSAFFMTEPDVASSDARNIGSRIERDGDEYvI 166
Cdd:PRK12341 71 MLVLEEVSKCGAPAflITNGQCIHsmrRFGSAEQLRKTAESTLEtGDPAYALALTEPGAGSDNNSATTTYTRKNGKVY-L 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 167 NGRKWWSSGAA-SPRCkvgIFMGITDPDESPYRQQSQILVPMDTPGVRV--VRELpvygrydghGGHP----EVEFVDVR 239
Cdd:PRK12341 150 NGQKTFITGAKeYPYM---LVLARDPQPKDPKKAFTLWWVDSSKPGIKInpLHKI---------GWHMlstcEVYLDNVE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 240 VPAGNLIGNEGDGFAIAQARLGPGRIHHCMRLIGMAERAFDLMCERALTREPFGRPIADQGVFQHWLAQARVRIEQARLL 319
Cdd:PRK12341 218 VEESDLVGEEGMGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNM 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 320 TLKAARLMDtvgnKGARMEISA--IKIVAPSMAEWVLDKAIQTHGGGGFSDDFVLAQMWAHARTLRMADGPDEVHEMALA 397
Cdd:PRK12341 298 VYKVAWQAD----NGQSLRTSAalAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAG 373
|
....*...
gi 919112682 398 RRELKRYR 405
Cdd:PRK12341 374 RQILKDYQ 381
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
117-402 |
3.03e-21 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 94.56 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 117 GTPAQQEEWLTPLLEGEIRSAFFMTEPDvASSDARNIGSRIERDGDEYVINGRKWWSSGAasPRCKVGIFMGITDPDESP 196
Cdd:PLN02519 125 GTPAQKEKYLPKLISGEHVGALAMSEPN-SGSDVVSMKCKAERVDGGYVLNGNKMWCTNG--PVAQTLVVYAKTDVAAGS 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 197 yRQQSQILVPMDTPGVRVVRELPVYGRydgHGGHP-EVEFVDVRVPAGNLIGNEGDGFAIAQARLGPGRIHHCMRLIGMA 275
Cdd:PLN02519 202 -KGITAFIIEKGMPGFSTAQKLDKLGM---RGSDTcELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLM 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 276 ERAFDLMCERALTREPFGRPIADQGVFQHWLAQARVRIEQARLLTLKAARLMDTvgNKGARMEISAIKIVAPSMAEWVLD 355
Cdd:PLN02519 278 QACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDN--GKVDRKDCAGVILCAAERATQVAL 355
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 919112682 356 KAIQTHGGGGFSDDFVLAQMWAHARTLRMADGPDEVHEMALARRELK 402
Cdd:PLN02519 356 QAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFK 402
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
17-401 |
7.65e-21 |
|
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: 93.61 E-value: 7.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 17 DELQDLLDTRILP-NEATYHEQIEASGDRHHHPAILEELKAEARERGLWNLFLPDETHGAGLTNLDYAHLAELTGRSV-- 93
Cdd:cd01153 3 EEVARLAENVLAPlNADGDREGPVFDDGRVVVPPPFKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDap 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 94 LMAPEALncaapdTGNMEVLHMFGTPAQQEEWLTPLLEGEIRSAFFMTEPDvASSDARNIGSRIERDGD-EYVINGRKWW 172
Cdd:cd01153 83 LMYASGT------QGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPD-AGSDLGALRTKAVYQADgSWRINGVKRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 173 SSGAASPRCKVGIFMGITDPDESP--YRQQSQILVP-----MDTPGVRVVR-ELPVygrydGHGGHP--EVEFVDVRVPa 242
Cdd:cd01153 156 ISAGEHDMSENIVHLVLARSEGAPpgVKGLSLFLVPkflddGERNGVTVARiEEKM-----GLHGSPtcELVFDNAKGE- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 243 gnLIGNEGDGFA-----IAQARLGPGrihhcMRLIGMAERAFDLMCERALTREPFGRP--------IADQGVFQHWLAQA 309
Cdd:cd01153 230 --LIGEEGMGLAqmfamMNGARLGVG-----TQGTGLAEAAYLNALAYAKERKQGGDLikaapavtIIHHPDVRRSLMTQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 310 RVRIEQARLLTLKAARLMD----TVGNKGARMEISAIK-----IVAPSMAEWVLDK---AIQTHGGGGFSDDFVLAQMWA 377
Cdd:cd01153 303 KAYAEGSRALDLYTATVQDlaerKATEGEDRKALSALAdlltpVVKGFGSEAALEAvsdAIQVHGGSGYTREYPIEQYYR 382
|
410 420
....*....|....*....|....
gi 919112682 378 HARTLRMADGPDEVHEMALARREL 401
Cdd:cd01153 383 DARITTIYEGTTGIQALDLIGRKI 406
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
119-396 |
1.14e-19 |
|
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: 90.12 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 119 PAQQEEWLTPLLEGEIR----SAFFMTEPDvASSDARNIGSRIERD-GDEYVINGRKWWSSGAASprckvGIFMGITDPD 193
Cdd:cd01154 128 PEELKQYLPGLLSDRYKtgllGGTWMTEKQ-GGSDLGANETTAERSgGGVYRLNGHKWFASAPLA-----DAALVLARPE 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 194 ESP--YRQQSQILVPMDTP-----GVRVVRELPVYGRYDGHGGhpEVEFVDVrvpAGNLIGNEGDGFAIAQARLGPGRIH 266
Cdd:cd01154 202 GAPagARGLSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATG--EVEFDDA---EAYLIGDEGKGIYYILEMLNISRLD 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 267 HCMRLIGMAERAFDLMCERALTREPFGRPIADQGVFQHWLAQARVRIEQARLLTLKAARLMD-TVGNKG-----ARMEIS 340
Cdd:cd01154 277 NAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDrAAADKPveahmARLATP 356
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 919112682 341 AIKIVAPSMAEWVLDKAIQTHGGGGFSDDFVLAQMWAHARTLRMADGPDEVheMAL 396
Cdd:cd01154 357 VAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNI--QAL 410
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
31-405 |
1.34e-18 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 86.81 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 31 EATYHEQIEasgdRHHHPailEELKAEARERGLWNLFLPDETHGAGLTNLDYAHLAELTGRsvLMAPEALNCAAPdtGNM 110
Cdd:PRK03354 26 EAYFAECDR----DSVYP---ERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGR--LGAPTYVLYQLP--GGF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 111 EVLHMFGTPAQQEEWLTPLLEGEIRSAFFMTEPDvASSDARNIGSRIERDGDEYVINGRKWWSSGAASPRCKVGIFMGIT 190
Cdd:PRK03354 95 NTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPG-AGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 191 DPDESPYrqqSQILVPMDTPGVRVvRELPVYG-RYDGHGghpEVEFVDVRVPAGNLIGNEGDGFAIAQARLGPGRIHHCM 269
Cdd:PRK03354 174 SPDKPVY---TEWFVDMSKPGIKV-TKLEKLGlRMDSCC---EITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 270 RLIGMAERAFDLMCERALTREPFGRPIADQGVFQHWLAQARVRIEQARLLTLKAARLMDTvGNKGaRMEISAIKIVAPSM 349
Cdd:PRK03354 247 TNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADN-GTIT-SGDAAMCKYFCANA 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 919112682 350 AEWVLDKAIQTHGGGGFSDDFVLAQMWAHARTLRMADGPDEVHEMALARRELKRYR 405
Cdd:PRK03354 325 AFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQYR 380
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
137-235 |
1.22e-17 |
|
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: 77.32 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 137 AFFMTEPDvASSDARNIGSR-IERDGDEYVINGRKWWSSGAasPRCKVGIFMGITDPDEsPYRQQSQILVPMDTPGVRVV 215
Cdd:pfam02770 1 AFALTEPG-AGSDVASLKTTaADGDGGGWVLNGTKWWITNA--GIADLFLVLARTGGDD-RHGGISLFLVPKDAPGVSVR 76
|
90 100
....*....|....*....|
gi 919112682 216 RELPVYGrYDGHgGHPEVEF 235
Cdd:pfam02770 77 RIETKLG-VRGL-PTGELVF 94
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
267-384 |
6.85e-13 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 65.44 E-value: 6.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 267 HCMRLIGMAERAFDLMCERALTREP--FGRPIADQGVFQHWLAQARVRIEQARLLTLKAARLMDTVGNKGA------RME 338
Cdd:pfam08028 2 IAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAAAGKpvtpalRAE 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 919112682 339 ISAIKIVAPSMAEWVLDKAIQTHGGGGFSDDFVLAQMWAHARTLRM 384
Cdd:pfam08028 82 ARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQ 127
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
14-133 |
6.66e-12 |
|
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: 61.71 E-value: 6.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 14 QLRDELQDLLDTRILPNEATYHEqieasgdRHHHPAileELKAEARERGLWNLFLPDETHGAGLTNLDYAHLAELTGRSV 93
Cdd:pfam02771 6 ALRDTVREFAEEEIAPHAAEWDE-------EGEFPR---ELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARAD 75
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 919112682 94 lmAPEALNCAAPDTGNMEVLHMFGTPAQQEEWLTPLLEGE 133
Cdd:pfam02771 76 --ASVALALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
53-338 |
2.80e-11 |
|
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: 64.65 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 53 ELKAEARERGLWNLFLPDETHGAGLTNLDYAHL-AELTG--RSVLMAPEAlncaapDTGNMEVLHMFGTPAQQEEWLTPL 129
Cdd:cd01163 26 EEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVvRELAAadSNIAQALRA------HFGFVEALLLAGPEQFRKRWFGRV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 130 LEGEIRSAFfMTEPDVASSDARNIgsRIERDGDEYVINGRKWWSSGAAsprckVGIFMGITDPDESpyRQQSQILVPMDT 209
Cdd:cd01163 100 LNGWIFGNA-VSERGSVRPGTFLT--ATVRDGGGYVLNGKKFYSTGAL-----FSDWVTVSALDEE--GKLVFAAVPTDR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 210 PGVRVVRELPVYG-RYDGHGghpEVEFVDVRVPAGNLIGNEGDGF------AIAQarlgpgrIHHCMRLIGMAERAFDLM 282
Cdd:cd01163 170 PGITVVDDWDGFGqRLTASG---TVTFDNVRVEPDEVLPRPNAPDrgtlltAIYQ-------LVLAAVLAGIARAALDDA 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919112682 283 CERALTRepfGRPIADQGVFQHW--------LAQARVRIEQARLLTLKAARLMDTVGNKGARME 338
Cdd:cd01163 240 VAYVRSR---TRPWIHSGAESARddpyvqqvVGDLAARLHAAEALVLQAARALDAAAAAGTALT 300
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
39-337 |
1.77e-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: 49.65 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 39 EASGDRHHHPAILEELkaeaRERGLWNLFLPDETHGAGLTNLDY----AHLAELTGRSVLMApeALNCAAPdtgnmEVLH 114
Cdd:cd01159 16 EAERARRLPDEVVRAL----REIGFFRMFVPKRYGGLEGDFAEFaeaiATLAEACGSAAWVA--SIVATHS-----RMLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 115 MFGTPAQQEewltpllegeirsaFFMTEPDVASSDARNIGSRIERDGDEYVINGRKWWSSGAASPRCKVGIFMgITDPDE 194
Cdd:cd01159 85 AFPPEAQEE--------------VWGDGPDTLLAGSYAPGGRAERVDGGYRVSGTWPFASGCDHADWILVGAI-VEDDDG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 195 SPY-------RQQSQILVPMDTPGVRvvrelpvygrydGHGGHpEVEFVDVRVPAGNLIgnEGDGFAIAQARLGPGRIH- 266
Cdd:cd01159 150 GPLprafvvpRAEYEIVDTWHVVGLR------------GTGSN-TVVVDDVFVPEHRTL--TAGDMMAGDGPGGSTPVYr 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 267 ----------HCMRLIGMAERAFDLMCERALTR---EPFGRPIADQGVFQHWLAQARVRIEQARLLTLKAARLMDTVGNK 333
Cdd:cd01159 215 mplrqvfplsFAAVSLGAAEGALAEFLELAGKRvrqYGAAVKMAEAPITQLRLAEAAAELDAARAFLERATRDLWAHALA 294
|
....
gi 919112682 334 GARM 337
Cdd:cd01159 295 GGPI 298
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
119-369 |
8.82e-05 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 44.74 E-value: 8.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 119 PAQQEEWLTPLLE----------GEIRSAFF---MTEPDvASSDARNIGSRIER-DGDEYVINGRKWWSSgaaSPRCKVG 184
Cdd:PRK11561 150 PAPFQDWLTPLLSdrydshllpgGQKRGLLIgmgMTEKQ-GGSDVLSNTTRAERlADGSYRLVGHKWFFS---VPQSDAH 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 185 IFMGITDPDESPYrqqsqiLVPMDTP-----GVRVVRELPVYGRYDGHGGhpEVEFVDVrvpAGNLIGNEGDGFAIAQAR 259
Cdd:PRK11561 226 LVLAQAKGGLSCF------FVPRFLPdgqrnAIRLERLKDKLGNRSNASS--EVEFQDA---IGWLLGEEGEGIRLILKM 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 260 LGPGRIHHCMRLIGMAERAFDLMCERALTREPFGRPIADQGVFQHWLAQARVRIEQARLLTLKAARLMDTVGNKG----A 335
Cdd:PRK11561 295 GGMTRFDCALGSHGLMRRAFSVAIYHAHQRQVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDRRADAKealwA 374
|
250 260 270
....*....|....*....|....*....|....*....
gi 919112682 336 RMEISAIKIV-----APSMAEwvldkAIQTHGGGGFSDD 369
Cdd:PRK11561 375 RLFTPAAKFVickrgIPFVAE-----AMEVLGGIGYCEE 408
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
13-365 |
3.96e-04 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 42.64 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 13 AQLRDELQDLLDtrilpNE-ATYHEQI---EASGDRHHHPailEELKAEARERGLWNLFLPDETHGAGLTNldYAH---L 85
Cdd:PRK13026 76 PTLTAEEQAFID-----NEvETLLTMLddwDIVQNRKDLP---PEVWDYLKKEGFFALIIPKEYGGKGFSA--YANstiV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 86 AELTGRSV-----LMAPEALncaapdtGNMEVLHMFGTPAQQEEWLTPLLEGEIRSAFFMTEPDvASSDARNIGS----- 155
Cdd:PRK13026 146 SKIATRSVsaavtVMVPNSL-------GPGELLTHYGTQEQKDYWLPRLADGTEIPCFALTGPE-AGSDAGAIPDtgivc 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 156 RIERDGDEYV---INGRKWWSSGAasPRCKV-GIFMGITDPDeSPYRQQSQI-----LVPMDTPGVRV-VRELP------ 219
Cdd:PRK13026 218 RGEFEGEEVLglrLTWDKRYITLA--PVATVlGLAFKLRDPD-GLLGDKKELgitcaLIPTDHPGVEIgRRHNPlgmafm 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 220 ---VYGRydghgghpevefvDVRVPAGNLIG---NEGDGFAIAQARLGPGR-IHHCMRLIGMAERAFDLMCERALTREPF 292
Cdd:PRK13026 295 ngtTRGK-------------DVFIPLDWIIGgpdYAGRGWRMLVECLSAGRgISLPALGTASGHMATRTTGAYAYVRRQF 361
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919112682 293 GRPIAD-QGVfqhwlAQARVRIeQARLLTLKAARLMDTVG-NKGARMEI-SAI-KIVAPSMAEWVLDKAIQTHGGGG 365
Cdd:PRK13026 362 GMPIGQfEGV-----QEALARI-AGNTYLLEAARRLTTTGlDLGVKPSVvTAIaKYHMTELARDVVNDAMDIHAGKG 432
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
59-153 |
2.70e-03 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 39.80 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919112682 59 RERGLWNLFLPDETHGAGLTNldYAH---LAELTGRSVL-----MAPEALncaapdtGNMEVLHMFGTPAQQEEWLTPLL 130
Cdd:PRK09463 119 KEHGFFGMIIPKEYGGLEFSA--YAHsrvLQKLASRSGTlavtvMVPNSL-------GPGELLLHYGTDEQKDHYLPRLA 189
|
90 100
....*....|....*....|...
gi 919112682 131 EGEIRSAFFMTEPDvASSDARNI 153
Cdd:PRK09463 190 RGEEIPCFALTSPE-AGSDAGSI 211
|
|
| |
