|
Name |
Accession |
Description |
Interval |
E-value |
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
7-392 |
2.15e-149 |
|
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: 428.73 E-value: 2.15e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 7 PELEDLLRRAREFMEAEVYPLE-------AAARQSFEEVLPAANDAREKCKAAGLWAPQMPTEYGGMGLGFLPHAHMSET 79
Cdd:cd01155 1 RKAQELRARVKAFMEEHVYPAEqefleyyAEGGDRWWTPPPIIEKLKAKAKAEGLWNLFLPEVSGLSGLTNLEYAYLAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 80 LGRSPMGHYVFGCQAPDAGNMEILHKFGTDPQKARWLQPLAAGEIRSCFSMTEPDRAGSNPTWMDTTAVRDGDDYVINGR 159
Cdd:cd01155 81 TGRSFFAPEVFNCQAPDTGNMEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDVASSDATNIECSIERDGDDYVINGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 160 KWFTTGGHLAD--FAIVMAVTNPD-APPHMRASQIIVPTDNPGFHHIRRLSImgdvgYGWQS----HSEIAYEDCRVPVE 232
Cdd:cd01155 161 KWWSSGAGDPRckIAIVMGRTDPDgAPRHRQQSMILVPMDTPGVTIIRPLSV-----FGYDDaphgHAEITFDNVRVPAS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 233 NLLGQEGFGFSIAQERLGPGRIHHCMRWLGICERAFDLMCERASRRmVAPKRPLGAQQAIQHWIAESRAEIDSGRLMVYQ 312
Cdd:cd01155 236 NLILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSR-EAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 313 AAWKIDREGTRAARSEISAIKFLVAGILQQVVDRAIQVHGGLGMTDDTPLAWFFRHERAARIYDGPDEVHKSALARAILK 392
Cdd:cd01155 315 AAHMIDTVGNKAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMELK 394
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
1-395 |
1.60e-133 |
|
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: 387.66 E-value: 1.60e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 1 MDFSTPPELEDLLRRAREFMEAEVYPLEAAARQsfEEVLPAanDAREKCKAAGLWAPQMPTEYGGMGLGFLPHAHMSETL 80
Cdd:COG1960 1 MDFELTEEQRALRDEVREFAEEEIAPEAREWDR--EGEFPR--ELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 81 GRSPMGhYVFGCQAPDaGNMEILHKFGTDPQKARWLQPLAAGEIRSCFSMTEPDrAGSNPTWMDTTAVRDGDDYVINGRK 160
Cdd:COG1960 77 ARADAS-LALPVGVHN-GAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPG-AGSDAAALRTTAVRDGDGYVLNGQK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 161 WFTTGGHLADFAIVMAVTNPDAPPHmRASQIIVPTDNPGFHHIRRLSIMGDVGygwQSHSEIAYEDCRVPVENLLGQEGF 240
Cdd:COG1960 154 TFITNAPVADVILVLARTDPAAGHR-GISLFLVPKDTPGVTVGRIEDKMGLRG---SDTGELFFDDVRVPAENLLGEEGK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 241 GFSIAQERLGPGRIHHCMRWLGICERAFDLMCERASRRmVAPKRPLGAQQAIQHWIAESRAEIDSGRLMVYQAAWKIDRE 320
Cdd:COG1960 230 GFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYARER-EQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAG 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490518557 321 gtRAARSEISAIKFLVAGILQQVVDRAIQVHGGLGMTDDTPLAWFFRHERAARIYDGPDEVHKSALARAILKKYG 395
Cdd:COG1960 309 --EDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
7-388 |
2.51e-102 |
|
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: 306.13 E-value: 2.51e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 7 PELEDLLRRAREFMEAEVYPLEAAARQSFEEvlpaandAREKCKAAGLWapqmpteyggmglgflphahmsetlgrspmg 86
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEE-------PWELLAELGLL------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 87 hyvfgcqapdaGNMEILHKFGTDPQKARWLQPLAAGEIRSCFSMTEPDrAGSNPTWMDTTAVRDGDDYVINGRKWFTTGG 166
Cdd:cd00567 43 -----------LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPG-AGSDLAGIRTTARKDGDGYVLNGRKIFISNG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 167 HLADFAIVMAVTNPDAPPHMRASQIIVPTDNPGFHHIRRLSIMGDVGygwQSHSEIAYEDCRVPVENLLGQEGFGFSIAQ 246
Cdd:cd00567 111 GDADLFIVLARTDEEGPGHRGISAFLVPADTPGVTVGRIWDKMGMRG---SGTGELVFDDVRVPEDNLLGEEGGGFELAM 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 247 ERLGPGRIHHCMRWLGICERAFDLMCERASRRmVAPKRPLGAQQAIQHWIAESRAEIDSGRLMVYQAAWKIDrEGTRAAR 326
Cdd:cd00567 188 KGLNVGRLLLAAVALGAARAALDEAVEYAKQR-KQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLD-QGPDEAR 265
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490518557 327 SEISAIKFLVAGILQQVVDRAIQVHGGLGMTDDTPLAWFFRHERAARIYDGPDEVHKSALAR 388
Cdd:cd00567 266 LEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
3-393 |
9.66e-95 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 301.33 E-value: 9.66e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 3 FSTPPELEDLLRRAREFMEAEVYPLEA-----AARQSFEEVLPAANDAREKCKAAGLWAPQMPTEYG------------- 64
Cdd:PLN02876 400 FVPSEKVLELRKKLIKFMEDHIYPMENefyklAQSSSRWTVHPEEERLKELAKKEGLWNLWIPLDSAararkllfednkh 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 65 -----------GMGLGFLPHAHMSETLGRSPMGHYVFGCQAPDAGNMEILHKFGTDPQKARWLQPLAAGEIRSCFSMTEP 133
Cdd:PLN02876 480 mvsgdsadqllGAGLSNLEYGYLCEIMGRSVWAPQVFNCGAPDTGNMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEP 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 134 DRAGSNPTWMDTTAVRDGDDYVINGRKWFTTGGH--LADFAIVMAVTNPDAPPHMRASQIIVPTDNPGFHHIRRLSIMG- 210
Cdd:PLN02876 560 QVASSDATNIECSIRRQGDSYVINGTKWWTSGAMdpRCRVLIVMGKTDFNAPKHKQQSMILVDIQTPGVQIKRPLLVFGf 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 211 -DVGYGwqsHSEIAYEDCRVPVENLLGQEGFGFSIAQERLGPGRIHHCMRWLGICERAFDLMCERASRRMVAPKRpLGAQ 289
Cdd:PLN02876 640 dDAPHG---HAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAFGKL-IAQH 715
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 290 QAIQHWIAESRAEIDSGRLMVYQAAWKIDREGTRAARSEISAIKFLVAGILQQVVDRAIQVHGGLGMTDDTPLAWFFRHE 369
Cdd:PLN02876 716 GSFLSDLAKCRVELEQTRLLVLEAADQLDRLGNKKARGIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATA 795
|
410 420
....*....|....*....|....
gi 1490518557 370 RAARIYDGPDEVHKSALARAILKK 393
Cdd:PLN02876 796 RTLRIADGPDEVHLGTIAKLELQR 819
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
7-392 |
3.65e-76 |
|
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: 240.63 E-value: 3.65e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 7 PELEDLLRRAREFMEAEVYPLeaAARQSFEEVLPAanDAREKCKAAGLWAPQMPTEYGGMGLGFLPHAHMSETLGRSPMG 86
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPL--AAEMDEKGEFPR--EVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 87 HYVFGCQAPDAGNMEILhKFGTDPQKARWLQPLAAGEIRSCFSMTEPDrAGSNPTWMDTTAVRDGDDYVINGRK-WFTTG 165
Cdd:cd01158 77 VAVIVSVHNSLGANPII-KFGTEEQKKKYLPPLATGEKIGAFALSEPG-AGSDAAALKTTAKKDGDDYVLNGSKmWITNG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 166 GHlADFAIVMAVTNPDAPPHmRASQIIVPTDNPGFHHIRRLSIMGDVGygwQSHSEIAYEDCRVPVENLLGQEGFGFSIA 245
Cdd:cd01158 155 GE-ADFYIVFAVTDPSKGYR-GITAFIVERDTPGLSVGKKEDKLGIRG---SSTTELIFEDVRVPKENILGEEGEGFKIA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 246 QERLGPGRIHHCMRWLGICERAFDLMCERASRRMvAPKRPLGAQQAIQHWIAESRAEIDSGRLMVYQAAWKIDRegtRAA 325
Cdd:cd01158 230 MQTLDGGRIGIAAQALGIAQAALDAAVDYAKERK-QFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDN---GEP 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490518557 326 RSEISAIKFLVAG-ILQQVVDRAIQVHGGLGMTDDTPLAWFFRHERAARIYDGPDEVHKSALARAILK 392
Cdd:cd01158 306 FIKEAAMAKLFASeVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
11-391 |
1.96e-64 |
|
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: 210.43 E-value: 1.96e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 11 DLLRRA-REFMEAEVYPLEaaarQSFEEVLPAANDAREKCKAAGLWAPQMPTEYGGMGLGFLPHAHMSETLGRspmghyv 89
Cdd:cd01160 4 DAFRDVvRRFFAKEVAPFH----HEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELAR------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 90 FGCQAP------DAGNMEILHkFGTDPQKARWLQPLAAGEIRSCFSMTEPDrAGSNPTWMDTTAVRDGDDYVINGRKWFT 163
Cdd:cd01160 73 AGGSGPglslhtDIVSPYITR-AGSPEQKERVLPQMVAGKKIGAIAMTEPG-AGSDLQGIRTTARKDGDHYVLNGSKTFI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 164 TGGHLADFAIVMAVTNPDAPPHMRASQIIVPTDNPGFHHIRRLSIMgdvgyGWQSH--SEIAYEDCRVPVENLLGQEGFG 241
Cdd:cd01160 151 TNGMLADVVIVVARTGGEARGAGGISLFLVERGTPGFSRGRKLKKM-----GWKAQdtAELFFDDCRVPAENLLGEENKG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 242 FSIAQERLGPGRIHHCMRWLGICERAFDLMCERASRRMvAPKRPLGAQQAIQHWIAESRAEIDSGRLMVYQAAWKidREG 321
Cdd:cd01160 226 FYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRK-AFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWR--HEQ 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 322 TRAARSEISAIKFLVAGILQQVVDRAIQVHGGLGMTDDTPLAWFFRHERAARIYDGPDEVHKSALARAIL 391
Cdd:cd01160 303 GRLDVAEASMAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
8-393 |
1.57e-55 |
|
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: 187.27 E-value: 1.57e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 8 ELEDLLRRAREFMEAEVYPleAAARQSFEEVLPAanDAREKCKAAGLWAPQMPTEYGGMGLGFLPHAHMSETLGrspmgh 87
Cdd:cd01162 4 EQRAIQEVARAFAAKEMAP--HAADWDQKKHFPV--DVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALS------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 88 yvFGCQAPDA----GNM--EILHKFGTDPQKARWLQPLAAGEIRSCFSMTEPDrAGSNPTWMDTTAVRDGDDYVINGRKW 161
Cdd:cd01162 74 --TGCVSTAAyisiHNMcaWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPG-SGSDAAALRTRAVREGDHYVLNGSKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 162 FTTGGHLADFAIVMAVTNPDAPPHMraSQIIVPTDNPGFHHIRRLSIMGdvgygW--QSHSEIAYEDCRVPVENLLGQEG 239
Cdd:cd01162 151 FISGAGDSDVYVVMARTGGEGPKGI--SCFVVEKGTPGLSFGANEKKMG-----WnaQPTRAVIFEDCRVPVENRLGGEG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 240 FGFSIAQERLGPGRIHHCMRWLGICERAFDL----MCERAsrrmvAPKRPLGAQQAIQHWIAESRAEIDSGRLMVYQAAW 315
Cdd:cd01162 224 QGFGIAMAGLNGGRLNIASCSLGAAQAALDLarayLEERK-----QFGKPLADFQALQFKLADMATELVASRLMVRRAAS 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490518557 316 KIDREgtRAARSEISAI-KFLVAGILQQVVDRAIQVHGGLGMTDDTPLAWFFRHERAARIYDGPDEVHKSALARAILKK 393
Cdd:cd01162 299 ALDRG--DPDAVKLCAMaKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
7-391 |
7.22e-52 |
|
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: 177.92 E-value: 7.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 7 PELEDLLRRAREFMEAEVYP-LEAAARQSFEEVLPAANDAREKCKAAGLWAPQMPTEYGGmglgflphahmsetLGRSPM 85
Cdd:cd01152 1 PSEEAFRAEVRAWLAAHLPPeLREESALGYREGREDRRRWQRALAAAGWAAPGWPKEYGG--------------RGASLM 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 86 GHYVFGCQ-----APDAGNMEILH-------KFGTDPQKARWLQPLAAGEIRSCFSMTEPDrAGSNPTWMDTTAVRDGDD 153
Cdd:cd01152 67 EQLIFREEmaaagAPVPFNQIGIDlagptilAYGTDEQKRRFLPPILSGEEIWCQGFSEPG-AGSDLAGLRTRAVRDGDD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 154 YVINGRKWFTTGGHLADFAIVMAVTNPDAPPHMRASQIIVPTDNPGFhHIRRL-SIMGDVgygwqSHSEIAYEDCRVPVE 232
Cdd:cd01152 146 WVVNGQKIWTSGAHYADWAWLLVRTDPEAPKHRGISILLVDMDSPGV-TVRPIrSINGGE-----FFNEVFLDDVRVPDA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 233 NLLGQEGFGFSIAQERLGPGRIHHCMRWLGICERAFDLMCERASRRMvapkrPLGAQQAIQHWIAESRAEIDSGRLMVYQ 312
Cdd:cd01152 220 NRVGEVNDGWKVAMTTLNFERVSIGGSAATFFELLLARLLLLTRDGR-----PLIDDPLVRQRLARLEAEAEALRLLVFR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 313 AAWKIDreGTRAARSEISAIKFLVAGILQQVVDRAIQVHG----GLGMTDDTPLA----WFFRHERAARIYDGPDEVHKS 384
Cdd:cd01152 295 LASALA--AGKPPGAEASIAKLFGSELAQELAELALELLGtaalLRDPAPGAELAgrweADYLRSRATTIYGGTSEIQRN 372
|
....*..
gi 1490518557 385 ALARAIL 391
Cdd:cd01152 373 IIAERLL 379
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
16-393 |
6.25e-47 |
|
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: 164.68 E-value: 6.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 16 AREFMEAEVYPLEAAARQSFEEVLPAANDAREkckaAGLWAPQMPTEYGGMGLGFLPHAHMSETLGRSPMGhYVFGCQAP 95
Cdd:cd01157 12 ARKFAREEIIPVAAEYDKSGEYPWPLIKRAWE----LGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTG-VQTAIEAN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 96 DAGNMEILHKfGTDPQKARWLQPLAAGEIRSCFSMTEPDrAGSNPTWMDTTAVRDGDDYVINGRK-WFTTGGHlADFAIV 174
Cdd:cd01157 87 SLGQMPVIIS-GNDEQKKKYLGRMTEEPLMCAYCVTEPG-AGSDVAGIKTKAEKKGDEYIINGQKmWITNGGK-ANWYFL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 175 MAVTNPD--APPHMRASQIIVPTDNPGFHHIRRLSIMGdvgygwQSHSE---IAYEDCRVPVENLLGQEGFGFSIAQERL 249
Cdd:cd01157 164 LARSDPDpkCPASKAFTGFIVEADTPGIQPGRKELNMG------QRCSDtrgITFEDVRVPKENVLIGEGAGFKIAMGAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 250 GPGRIHHCMRWLGICERAFDLMCERASRRMVAPKrPLGAQQAIQHWIAESRAEIDSGRLMVYQAAWKID--REGTRAArs 327
Cdd:cd01157 238 DKTRPPVAAGAVGLAQRALDEATKYALERKTFGK-LIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDsgRRNTYYA-- 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490518557 328 eiSAIKFLVAGILQQVVDRAIQVHGGLGMTDDTPLAWFFRHERAARIYDGPDEVHKSALARAILKK 393
Cdd:cd01157 315 --SIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
1-394 |
1.09e-46 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 164.13 E-value: 1.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 1 MDFSTPPELEDLLRRAREFMEAEVypLEAAARQSFEE-VLPaandaREKCKA---AGLWAPQMPTEYGGMGLGFLPHAHM 76
Cdd:PRK12341 1 MDFSLTEEQELLLASIRELITRNF--PEEYFRTCDENgTYP-----REFMRAladNGISMLGVPEEFGGTPADYVTQMLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 77 SETLGRSPMGHYVFGcqapDAGNMEILHKFGTDPQKAR-WLQPLAAGEIRSCFSMTEPdRAGSNPTWMDTTAVR-DGDDY 154
Cdd:PRK12341 74 LEEVSKCGAPAFLIT----NGQCIHSMRRFGSAEQLRKtAESTLETGDPAYALALTEP-GAGSDNNSATTTYTRkNGKVY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 155 vINGRKWFTTGGHLADFAIVMAvTNPDAP-PHMRASQIIVPTDNPGFhhirRLSIMGDVGYGWQSHSEIAYEDCRVPVEN 233
Cdd:PRK12341 149 -LNGQKTFITGAKEYPYMLVLA-RDPQPKdPKKAFTLWWVDSSKPGI----KINPLHKIGWHMLSTCEVYLDNVEVEESD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 234 LLGQEGFGFSIAQERLGPGRIHHCMRWLGICERAFDLMCERASRRMVAPKrPLGAQQAIQHWIAESRAEIDSGRLMVYQA 313
Cdd:PRK12341 223 LVGEEGMGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGK-PIGHNQLIQEKLTLMAIKIENMRNMVYKV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 314 AWKIDrEGTRAARSeiSAI-KFLVAGILQQVVDRAIQVHGGLGMTDDTPLAWFFRHERAARIYDGPDEVHKSALARAILK 392
Cdd:PRK12341 302 AWQAD-NGQSLRTS--AALaKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILK 378
|
..
gi 1490518557 393 KY 394
Cdd:PRK12341 379 DY 380
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
7-395 |
9.00e-46 |
|
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: 162.64 E-value: 9.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 7 PELEDLLRRAREFMEAEVYPLEaaarQSFEEV-LPAANDAREK--------CKAAGLWAPQMPTEYGGMGLGFLPHAHMS 77
Cdd:cd01161 18 PYPSVLTEEQTEELNMLVGPVE----KFFEEVnDPAKNDQLEKiprktltqLKELGLFGLQVPEEYGGLGLNNTQYARLA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 78 ETLGRSPMGHYVFGCQApDAGNMEILHkFGTDPQKARWLQPLAAGEIRSCFSMTEPDrAGSNPTWMDTTAVR--DGDDYV 155
Cdd:cd01161 94 EIVGMDLGFSVTLGAHQ-SIGFKGILL-FGTEAQKEKYLPKLASGEWIAAFALTEPS-SGSDAASIRTTAVLseDGKHYV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 156 INGRKWFTTGGHLADFAIVMA---VTNPDAPPHMRASQIIVPTDNPGFHHIRRLSIMGDVGygwQSHSEIAYEDCRVPVE 232
Cdd:cd01161 171 LNGSKIWITNGGIADIFTVFAkteVKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKG---SNTAEVYFEDVKIPVE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 233 NLLGQEGFGFSIAQERLGPGRIHHCMRWLGICERAFDLMCERASRRmVAPKRPLGAQQAIQHWIAESRAEIDSGRLMVYQ 312
Cdd:cd01161 248 NVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNR-KQFGKKIHEFGLIQEKLANMAILQYATESMAYM 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 313 AAWKIDREGTRAARSEISAIKFLVAGILQQVVDRAIQVHGGLGMTDDTPLAWFFRHERAARIYDGPDEVHKSALARAILK 392
Cdd:cd01161 327 TSGNMDRGLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQ 406
|
...
gi 1490518557 393 KYG 395
Cdd:cd01161 407 HAG 409
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
8-392 |
3.43e-45 |
|
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: 160.27 E-value: 3.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 8 ELEDLLRR-AREFMEAEVYPLeaAARQSFEEVLPAanDAREKCKAAGLWAPQMPTEYGGMGLGFLPHAHMSETLGR-SPM 85
Cdd:cd01156 4 DEIEMLRQsVREFAQKEIAPL--AAKIDRDNEFPR--DLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRaSGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 86 GHYVFGCQApdagNMEI--LHKFGTDPQKARWLQPLAAGEIRSCFSMTEPDrAGSNPTWMDTTAVRDGDDYVINGRKWFT 163
Cdd:cd01156 80 VALSYGAHS----NLCInqIYRNGSAAQKEKYLPKLISGEHIGALAMSEPN-AGSDVVSMKLRAEKKGDRYVLNGSKMWI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 164 TGGHLADFAIVMAVTNPDAPPHmRASQIIVPTDNPGFHHIRRLSIMGDVGygwQSHSEIAYEDCRVPVENLLGQEGFGFS 243
Cdd:cd01156 155 TNGPDADTLVVYAKTDPSAGAH-GITAFIVEKGMPGFSRAQKLDKLGMRG---SNTCELVFEDCEVPEENILGGENKGVY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 244 IAQ-----ERL----GPgrihhcmrwLGICERAFDLMCERASRRMvAPKRPLGAQQAIQHWIAESRAEIDSGRLMVYQAA 314
Cdd:cd01156 231 VLMsgldyERLvlagGP---------IGIMQAALDVAIPYAHQRK-QFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVA 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490518557 315 WKIDReGTRAARSEISAIKFlVAGILQQVVDRAIQVHGGLGMTDDTPLAWFFRHERAARIYDGPDEVHKSALARAILK 392
Cdd:cd01156 301 KACDR-GNMDPKDAAGVILY-AAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
241-390 |
4.78e-40 |
|
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.
Pssm-ID: 395354 [Multi-domain] Cd Length: 149 Bit Score: 139.70 E-value: 4.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 241 GFSIAQERLGPGRIHHCMRWLGICERAFDLMCERASRRmVAPKRPLGAQQAIQHWIAESRAEIDSGRLMVYQAAWKIDRE 320
Cdd:pfam00441 3 GFRVAMETLNHERLAIAAMALGLARRALDEALAYARRR-KAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 321 GtrAARSEISAIKFLVAGILQQVVDRAIQVHGGLGMTDDTPLAWFFRHERAARIYDGPDEVHKSALARAI 390
Cdd:pfam00441 82 G--PDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
8-390 |
2.46e-35 |
|
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: 134.02 E-value: 2.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 8 ELEDLLRR-AREFMEAEVYPLEAAARQsfEEVLPAanDAREKCKAAGLWAPQmPTEYGGMGLGFLPHAHMSETLGRSPMG 86
Cdd:cd01151 15 EEERAIRDtAREFCQEELAPRVLEAYR--EEKFDR--KIIEEMGELGLLGAT-IKGYGCAGLSSVAYGLIAREVERVDSG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 87 HYVF-GCQAPDAgnMEILHKFGTDPQKARWLQPLAAGEIRSCFSMTEPDrAGSNPTWMDTTAVRDGDDYVINGRKWFTTG 165
Cdd:cd01151 90 YRSFmSVQSSLV--MLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPN-HGSDPGGMETRARKDGGGYKLNGSKTWITN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 166 GHLADFAIVMAVTNPDapphmraSQI---IVPTDNPGFhhiRRLSIMGDVGYGWQSHSEIAYEDCRVPVENLL-GQEGFG 241
Cdd:cd01151 167 SPIADVFVVWARNDET-------GKIrgfILERGMKGL---SAPKIQGKFSLRASITGEIVMDNVFVPEENLLpGAEGLR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 242 --FS-IAQERLGPGrihhcmrW--LGICERAFDlMCERASRRMVAPKRPLGAQQAIQHWIAESRAEIDSGRLMVYQAAwK 316
Cdd:cd01151 237 gpFKcLNNARYGIA-------WgaLGAAEDCYH-TARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVG-R 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490518557 317 IDREGtRAARSEISAIKFLVAGILQQVVDRAIQVHGGLGMTDDTPLAWFFRHERAARIYDGPDEVHKSALARAI 390
Cdd:cd01151 308 LKDQG-KATPEQISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAI 380
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
1-394 |
2.67e-34 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 131.11 E-value: 2.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 1 MDFSTPPELEDLLRRAREFMEAEVYplEAAARQSFEEVLPAANDAREKCKAaGLWAPQMPTEYGGMGLGFLPHAHMSETL 80
Cdd:PRK03354 1 MDFNLNDEQELFVAGIRELMASENW--EAYFAECDRDSVYPERFVKALADM-GIDSLLIPEEHGGLDAGFVTLAAVWMEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 81 GRSPMGHYVFgCQAPDAGNMEILHkfGTDPQKARWLQPLAAGEIRSCFSMTEPDrAGSNPTWMDTTAVRDGDDYVINGRK 160
Cdd:PRK03354 78 GRLGAPTYVL-YQLPGGFNTFLRE--GTQEQIDKIMAFRGTGKQMWNSAITEPG-AGSDVGSLKTTYTRRNGKVYLNGSK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 161 WFTTGGHLADFAIVMAvTNPDAPPHMRASQIIVPTDNPGFhhirRLSIMGDVGYGWQSHSEIAYEDCRVPVENLLGQEGF 240
Cdd:PRK03354 154 CFITSSAYTPYIVVMA-RDGASPDKPVYTEWFVDMSKPGI----KVTKLEKLGLRMDSCCEITFDDVELDEKDMFGREGN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 241 GFSIAQERLGPGRIHHCMRWLGICERAFDLMCERASRRmVAPKRPLGAQQAIQHWIAESRAEIDSGRLMVYQAAWKIDRe 320
Cdd:PRK03354 229 GFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQR-VQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADN- 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490518557 321 GTrAARSEISAIKFLVAGILQQVVDRAIQVHGGLGMTDDTPLAWFFRHERAARIYDGPDEVHKSALARAILKKY 394
Cdd:PRK03354 307 GT-ITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQY 379
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
60-393 |
7.53e-31 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 121.91 E-value: 7.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 60 PTEYGGMGLGFLPHAHMSETLGRSPmGHYVFGCQAPDAGNMEILHKFGTDPQKARWLQPLAAGEIRSCFSMTEPDrAGSN 139
Cdd:PLN02519 79 PEEYGGLGLGYLYHCIAMEEISRAS-GSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPN-SGSD 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 140 PTWMDTTAVRDGDDYVINGRKWFTTGGHLADFAIVMAVTNPDAPPHmRASQIIVPTDNPGFHHIRRLSIMGDVGygwQSH 219
Cdd:PLN02519 157 VVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTDVAAGSK-GITAFIIEKGMPGFSTAQKLDKLGMRG---SDT 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 220 SEIAYEDCRVPVENLLGQEGFGFSIAQERLGPGRIHHCMRWLGICERAFDLMCERASRRMvAPKRPLGAQQAIQHWIAES 299
Cdd:PLN02519 233 CELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQRE-QFGRPIGEFQFIQGKLADM 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 300 RAEIDSGRLMVYQAAWKIDRegTRAARSEISAIKFLVAGILQQVVDRAIQVHGGLGMTDDTPLAWFFRHERAARIYDGPD 379
Cdd:PLN02519 312 YTSLQSSRSYVYSVARDCDN--GKVDRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTS 389
|
330
....*....|....
gi 1490518557 380 EVHKSALARAILKK 393
Cdd:PLN02519 390 EIRRMLIGRELFKE 403
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
92-392 |
9.67e-30 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 118.89 E-value: 9.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 92 CQAPDAGNMEILHKF---GTDPQKARWLQPLAAGEIRSCFSMTEPDrAGSNPTWMDTTAVRDGD-DYVINGRKWFTTGGH 167
Cdd:PTZ00461 116 CLAYLAHSMLFVNNFyysASPAQRARWLPKVLTGEHVGAMGMSEPG-AGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGT 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 168 LADFAIVMAVTNPdapphmRASQIIVPTDNPGFHHIRRLSIMGDVGygwqSH-SEIAYEDCRVPVENLLGQEGFGFSIAQ 246
Cdd:PTZ00461 195 VADVFLIYAKVDG------KITAFVVERGTKGFTQGPKIDKCGMRA----SHmCQLFFEDVVVPAENLLGEEGKGMVGMM 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 247 ERLGPGRIHHCMRWLGICERAFDLMCERASRRMvAPKRPLGAQQAIQHWIAESRAEIDSGRLMVYQAAWKI-----DREG 321
Cdd:PTZ00461 265 RNLELERVTLAAMAVGIAERSVELMTSYASERK-AFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVhpgnkNRLG 343
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490518557 322 TRAArseisaiKFLVAGILQQVVDRAIQVHGGLGMTDDTPLAWFFRHERAARIYDGPDEVHKSALARAILK 392
Cdd:PTZ00461 344 SDAA-------KLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLK 407
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
52-391 |
1.06e-26 |
|
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: 110.17 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 52 AGLWAPQMPTEYGGMGLGFLPHAHMSETLGR--SPMgHYVFGCQapdaGNMEILHKFGTDPQKARWLQPLAAGEIRSCFS 129
Cdd:cd01153 48 AGWMALGVPEEYGGQGLPITVYSALAEIFSRgdAPL-MYASGTQ----GAAATLLAHGTEAQREKWIPRLAEGEWTGTMC 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 130 MTEPDrAGSNPTWMDTTAVRDGD-DYVINGRKWFTTGG-HLADFAIVMAV--TNPDAPPHMRA-SQIIVPT--DNPGFHH 202
Cdd:cd01153 123 LTEPD-AGSDLGALRTKAVYQADgSWRINGVKRFISAGeHDMSENIVHLVlaRSEGAPPGVKGlSLFLVPKflDDGERNG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 203 IRRLSIMGDVGYGWQSHSEIAYEDCRVPvenLLGQEGFGFS-----IAQERLGPGrihhcMRWLGICERAFDLMCERASR 277
Cdd:cd01153 202 VTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMGLAqmfamMNGARLGVG-----TQGTGLAEAAYLNALAYAKE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 278 R-------MVAPKRPLGAQQAIQHWIAESRAEIDSGRLMVYQAAWKIDREGTRAARSEISAIKFLVAGILQ--------- 341
Cdd:cd01153 274 RkqggdliKAAPAVTIIHHPDVRRSLMTQKAYAEGSRALDLYTATVQDLAERKATEGEDRKALSALADLLTpvvkgfgse 353
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1490518557 342 ---QVVDRAIQVHGGLGMTDDTPLAWFFRHERAARIYDGPDEVHKSALARAIL 391
Cdd:cd01153 354 aalEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQALDLIGRKI 406
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
127-210 |
3.86e-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: 87.34 E-value: 3.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 127 CFSMTEPDrAGSNPTWMDTTAV-RDGDDYVINGRKWFTTGGHLADFAIVMAVTNPDAPPHmRASQIIVPTDNPGFHHIRR 205
Cdd:pfam02770 1 AFALTEPG-AGSDVASLKTTAAdGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHG-GISLFLVPKDAPGVSVRRI 78
|
....*
gi 1490518557 206 LSIMG 210
Cdd:pfam02770 79 ETKLG 83
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
6-123 |
8.11e-19 |
|
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: 81.36 E-value: 8.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 6 PPELEDLLRRAREFMEAEVYPLEAAARQsfEEVLPAanDAREKCKAAGLWAPQMPTEYGGMGLGFLPHAHMSETLGRSPM 85
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDE--EGEFPR--ELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADA 76
|
90 100 110
....*....|....*....|....*....|....*...
gi 1490518557 86 GHYVFgCQAPDAGNMEILHKFGTDPQKARWLQPLAAGE 123
Cdd:pfam02771 77 SVALA-LSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
14-350 |
8.72e-17 |
|
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: 81.22 E-value: 8.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 14 RRAREFMEAEVyplEAAARQSFEEVLPAAndAREKCKAAGLWAPQMPTEYGGMGLGFLPHAHMSETLGR--SPMGHyVFG 91
Cdd:cd01163 1 ARARPLAARIA---EGAAERDRQRGLPYE--EVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAadSNIAQ-ALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 92 cqaPDAGNMEILHKFGTDPQKARWLQPLAAGEIrscFSMTEPDRAGSNPTWMDTTAVRDGDDYVINGRKWFTTGGHLADF 171
Cdd:cd01163 75 ---AHFGFVEALLLAGPEQFRKRWFGRVLNGWI---FGNAVSERGSVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDW 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 172 AIVMAVTNPDapphmRASQIIVPTDNPGfhhirrLSIMGDvgygWQ--------SHSEIaYEDCRVPVENLLG------Q 237
Cdd:cd01163 149 VTVSALDEEG-----KLVFAAVPTDRPG------ITVVDD----WDgfgqrltaSGTVT-FDNVRVEPDEVLPrpnapdR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 238 EGFGFSIAQerlgpgrIHHCMRWLGICERAFDlmceRASRRMVAPKRP---LGAQQA-----IQHWIAESRAEIDSGRLM 309
Cdd:cd01163 213 GTLLTAIYQ-------LVLAAVLAGIARAALD----DAVAYVRSRTRPwihSGAESArddpyVQQVVGDLAARLHAAEAL 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1490518557 310 VYQAAWKIDR---EGTRAARSEISAIKFLVAGILQQVVDRAIQV 350
Cdd:cd01163 282 VLQAARALDAaaaAGTALTAEARGEAALAVAAAKVVVTRLALDA 325
|
|
| sulfur_SfnB |
TIGR04022 |
sulfur acquisition oxidoreductase, SfnB family; Members of this protein family belong to the ... |
13-319 |
2.48e-16 |
|
sulfur acquisition oxidoreductase, SfnB family; Members of this protein family belong to the greater family of acyl-CoA dehydrogenases. This family includes the sulfate starvation induced protein SfnB of Pseudomonas putida strain DS1, which is both encoded nearby to and phylogenetically closely correlated with the dimethyl sulphone monooxygenase SfnG. This family shows considerable sequence similarity to the Rhodococcus dibenzothiophene desulfurization enzyme DszC, although that enzyme falls outside of the scope of this family. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 274924 [Multi-domain] Cd Length: 391 Bit Score: 80.00 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 13 LRRAREFmeAEVYPLEAAARQSfEEVLPAanDAREKCKAAGLWAPQMPTEYGGMGLGFLPHAHMSET-------LGRSPM 85
Cdd:TIGR04022 11 LEIARRL--AAEFAPGAAERDR-ERRLPW--AELDAFSQSGLWGITVPRAYGGAGVSYATLAEVIAIisaadpsLGQIPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 86 GHYVFgcqapdagnMEILHKFGTDPQKARWLQPLAAGEiRscFSMTEPDRAGSNPTWMDTTAVRDGDDYVINGRKWFTTG 165
Cdd:TIGR04022 86 NHFYA---------LEVLRLTGSEEQKRFFFGEVLAGE-R--FGNAFSERGTRNVLDFQTRLRRDGDGYRLNGRKFYSTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 166 GHLADFAIVMAVTNPDapphmRASQIIVPTDNPGfhhirrLSIMGDvgygWQSHSE-------IAYEDCRVPVENLlgqe 238
Cdd:TIGR04022 154 ALFAHWIPVLALDDEG-----RAVLAFVPRDAPG------LTVIDD----WSGFGQrttasgtVLLDDVRVPAEHV---- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 239 gFGFSIAQER---LGP-GRIHHCMRWLGICERAFDLMCERAsRRMVAPKRPLGAQQA-----IQHWIAESRAEIDSGRLM 309
Cdd:TIGR04022 215 -VPIQRAFDRptaAGPvAQIIHAAIDAGIARAALADTLAFV-RERARPWIDSGVERAsddplTIAEVGDLAIRLHAAEAL 292
|
330
....*....|
gi 1490518557 310 VYQAAWKIDR 319
Cdd:TIGR04022 293 LERAGRAVDA 302
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
130-381 |
4.23e-16 |
|
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: 79.34 E-value: 4.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 130 MTEpDRAGSNPTWMDTTAVRDGDD-YVINGRKWFTTGGhLADFAIVMAVTnPDAPPHMRA-SQIIVPTDNPG----FHHI 203
Cdd:cd01154 153 MTE-KQGGSDLGANETTAERSGGGvYRLNGHKWFASAP-LADAALVLARP-EGAPAGARGlSLFLVPRLLEDgtrnGYRI 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 204 RRLSimGDVGYGWQSHSEIAYEDCrvpVENLLGQEGFGFSIAQERLGPGRIHHCMRWLGICERAFDLMCERASRRMVAPK 283
Cdd:cd01154 230 RRLK--DKLGTRSVATGEVEFDDA---EAYLIGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 284 rPLGAQQAIQHWIAESRAEIDSGRLMVYQAAWKIDREGTRA------ARSEISAIKFLVAGILQQVVDRAIQVHGGLGMT 357
Cdd:cd01154 305 -PLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKpveahmARLATPVAKLIACKRAAPVTSEAMEVFGGNGYL 383
|
250 260
....*....|....*....|....
gi 1490518557 358 DDTPLAWFFRHERAARIYDGPDEV 381
Cdd:cd01154 384 EEWPVARLHREAQVTPIWEGTGNI 407
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
261-380 |
1.05e-14 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 70.45 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 261 LGICERAFDLMCERASRR-MVAPKRPLGAQQAIQHWIAESRAEIDSGRLMVYQAAWKI------DREGTRAARSEISAIK 333
Cdd:pfam08028 7 LGAARAALAEFTERARGRvRAYFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIeaaaaaGKPVTPALRAEARRAA 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1490518557 334 FLVAGILQQVVDRAIQVHGGLGMTDDTPLAWFFRHERAARIYDGPDE 380
Cdd:pfam08028 87 AFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
9-397 |
1.20e-09 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 59.88 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 9 LEDLLRRAREFMEAEVYPLEAA--------ARQSFEEVLPAANDAREKCKAAGLWAPQMPTEYGGMGLGFLPHAHMSETL 80
Cdd:PTZ00456 60 MDSLLEEASKLATQTLLPLYESsdsegcvlLKDGNVTTPKGFKEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELM 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 81 GRSPMGHYVFGCQApdAGNMEILHKFGTDPQKARWLQPLAAGEIRSCFSMTEPdRAGSNPTWMDTTAVRDGD-DYVINGR 159
Cdd:PTZ00456 140 ATANWGFSMYPGLS--IGAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEP-QCGTDLGQVKTKAEPSADgSYKITGT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 160 KWFTTGG-HlaDFA-----IVMAVTnPDAPPHMRA-SQIIVP----TDNPGFHHIRRLSIMG---DVGYGWQSHSEIAYE 225
Cdd:PTZ00456 217 KIFISAGdH--DLTenivhIVLARL-PNSLPTTKGlSLFLVPrhvvKPDGSLETAKNVKCIGlekKMGIKGSSTCQLSFE 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 226 DcrvPVENLLGQEGFGFSIAQERLGPGRIHHCMRWLGICERAFDLMCERASRRMV-----APKRPLGAQQAIQH------ 294
Cdd:PTZ00456 294 N---SVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRSmralsGTKEPEKPADRIIChanvrq 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 295 --WIAESRAE------IDSGRLMVYQAAWKiDREGTRAARSEISAIKFLVAGILQ----QVVDRAIQVHGGLGMTDDTPL 362
Cdd:PTZ00456 371 niLFAKAVAEggrallLDVGRLLDIHAAAK-DAATREALDHEIGFYTPIAKGCLTewgvEAASRCLQVWGGHGYIKGNGM 449
|
410 420 430
....*....|....*....|....*....|....*.
gi 1490518557 363 AWFFRHERAARIYDGPDEVHK-SALARAILKKYGIE 397
Cdd:PTZ00456 450 EQILRDARIGTLYEGTTGIQAlDFIGRKVLSLKGGN 485
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
107-235 |
5.00e-09 |
|
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: 58.11 E-value: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 107 GTDPQKARWLQPLAAGEIRSCFSMTEPDRaGSNPTWMDTTAVRD--GDDYVIN-----GRKWFTTG-GHLADFAIVMAvt 178
Cdd:cd01150 117 GTDEHQDYWLQGANNLEIIGCFAQTELGH-GSNLQGLETTATYDplTQEFVINtpdftATKWWPGNlGKTATHAVVFA-- 193
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490518557 179 npdapphmrasQIIVPTDNPGFH----HIRRLS-------IM-GDVG--YGWQ--SHSEIAYEDCRVPVENLL 235
Cdd:cd01150 194 -----------QLITPGKNHGLHafivPIRDPKthqplpgVTvGDIGpkMGLNgvDNGFLQFRNVRIPRENLL 255
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
7-274 |
8.65e-09 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 56.78 E-value: 8.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 7 PELEDLLRRAREFMEAEVYPLEAAARQSFE---EVLPaandareKCKAAGLwAPQMPTEYGGMGLGFLPHAHMSETLGRS 83
Cdd:PLN02526 31 PEEQALRKRVRECMEKEVAPIMTEYWEKAEfpfHIIP-------KLGSLGI-AGGTIKGYGCPGLSITASAIATAEVARV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 84 PMGHYVFgCQAPDAGNMEILHKFGTDPQKARWLQPLAAGEIRSCFSMTEPDRaGSNPTWMDTTAVRDGDDYVINGRKWFT 163
Cdd:PLN02526 103 DASCSTF-ILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDY-GSDASSLNTTATKVEGGWILNGQKRWI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 164 TGGHLADFAIVMAvtnpdapPHMRASQI---IVPTDNPGFhhiRRLSIMGDVGYGWQSHSEIAYEDCRVPVENLLgqEGF 240
Cdd:PLN02526 181 GNSTFADVLVIFA-------RNTTTNQIngfIVKKGAPGL---KATKIENKIGLRMVQNGDIVLKDVFVPDEDRL--PGV 248
|
250 260 270
....*....|....*....|....*....|....*
gi 1490518557 241 -GFSIAQERLGPGRIHHCMRWLGICERAFDlMCER 274
Cdd:PLN02526 249 nSFQDTNKVLAVSRVMVAWQPIGISMGVYD-MCHR 282
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
50-138 |
2.36e-07 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 52.90 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 50 KAAGLWAPQMPTEYGGmgLGFLPHAHM---------SETLGRSPMghyvfgcqAPDA-GNMEILHKFGTDPQKARWLQPL 119
Cdd:PRK09463 119 KEHGFFGMIIPKEYGG--LEFSAYAHSrvlqklasrSGTLAVTVM--------VPNSlGPGELLLHYGTDEQKDHYLPRL 188
|
90
....*....|....*....
gi 1490518557 120 AAGEIRSCFSMTEPdRAGS 138
Cdd:PRK09463 189 ARGEEIPCFALTSP-EAGS 206
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
146-373 |
2.73e-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: 48.88 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 146 TAVRDGDDYVINGRKWFTTGGHLADFAIVMA-VTNPDAPPHMRASQI------IVPT-DNPGF-----HHI--------- 203
Cdd:cd01159 112 RAERVDGGYRVSGTWPFASGCDHADWILVGAiVEDDDGGPLPRAFVVpraeyeIVDTwHVVGLrgtgsNTVvvddvfvpe 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 204 -RRLSIMGDVgygwQSHSEIAYEDC-RVPVENLLGQEgfgfsiaqerlgpgrihHCMRWLGICERAFDLMCERASRRMVA 281
Cdd:cd01159 192 hRTLTAGDMM----AGDGPGGSTPVyRMPLRQVFPLS-----------------FAAVSLGAAEGALAEFLELAGKRVRQ 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 282 PKRPLGAQQA--IQHWIAESRAEIDSGRLMVYQA---AWKIDREGTRAA---RSEISAIKFLVAGILQQVVDRAIQVHGG 353
Cdd:cd01159 251 YGAAVKMAEApiTQLRLAEAAAELDAARAFLERAtrdLWAHALAGGPIDveeRARIRRDAAYAAKLSAEAVDRLFHAAGG 330
|
250 260
....*....|....*....|
gi 1490518557 354 LGMTDDTPLAWFFRHERAAR 373
Cdd:cd01159 331 SALYTASPLQRIWRDIHAAA 350
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
50-148 |
2.96e-06 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 49.57 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 50 KAAGLWAPQMPTEYGGmgLGFLPHAH---MSETLGRSpmghyvfGCQA-----PDA-GNMEILHKFGTDPQKARWLQPLA 120
Cdd:PRK13026 118 KKEGFFALIIPKEYGG--KGFSAYANstiVSKIATRS-------VSAAvtvmvPNSlGPGELLTHYGTQEQKDYWLPRLA 188
|
90 100
....*....|....*....|....*...
gi 1490518557 121 AGEIRSCFSMTEPDrAGSNPTWMDTTAV 148
Cdd:PRK13026 189 DGTEIPCFALTGPE-AGSDAGAIPDTGI 215
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
54-266 |
3.22e-05 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 46.03 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 54 LWAPQMPTEYGGMGLGFLPHAHMSETLGR-------SPMGHYVFGCQapdagnmeILHKFGTDPQKARWLQPLAAGEIRS 126
Cdd:PTZ00457 65 LYGARIATEYGGLGLGHTAHALIYEEVGTncdskllSTIQHSGFCTY--------LLSTVGSKELKGKYLTAMSDGTIMM 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 127 CFSMTEPdrAGSNPTWMDTTAV-RDGDDYVINGRK--WFTTGG-HLADFAIVMAVTNPDAPPHM--RASQIIVPTDNPGf 200
Cdd:PTZ00457 137 GWATEEG--CGSDISMNTTKASlTDDGSYVLTGQKrcEFAASAtHFLVLAKTLTQTAAEEGATEvsRNSFFICAKDAKG- 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490518557 201 hhirrLSIMGDVgygwqshseIAYEDcrVPVENLLGQEGFGFSIAQERLGPGRIHHCMRWLGICER 266
Cdd:PTZ00457 214 -----VSVNGDS---------VVFEN--TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKR 263
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
107-235 |
1.59e-04 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 43.68 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490518557 107 GTDPQKARWLQPLAAGEIRSCFSMTEPDRaGSNPTWMDTTAVRD--GDDYVING------RKWFTTGGHLADFAIVMAvt 178
Cdd:PTZ00460 110 GTDEQINLWMPSLLNFEIVGCYAQTELGH-GSDVQNLETTATYDkqTNEFVIHTpsveavKFWPGELGFLCNFALVYA-- 186
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490518557 179 npdapphmrasQIIVPTDNPGFH----HIRRLS--------IMGDV----GYGWQSHSEIAYEDCRVPVENLL 235
Cdd:PTZ00460 187 -----------KLIVNGKNKGVHpfmvRIRDKEthkplqgvEVGDIgpkmGYAVKDNGFLSFDHYRIPLDSLL 248
|
|
| |
