|
Name |
Accession |
Description |
Interval |
E-value |
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
72-420 |
3.34e-78 |
|
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: 247.06 E-value: 3.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 72 DLSLTEEQQMTSEAMSQFAQEVLLELAHDADQTAQFPESLWQYVEDLGLNYYALPEALGGvaAEQNIVSNLLIAEKLAEG 151
Cdd:COG1960 2 DFELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGG--LGLSLVELALVLEELARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 152 DFSLTAGLLSTFSVINAITRWGSTEVQSMYLPCFAEDsDITATFAVQEATPAFNPYVLKTKASLENDQYFIEGEKTLVIL 231
Cdd:COG1960 80 DASLALPVGVHNGAAEALLRFGTEEQKERYLPRLASG-EWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 232 GDLADVFLVSADFNGKPD-----VFVVQAG-DTISIKST-PAMGLKAAETATLKFSHT---PALRLGATD--FDY-TAFL 298
Cdd:COG1960 159 APVADVILVLARTDPAAGhrgisLFLVPKDtPGVTVGRIeDKMGLRGSDTGELFFDDVrvpAENLLGEEGkgFKIaMSTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 299 DLGNLMWCAMAVGTCEAVKAYCIKYANERTAFGEPISHRQSVAFMIADMAIEIDAMRMLILNAASLAEAGKPFHREAYLA 378
Cdd:COG1960 239 NAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMA 318
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1842333380 379 RLLCAEKSMKIGTDGVQILGGHGFTKEHPVERWYRDLRATAI 420
Cdd:COG1960 319 KLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTI 360
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
77-420 |
4.54e-69 |
|
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: 223.30 E-value: 4.54e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 77 EEQQMTSEAMSQFAQEVLLELAHDADQTAQFPESLWQYVEDLGLNYYALPEALGGvaAEQNIVSNLLIAEKLAEGDFSLT 156
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGG--AGLDFLAYAIAIEELAKVDASVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 157 AGLLSTFSVI-NAITRWGSTEVQSMYLPCFAEDSDITAtFAVQEATPAFNPYVLKTKASLENDQYFIEGEKTLVILGDLA 235
Cdd:cd01158 79 VIVSVHNSLGaNPIIKFGTEEQKKKYLPPLATGEKIGA-FALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 236 DVFLVSAdfNGKPDV-------FVVQAGD---TISiKSTPAMGLKAAETATLKFSH--TPALR-LGATDFDYT---AFLD 299
Cdd:cd01158 158 DFYIVFA--VTDPSKgyrgitaFIVERDTpglSVG-KKEDKLGIRGSSTTELIFEDvrVPKENiLGEEGEGFKiamQTLD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 300 LGNLMWCAMAVGTCEAVKAYCIKYANERTAFGEPISHRQSVAFMIADMAIEIDAMRMLILNAASLAEAGKPFHREAYLAR 379
Cdd:cd01158 235 GGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAK 314
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1842333380 380 LLCAEKSMKIGTDGVQILGGHGFTKEHPVERWYRDLRATAI 420
Cdd:cd01158 315 LFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEI 355
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
77-421 |
4.67e-47 |
|
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: 164.38 E-value: 4.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 77 EEQQMTSEAMSQFAQEVLLELAHDADQTAQFPEslwqyvedlglnyyalpealggvaaeqnivsnlliaEKLAEgdfslt 156
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPW------------------------------------ELLAE------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 157 AGLLStfsVINAITRWGSTEVQSMYLPCFAEDSDITAtFAVQEATPAFNPYVLKTKASLENDQYFIEGEKTLVILGDLAD 236
Cdd:cd00567 39 LGLLL---GAALLLAYGTEEQKERYLPPLASGEAIAA-FALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDAD 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 237 VFLVSADFNGKPD------VFVVQAgDTISIKSTPA---MGLKAAETATLKFS--HTPALRL---GATDFDYT-AFLDLG 301
Cdd:cd00567 115 LFIVLARTDEEGPghrgisAFLVPA-DTPGVTVGRIwdkMGMRGSGTGELVFDdvRVPEDNLlgeEGGGFELAmKGLNVG 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 302 NLMWCAMAVGTCEAVKAYCIKYANERTAFGEPISHRQSVAFMIADMAIEIDAMRMLILNAASLAEAGKPFHR-EAYLARL 380
Cdd:cd00567 194 RLLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARlEAAMAKL 273
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1842333380 381 LCAEKSMKIGTDGVQILGGHGFTKEHPVERWYRDLRATAIL 421
Cdd:cd00567 274 FATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIA 314
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
77-420 |
1.52e-43 |
|
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: 156.12 E-value: 1.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 77 EEQQMTSEAMSQFAQEVLLELAHDADQTAQFPESLWQYVEDLGLNYYALPEALGGVAAeqNIVSNLLIAEKLAEGDFSLT 156
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGG--DLLSAAVLWEELARAGGSGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 157 AGLLSTFSVINAITRWGSTEVQSMYLPCFAEDSDITAtFAVQEATPAFNPYVLKTKASLENDQYFIEGEKTLVILGDLAD 236
Cdd:cd01160 79 GLSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGA-IAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 237 VFLVSADFNGKP------DVFVVQAGDTISIKSTP--AMGLKAAETATLKFS--HTPALRL-GATDFDYTAFL-DLGN-- 302
Cdd:cd01160 158 VVIVVARTGGEArgaggiSLFLVERGTPGFSRGRKlkKMGWKAQDTAELFFDdcRVPAENLlGEENKGFYYLMqNLPQer 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 303 LMWCAMAVGTCEAVKAYCIKYANERTAFGEPISHRQSVAFMIADMAIEIDAMRMLILNAASLAEAGKPFHREAYLARLLC 382
Cdd:cd01160 238 LLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWA 317
|
330 340 350
....*....|....*....|....*....|....*...
gi 1842333380 383 AEKSMKIGTDGVQILGGHGFTKEHPVERWYRDLRATAI 420
Cdd:cd01160 318 TELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPI 355
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
75-414 |
8.00e-43 |
|
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: 154.49 E-value: 8.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 75 LTEEQQMTSEAMSQFAQEVLLELAHDADQTAQFPESLWQYVEDLGLNYYALPEALGGVAAeqNIVSNLLIAEKL--AEGD 152
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGM--GYLAHVIIMEEIsrASGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 153 FSLTAGLLSTFsVINAITRWGSTEVQSMYLPCFAEDSDITAtFAVQEATPAFNPYVLKTKASLENDQYFIEGEKTLVILG 232
Cdd:cd01156 80 VALSYGAHSNL-CINQIYRNGSAAQKEKYLPKLISGEHIGA-LAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 233 DLADVFLVSADFNGKPDV-----FVVQAGDT--ISIKSTPAMGLKAAETATLKFSH--TPALR-LGATD---FDYTAFLD 299
Cdd:cd01156 158 PDADTLVVYAKTDPSAGAhgitaFIVEKGMPgfSRAQKLDKLGMRGSNTCELVFEDceVPEENiLGGENkgvYVLMSGLD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 300 LGNLMWCAMAVGTCEAVKAYCIKYANERTAFGEPISHRQSVAFMIADMAIEIDAMRMLILNAASLAEAGKPFHREAYLAR 379
Cdd:cd01156 238 YERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVI 317
|
330 340 350
....*....|....*....|....*....|....*
gi 1842333380 380 LLCAEKSMKIGTDGVQILGGHGFTKEHPVERWYRD 414
Cdd:cd01156 318 LYAAEKATQVALDAIQILGGNGYINDYPTGRLLRD 352
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
75-420 |
4.86e-36 |
|
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: 136.18 E-value: 4.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 75 LTEEQQMTSEAMSQFAQEVLLELAHDADQTAQFPESLWQYVEDLGLNYYALPEALGGVAaeQNIVSNLLIAEKLAEGDFS 154
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLG--LGTFDTCLITEELAYGCTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 155 LTAGLLSTFSVINAITRWGSTEVQSMYLPCFAEDSdITATFAVQEATPAFNPYVLKTKASLENDQYFIEGEKTLVILGDL 234
Cdd:cd01157 79 VQTAIEANSLGQMPVIISGNDEQKKKYLGRMTEEP-LMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 235 ADVFLVSADFNGKPDV--------FVVQAgDTISI---KSTPAMGLKAAETATLKFS--HTPA----------LRLGATD 291
Cdd:cd01157 158 ANWYFLLARSDPDPKCpaskaftgFIVEA-DTPGIqpgRKELNMGQRCSDTRGITFEdvRVPKenvligegagFKIAMGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 292 FDYTafldlgNLMWCAMAVGTCEAVKAYCIKYANERTAFGEPISHRQSVAFMIADMAIEIDAMRMLILNAASLAEAGKPF 371
Cdd:cd01157 237 FDKT------RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRN 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1842333380 372 HREAYLARLLCAEKSMKIGTDGVQILGGHGFTKEHPVERWYRDLRATAI 420
Cdd:cd01157 311 TYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQI 359
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
295-421 |
4.75e-32 |
|
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: 118.90 E-value: 4.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 295 TAFLDLGNLMWCAMAVGTCEAVKAYCIKYANERTAFGEPISHRQSVAFMIADMAIEIDAMRMLILNAASLAEAGKPFHRE 374
Cdd:pfam00441 8 METLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAGGPDGAE 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1842333380 375 AYLARLLCAEKSMKIGTDGVQILGGHGFTKEHPVERWYRDLRATAIL 421
Cdd:pfam00441 88 ASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIG 134
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
72-420 |
2.17e-31 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 123.30 E-value: 2.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 72 DLSLTEEQQMTSEAMSQF-AQEVLLELAHDADQTAQFPESLWQYVEDLGLNYYALPEALGGVAAEqnIVSNLLIAEKLAE 150
Cdd:PRK12341 2 DFSLTEEQELLLASIRELiTRNFPEEYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPAD--YVTQMLVLEEVSK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 151 gdFSLTAGLLSTFSVINAITRWGStevqsmylpcfAEDSDITATFAVQEATPAF-----------NPYVLKTKASLENDQ 219
Cdd:PRK12341 80 --CGAPAFLITNGQCIHSMRRFGS-----------AEQLRKTAESTLETGDPAYalaltepgagsDNNSATTTYTRKNGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 220 YFIEGEKTLVILGDLADVFLVSADFNGKPDV-------FVVQAGDTISIKSTPAMGLKAAETATLKFSHTPALRLGATDF 292
Cdd:PRK12341 147 VYLNGQKTFITGAKEYPYMLVLARDPQPKDPkkaftlwWVDSSKPGIKINPLHKIGWHMLSTCEVYLDNVEVEESDLVGE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 293 DYTAFLDL-GN-----LMWCAMAVGTCEAVKAYCIKYANERTAFGEPISHRQSVAFMIADMAIEIDAMRMLILNAASLAE 366
Cdd:PRK12341 227 EGMGFLNVmYNfemerLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQAD 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1842333380 367 AGKPFHREAYLARLLCAEKSMKIGTDGVQILGGHGFTKEHPVERWYRDLRATAI 420
Cdd:PRK12341 307 NGQSLRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERI 360
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
75-416 |
4.41e-31 |
|
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: 122.96 E-value: 4.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 75 LTEEQQMTSEAMSQFAQEVLLelAHDADQTAQFPESLWQYVEDLGLNYYALPEALGGVAAEQNIVSnlLIAEKL-AEGDF 153
Cdd:cd01161 27 QTEELNMLVGPVEKFFEEVND--PAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYA--RLAEIVgMDLGF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 154 SLTAGLLSTFSVInAITRWGSTEVQSMYLPCFAEDSDITAtFAVQEATPAFNPYVLKTKASL--ENDQYFIEGEKTLVIL 231
Cdd:cd01161 103 SVTLGAHQSIGFK-GILLFGTEAQKEKYLPKLASGEWIAA-FALTEPSSGSDAASIRTTAVLseDGKHYVLNGSKIWITN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 232 GDLADVFLVSA-----DFNG----KPDVFVVQA--GDTISIKSTPAMGLKAAETATLKFSHT--PALR-LGAT-DFDYTA 296
Cdd:cd01161 181 GGIADIFTVFAktevkDATGsvkdKITAFIVERsfGGVTNGPPEKKMGIKGSNTAEVYFEDVkiPVENvLGEVgDGFKVA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 297 F--LDLGNLMWCAMAVGTCEAVKAYCIKYANERTAFGEPISHRQSVAFMIADMAIEIDAMRMLILNAASLAEAG--KPFH 372
Cdd:cd01161 261 MniLNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGlkAEYQ 340
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1842333380 373 REAYLARLLCAEKSMKIGTDGVQILGGHGFTKEHPVERWYRDLR 416
Cdd:cd01161 341 IEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLR 384
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
75-421 |
8.85e-30 |
|
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: 118.70 E-value: 8.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 75 LTEEQQMTSEAMSQFAQEVLLELAHDADQTAQFPESLWQYVEDLGLNYYALPEALGGVAAEQniVSNLLIAEKLAEGDFS 154
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSR--LDASIIFEALSTGCVS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 155 LTAGLlstfSVINA----ITRWGSTEVQSMYLPCFAEdSDITATFAVQEATPAFNPYVLKTKASLENDQYFIEGEKTLVI 230
Cdd:cd01162 79 TAAYI----SIHNMcawmIDSFGNDEQRERFLPDLCT-MEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFIS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 231 LGDLADVFLVSADFNGKP----DVFVVQAG-DTISI-KSTPAMGLKAAETATLKFS--HTPAL-RLGATDFDYT---AFL 298
Cdd:cd01162 154 GAGDSDVYVVMARTGGEGpkgiSCFVVEKGtPGLSFgANEKKMGWNAQPTRAVIFEdcRVPVEnRLGGEGQGFGiamAGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 299 DLGNLMWCAMAVGTCEAVKAYCIKYANERTAFGEPISHRQSVAFMIADMAIEIDAMRMLILNAASLAEAGKPfhrEAY-- 376
Cdd:cd01162 234 NGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDP---DAVkl 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1842333380 377 --LARLLCAEKSMKIGTDGVQILGGHGFTKEHPVERWYRDLRATAIL 421
Cdd:cd01162 311 caMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQIL 357
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
70-418 |
3.28e-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: 111.68 E-value: 3.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 70 LFDLSLTEEQQMTSEAMSQFAQEVLLELAHDADQTAQFPESLWQYVEDLGLnYYALPEALGGvaAEQNIVSNLLIAEKLA 149
Cdd:cd01151 8 NLDDLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGL-LGATIKGYGC--AGLSSVAYGLIAREVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 150 EGDfsltAGLLSTFSV-----INAITRWGSTEVQSMYLPCFAEdSDITATFAVQEATPAFNPYVLKTKASLENDQYFIEG 224
Cdd:cd01151 85 RVD----SGYRSFMSVqsslvMLPIYDFGSEEQKQKYLPKLAS-GELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 225 EKTLVILGDLADVFLVSA--DFNGKPDVFVVQAG-DTISIKSTPA-MGLKAAETATLKFSH--------TPALR-LGATd 291
Cdd:cd01151 160 SKTWITNSPIADVFVVWArnDETGKIRGFILERGmKGLSAPKIQGkFSLRASITGEIVMDNvfvpeenlLPGAEgLRGP- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 292 fdyTAFLDLGNLM--WCAMavGTCEAVKAYCIKYANERTAFGEPISHRQSVAFMIADMAIEIDAMRMLILNAASLAEAGK 369
Cdd:cd01151 239 ---FKCLNNARYGiaWGAL--GAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGK 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1842333380 370 PFHREAYLARLLCAEKSMKIGTDGVQILGGHGFTKEHPVERWYRDLRAT 418
Cdd:cd01151 314 ATPEQISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESV 362
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
72-416 |
1.37e-26 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 109.92 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 72 DLSLTEEQQMTSEAMSQF-AQEVLLELAHDADQTAQFPESLWQYVEDLGLNYYALPEALGGVaaEQNIVSNLLIAEKLA- 149
Cdd:PRK03354 2 DFNLNDEQELFVAGIRELmASENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGL--DAGFVTLAAVWMELGr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 150 EGD-----FSLTAGllstfsvINAITRWGSTEVQSMYLPCFAEDSDITaTFAVQEATPAFNPYVLKTKASLENDQYFIEG 224
Cdd:PRK03354 80 LGAptyvlYQLPGG-------FNTFLREGTQEQIDKIMAFRGTGKQMW-NSAITEPGAGSDVGSLKTTYTRRNGKVYLNG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 225 EKTLVILGDLADVFLVSADFNGKPDV------FVVQAGDTISIKSTPAMGLKAAETATLKFSHTP------------ALR 286
Cdd:PRK03354 152 SKCFITSSAYTPYIVVMARDGASPDKpvytewFVDMSKPGIKVTKLEKLGLRMDSCCEITFDDVEldekdmfgregnGFN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 287 LGATDFDYTAFLdlgnlmwcamaVGTCEAVKAYC-----IKYANERTAFGEPISHRQSVAFMIADMAIEIDAMRMLILNA 361
Cdd:PRK03354 232 RVKEEFDHERFL-----------VALTNYGTAMCafedaARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEA 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1842333380 362 ASLAEAGKPFHREAYLARLLCAEKSMKIGTDGVQILGGHGFTKEHPVERWYRDLR 416
Cdd:PRK03354 301 AWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLR 355
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
76-420 |
1.68e-26 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 110.41 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 76 TEEQQMTSEAMSQFAQEVLLELAHDADQTAQFPESLWQYVEDLGLNYYALPEALGGvaAEQNIVSNLLIAEKLAEGD--F 153
Cdd:PTZ00461 38 TPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGG--AGMDAVAAVIIHHELSKYDpgF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 154 SLtAGLLSTFSVINAITRWGSTEVQSMYLPCFAEDSDITAtFAVQEATPAFNPYVLKTKAS-LENDQYFIEGEKTLVILG 232
Cdd:PTZ00461 116 CL-AYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGA-MGMSEPGAGTDVLGMRTTAKkDSNGNYVLNGSKIWITNG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 233 DLADVFLVSADFNGKPDVFVVQAGdTISIKSTPAM---GLKAAETATLKFSHT--PALRLGATD----FDYTAFLDLGNL 303
Cdd:PTZ00461 194 TVADVFLIYAKVDGKITAFVVERG-TKGFTQGPKIdkcGMRASHMCQLFFEDVvvPAENLLGEEgkgmVGMMRNLELERV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 304 MWCAMAVGTCEAVKAYCIKYANERTAFGEPISHRQSVAFMIADMAIEIDAMRMLILNAASLAEAGKPFHREAYLARLLCA 383
Cdd:PTZ00461 273 TLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKLFAT 352
|
330 340 350
....*....|....*....|....*....|....*..
gi 1842333380 384 EKSMKIGTDGVQILGGHGFTKEHPVERWYRDLRATAI 420
Cdd:PTZ00461 353 PIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEI 389
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
84-427 |
7.42e-24 |
|
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: 102.47 E-value: 7.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 84 EAMSQFAQEVLLELAHDADQ------------TAQFPESLWQYVEDlGLNYYALPEALGGVAAEQNIVSnlLIAEKLAEG 151
Cdd:cd01153 3 EEVARLAENVLAPLNADGDRegpvfddgrvvvPPPFKEALDAFAEA-GWMALGVPEEYGGQGLPITVYS--ALAEIFSRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 152 DFSLTAGLLSTfSVINAITRWGSTEVQSMYLPCFAEdSDITATFAVQEATPAFNPYVLKTKASLEND-QYFIEGEKTLVI 230
Cdd:cd01153 80 DAPLMYASGTQ-GAAATLLAHGTEAQREKWIPRLAE-GEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFIS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 231 LGD--LAD--VFLVSADFNGKP------DVFVVQAGD------TISIKSTP-AMGLKAAETATLKFSHTPALRLGATD-- 291
Cdd:cd01153 158 AGEhdMSEniVHLVLARSEGAPpgvkglSLFLVPKFLddgernGVTVARIEeKMGLHGSPTCELVFDNAKGELIGEEGmg 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 292 FDYT-AFLDLGNLMWCAMAVGTCEAVKAYCIKYANERTAFGEP--------ISHRQSVAFMIADMAIEIDAMRMLILNAA 362
Cdd:cd01153 238 LAQMfAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLikaapavtIIHHPDVRRSLMTQKAYAEGSRALDLYTA 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1842333380 363 SL--AEAGKPFHREAY-----LARLL-------CAEKSMKIGTDGVQILGGHGFTKEHPVERWYRDLRATAIlHSGLHA 427
Cdd:cd01153 318 TVqdLAERKATEGEDRkalsaLADLLtpvvkgfGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTI-YEGTTG 395
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
72-414 |
2.02e-22 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 98.41 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 72 DLSLTEEQQMTSEAMSQFAQEVLLELAHDADQTAQFPES--LWQYVEDLGLNYYALPEALGGVAAeqNIVSNLLIAEKL- 148
Cdd:PLN02519 23 SLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDvnLWKLMGDFNLHGITAPEEYGGLGL--GYLYHCIAMEEIs 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 149 -AEGDFSLTAGLLSTFsVINAITRWGSTEVQSMYLPCFAEDSDITAtFAVQEATPAFNPYVLKTKASLENDQYFIEGEKT 227
Cdd:PLN02519 101 rASGSVGLSYGAHSNL-CINQLVRNGTPAQKEKYLPKLISGEHVGA-LAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 228 LVILGDLADVFLVSAdfngKPDVFVVQAGDTISI--KSTPA---------MGLKAAETATLKFSH--TPALRL----GAT 290
Cdd:PLN02519 179 WCTNGPVAQTLVVYA----KTDVAAGSKGITAFIieKGMPGfstaqkldkLGMRGSDTCELVFENcfVPEENVlgqeGKG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 291 DFDYTAFLDLGNLMWCAMAVGTCEAVKAYCIKYANERTAFGEPISHRQSVAFMIADMAIEIDAMRMLILNAASLAEAGKP 370
Cdd:PLN02519 255 VYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKV 334
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1842333380 371 FHREAYLARLLCAEKSMKIGTDGVQILGGHGFTKEHPVERWYRD 414
Cdd:PLN02519 335 DRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRD 378
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
76-183 |
4.95e-17 |
|
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: 76.35 E-value: 4.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 76 TEEQQMTSEAMSQFAQEVLLELAHDADQTAQFPESLWQYVEDLGLNYYALPEALGGvaAEQNIVSNLLIAEKLAEGDFSL 155
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGG--AGLDYLAYALVAEELARADASV 78
|
90 100
....*....|....*....|....*....
gi 1842333380 156 TAGL-LSTFSVINAITRWGSTEVQSMYLP 183
Cdd:pfam02771 79 ALALsVHSSLGAPPILRFGTEEQKERYLP 107
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
211-420 |
4.74e-14 |
|
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: 73.56 E-value: 4.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 211 TKASLENDQYFIEGEKTLVIlGDLADVFLVSADFNGKPD------VFVVQ------AGDTISIKSTP-AMGLKAAETATL 277
Cdd:cd01154 168 TAERSGGGVYRLNGHKWFAS-APLADAALVLARPEGAPAgarglsLFLVPrlledgTRNGYRIRRLKdKLGTRSVATGEV 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 278 KFSHTPALRLGATDFDYTAFLDLGNL--MWCAM-AVGTCEA--VKAYCikYANERTAFGEPISHRQSVAFMIADMAIEID 352
Cdd:cd01154 247 EFDDAEAYLIGDEGKGIYYILEMLNIsrLDNAVaALGIMRRalSEAYH--YARHRRAFGKPLIDHPLMRRDLAEMEVDVE 324
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1842333380 353 AMRMLILNAASL---AEAGKPfhREAYLARLL-------CAEKSMKIGTDGVQILGGHGFTKEHPVERWYRDLRATAI 420
Cdd:cd01154 325 AATALTFRAARAfdrAAADKP--VEAHMARLAtpvakliACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPI 400
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
306-425 |
6.86e-12 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 62.36 E-value: 6.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 306 CAMAVGTCEAVKAYCIKYANERT--AFGEPISHRQSVAFMIADMAIEIDAMRMLILNAASLAEA----GKPFH----REA 375
Cdd:pfam08028 3 AAAALGAARAALAEFTERARGRVraYFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAaaaaGKPVTpalrAEA 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1842333380 376 YLARLLCAEKSMKIGTDGVQILGGHGFTKEHPVERWYRDLRATAIlHSGL 425
Cdd:pfam08028 83 RRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQ-HAAV 131
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
67-424 |
1.09e-07 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 54.10 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 67 KKNLFDlSLTEEqqmtseaMSQFAQEVLLELAHDAD-------QTAQ------FPESLWQYVEDlGLNYYALPEALGGVA 133
Cdd:PTZ00456 56 TKELMD-SLLEE-------ASKLATQTLLPLYESSDsegcvllKDGNvttpkgFKEAYQALKAG-GWTGISEPEEYGGQA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 134 AEQNIvsNLLIAEKLAEGD--FSLTAGLlsTFSVINAITRWGSTEVQSMYLPCFAEdSDITATFAVQEATPAFNPYVLKT 211
Cdd:PTZ00456 127 LPLSV--GFITRELMATANwgFSMYPGL--SIGAANTLMAWGSEEQKEQYLTKLVS-GEWSGTMCLTEPQCGTDLGQVKT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 212 KASLEND-QYFIEGEKTLVILGD-----------LA------------DVFLVSADFNgKPDVFVVQAGDTISIKSTPAM 267
Cdd:PTZ00456 202 KAEPSADgSYKITGTKIFISAGDhdltenivhivLArlpnslpttkglSLFLVPRHVV-KPDGSLETAKNVKCIGLEKKM 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 268 GLKAAETATLKFSHTPALRLGATDFDYTAFLDLGNLMWCAMAV-GTCEAVKAY--CIKYANERTAFGEPISHRQsvAFMI 344
Cdd:PTZ00456 281 GIKGSSTCQLSFENSVGYLIGEPNAGMKQMFTFMNTARVGTALeGVCHAELAFqnALRYARERRSMRALSGTKE--PEKP 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 345 ADMAIEIDAMRMLILNAASLAEAGKPFHREayLARLL---------CAEKSM--KIG------------------TDGVQ 395
Cdd:PTZ00456 359 ADRIICHANVRQNILFAKAVAEGGRALLLD--VGRLLdihaaakdaATREALdhEIGfytpiakgcltewgveaaSRCLQ 436
|
410 420
....*....|....*....|....*....
gi 1842333380 396 ILGGHGFTKEHPVERWYRDLRATAiLHSG 424
Cdd:PTZ00456 437 VWGGHGYIKGNGMEQILRDARIGT-LYEG 464
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
286-425 |
9.03e-06 |
|
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, which is active against Gram-positive bacteria. Polyketides are secondary metabolites, which have important biological functions such as antitumor, immunosupressive or antibiotic activities. NcnH is a hydroxylase involved in the biosynthesis of naphthocyclinone and possibly other polyketides.
Pssm-ID: 173848 [Multi-domain] Cd Length: 370 Bit Score: 47.34 E-value: 9.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 286 RLGATDFDYTAFLDLGNLMWCAMAVGTCEAVKAYCIKYANER---TAFGEPISHRQSVAFMIADMAIEIDAMRMLILNAA 362
Cdd:cd01159 206 PGGSTPVYRMPLRQVFPLSFAAVSLGAAEGALAEFLELAGKRvrqYGAAVKMAEAPITQLRLAEAAAELDAARAFLERAT 285
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1842333380 363 S----LAEAGKPFH-REAYLARLLCAEKSmKIGTDGVQIL----GGHGFTKEHPVERWYRDLRATAiLHSGL 425
Cdd:cd01159 286 RdlwaHALAGGPIDvEERARIRRDAAYAA-KLSAEAVDRLfhaaGGSALYTASPLQRIWRDIHAAA-QHAAL 355
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
194-279 |
1.92e-04 |
|
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: 40.34 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 194 TFAVQEATPAFNPYVLKTKA-SLENDQYFIEGEKTLVILGDLADVFLVSA-----DFNGKPDVFVVQAGDT-ISIKSTPA 266
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLArtggdDRHGGISLFLVPKDAPgVSVRRIET 80
|
90
....*....|....
gi 1842333380 267 -MGLKAAETATLKF 279
Cdd:pfam02770 81 kLGVRGLPTGELVF 94
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
301-419 |
2.40e-04 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 43.63 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842333380 301 GNLMWCAMAVGTCEAVKAYCIKYANERTAFGEPISHRQSVAFMIADMAIEIDAMRMLILNAA-SLAEAGKPFHREAY-LA 378
Cdd:PLN02876 679 GRLHHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAAdQLDRLGNKKARGIIaMA 758
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1842333380 379 RLLCAEKSMKIGTDGVQILGGHGFTKEHPVERwyrdLRATA 419
Cdd:PLN02876 759 KVAAPNMALKVLDMAMQVHGAAGVSSDTVLAH----LWATA 795
|
|
| |
