|
Name |
Accession |
Description |
Interval |
E-value |
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
66-442 |
1.04e-119 |
|
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: 354.15 E-value: 1.04e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 66 MQKSLGKLIEEKINPNVAKWEQDGRYPAHLVfKMLGDHGVFGVNKPEAFGGTGTDIAMATAIAEQMGAInCGSIPMSVMV 145
Cdd:COG1960 12 LRDEVREFAEEEIAPEAREWDREGEFPRELW-RKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARA-DASLALPVGV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 146 qTDMSTPALAQFGSDALRERFLRPSITGDLVSSLAVSEPHAGSDVSAVHTHARRQGSDLIINGSKMWITNGGQADWACVL 225
Cdd:COG1960 90 -HNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVADVILVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 226 VNTSNTSNvHKNKSLVCVPLDAVGVHRSTPLDKLGMRSSDTVQLFFEDVRVPSSYIIGEEGRGFGYQMKQFNDERLVTVA 305
Cdd:COG1960 169 ARTDPAAG-HRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGRLGLAA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 306 VGLLPLQKCIDETIEYARDRLLFGKTLLDQQYIQFQLAELEAELEATRALLYRTVLARSRGDDVSMLTAMAKLKIGRLAR 385
Cdd:COG1960 248 QALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLFATEAAL 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 17505929 386 AITDQCLQVWGGAGYLNENGISRAFRDFRLFSIGAGCDEVMMRIIhkaqSRRQLKKA 442
Cdd:COG1960 328 EVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLII----ARRLLGRP 380
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
149-430 |
1.95e-98 |
|
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: 297.66 E-value: 1.95e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 149 MSTPALAQFGSDALRERFLRPSITGDLVSSLAVSEPHAGSDVSAVHTHARRQGSDLIINGSKMWITNGGQADWACVLVNT 228
Cdd:cd00567 43 LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLART 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 229 SNTSNVHKNKSLVCVPLDAVGVHRSTPLDKLGMRSSDTVQLFFEDVRVPSSYIIGEEGRGFGYQMKQFNDERLVTVAVGL 308
Cdd:cd00567 123 DEEGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLLAAVAL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 309 LPLQKCIDETIEYARDRLLFGKTLLDQQYIQFQLAELEAELEATRALLYRTVLARSRG-DDVSMLTAMAKLKIGRLARAI 387
Cdd:cd00567 203 GAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGpDEARLEAAMAKLFATEAAREV 282
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 17505929 388 TDQCLQVWGGAGYLNENGISRAFRDFRLFSIGAGCDEVMMRII 430
Cdd:cd00567 283 ADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLII 325
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
61-432 |
2.14e-98 |
|
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: 299.42 E-value: 2.14e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 61 ETHFVMQKSLGKLIEEKINPNVAKWEQDGRYPAHLVFKMlGDHGVFGVNKPEAFGGTGTDIAMATAIAEQMGAINCGSIp 140
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKA-GEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGSGP- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 141 mSVMVQTDMSTPALAQFGSDALRERFLRPSITGDLVSSLAVSEPHAGSDVSAVHTHARRQGSDLIINGSKMWITNGGQAD 220
Cdd:cd01160 79 -GLSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 221 WACVLVNTSNTSNVHKNKSLVCVPLDAVGVHRSTPLDKLGMRSSDTVQLFFEDVRVPSSYIIGEEGRGFGYQMKQFNDER 300
Cdd:cd01160 158 VVIVVARTGGEARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQER 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 301 LVTVAVGLLPLQKCIDETIEYARDRLLFGKTLLDQQYIQFQLAELEAELEATRALLYRTVLARSRGDDVSMLTAMAKLKI 380
Cdd:cd01160 238 LLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWA 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 17505929 381 GRLARAITDQCLQVWGGAGYLNENGISRAFRDFRLFSIGAGCDEVMMRIIHK 432
Cdd:cd01160 318 TELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISR 369
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
61-433 |
6.14e-93 |
|
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: 285.32 E-value: 6.14e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 61 ETHFVMQKSLGKLIEEKINPNVAKWEQDGRYPAHLVFKMlGDHGVFGVNKPEAFGGTGTDIaMATAIA-EQMGAInCGSI 139
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEM-AELGLMGIPIPEEYGGAGLDF-LAYAIAiEELAKV-DASV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 140 PMSVMVQTDMSTPALAQFGSDALRERFLRPSITGDLVSSLAVSEPHAGSDVSAVHTHARRQGSDLIINGSKMWITNGGQA 219
Cdd:cd01158 78 AVIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 220 DWACVLVNTsNTSNVHKNKSLVCVPLDAVGVHRSTPLDKLGMRSSDTVQLFFEDVRVPSSYIIGEEGRGFGYQMKQFNDE 299
Cdd:cd01158 158 DFYIVFAVT-DPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 300 RLVTVAVGLLPLQKCIDETIEYARDRLLFGKTLLDQQYIQFQLAELEAELEATRALLYRTVLARSRGDDVSMLTAMAKLK 379
Cdd:cd01158 237 RIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLF 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 17505929 380 IGRLARAITDQCLQVWGGAGYLNENGISRAFRDFRLFSIGAGCDEVMMRIIHKA 433
Cdd:cd01158 317 ASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKH 370
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
59-433 |
5.46e-78 |
|
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: 246.94 E-value: 5.46e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 59 YDETHFVMQKSLGKLIEEKINPNVAKWEQDGRYPAHLvFKMLGDHGVFGVNKPEAFGGTGTDIaMATAIAEQMGAINCGS 138
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDL-WRKMGKLGLLGITAPEEYGGSGMGY-LAHVIIMEEISRASGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 139 IPMSVMVQTDMSTPALAQFGSDALRERFLRPSITGDLVSSLAVSEPHAGSDVSAVHTHARRQGSDLIINGSKMWITNGGQ 218
Cdd:cd01156 80 VALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 219 ADWACVLVNTsNTSNVHKNKSLVCVPLDAVGVHRSTPLDKLGMRSSDTVQLFFEDVRVPSSYIIGEEGRGFGYQMKQFND 298
Cdd:cd01156 160 ADTLVVYAKT-DPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 299 ERLVTVA--VGLlpLQKCIDETIEYARDRLLFGKTLLDQQYIQFQLAELEAELEATRALLYRTVLARSRGDDVSMLTAMA 376
Cdd:cd01156 239 ERLVLAGgpIGI--MQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGV 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 17505929 377 KLKIGRLARAITDQCLQVWGGAGYLNENGISRAFRDFRLFSIGAGCDEVMMRIIHKA 433
Cdd:cd01156 317 ILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRE 373
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
69-441 |
3.63e-65 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 213.82 E-value: 3.63e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 69 SLGKLIEEKINPN-VAKWEQDGRYPAHLvFKMLGDHGVFGVNKPEAFGGTGTDIAMATAIAEQMgAINCGSIPM--SVMV 145
Cdd:PRK12341 15 SIRELITRNFPEEyFRTCDENGTYPREF-MRALADNGISMLGVPEEFGGTPADYVTQMLVLEEV-SKCGAPAFLitNGQC 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 146 QTDMSTpalaqFGSD-ALRERFLRPSITGDLVSSLAVSEPHAGSDVSAVHTHARRQGSDLIINGSKMWITNGGQADWACV 224
Cdd:PRK12341 93 IHSMRR-----FGSAeQLRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAKEYPYMLV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 225 LVNTSNTSNVHKNKSLVCVPLDAVGVHRStPLDKLGMRSSDTVQLFFEDVRVPSSYIIGEEGRGFGYQMKQFNDERLVTV 304
Cdd:PRK12341 168 LARDPQPKDPKKAFTLWWVDSSKPGIKIN-PLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFEMERLINA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 305 AVGLLPLQKCIDETIEYARDRLLFGKTLLDQQYIQFQLAELEAELEATRALLYRTVLARSRGDDVSMLTAMAKLKIGRLA 384
Cdd:PRK12341 247 ARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAALAKLYCARTA 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 17505929 385 RAITDQCLQVWGGAGYLNENGISRAFRDFRLFSIGAGCDEVMmriIHKAqSRRQLKK 441
Cdd:PRK12341 327 MEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIM---IYIA-GRQILKD 379
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
65-437 |
3.72e-62 |
|
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: 205.75 E-value: 3.72e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 65 VMQKSLGKLIEEKINPNVAKWEQDGRYPAHlVFKMLGDHGVFGVNKPEAFGGTGTDIAMATAIAEQMgAINCGSIPMSVM 144
Cdd:cd01162 7 AIQEVARAFAAKEMAPHAADWDQKKHFPVD-VLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEAL-STGCVSTAAYIS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 145 VQtDMSTPALAQFGSDALRERFLRPSITGDLVSSLAVSEPHAGSDVSAVHTHARRQGSDLIINGSKMWITNGGQADWACV 224
Cdd:cd01162 85 IH-NMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDVYVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 225 LVNTSNTSNvhKNKSLVCVPLDAVGVHRSTPLDKLGMRSSDTVQLFFEDVRVPSSYIIGEEGRGFGYQMKQFNDERLVTV 304
Cdd:cd01162 164 MARTGGEGP--KGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 305 AVGLLPLQKCIDETIEYARDRLLFGKTLLDQQYIQFQLAELEAELEATRALLYRTVLARSRGD-DVSMLTAMAKLKIGRL 383
Cdd:cd01162 242 SCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDpDAVKLCAMAKRFATDE 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 17505929 384 ARAITDQCLQVWGGAGYLNENGISRAFRDFRLFSIGAGCDEVMMRIIHKAQSRR 437
Cdd:cd01162 322 CFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
26-430 |
1.07e-57 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 195.10 E-value: 1.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 26 RSSNLGNQRRSVSVAVTSTSPKsekpvarehMIYDETHFVMQKSLGKLIEEKINPNVAKWEQDGRYPAHL-VFKMLGDHG 104
Cdd:PLN02519 2 LLSAAKARRRGLARRFSSSSSS---------LLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVnLWKLMGDFN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 105 VFGVNKPEAFGGTGTDIaMATAIAEQMGAINCGSIPMSVMVQTDMSTPALAQFGSDALRERFLRPSITGDLVSSLAVSEP 184
Cdd:PLN02519 73 LHGITAPEEYGGLGLGY-LYHCIAMEEISRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 185 HAGSDVSAVHTHARRQGSDLIINGSKMWITNGGQADWACVLVNTSNTSNVHKNKSLVcVPLDAVGVHRSTPLDKLGMRSS 264
Cdd:PLN02519 152 NSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTDVAAGSKGITAFI-IEKGMPGFSTAQKLDKLGMRGS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 265 DTVQLFFEDVRVPSSYIIGEEGRGFGYQMKQFNDERLVTVAVGLLPLQKCIDETIEYARDRLLFGKTLLDQQYIQFQLAE 344
Cdd:PLN02519 231 DTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLAD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 345 LEAELEATRALLYRTVLARSRGDDVSMLTAMAKLKIGRLARAITDQCLQVWGGAGYLNENGISRAFRDFRLFSIGAGCDE 424
Cdd:PLN02519 311 MYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSE 390
|
....*.
gi 17505929 425 VMMRII 430
Cdd:PLN02519 391 IRRMLI 396
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
61-432 |
1.22e-57 |
|
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: 193.96 E-value: 1.22e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 61 ETHFVMQKSLGKLIEEKINPNVAKWEQDGRYPAHLVfKMLGDHGVFGVNKPEAFGGTGTDIAMATAIAEQMgAINCGSIp 140
Cdd:cd01157 3 EQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLI-KRAWELGLMNTHIPEDCGGLGLGTFDTCLITEEL-AYGCTGV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 141 msvmvQTDMSTPALAQF-----GSDALRERFLRPSITGDLVSSLAVSEPHAGSDVSAVHTHARRQGSDLIINGSKMWITN 215
Cdd:cd01157 80 -----QTAIEANSLGQMpviisGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 216 GGQADWACVLVNTSNTSNVHKNKSLV--CVPLDAVGVHRSTPLDKLGMRSSDTVQLFFEDVRVPSSYIIGEEGRGFGYQM 293
Cdd:cd01157 155 GGKANWYFLLARSDPDPKCPASKAFTgfIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 294 KQFNDERLVtVAVGLLPL-QKCIDETIEYARDRLLFGKTLLDQQYIQFQLAELEAELEATRALLYRTVLARSRGDDVSML 372
Cdd:cd01157 235 GAFDKTRPP-VAAGAVGLaQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYY 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 373 TAMAKLKIGRLARAITDQCLQVWGGAGYLNENGISRAFRDFRLFSIGAGCDEVMMRIIHK 432
Cdd:cd01157 314 ASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISR 373
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
61-426 |
5.30e-57 |
|
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: 193.45 E-value: 5.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 61 ETHFVMQKSLGKLIEEKINPnvAKWEQDGRYPAHLVfKMLGDHGVFGVNKPEAFGGTGTDIAMATAIAEQMGAinCGSIP 140
Cdd:cd01161 29 EELNMLVGPVEKFFEEVNDP--AKNDQLEKIPRKTL-TQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGM--DLGFS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 141 MSVMVQTDMSTPALAQFGSDALRERFLRPSITGDLVSSLAVSEPHAGSDVSAVHTHARRQ--GSDLIINGSKMWITNGGQ 218
Cdd:cd01161 104 VTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSedGKHYVLNGSKIWITNGGI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 219 ADWACVLVNT---SNTSNVHKNKSLVCVPLDAVGVHRSTPLDKLGMRSSDTVQLFFEDVRVPSSYIIGEEGRGFGYQMKQ 295
Cdd:cd01161 184 ADIFTVFAKTevkDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMNI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 296 FNDERLVTVAVGLLPLQKCIDETIEYARDRLLFGKTLLDQQYIQFQLAELEAELEATRALLYRT--VLARSRGDDVSMLT 373
Cdd:cd01161 264 LNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTsgNMDRGLKAEYQIEA 343
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 17505929 374 AMAKLKIGRLARAITDQCLQVWGGAGYLNENGISRAFRDFRLFSIGAGCDEVM 426
Cdd:cd01161 344 AISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEIL 396
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
98-430 |
1.81e-50 |
|
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: 175.23 E-value: 1.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 98 KMLGDHGVFGVNKPEAFGGTGTDIAMATAIAEQMGAInCGSIPMSvMVQTDMSTPALAQFGSDALRERFLRPSITGDLVS 177
Cdd:cd01152 42 RALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAA-GAPVPFN-QIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIW 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 178 SLAVSEPHAGSDVSAVHTHARRQGSDLIINGSKMWITNGGQADWACVLVNTSNTSNVHKNKSLVCVPLDAVGVHRsTPLD 257
Cdd:cd01152 120 CQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDPEAPKHRGISILLVDMDSPGVTV-RPIR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 258 KLgMRSSDTVQLFFEDVRVPSSYIIGEEGRGFGYQMKQFNDERLVTVAVGLLPLQKCIDETIEYARDrllfGKTLLDQQY 337
Cdd:cd01152 199 SI-NGGEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIGGSAATFFELLLARLLLLTRD----GRPLIDDPL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 338 IQFQLAELEAELEATRALLYRTVLARSRGDDVSMLTAMAKLKIGRLARAITDQCLQVWGGAGYLNENG--------ISRA 409
Cdd:cd01152 274 VRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFGSELAQELAELALELLGTAALLRDPApgaelagrWEAD 353
|
330 340
....*....|....*....|.
gi 17505929 410 FRDFRLFSIGAGCDEVMMRII 430
Cdd:cd01152 354 YLRSRATTIYGGTSEIQRNII 374
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
34-432 |
2.97e-49 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 172.81 E-value: 2.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 34 RRSVSVAVTSTSPKSEkpVAREHM-IYDET--HFVMQKSLGKLIEEKINPNVAKWEQDGRYPAHLvFKMLGDHGVFGVNK 110
Cdd:PTZ00461 11 RRSATCGWTAAATMTS--ASRAFMdLYNPTpeHAALRETVAKFSREVVDKHAREDDINMHFNRDL-FKQLGDLGVMGVTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 111 PEAFGGTGTDIAMATAIAEQMGAINCGsIPMSVMVQTDMSTPALAQFGSDALRERFLRPSITGDLVSSLAVSEPHAGSDV 190
Cdd:PTZ00461 88 PEADGGAGMDAVAAVIIHHELSKYDPG-FCLAYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 191 SAVHTHARRQGS-DLIINGSKMWITNGGQADwaCVLVntsnTSNVHKNKSLVCVPLDAVGVHRSTPLDKLGMRSSDTVQL 269
Cdd:PTZ00461 167 LGMRTTAKKDSNgNYVLNGSKIWITNGTVAD--VFLI----YAKVDGKITAFVVERGTKGFTQGPKIDKCGMRASHMCQL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 270 FFEDVRVPSSYIIGEEGRGFGYQMKQFNDERLVTVAVGLLPLQKCIDETIEYARDRLLFGKTLLDQQYIQFQLAELEAEL 349
Cdd:PTZ00461 241 FFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 350 EATRALLYRTVLARSRGDDVSMLTAMAKLKIGRLARAITDQCLQVWGGAGYLNENGISRAFRDFRLFSIGAGCDEVMMRI 429
Cdd:PTZ00461 321 EAAKALVYSVSHNVHPGNKNRLGSDAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKN 400
|
...
gi 17505929 430 IHK 432
Cdd:PTZ00461 401 ITK 403
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
286-433 |
3.41e-42 |
|
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.
Pssm-ID: 395354 [Multi-domain] Cd Length: 149 Bit Score: 146.25 E-value: 3.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 286 GRGFGYQMKQFNDERLVTVAVGLLPLQKCIDETIEYARDRLLFGKTLLDQQYIQFQLAELEAELEATRALLYRTVLARSR 365
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17505929 366 GDDVSMLTAMAKLKIGRLARAITDQCLQVWGGAGYLNENGISRAFRDFRLFSIGAGCDEVMMRIIHKA 433
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARR 148
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
70-421 |
1.75e-38 |
|
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: 143.68 E-value: 1.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 70 LGKLIEEKINPNVAKWEQDG--------RYPAHLV--FKMLGDHGVFGVNKPEAFGGTGTDIAMATAIAEQMGAincGSI 139
Cdd:cd01153 5 VARLAENVLAPLNADGDREGpvfddgrvVVPPPFKeaLDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSR---GDA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 140 PMSVMVQTDMSTPALAQFGSDALRERFLRPSITGDLVSSLAVSEPHAGSDVSAVHTHARRQGS-DLIINGSKMWITNGGQ 218
Cdd:cd01153 82 PLMYASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGEH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 219 ADWA----CVLVNTSNTSNVHKNKSLVCVPLDAVGVHRSTPL-----DKLGMRSSDTVQLFFEDVRVPssyIIGEEGRGF 289
Cdd:cd01153 162 DMSEnivhLVLARSEGAPPGVKGLSLFLVPKFLDDGERNGVTvarieEKMGLHGSPTCELVFDNAKGE---LIGEEGMGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 290 GYQMKQFNDERLVTVAVGLLPLQKCIDETIEYARDRLLFGKTLLDQQYIQFQLAELEAELEATRALLYRTVLA------- 362
Cdd:cd01153 239 AQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAPAVTIIHHPDVRRSLMTQKAYAEGSRAldlytat 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17505929 363 --------RSRGDDVS-------MLTAMAKLKIGRLARAITDQCLQVWGGAGYLNENGISRAFRDFRLFSIGAG 421
Cdd:cd01153 319 vqdlaerkATEGEDRKalsaladLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEG 392
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
83-437 |
6.28e-36 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 136.11 E-value: 6.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 83 AKWEQDGRYPAHLVfKMLGDHGVFGVNKPEAFGGTGTDIAMATAIAEQMGAINCgsiPMSVMVQTDMSTPALAQFGSDAL 162
Cdd:PRK03354 30 AECDRDSVYPERFV-KALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGA---PTYVLYQLPGGFNTFLREGTQEQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 163 RERFLRPSITGDLVSSLAVSEPHAGSDVSAVHTHARRQGSDLIINGSKMWITNGGQADWACVLVNTSNTSNVHKNKSLVc 242
Cdd:PRK03354 106 IDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASPDKPVYTEWF- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 243 VPLDAVGVHRStPLDKLGMRSSDTVQLFFEDVRVPSSYIIGEEGRGFGYQMKQFNDERLVTVAVGLLPLQKCIDETIEYA 322
Cdd:PRK03354 185 VDMSKPGIKVT-KLEKLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 323 RDRLLFGKTLLDQQYIQFQLAELEAELEATRALLYRTVLARSRGDDVSMLTAMAKLKIGRLARAITDQCLQVWGGAGYLN 402
Cdd:PRK03354 264 NQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAG 343
|
330 340 350
....*....|....*....|....*....|....*
gi 17505929 403 ENGISRAFRDFRLFSIGAGCDEVMMRIIHKAQSRR 437
Cdd:PRK03354 344 NHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQ 378
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
67-412 |
3.34e-34 |
|
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: 131.71 E-value: 3.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 67 QKSLGKLIEEKINPNVAKWEQDGRYPAHLvFKMLGDHGVFGVNkPEAFGGTGTDIAMATAIAEQMGAINCGsIPMSVMVQ 146
Cdd:cd01151 21 RDTAREFCQEELAPRVLEAYREEKFDRKI-IEEMGELGLLGAT-IKGYGCAGLSSVAYGLIAREVERVDSG-YRSFMSVQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 147 TDMSTPALAQFGSDALRERFLRPSITGDLVSSLAVSEPHAGSDVSAVHTHARRQGSDLIINGSKMWITNGGQADWACVLV 226
Cdd:cd01151 98 SSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIADVFVVWA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 227 NTSNTSNVHKnkslVCVPLDAVGVHRSTPLDKLGMRSSDTVQLFFEDVRVPSSYIIgEEGRGFGYQMKQFNDERLVTVAV 306
Cdd:cd01151 178 RNDETGKIRG----FILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL-PGAEGLRGPFKCLNNARYGIAWG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 307 GLLPLQKCIDETIEYARDRLLFGKTLLDQQYIqfQLAELEAELEATRALLYRTVLAR--SRGDDVSMLTAMAKLKIGRLA 384
Cdd:cd01151 253 ALGAAEDCYHTARQYVLDRKQFGRPLAAFQLV--QKKLADMLTEIALGLLACLRVGRlkDQGKATPEQISLLKRNNCGKA 330
|
330 340
....*....|....*....|....*...
gi 17505929 385 RAITDQCLQVWGGAGYLNENGISRAFRD 412
Cdd:cd01151 331 LEIARTAREMLGGNGISDEYHIIRHMVN 358
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
111-436 |
9.74e-29 |
|
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: 116.72 E-value: 9.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 111 PEAFGGTGTDIAMATAIAEQMG-------AINCGSiP----MSVmvqtdmstpaLAQFGSDALRERFLRPSITGDLVSSL 179
Cdd:cd01155 61 PEVSGLSGLTNLEYAYLAEETGrsffapeVFNCQA-PdtgnMEV----------LHRYGSEEQKKQWLEPLLDGKIRSAF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 180 AVSEPH-AGSDVSAVHTHARRQGSDLIINGSKMWITNGGQADW--ACVLVNTSNTSN-VHKNKSLVCVPLDAVGVHRSTP 255
Cdd:cd01155 130 AMTEPDvASSDATNIECSIERDGDDYVINGRKWWSSGAGDPRCkiAIVMGRTDPDGApRHRQQSMILVPMDTPGVTIIRP 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 256 LDKLGmrSSDT----VQLFFEDVRVPSSYIIGEEGRGFGYQMKQFNDERL--VTVAVGLlpLQKCIDETIEYARDRLLFG 329
Cdd:cd01155 210 LSVFG--YDDAphghAEITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIhhCMRLIGA--AERALELMCQRAVSREAFG 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 330 KTLLDQQYIQFQLAELEAELEATRALLYRTVLARSRGDDVSMLT--AMAKLKIGRLARAITDQCLQVWGGAGYLNENGIS 407
Cdd:cd01155 286 KKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTVGNKAARKeiAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLA 365
|
330 340
....*....|....*....|....*....
gi 17505929 408 RAFRDFRLFSIGAGCDEVMMRIIHKAQSR 436
Cdd:cd01155 366 NMYAWARTLRIADGPDEVHLRSIARMELK 394
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
60-174 |
2.35e-27 |
|
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: 105.24 E-value: 2.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 60 DETHFVMQKSLGKLIEEKINPNVAKWEQDGRYPAHLvFKMLGDHGVFGVNKPEAFGGTGTDIAMATAIAEQMGAInCGSI 139
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPREL-WKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARA-DASV 78
|
90 100 110
....*....|....*....|....*....|....*
gi 17505929 140 PMSVMVQTDMSTPALAQFGSDALRERFLRPSITGD 174
Cdd:pfam02771 79 ALALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
147-426 |
1.65e-26 |
|
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: 110.54 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 147 TDMSTPALAQFGSDALRERFLRpsITGD-----LVSSLAVSEPHAGSDVSAVHTHARRQGSDL-IINGSKmWITNGGQAD 220
Cdd:cd01154 116 TDAAVYALRKYGPEELKQYLPG--LLSDryktgLLGGTWMTEKQGGSDLGANETTAERSGGGVyRLNGHK-WFASAPLAD 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 221 WACVLVNTSNTSNVHKNKSLVCVP-------LDAVGVHRSTplDKLGMRSSDTVQLFFEDVrvpSSYIIGEEGRGFGYQM 293
Cdd:cd01154 193 AALVLARPEGAPAGARGLSLFLVPrlledgtRNGYRIRRLK--DKLGTRSVATGEVEFDDA---EAYLIGDEGKGIYYIL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 294 KQFNDERLVTVAVGLLPLQKCIDETIEYARDRLLFGKTLLDQQYIQFQLAELEAELEATRALLYRTVLA--RSRGDD--- 368
Cdd:cd01154 268 EMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAfdRAAADKpve 347
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17505929 369 ---VSMLTAMAKLKIGRLARAITDQCLQVWGGAGYLNENGISRAFRDFRLFSIGAGCDEVM 426
Cdd:cd01154 348 ahmARLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQ 408
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
178-272 |
8.25e-20 |
|
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: 83.87 E-value: 8.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 178 SLAVSEPHAGSDVSAVHTHA-RRQGSDLIINGSKMWITNGGQADWACVLVNTSNTSNvHKNKSLVCVPLDAVGVHRSTPL 256
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDR-HGGISLFLVPKDAPGVSVRRIE 79
|
90
....*....|....*.
gi 17505929 257 DKLGMRSSDTVQLFFE 272
Cdd:pfam02770 80 TKLGVRGLPTGELVFD 95
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
97-421 |
9.41e-20 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 91.85 E-value: 9.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 97 FKMLGDHGVFGVNKPEAFGGTGTDIAMATAIAEQMGAINCGSIPMSVMVQTDMSTpaLAQFGSDALRERFLRPSITGDLV 176
Cdd:PTZ00456 105 YQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPGLSIGAANT--LMAWGSEEQKEQYLTKLVSGEWS 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 177 SSLAVSEPHAGSDVSAVHTHARRQGS-DLIINGSKMWITnGGQADWA-----CVLVNTSNTSNVHKNKSLVCVP------ 244
Cdd:PTZ00456 183 GTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFIS-AGDHDLTenivhIVLARLPNSLPTTKGLSLFLVPrhvvkp 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 245 ---------LDAVGVHRstpldKLGMRSSDTVQLFFEDvrvPSSYIIGEEGRGFgYQMKQF-NDERLVTVAVGLLPLQKC 314
Cdd:PTZ00456 262 dgsletaknVKCIGLEK-----KMGIKGSSTCQLSFEN---SVGYLIGEPNAGM-KQMFTFmNTARVGTALEGVCHAELA 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 315 IDETIEYARDRL----LFGKT--------LLDQQYIQFQLAELEAELEATRALLYRT-------------VLARSRGDDV 369
Cdd:PTZ00456 333 FQNALRYARERRsmraLSGTKepekpadrIICHANVRQNILFAKAVAEGGRALLLDVgrlldihaaakdaATREALDHEI 412
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 17505929 370 SMLTAMAKLKIGRLARAITDQCLQVWGGAGYLNENGISRAFRDFRLFSIGAG 421
Cdd:PTZ00456 413 GFYTPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEG 464
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
154-437 |
2.10e-19 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 91.01 E-value: 2.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 154 LAQFGSDALRERFLRPSITGDLVSSLAVSEPH-AGSDVSAVHTHARRQGSDLIINGSKMWITngGQADWAC----VLVNT 228
Cdd:PLN02876 529 LLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTS--GAMDPRCrvliVMGKT 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 229 SNTSNVHKNKSLVCVPLDAVGVHRSTPLDKLGMRSS--DTVQLFFEDVRVPSSYIIGEEGRGFGYQMKQFNDERLVTVAV 306
Cdd:PLN02876 607 DFNAPKHKQQSMILVDIQTPGVQIKRPLLVFGFDDAphGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMR 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 307 GLLPLQKCIDETIEYARDRLLFGKTLLDQQYIQFQLAELEAELEATRALLYRTVLARSR-GDDVSMLT-AMAKLKIGRLA 384
Cdd:PLN02876 687 LIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDRlGNKKARGIiAMAKVAAPNMA 766
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 17505929 385 RAITDQCLQVWGGAGYLNENGISRAFRDFRLFSIGAGCDEVMMRIIHKAQSRR 437
Cdd:PLN02876 767 LKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEVHLGTIAKLELQR 819
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
37-277 |
1.55e-16 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 81.05 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 37 VSVAVTSTSPKSE-KPVAREHMIYDETHFVMQKSLGKLI----EEKINPNVAKWEQDGRYPAHLVFKmLGDHGVFGvNKP 111
Cdd:PLN02526 2 VSVAFPQATPASIfPPSVSDYYQFDDLLTPEEQALRKRVrecmEKEVAPIMTEYWEKAEFPFHIIPK-LGSLGIAG-GTI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 112 EAFGGTGTDI-AMATAIAEQmgAINCGSIPMSVMVQTDMSTPALAQFGSDALRERFLrPSITG-DLVSSLAVSEPHAGSD 189
Cdd:PLN02526 80 KGYGCPGLSItASAIATAEV--ARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYL-PSLAQlDTVACWALTEPDYGSD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 190 VSAVHTHARRQGSDLIINGSKMWITNGGQADWACVLVNTSNTSNVHKnkslVCVPLDAVGVHRSTPLDKLGMRSSDTVQL 269
Cdd:PLN02526 157 ASSLNTTATKVEGGWILNGQKRWIGNSTFADVLVIFARNTTTNQING----FIVKKGAPGLKATKIENKIGLRMVQNGDI 232
|
....*...
gi 17505929 270 FFEDVRVP 277
Cdd:PLN02526 233 VLKDVFVP 240
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
301-412 |
1.07e-10 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 59.28 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 301 LVTVAVGLLplQKCIDETIEYARDR--LLFGKTLLDQQYIQFQLAELEAELEATRALLYRTV----LARSRGDDVSMLT- 373
Cdd:pfam08028 2 IAAAALGAA--RAALAEFTERARGRvrAYFGVPLAEDPATQLALAEAAARIDAARLLLERAAarieAAAAAGKPVTPALr 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 17505929 374 ---AMAKLKIGRLARAITDQCLQVWGGAGYLNENGISRAFRD 412
Cdd:pfam08028 80 aeaRRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRD 121
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
175-432 |
1.24e-08 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 57.07 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 175 LVSSLAVSEPHAGSDVSAVHTHARR-QGSDLIINGSKmWITNGGQADWACVLVNTSNtsnvhknkSLVC--VP------- 244
Cdd:PRK11561 178 LLIGMGMTEKQGGSDVLSNTTRAERlADGSYRLVGHK-WFFSVPQSDAHLVLAQAKG--------GLSCffVPrflpdgq 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 245 LDAVGVHRSTplDKLGMRSSDTVQLFFEDVrvpSSYIIGEEGRGFGYQMKQFNDERLvTVAVGLLPL-QKCIDETIEYAR 323
Cdd:PRK11561 249 RNAIRLERLK--DKLGNRSNASSEVEFQDA---IGWLLGEEGEGIRLILKMGGMTRF-DCALGSHGLmRRAFSVAIYHAH 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 324 DRLLFGKTLLDQQYIQFQLAELEAELEATRALLYRTVLARSRGDDVS------MLTAMAKLKIGRLARAITDQCLQVWGG 397
Cdd:PRK11561 323 QRQVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDRRADAKealwarLFTPAAKFVICKRGIPFVAEAMEVLGG 402
|
250 260 270
....*....|....*....|....*....|....*....
gi 17505929 398 AGYLNENGISRAFRDFRLFSIGAGCDEVM----MRIIHK 432
Cdd:PRK11561 403 IGYCEESELPRLYREMPVNSIWEGSGNIMcldvLRVLNK 441
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
76-414 |
4.08e-08 |
|
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, which catalyzes the first two steps of DBT desulfurization in mesophilic bacteria. DszC converts DBT to DBT-sulfoxide, which is then converted to DBT-sulfone. Bacteria with this enzyme are candidates for the removal of organic sulfur compounds from fossil fuels, which pollute the environment. An equivalent enzyme tdsC, is found in thermophilic bacteria. This alignment also contains a closely related uncharacterized subgroup.
Pssm-ID: 173852 [Multi-domain] Cd Length: 377 Bit Score: 55.02 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 76 EKINPNVAKWEQDGRYPaHLVFKMLGDHGVFGVNKPEAFGGTGTDIAMATAIAEQMGAINcGSIPMSVMVQTDMsTPALA 155
Cdd:cd01163 8 ARIAEGAAERDRQRGLP-YEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAAD-SNIAQALRAHFGF-VEALL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 156 QFGSDALRERFLRPSITGDLVSSlAVSE---PHAGSDVSAVHTHarrqGSDLIINGSKMWITNGGQADWACVLVNTSNTS 232
Cdd:cd01163 85 LAGPEQFRKRWFGRVLNGWIFGN-AVSErgsVRPGTFLTATVRD----GGGYVLNGKKFYSTGALFSDWVTVSALDEEGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 233 NVHknkslVCVPLDAVGVHRSTPLDKLGMRSSDTVQLFFEDVRVPSSYIIG-----EEGRGFG--YQMKqfnderLVTVA 305
Cdd:cd01163 160 LVF-----AAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPrpnapDRGTLLTaiYQLV------LAAVL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 306 VGLlpLQKCIDETIEYARDRllfGKTLL--------DQQYIQFQLAELEAELEATRALL-------------YRTVLARS 364
Cdd:cd01163 229 AGI--ARAALDDAVAYVRSR---TRPWIhsgaesarDDPYVQQVVGDLAARLHAAEALVlqaaraldaaaaaGTALTAEA 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 17505929 365 RGdDVSMLTAMAKLKIGRLARAITDQCLQVWGGAGYLNENGISRAFRDFR 414
Cdd:cd01163 304 RG-EAALAVAAAKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNAR 352
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
86-412 |
5.70e-04 |
|
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: 41.95 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 86 EQDGRYPAHLVfKMLGDHGVFGVNKPEAFGGTGTDIAMATAIAEQMGAInCGSIPMSVMVQTdMSTPALAQFGSDAlRER 165
Cdd:cd01159 18 ERARRLPDEVV-RALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEA-CGSAAWVASIVA-THSRMLAAFPPEA-QEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 166 FLRPSITGDLVSSLAVSEPhagsdvsavhthARRQGSDLIINGSKMWITNGGQADWACVLVNTSNTSNVHKNKSLVcVPL 245
Cdd:cd01159 94 VWGDGPDTLLAGSYAPGGR------------AERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDDGGPLPRAFV-VPR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 246 DAVGVhRSTpLDKLGMRSSDTVQLFFEDVRVPSSYII----GEEGRGFG-----YQM--KQFNDerLVTVAVGLLPLQKC 314
Cdd:cd01159 161 AEYEI-VDT-WHVVGLRGTGSNTVVVDDVFVPEHRTLtagdMMAGDGPGgstpvYRMplRQVFP--LSFAAVSLGAAEGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505929 315 IDETIEYARDR---LLFGKTLLDQQYIQFQLAELEAELEATRALLYRTV-----LARSRGDDVSMLTAMAKLKIGRLAR- 385
Cdd:cd01159 237 LAEFLELAGKRvrqYGAAVKMAEAPITQLRLAEAAAELDAARAFLERATrdlwaHALAGGPIDVEERARIRRDAAYAAKl 316
|
330 340
....*....|....*....|....*....
gi 17505929 386 --AITDQCLQVWGGAGYLNENGISRAFRD 412
Cdd:cd01159 317 saEAVDRLFHAAGGSALYTASPLQRIWRD 345
|
|
| |
