|
Name |
Accession |
Description |
Interval |
E-value |
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
48-414 |
0e+00 |
|
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: 712.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 48 FDWQDPLVLEEQLTTDEILIRDTFRTYCQERLMPRILLANRNEVFHREIISEMGELGVLGPTIKGYGCAGVSSVAYGLLA 127
Cdd:cd01151 1 FNWEDPLNLDDLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIKGYGCAGLSSVAYGLIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 128 RELERVDSGYRSAMSVQSSLVMHPIYAYGSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSMETRAHYNssNKSYTLN 207
Cdd:cd01151 81 REVERVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKD--GGGYKLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 208 GTKTWITNSPMADLFVVWARC-EDGCIRGFLLEKGMRGLSAPRIQGKFSLRASATGMIIMDGVEVPEENVLPGASSLGGP 286
Cdd:cd01151 159 GSKTWITNSPIADVFVVWARNdETGKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAEGLRGP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 287 FGCLNNARYGIAWGVLGASEFCLHTARQYALDRMQFGVPLARNQLIQKKLADMLTEITLGLHACLQLGRLKDQDKAAPEM 366
Cdd:cd01151 239 FKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQ 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 7669494 367 VSLLKRNNCGKALDIARQARDMLGGNGISDEYHVIRHAMNLEAVNTYE 414
Cdd:cd01151 319 ISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYE 366
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
59-414 |
1.62e-118 |
|
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: 350.29 E-value: 1.62e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 59 QLTTDEILIRDTFRTYCQERLMPRILLANRNEVFHREIISEMGELGVLGPTI-KGYGCAGVSSVAYGLLARELERVDSGY 137
Cdd:COG1960 4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIpEEYGGLGLSLVELALVLEELARADASL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 138 RSAMSVQSSlVMHPIYAYGSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSMETRAHYNssNKSYTLNGTKTWITNSP 217
Cdd:COG1960 84 ALPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRD--GDGYVLNGQKTFITNAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 218 MADLFVVWARCEDGC----IRGFLLEKGMRGLSAPRIQGKFSLRASATGMIIMDGVEVPEENVLPGAS-SLGGPFGCLNN 292
Cdd:COG1960 161 VADVILVLARTDPAAghrgISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGkGFKIAMSTLNA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 293 ARYGIAWGVLGASEFCLHTARQYALDRMQFGVPLARNQLIQKKLADMLTEITLGLHACLQLGRLKDQDKAAPEMVSLLKR 372
Cdd:COG1960 241 GRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKL 320
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 7669494 373 NNCGKALDIARQARDMLGGNGISDEYHVIRHAMNLEAVNTYE 414
Cdd:COG1960 321 FATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYE 362
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
66-414 |
1.72e-90 |
|
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: 276.86 E-value: 1.72e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 66 LIRDTFRTYCQERLMPRILLANRNEVFHREIISEMGELGVlgptikgygcagvssvaygllarelervdsgyrsamsvqs 145
Cdd:cd00567 5 ELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLLG---------------------------------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 146 slvMHPIYAYGSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSMETRAHYnsSNKSYTLNGTKTWITNSPMADLFVVW 225
Cdd:cd00567 45 ---AALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARK--DGDGYVLNGRKIFISNGGDADLFIVL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 226 ARCED-----GCIRGFLLEKGMRGLSAPRIQGKFSLRASATGMIIMDGVEVPEENVL-PGASSLGGPFGCLNNARYGIAW 299
Cdd:cd00567 120 ARTDEegpghRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLgEEGGGFELAMKGLNVGRLLLAA 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 300 GVLGASEFCLHTARQYALDRMQFGVPLARNQLIQKKLADMLTEITLGLHACLQLGRLKDQDKA-APEMVSLLKRNNCGKA 378
Cdd:cd00567 200 VALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDeARLEAAMAKLFATEAA 279
|
330 340 350
....*....|....*....|....*....|....*.
gi 7669494 379 LDIARQARDMLGGNGISDEYHVIRHAMNLEAVNTYE 414
Cdd:cd00567 280 REVADLAMQIHGGRGYSREYPVERYLRDARAARIAE 315
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
63-403 |
8.39e-84 |
|
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: 261.43 E-value: 8.39e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 63 DEILIRDTFRTYCQERLMPRILLANRNEVFHREIISEMGELGVLGPTI-KGYGCAGVSSVAYGLLARELERVDSGYRSAM 141
Cdd:cd01158 2 EHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIpEEYGGAGLDFLAYAIAIEELAKVDASVAVIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 142 SVQSSLVMHPIYAYGSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSMETRAHYNSSNksYTLNGTKTWITNSPMADL 221
Cdd:cd01158 82 SVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDD--YVLNGSKMWITNGGEADF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 222 FVVWARCEDGC----IRGFLLEKGMRGLSAPRIQGKFSLRASATGMIIMDGVEVPEENVLpgasslgGPFG--------C 289
Cdd:cd01158 160 YIVFAVTDPSKgyrgITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENIL-------GEEGegfkiamqT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 290 LNNARYGIAWGVLGASEFCLHTARQYALDRMQFGVPLARNQLIQKKLADMLTEITLGLHACLQLGRLKDQDKAAPEMVSL 369
Cdd:cd01158 233 LDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAM 312
|
330 340 350
....*....|....*....|....*....|....
gi 7669494 370 LKRNNCGKALDIARQARDMLGGNGISDEYHVIRH 403
Cdd:cd01158 313 AKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERY 346
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
56-414 |
1.40e-78 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 249.38 E-value: 1.40e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 56 LEEQLTTDEILIRDTFRTYCQERLMPRILLANRNEVFHREIISEMGELGVLGPTIKGYGCAGVSSVAYGLLARELERVDS 135
Cdd:PLN02526 25 FDDLLTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIKGYGCPGLSITASAIATAEVARVDA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 136 GYRSAMSVQSSLVMHPIYAYGSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSMETRAhyNSSNKSYTLNGTKTWITN 215
Cdd:PLN02526 105 SCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTA--TKVEGGWILNGQKRWIGN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 216 SPMADLFVVWAR-CEDGCIRGFLLEKGMRGLSAPRIQGKFSLRASATGMIIMDGVEVPEENVLPGASSLGGPFGCLNNAR 294
Cdd:PLN02526 183 STFADVLVIFARnTTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNSFQDTNKVLAVSR 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 295 YGIAWGVLGASEFCLHTARQYALDRMQFGVPLARNQLIQKKLADMLTEITLGLHACLQLGRLKDQDKAAPEMVSLLKRNN 374
Cdd:PLN02526 263 VMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGKAWI 342
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 7669494 375 CGKALDIARQARDMLGGNGISDEYHVIRHAMNLEAVNTYE 414
Cdd:PLN02526 343 TKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYE 382
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
60-402 |
2.19e-68 |
|
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: 221.52 E-value: 2.19e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 60 LTTDEILIRDTFRTYCQERLMPRILLANRNEVFHREIISEMGELGVLGPTI-KGYGCAGVSSVAYGLLARELERVDSGYR 138
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITApEEYGGSGMGYLAHVIIMEEISRASGSVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 139 SAMSVQSSLVMHPIYAYGSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSMETRAHYNSSNksYTLNGTKTWITNSPM 218
Cdd:cd01156 82 LSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDR--YVLNGSKMWITNGPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 219 ADLFVVWARCE-----DGcIRGFLLEKGMRGLSAPRIQGKFSLRASATGMIIMDGVEVPEENVLPGASS-----LGGpfg 288
Cdd:cd01156 160 ADTLVVYAKTDpsagaHG-ITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKgvyvlMSG--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 289 cLNNARYGIAWGVLGASEFCLHTARQYALDRMQFGVPLARNQLIQKKLADMLTEitlgLHAC----------LQLGRLKD 358
Cdd:cd01156 236 -LDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTR----LNASrsylytvakaCDRGNMDP 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 7669494 359 QDKAAPEMVSllkrnnCGKALDIARQARDMLGGNGISDEYHVIR 402
Cdd:cd01156 311 KDAAGVILYA------AEKATQVALDAIQILGGNGYINDYPTGR 348
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
52-402 |
8.05e-63 |
|
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: 208.09 E-value: 8.05e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 52 DPLVLEEQLTTDEILIRDTFRTYCQERLMPRILlaNRNEVFHREIISEMGELGVLGPTI-KGYGCAGVSSVAYGLLArEL 130
Cdd:cd01161 19 YPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKN--DQLEKIPRKTLTQLKELGLFGLQVpEEYGGLGLNNTQYARLA-EI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 131 ERVDSGYRSAMSVQSSLVMHPIYAYGSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSMETRAHYNSSNKSYTLNGTK 210
Cdd:cd01161 96 VGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSEDGKHYVLNGSK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 211 TWITNSPMADLFVVWARCE----DGC----IRGFLLEKGMRGLSAPRIQGKFSLRASATGMIIMDGVEVPEENVLpgaSS 282
Cdd:cd01161 176 IWITNGGIADIFTVFAKTEvkdaTGSvkdkITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVL---GE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 283 LGGPF----GCLNNARYGIAWGVLGASEFCLHTARQYALDRMQFGVPLARNQLIQKKLADMLTEITLGLHACLQLGRLKD 358
Cdd:cd01161 253 VGDGFkvamNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMD 332
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 7669494 359 QD-KAAPEMVSLLKRNNCGKALD-IARQARDMLGGNGISDEYHVIR 402
Cdd:cd01161 333 RGlKAEYQIEAAISKVFASEAAWlVVDEAIQIHGGMGFMREYGVER 378
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
66-402 |
1.40e-54 |
|
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: 185.40 E-value: 1.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 66 LIRDTFRTYCQERLMPRILLANRNEVFHREIISEMGELGVLGPTI-KGYGCAGVSSVAYGLLARELERVdSGYRSAMSVQ 144
Cdd:cd01160 5 AFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFpEEYGGIGGDLLSAAVLWEELARA-GGSGPGLSLH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 145 SSLVMHPIYAYGSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSMETRAHYNSSNksYTLNGTKTWITNSPMADLFVV 224
Cdd:cd01160 84 TDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDH--YVLNGSKTFITNGMLADVVIV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 225 WARCE-----DGCIRGFLLEKGMRGLSAPRIQGKFSLRASATGMIIMDGVEVPEENVLpGASSLGGPF--GCLNNARYGI 297
Cdd:cd01160 162 VARTGgeargAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLL-GEENKGFYYlmQNLPQERLLI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 298 AWGVLGASEFCLHTARQYALDRMQFGVPLARNQLIQKKLADMLTEITLG---LHACLQLGRLKDQDKAAPEMVsllkRNN 374
Cdd:cd01160 241 AAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTrafLDNCAWRHEQGRLDVAEASMA----KYW 316
|
330 340
....*....|....*....|....*....
gi 7669494 375 CGKALD-IARQARDMLGGNGISDEYHVIR 402
Cdd:cd01160 317 ATELQNrVAYECVQLHGGWGYMREYPIAR 345
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
60-418 |
4.78e-50 |
|
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: 173.78 E-value: 4.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 60 LTTDEILIRDTFRTYCQERLMPRILLANRNEVFHREIISEMGELGVLGPTIKG-YGCAGVSSVAYGLLARELERVDSGYR 138
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDdVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 139 SAMSVQSsLVMHPIYAYGSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSMETRAhyNSSNKSYTLNGTKTWITNSPM 218
Cdd:cd01162 81 AYISIHN-MCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRA--VREGDHYVLNGSKAFISGAGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 219 ADLFVVWARC-EDGC--IRGFLLEKGMRGLSAPRIQGKFSLRASATGMIIMDGVEVPEENVLPGAsslGGPFGC----LN 291
Cdd:cd01162 158 SDVYVVMARTgGEGPkgISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGE---GQGFGIamagLN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 292 NARYGIAWGVLGASEFCLHTARQYALDRMQFGVPLARNQLIQKKLADMLTEIT-----LGLHAClqlgRLKDQDKAAPEM 366
Cdd:cd01162 235 GGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVasrlmVRRAAS----ALDRGDPDAVKL 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 7669494 367 VSLLKRNNCGKALDIARQARDMLGGNGISDEYHV------IRHAMNLEAVNtyEVVQM 418
Cdd:cd01162 311 CAMAKRFATDECFDVANQALQLHGGYGYLKDYPVeqyvrdLRVHQILEGTN--EIMRL 366
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
68-398 |
4.89e-47 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 166.59 E-value: 4.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 68 RDTFRTYCQERLMPRILLANRNEVFHREI--ISEMGELGVLGPTI-KGYGCAGVSSVAYGLLARELERVDSGYRSAMSVQ 144
Cdd:PLN02519 34 KESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGITApEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAH 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 145 SSLVMHPIYAYGSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSMETRAhyNSSNKSYTLNGTKTWITNSPMADLFVV 224
Cdd:PLN02519 114 SNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKA--ERVDGGYVLNGNKMWCTNGPVAQTLVV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 225 WARCEDGC----IRGFLLEKGMRGLSAPRIQGKFSLRASATGMIIMDGVEVPEENVLPGASS-----LGGpfgcLNNARY 295
Cdd:PLN02519 192 YAKTDVAAgskgITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKgvyvmMSG----LDLERL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 296 GIAWGVLGASEFCLHTARQYALDRMQFGVPLARNQLIQKKLADMLTEITLGLHACLQLGRLKDQDKAAPEMVSLLKRNNC 375
Cdd:PLN02519 268 VLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILCAA 347
|
330 340
....*....|....*....|...
gi 7669494 376 GKALDIARQARDMLGGNGISDEY 398
Cdd:PLN02519 348 ERATQVALQAIQCLGGNGYINEY 370
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
33-342 |
1.80e-46 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 165.11 E-value: 1.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 33 GGRTQSQLAKSSRPEFDWQDPlvleeqlTTDEILIRDTFRTYCQERLMPRILLANRNEVFHREIISEMGELGVLGPTI-K 111
Cdd:PTZ00461 17 GWTAAATMTSASRAFMDLYNP-------TPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVpE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 112 GYGCAGVSSVAYGLLARELERVDSGYRSAMSVQSSLVMHPIYAYGSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSM 191
Cdd:PTZ00461 90 ADGGAGMDAVAAVIIHHELSKYDPGFCLAYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 192 ETRAHyNSSNKSYTLNGTKTWITNSPMADLFVVWARCeDGCIRGFLLEKGMRGLS-APRIQgKFSLRASATGMIIMDGVE 270
Cdd:PTZ00461 170 RTTAK-KDSNGNYVLNGSKIWITNGTVADVFLIYAKV-DGKITAFVVERGTKGFTqGPKID-KCGMRASHMCQLFFEDVV 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7669494 271 VPEENVLPGASSlgGPFGCLNN---ARYGIAWGVLGASEFCLHTARQYALDRMQFGVPLARNQLIQKKLADMLTE 342
Cdd:PTZ00461 247 VPAENLLGEEGK--GMVGMMRNlelERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYAD 319
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
60-400 |
1.40e-43 |
|
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: 156.59 E-value: 1.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 60 LTTDEILIRDTFRTYCQERLMPRILLANRNEVFHREIISEMGELGVLGPTI-KGYGCAGVSSVAYGLLARELERVDSGYR 138
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIpEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 139 SAMSVqSSLVMHPIYAYGSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSMETRAHynSSNKSYTLNGTKTWITNSPM 218
Cdd:cd01157 81 TAIEA-NSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAE--KKGDEYIINGQKMWITNGGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 219 ADLFVVWARCE-------DGCIRGFLLEKGMRGLSAPRIQGKFSLRASATGMIIMDGVEVPEENVLPGAsslGGPF---- 287
Cdd:cd01157 158 ANWYFLLARSDpdpkcpaSKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGE---GAGFkiam 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 288 GCLNNARYGIAWGVLGASEFCLHTARQYALDRMQFGVPLARNQLIQKKLADMLTEITLGLHACLQLGRLKDQDKAAPEMV 367
Cdd:cd01157 235 GAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYA 314
|
330 340 350
....*....|....*....|....*....|...
gi 7669494 368 SLLKRNNCGKALDIARQARDMLGGNGISDEYHV 400
Cdd:cd01157 315 SIAKAFAADIANQLATDAVQIFGGNGFNSEYPV 347
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
61-172 |
1.03e-40 |
|
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: 140.68 E-value: 1.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 61 TTDEILIRDTFRTYCQERLMPRILLANRNEVFHREIISEMGELGVLGPTI-KGYGCAGVSSVAYGLLARELERVDSGYRS 139
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIpEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|...
gi 7669494 140 AMSVQSSLVMHPIYAYGSEEQRQKYLPQLAKGE 172
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
176-267 |
1.07e-24 |
|
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: 97.35 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 176 CFGLTEPNSGSDPSSMETRAhYNSSNKSYTLNGTKTWITNSPMADLFVVWARCE----DGCIRGFLLEKGMRGLSAPRIQ 251
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTA-ADGDGGGWVLNGTKWWITNAGIADLFLVLARTGgddrHGGISLFLVPKDAPGVSVRRIE 79
|
90
....*....|....*.
gi 7669494 252 GKFSLRASATGMIIMD 267
Cdd:pfam02770 80 TKLGVRGLPTGELVFD 95
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
152-414 |
7.16e-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: 7.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 152 IYAYGSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSMETRAHYnSSNKSYTLNGTKTWITN--SPMAD--LFVVWAR 227
Cdd:cd01153 96 LLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVY-QADGSWRINGVKRFISAgeHDMSEniVHLVLAR 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 228 CEDGC--IRG---FLLEK----GMR-GLSAPRIQGKFSLRASATGMIIMDGVEVP---EENvlpgaSSLGGPFGCLNNAR 294
Cdd:cd01153 175 SEGAPpgVKGlslFLVPKflddGERnGVTVARIEEKMGLHGSPTCELVFDNAKGEligEEG-----MGLAQMFAMMNGAR 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 295 YGIAWGVLGASEFCLHTARQYALDRMQFGVPLA-------------RNQLIQKKL-------ADM--LTEITLGLHACLQ 352
Cdd:cd01153 250 LGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKaapavtiihhpdvRRSLMTQKAyaegsraLDLytATVQDLAERKATE 329
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7669494 353 LGRLKDQDKAAPEMVSLLKRNNCGKALDIARQARDMLGGNGISDEYHVIRHAMNLEAVNTYE 414
Cdd:cd01153 330 GEDRKALSALADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYE 391
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
146-402 |
4.65e-23 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 99.80 E-value: 4.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 146 SLVMHPIYAYGSEEQ-RQKYLPQLAKGELLGCFGLTEPNSGSDPSSMETRahYNSSNKSYTLNGTKTWITNSPMADLFVV 224
Cdd:PRK12341 90 GQCIHSMRRFGSAEQlRKTAESTLETGDPAYALALTEPGAGSDNNSATTT--YTRKNGKVYLNGQKTFITGAKEYPYMLV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 225 WAR-CED----GCIRGFLLEkgmrgLSAPRIQ----GKFSLRASATGMIIMDGVEVpEENVLPGASSLGgpF----GCLN 291
Cdd:PRK12341 168 LARdPQPkdpkKAFTLWWVD-----SSKPGIKinplHKIGWHMLSTCEVYLDNVEV-EESDLVGEEGMG--FlnvmYNFE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 292 NARYGIAWGVLGASEFCLHTARQYALDRMQFGVPLARNQLIQKKLADMLTEI----TLGLHACLQlgrlKDQDKAAPEMV 367
Cdd:PRK12341 240 MERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIenmrNMVYKVAWQ----ADNGQSLRTSA 315
|
250 260 270
....*....|....*....|....*....|....*
gi 7669494 368 SLLKRNNCGKALDIARQARDMLGGNGISDEYHVIR 402
Cdd:PRK12341 316 ALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSR 350
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
288-403 |
5.66e-22 |
|
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: 91.55 E-value: 5.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 288 GCLNNARYGIAWGVLGASEFCLHTARQYALDRMQFGVPLARNQLIQKKLADMLTEITLGLHACLQLGRLKDQDKAAPEMV 367
Cdd:pfam00441 9 ETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAGGPDGAEA 88
|
90 100 110
....*....|....*....|....*....|....*.
gi 7669494 368 SLLKRNNCGKALDIARQARDMLGGNGISDEYHVIRH 403
Cdd:pfam00441 89 SMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERL 124
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
152-403 |
1.44e-21 |
|
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of several genes involved in the SOS adaptive response to DNA alkylation damage, whose expression is activated by the Ada protein. Its function has not been entirely elucidated; however, it is similar in sequence and function to acyl-CoA dehydrogenases. It has been proposed that aidB directly destroys DNA alkylating agents such as nitrosoguanidines (nitrosated amides) or their reaction intermediates.
Pssm-ID: 173843 [Multi-domain] Cd Length: 418 Bit Score: 95.90 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 152 IYAYGSEEQRQKYLPQLAKGE---LLGCFGLTEPNSGSDPSSMETRAHYNSSnKSYTLNGTKtWITNSPMADLFVVWARC 228
Cdd:cd01154 123 LRKYGPEELKQYLPGLLSDRYktgLLGGTWMTEKQGGSDLGANETTAERSGG-GVYRLNGHK-WFASAPLADAALVLARP 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 229 EDG--CIRG---FL----LEKGMR-GLSAPRIQGKFSLRASATGMIIMDGVEV----PEENVLPGASSLggpfgcLNNAR 294
Cdd:cd01154 201 EGApaGARGlslFLvprlLEDGTRnGYRIRRLKDKLGTRSVATGEVEFDDAEAyligDEGKGIYYILEM------LNISR 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 295 YGIAWGVLGASEFCLHTARQYALDRMQFGVPLARNQLIQKKLADMLTEITLGLHACLQLGRLKDQDKAAPE--------M 366
Cdd:cd01154 275 LDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKPveahmarlA 354
|
250 260 270
....*....|....*....|....*....|....*..
gi 7669494 367 VSLLKRNNCGKALDIARQARDMLGGNGISDEYHVIRH 403
Cdd:cd01154 355 TPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARL 391
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
156-402 |
1.08e-20 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 92.97 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 156 GSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSMETRahYNSSNKSYTLNGTKTWITNSPMADLFVVWARCEDGCIRG 235
Cdd:PRK03354 101 GTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTT--YTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASPDKP 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 236 FLLEkGMRGLSAPRIQ----GKFSLRASATGMIIMDGVEVPEENVlpgasslggpFGCLNNA-----------RYGIAWG 300
Cdd:PRK03354 179 VYTE-WFVDMSKPGIKvtklEKLGLRMDSCCEITFDDVELDEKDM----------FGREGNGfnrvkeefdheRFLVALT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 301 VLGASEFCLHTARQYALDRMQFGVPLARNQLIQKKLADMLTEITLGLHACLQLGRLKDQDKAAPEMVSLLKRNNCGKALD 380
Cdd:PRK03354 248 NYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKYFCANAAFE 327
|
250 260
....*....|....*....|..
gi 7669494 381 IARQARDMLGGNGISDEYHVIR 402
Cdd:PRK03354 328 VVDSAMQVLGGVGIAGNHRISR 349
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
116-398 |
3.80e-16 |
|
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: 79.74 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 116 AGVSSVAYGLLARELERV------------DSGYrsamsvqsslvMHPIYAYGSEEQRQKYLPQLAKGELLGCFGLTEPN 183
Cdd:cd01155 67 SGLTNLEYAYLAEETGRSffapevfncqapDTGN-----------MEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 184 -SGSDPSSMETRAHYNSSnkSYTLNGTKTWITNS--PMADLFVVWARCE-DGCIRG-----FLLEKGMRGLSAPRIQGKF 254
Cdd:cd01155 136 vASSDATNIECSIERDGD--DYVINGRKWWSSGAgdPRCKIAIVMGRTDpDGAPRHrqqsmILVPMDTPGVTIIRPLSVF 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 255 SLRASATGM--IIMDGVEVPEENVLPGAsslGGPF----GCLNNARYGIAWGVLGASEFCLHTARQYALDRMQFGVPLAR 328
Cdd:cd01155 214 GYDDAPHGHaeITFDNVRVPASNLILGE---GRGFeiaqGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQ 290
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7669494 329 NQLIQKKLADMLTEITLGLHACLQLGRLKDQ--DKAAPEMVSLLKRNNCGKALDIARQARDMLGGNGISDEY 398
Cdd:cd01155 291 HGVVAHWIAKSRIEIEQARLLVLKAAHMIDTvgNKAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDT 362
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
67-220 |
3.57e-14 |
|
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: 73.54 E-value: 3.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 67 IRDTFRTYCQERLMPRILLANRNEV-----FHREIISEMGELGVLGPTI-KGYGCAGVSSVAYGLLARELERVDSGYRSA 140
Cdd:cd01152 6 FRAEVRAWLAAHLPPELREESALGYregreDRRRWQRALAAAGWAAPGWpKEYGGRGASLMEQLIFREEMAAAGAPVPFN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 141 MSVQSSLVmHPIYAYGSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSMETRAHYNSSNksYTLNGTKTWITNSPMAD 220
Cdd:cd01152 86 QIGIDLAG-PTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDD--WVVNGQKIWTSGAHYAD 162
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
124-320 |
1.56e-13 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 72.59 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 124 GLLARELERVDSGYRSAMSVQSSLVMHPIYAYGSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSMETRAHyNSSNKS 203
Cdd:PTZ00456 132 GFITRELMATANWGFSMYPGLSIGAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAE-PSADGS 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 204 YTLNGTKTWIT--NSPMAD--LFVVWARCEDGC-----IRGFLLEKGM----------RGLSAPRIQGKFSLRASATGMI 264
Cdd:PTZ00456 211 YKITGTKIFISagDHDLTEniVHIVLARLPNSLpttkgLSLFLVPRHVvkpdgsletaKNVKCIGLEKKMGIKGSSTCQL 290
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 7669494 265 IMD---GVEVPEENvlpgaSSLGGPFGCLNNARYGIAWGVLGASEFCLHTARQYALDRM 320
Cdd:PTZ00456 291 SFEnsvGYLIGEPN-----AGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERR 344
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
126-397 |
1.94e-13 |
|
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: 71.98 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 126 LARELERVDSGYRSAMSVQSSLVMHPIYAYGSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSMETRAHYNSSNKSYT 205
Cdd:cd01150 87 LTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDPLTQEFV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 206 LN-----GTKTWITN-SPMADLFVVWAR--CEDGC--IRGFLLE-------KGMRGLSAPRIQGKFSLRASATGMIIMDG 268
Cdd:cd01150 167 INtpdftATKWWPGNlGKTATHAVVFAQliTPGKNhgLHAFIVPirdpkthQPLPGVTVGDIGPKMGLNGVDNGFLQFRN 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 269 VEVPEENVL--------------PGASS---LGGPFGCLNNARYGIAWGVLGASEFCLHTARQYALDRMQFG-------V 324
Cdd:cd01150 247 VRIPRENLLnrfgdvspdgtyvsPFKDPnkrYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGpkpsdpeV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 325 PLARNQLIQKKLADML----------TEITLGLHAClQLGRLKDQDKAAPEMVSL---LKRNN---CGKALDIARQArdm 388
Cdd:cd01150 327 QILDYQLQQYRLFPQLaaayafhfaaKSLVEMYHEI-IKELLQGNSELLAELHALsagLKAVAtwtAAQGIQECREA--- 402
|
....*....
gi 7669494 389 LGGNGISDE 397
Cdd:cd01150 403 CGGHGYLAM 411
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
147-339 |
4.07e-12 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 68.06 E-value: 4.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 147 LVMHpiyaYGSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSME-----TRAHYNSSNK-SYTLNGTKTWITNSPMAD 220
Cdd:PRK13026 170 LLTH----YGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPdtgivCRGEFEGEEVlGLRLTWDKRYITLAPVAT 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 221 LFVVWARCEDGciRGFLLEKGMRGL-------SAPRIQ-GKfslRASATGMIIMDG------VEVPEENVLPGASSLGGp 286
Cdd:PRK13026 246 VLGLAFKLRDP--DGLLGDKKELGItcaliptDHPGVEiGR---RHNPLGMAFMNGttrgkdVFIPLDWIIGGPDYAGR- 319
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7669494 287 fG------CLNNARyGIAWGVLGA--SEFCLHTARQYALDRMQFGVPLARNQLIQKKLADM 339
Cdd:PRK13026 320 -GwrmlveCLSAGR-GISLPALGTasGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARI 378
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
147-191 |
1.25e-11 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 66.76 E-value: 1.25e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 7669494 147 LVMHpiyaYGSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSM 191
Cdd:PRK09463 171 LLLH----YGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSI 211
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
94-410 |
1.99e-07 |
|
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: 52.71 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 94 REIISEMGELGVLGPtiKGYGCAGVS-SVAYGLLaRELERVDS------GYRSAMSVQSSLVmhpiyayGSEEQRQKYLP 166
Cdd:cd01163 28 VALLRQSGLGTLRVP--KEYGGLGASlPDLYEVV-RELAAADSniaqalRAHFGFVEALLLA-------GPEQFRKRWFG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 167 QLAKGELLGCfGLTEpNSGSDPSSMETRAHynSSNKSYTLNGTKTWITNSPMADLFVVWARCEDGCIRGFLLEKGMRGLS 246
Cdd:cd01163 98 RVLNGWIFGN-AVSE-RGSVRPGTFLTATV--RDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGKLVFAAVPTDRPGIT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 247 APRIQGKFSLRASATGMIIMDGVEVPEENVLPGAS-----SLGGPFGCLN--NARYGIAWGVLG-ASEFCLHTARQYAld 318
Cdd:cd01163 174 VVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPNapdrgTLLTAIYQLVlaAVLAGIARAALDdAVAYVRSRTRPWI-- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 319 rmQFGVPLAR-NQLIQKKLADMLTEITLGLHACLQLGRLKDQDKAAPEMVSLLKRNNC------------GKALDIARQA 385
Cdd:cd01163 252 --HSGAESARdDPYVQQVVGDLAARLHAAEALVLQAARALDAAAAAGTALTAEARGEAalavaaakvvvtRLALDATSRL 329
|
330 340
....*....|....*....|....*
gi 7669494 386 RDMLGGNGISDEYHVIRHAMNLEAV 410
Cdd:cd01163 330 FEVGGASATAREHNLDRHWRNARTH 354
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
141-348 |
2.32e-07 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 52.94 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 141 MSVQSSLVMHPIYAYGSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSMETRAHYNSSNKSYTLN-----GTKTWITN 215
Cdd:PLN02636 141 LGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLTDEFVINtpndgAIKWWIGN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 216 SPMADLFV-VWARC----------EDGCIRGFLLE-KGMRGLSA-PRIQ-----GKFSLRASATGMIIMDGVEVPEENVL 277
Cdd:PLN02636 221 AAVHGKFAtVFARLklpthdskgvSDMGVHAFIVPiRDMKTHQVlPGVEirdcgHKVGLNGVDNGALRFRSVRIPRDNLL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 278 ----------PGASSL-------GGPFGCLNNARYGIAWGVLGASEFCLHTARQYALDRMQFGVP------LARNQLIQK 334
Cdd:PLN02636 301 nrfgdvsrdgKYTSSLptinkrfAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPkqpeisILDYQSQQH 380
|
250
....*....|....
gi 7669494 335 KLADMLTEiTLGLH 348
Cdd:PLN02636 381 KLMPMLAS-TYAFH 393
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
152-277 |
6.72e-07 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 51.38 E-value: 6.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 152 IYAYGSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSMETRAHYNSSNKSY-----TLNGTKTWITNSPMADLF-VVW 225
Cdd:PLN02443 110 IKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFvihspTLTSSKWWPGGLGKVSTHaVVY 189
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7669494 226 ARC----EDGCIRGFLLE-------KGMRGLSAPRIQGKFSLRASAT---GMIIMDGVEVPEENVL 277
Cdd:PLN02443 190 ARLitngKDHGIHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTmdnGFLRFDHVRIPRDQML 255
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
94-403 |
2.96e-06 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 49.79 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 94 REIISEMGELGVLGPTIKGYGCAGVSSVAYGLLARELERvdsgyrsamSVQSSLV----------MHPIYAYGSEEQRQK 163
Cdd:PLN02876 470 RKLLFEDNKHMVSGDSADQLLGAGLSNLEYGYLCEIMGR---------SVWAPQVfncgapdtgnMEVLLRYGNKEQQLE 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 164 YLPQLAKGELLGCFGLTEPN-SGSDPSSMEtrAHYNSSNKSYTLNGTKTWITNS--PMADLFVVWARCEDGCIRG----- 235
Cdd:PLN02876 541 WLIPLLEGKIRSGFAMTEPQvASSDATNIE--CSIRRQGDSYVINGTKWWTSGAmdPRCRVLIVMGKTDFNAPKHkqqsm 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 236 FLLEKGMRGLSAPRIQGKFSLRASATGM--IIMDGVEVPEENVLPGAsslGGPF----GCLNNARYGIAWGVLGASEFCL 309
Cdd:PLN02876 619 ILVDIQTPGVQIKRPLLVFGFDDAPHGHaeISFENVRVPAKNILLGE---GRGFeiaqGRLGPGRLHHCMRLIGAAERGM 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 310 HTARQYALDRMQFGVPLARNQLIQKKLADMLTEIT----LGLHACLQLGRLKDQD-KAAPEMVSLLKRNNCGKALDIARQ 384
Cdd:PLN02876 696 QLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEqtrlLVLEAADQLDRLGNKKaRGIIAMAKVAAPNMALKVLDMAMQ 775
|
330
....*....|....*....
gi 7669494 385 ARdmlGGNGISDEYhVIRH 403
Cdd:PLN02876 776 VH---GAAGVSSDT-VLAH 790
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
142-212 |
2.97e-03 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 39.83 E-value: 2.97e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7669494 142 SVQSSLVMHPIYAYGSEEQRQKYLPQLAKGELLGCFGLTEPNSGSDPSSMETRAHYNSSNKSYTLN-----GTKTW 212
Cdd:PTZ00460 96 TVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHtpsveAVKFW 171
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
204-416 |
9.77e-03 |
|
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: 38.10 E-value: 9.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 204 YTLNGTKTWITNSPMADLFVVWARCED----GCIRGFLLEKgmrglSAPRIQGKFS---LRASATGMIIMDGVEVPEENV 276
Cdd:cd01159 120 YRVSGTWPFASGCDHADWILVGAIVEDddggPLPRAFVVPR-----AEYEIVDTWHvvgLRGTGSNTVVVDDVFVPEHRT 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 277 LPGASSLGGPFGCLNNARYGIAWG----------VLGASEFCLHTARQYALDRMQ---FGVPLARNQLIQKKLADMLTEI 343
Cdd:cd01159 195 LTAGDMMAGDGPGGSTPVYRMPLRqvfplsfaavSLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAEL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7669494 344 TlglHACLQLGRLKDQ-------DKAAPEMVSLLKRNNCGKALDIARQARDML----GGNGISDEYHVIR-----HAMNL 407
Cdd:cd01159 275 D---AARAFLERATRDlwahalaGGPIDVEERARIRRDAAYAAKLSAEAVDRLfhaaGGSALYTASPLQRiwrdiHAAAQ 351
|
....*....
gi 7669494 408 EAVNTYEVV 416
Cdd:cd01159 352 HAALNPETA 360
|
|
| |
