|
Name |
Accession |
Description |
Interval |
E-value |
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
9-392 |
1.01e-144 |
|
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: 415.99 E-value: 1.01e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 9 SDFYGFQQQLTEQERASLGQLRQYLEREVAPIADAYWARAEFPMQVIAPLAELGM-------YG-PGVplvrqfenSAVY 80
Cdd:cd01151 4 EDPLNLDDLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLlgatikgYGcAGL--------SSVA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 81 RGWAALELGRVDASVATFIGVQSGLAMNSIAVAGSDEQQREWLPRMATGEIVGAFGLTEPYSGSDSAkGLRTTARREGDE 160
Cdd:cd01151 76 YGLIAREVERVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPG-GMETRARKDGGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 161 WVLDGEKRWIGNATFADVVVIWAKDVADGQVKGFLVTTDTAGFTATKIEDKIALRGVQNADIVMQDVRVPESRRLQNATS 240
Cdd:cd01151 155 YKLNGSKTWITNSPIADVFVVWARNDETGKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAEG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 241 FRSTAEVLRLTRTEVAWQAVGIAVGAYEAALAYARERIQFGKPIAAHQLVQDLLVKSLSNITASIALCTQASAMQDAGVG 320
Cdd:cd01151 235 LRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKA 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1930971987 321 GDEHSALAKAFATAKMRETVAWCREVQGGNGIVLDKGVARFFADAEAIYSYEGTREVNTLIVGRAITGQAAF 392
Cdd:cd01151 315 TPEQISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAITGIQAF 386
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
2-392 |
8.40e-131 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 381.51 E-value: 8.40e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 2 PAT--PLLESDFYGFQQQLTEQERASLGQLRQYLEREVAPIADAYWARAEFPMQVIAPLAELGMYG--------PGVPLV 71
Cdd:PLN02526 11 PASifPPSVSDYYQFDDLLTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGgtikgygcPGLSIT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 72 rqfeNSAVyrgwAALELGRVDASVATFIGVQSGLAMNSIAVAGSDEQQREWLPRMATGEIVGAFGLTEPYSGSDsAKGLR 151
Cdd:PLN02526 91 ----ASAI----ATAEVARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSD-ASSLN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 152 TTARREGDEWVLDGEKRWIGNATFADVVVIWAKDVADGQVKGFLVTTDTAGFTATKIEDKIALRGVQNADIVMQDVRVPE 231
Cdd:PLN02526 162 TTATKVEGGWILNGQKRWIGNSTFADVLVIFARNTTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 232 SRRLQNATSFRSTAEVLRLTRTEVAWQAVGIAVGAYEAALAYARERIQFGKPIAAHQLVQDLLVKSLSNITASIALCTQA 311
Cdd:PLN02526 242 EDRLPGVNSFQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 312 SAMQDAGVGGDEHSALAKAFATAKMRETVAWCREVQGGNGIVLDKGVARFFADAEAIYSYEGTREVNTLIVGRAITGQAA 391
Cdd:PLN02526 322 CKLYESGKMTPGHASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREITGIAS 401
|
.
gi 1930971987 392 F 392
Cdd:PLN02526 402 F 402
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
17-391 |
2.03e-115 |
|
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: 341.05 E-value: 2.03e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 17 QLTEQERASLGQLRQYLEREVAPIADAYWARAEFPMQVIAPLAELGMYGPGVPlvRQF---ENSAVYRGWAALELGRVDA 93
Cdd:COG1960 4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIP--EEYgglGLSLVELALVLEELARADA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 94 SVATFIGVQSGlAMNSIAVAGSDEQQREWLPRMATGEIVGAFGLTEPYSGSDSAkGLRTTARREGDEWVLDGEKRWIGNA 173
Cdd:COG1960 82 SLALPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAA-ALRTTAVRDGDGYVLNGQKTFITNA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 174 TFADVVVIWAKDVADGQVKG---FLVTTDTAGFTATKIEDKIALRGVQNADIVMQDVRVPESRRLQNA-TSFRSTAEVLR 249
Cdd:COG1960 160 PVADVILVLARTDPAAGHRGislFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEgKGFKIAMSTLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 250 LTRTEVAWQAVGIAVGAYEAALAYARERIQFGKPIAAHQLVQDLLVKSLSNITASIALCTQASAMQDAGVGGDEHSALAK 329
Cdd:COG1960 240 AGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAK 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1930971987 330 AFATAKMRETVAWCREVQGGNGIVLDKGVARFFADAEAIYSYEGTREVNTLIVGRAITGQAA 391
Cdd:COG1960 320 LFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
20-386 |
2.05e-82 |
|
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: 256.43 E-value: 2.05e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 20 EQERASLGQLRQYLEREVAPIADAYWARAEFPMQVIAPLAELGMYGPGVP--LVRQFENSAVYrGWAALELGRVDASVAT 97
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPeeYGGAGLDFLAY-AIAIEELAKVDASVAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 98 FIGVQSGLAMNSIAVAGSDEQQREWLPRMATGEIVGAFGLTEPYSGSDSAkGLRTTARREGDEWVLDGEKRWIGNATFAD 177
Cdd:cd01158 80 IVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAA-ALKTTAKKDGDDYVLNGSKMWITNGGEAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 178 VVVIWAKDVADGQVKG---FLVTTDTAGFTATKIEDKIALRGVQNADIVMQDVRVPESRRL-QNATSFRSTAEVLRLTRT 253
Cdd:cd01158 159 FYIVFAVTDPSKGYRGitaFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILgEEGEGFKIAMQTLDGGRI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 254 EVAWQAVGIAVGAYEAALAYARERIQFGKPIAAHQLVQDLLVKSLSNITASIALCTQASAMQDAGVGGDEHSALAKAFAT 333
Cdd:cd01158 239 GIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFAS 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1930971987 334 AKMRETVAWCREVQGGNGIVLDKGVARFFADAEAIYSYEGTREVNTLIVGRAI 386
Cdd:cd01158 319 EVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHL 371
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
105-384 |
1.55e-69 |
|
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: 221.77 E-value: 1.55e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 105 LAMNSIAVAGSDEQQREWLPRMATGEIVGAFGLTEPYSGSDSAkGLRTTARREGDEWVLDGEKRWIGNATFADVVVIWAK 184
Cdd:cd00567 43 LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLA-GIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLAR 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 185 -DVADGQVKG---FLVTTDTAGFTATKIEDKIALRGVQNADIVMQDVRVPESRRL-QNATSFRSTAEVLRLTRTEVAWQA 259
Cdd:cd00567 122 tDEEGPGHRGisaFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLgEEGGGFELAMKGLNVGRLLLAAVA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 260 VGIAVGAYEAALAYARERIQFGKPIAAHQLVQDLLVKSLSNITASIALCTQASAMQDAGVGGDEH-SALAKAFATAKMRE 338
Cdd:cd00567 202 LGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLeAAMAKLFATEAARE 281
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1930971987 339 TVAWCREVQGGNGIVLDKGVARFFADAEAIYSYEGTREVNTLIVGR 384
Cdd:cd00567 282 VADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
18-386 |
1.05e-55 |
|
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: 187.62 E-value: 1.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 18 LTEQERASLGQLRQYLEREVAPIADAYWARAEFPMQVIAPLAELGMYGPGVPlvRQFENSA---VYRGWAALELGRVDAS 94
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAP--EEYGGSGmgyLAHVIIMEEISRASGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 95 VATFIGVQSGLAMNSIAVAGSDEQQREWLPRMATGEIVGAFGLTEPYSGSDsAKGLRTTARREGDEWVLDGEKRWIGNAT 174
Cdd:cd01156 80 VALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSD-VVSMKLRAEKKGDRYVLNGSKMWITNGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 175 FADVVVIWAKDVADGQVKG---FLVTTDTAGFTATKIEDKIALRGVQNADIVMQDVRVPESRRLQNATsfrSTAEV---- 247
Cdd:cd01156 159 DADTLVVYAKTDPSAGAHGitaFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGEN---KGVYVlmsg 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 248 LRLTRTEVAWQAVGIAVGAYEAALAYARERIQFGKPIAAHQLVQDLLVKSLSNITASIALCTQASAMQDAGvGGDEHSAL 327
Cdd:cd01156 236 LDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRG-NMDPKDAA 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1930971987 328 AKAFATAKMRETVAwcRE-VQ--GGNGIVLDKGVARFFADAEAiysYE---GTREVNTLIVGRAI 386
Cdd:cd01156 315 GVILYAAEKATQVA--LDaIQilGGNGYINDYPTGRLLRDAKL---YEigaGTSEIRRMVIGREL 374
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
29-386 |
8.00e-55 |
|
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: 185.01 E-value: 8.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 29 LRQYLEREVAPIADAYWARAEFPMQVIAPLAELGMYGPGVP-----LVRQFENSAVyrgwAALELGRVDASVATFIgVQS 103
Cdd:cd01160 10 VRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPeeyggIGGDLLSAAV----LWEELARAGGSGPGLS-LHT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 104 GLAMNSIAVAGSDEQQREWLPRMATGEIVGAFGLTEPYSGSDSAkGLRTTARREGDEWVLDGEKRWIGNATFADVVVIWA 183
Cdd:cd01160 85 DIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQ-GIRTTARKDGDHYVLNGSKTFITNGMLADVVIVVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 184 KDVADGQVKG----FLVTTDTAGFTATKIEDKIALRGVQNADIVMQDVRVPESRRL-QNATSFRSTAEVLRLTRTEVAWQ 258
Cdd:cd01160 164 RTGGEARGAGgislFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLgEENKGFYYLMQNLPQERLLIAAG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 259 AVGIAVGAYEAALAYARERIQFGKPIAAHQLVQDLLVKSLSNITASIALCTQASAMQDAGVGGDEHSALAKAFATAKMRE 338
Cdd:cd01160 244 ALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATELQNR 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1930971987 339 TVAWCREVQGGNGIVLDKGVARFFADAEAIYSYEGTREVNTLIVGRAI 386
Cdd:cd01160 324 VAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQM 371
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
18-389 |
1.17e-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: 174.17 E-value: 1.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 18 LTEQERASLGQLRQYLEREVAPIADAYWARAEFPMQVIAPLAELGMYG-------PGVPLVRqFENSAVYRgwaALELGr 90
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGiyirddvGGSGLSR-LDASIIFE---ALSTG- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 91 vDASVATFIGVQSgLAMNSIAVAGSDEQQREWLPRMATGEIVGAFGLTEPYSGSDSAKgLRTTARREGDEWVLDGEKRWI 170
Cdd:cd01162 76 -CVSTAAYISIHN-MCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAA-LRTRAVREGDHYVLNGSKAFI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 171 GNATFADVVVIWAKDVADGQ--VKGFLVTTDTAGFTATKIEDKIALRGVQNADIVMQDVRVPESRRL-QNATSFRSTAEV 247
Cdd:cd01162 153 SGAGDSDVYVVMARTGGEGPkgISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLgGEGQGFGIAMAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 248 LRLTRTEVAWQAVGIAVGAYEAALAYARERIQFGKPIAAHQLVQDLLVKSLSNITAS-IALCTQASAMQDAGVGGDEHSA 326
Cdd:cd01162 233 LNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASrLMVRRAASALDRGDPDAVKLCA 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1930971987 327 LAKAFATAKMRETVAWCREVQGGNGIVLDKGVARFFADAEAIYSYEGTREVNTLIVGRAITGQ 389
Cdd:cd01162 313 MAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
13-388 |
3.79e-50 |
|
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: 173.81 E-value: 3.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 13 GFQQQLTEQERASLGQLRQYLEREVAPIADAywARAEFPMQVIAPLAELGMYGPGVPlvRQFENSavyrGWAALELGRV- 91
Cdd:cd01161 22 VLTEEQTEELNMLVGPVEKFFEEVNDPAKND--QLEKIPRKTLTQLKELGLFGLQVP--EEYGGL----GLNNTQYARLa 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 92 -----DASVATFIGVQSGLAMNSIAVAGSDEQQREWLPRMATGEIVGAFGLTEPYSGSDSAkGLRTTARR--EGDEWVLD 164
Cdd:cd01161 94 eivgmDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAA-SIRTTAVLseDGKHYVLN 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 165 GEKRWIGNATFADVVVIWAK---DVADGQVK----GFLVTTDTAGFTATKIEDKIALRGVQNADIVMQDVRVPESRRL-Q 236
Cdd:cd01161 173 GSKIWITNGGIADIFTVFAKtevKDATGSVKdkitAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLgE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 237 NATSFRSTAEVLRLTRTEVAWQAVGIAVGAYEAALAYARERIQFGKPIAAHQLVQDLLVKSLSNITASIALCTQASAMQD 316
Cdd:cd01161 253 VGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMD 332
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1930971987 317 AGVGGDEH--SALAKAFATAKMRETVAWCREVQGGNGIVLDKGVARFFADAEAIYSYEGTREVNTLIVgrAITG 388
Cdd:cd01161 333 RGLKAEYQieAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFI--ALTG 404
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
18-389 |
8.56e-49 |
|
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: 169.30 E-value: 8.56e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 18 LTEQERASLGQLRQYLEREVAPIADAYWARAEFPMQVIAPLAELGMYGPGVPlvrqfensavyRGWAALELGRVDASVAT 97
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIP-----------EDCGGLGLGTFDTCLIT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 98 ------FIGVQSGLAMNSIA-----VAGSDEQQREWLPRMATGEIVGAFGLTEPYSGSDSAkGLRTTARREGDEWVLDGE 166
Cdd:cd01157 70 eelaygCTGVQTAIEANSLGqmpviISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVA-GIKTKAEKKGDEYIINGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 167 KRWIGNATFADVVVIWAKDVADGQV------KGFLVTTDTAGFTATKIEDKIALRGVQNADIVMQDVRVP-ESRRLQNAT 239
Cdd:cd01157 149 KMWITNGGKANWYFLLARSDPDPKCpaskafTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPkENVLIGEGA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 240 SFRSTAEVLRLTRTEVAWQAVGIAVGAYEAALAYARERIQFGKPIAAHQLVQDLLVKSLSNITASiALCTQASAMQ-DAG 318
Cdd:cd01157 229 GFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELA-RLAYQRAAWEvDSG 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1930971987 319 VGGDEHSALAKAFATAKMRETVAWCREVQGGNGIVLDKGVARFFADAEAIYSYEGTREVNTLIVGRAITGQ 389
Cdd:cd01157 308 RRNTYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
50-376 |
6.98e-40 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 146.62 E-value: 6.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 50 FPMQVIAPLAELGMYGPGVPlvrQFENSAVYRGWAAL----ELGRVDASVATFIGVQSGLAMNSIAVAGSDEQQREWLPR 125
Cdd:PTZ00461 69 FNRDLFKQLGDLGVMGVTVP---EADGGAGMDAVAAViihhELSKYDPGFCLAYLAHSMLFVNNFYYSASPAQRARWLPK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 126 MATGEIVGAFGLTEPYSGSDsAKGLRTTARREGDE-WVLDGEKRWIGNATFADVVVIWAKdvADGQVKGFLVTTDTAGFT 204
Cdd:PTZ00461 146 VLTGEHVGAMGMSEPGAGTD-VLGMRTTAKKDSNGnYVLNGSKIWITNGTVADVFLIYAK--VDGKITAFVVERGTKGFT 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 205 ATKIEDKIALRGVQNADIVMQDVRVPESRRL-QNATSFRSTAEVLRLTRTEVAWQAVGIAVGAYEAALAYARERIQFGKP 283
Cdd:PTZ00461 223 QGPKIDKCGMRASHMCQLFFEDVVVPAENLLgEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKP 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 284 IAAHQLVQDLLVKSLSNITASIALCTQASAMQDAGVGGDEHSALAKAFATAKMRETVAWCREVQGGNGIVLDKGVARFFA 363
Cdd:PTZ00461 303 ISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWR 382
|
330
....*....|...
gi 1930971987 364 DAEAIYSYEGTRE 376
Cdd:PTZ00461 383 DAKLLEIGGGTIE 395
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
28-384 |
7.25e-38 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 140.78 E-value: 7.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 28 QLRQYLEREVAPIADAYWARAEFPMQV--IAPLAELGMYGPGVPlvRQFENSAV---YRGWAALELGRVDASVATFIGVQ 102
Cdd:PLN02519 36 SVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGITAP--EEYGGLGLgylYHCIAMEEISRASGSVGLSYGAH 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 103 SGLAMNSIAVAGSDEQQREWLPRMATGEIVGAFGLTEPYSGSDSAkGLRTTARREGDEWVLDGEKRWIGNATFADVVVIW 182
Cdd:PLN02519 114 SNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVV-SMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVY 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 183 AK-DVADGQ--VKGFLVTTDTAGFTATKIEDKIALRGVQNADIVMQDVRVPESRRL-QNATSFRSTAEVLRLTRTEVAWQ 258
Cdd:PLN02519 193 AKtDVAAGSkgITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLgQEGKGVYVMMSGLDLERLVLAAG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 259 AVGIAVGAYEAALAYARERIQFGKPIAAHQLVQDLLVKSLSNITASIALCTQASAMQDAGVGGDEHSALAKAFATAKMRE 338
Cdd:PLN02519 273 PLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILCAAERATQ 352
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1930971987 339 TVAWCREVQGGNGIVLDKGVARFFADAEAIYSYEGTREVNTLIVGR 384
Cdd:PLN02519 353 VALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGR 398
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
17-389 |
3.37e-32 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 124.94 E-value: 3.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 17 QLTEQERASLGQLRQYLEREVApiaDAYWA----RAEFPMQVIAPLAELGMYGPGVPLvrqfENSAVYRGWAAL-----E 87
Cdd:PRK03354 4 NLNDEQELFVAGIRELMASENW---EAYFAecdrDSVYPERFVKALADMGIDSLLIPE----EHGGLDAGFVTLaavwmE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 88 LGRVDASvaTFIGVQSGLAMNSIAVAGSDEQQREWLPRMATGEIVGAFGLTEPYSGSDsAKGLRTTARREGDEWVLDGEK 167
Cdd:PRK03354 77 LGRLGAP--TYVLYQLPGGFNTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSD-VGSLKTTYTRRNGKVYLNGSK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 168 RWIGNATFADVVVIWAKDVADGQVKGF---LVTTDTAGFTATKIEdKIALRGVQNADIVMQDVRVPESRRL-QNATSFRS 243
Cdd:PRK03354 154 CFITSSAYTPYIVVMARDGASPDKPVYtewFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFgREGNGFNR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 244 TAEVLRLTRTEVAWQAVGIAVGAYEAALAYARERIQFGKPIAAHQLVQDLLVKSLSNITASIALCTQASAMQDAGVGGDE 323
Cdd:PRK03354 233 VKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSG 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1930971987 324 HSALAKAFATAKMRETVAWCREVQGGNGIVLDKGVARFFADAEAIYSYEGTREVNTLIVGRAITGQ 389
Cdd:PRK03354 313 DAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQ 378
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
19-130 |
3.11e-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: 104.08 E-value: 3.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 19 TEQERASLGQLRQYLEREVAPIADAYWARAEFPMQVIAPLAELGMYGPGVPlvrqfE------NSAVYRGWAALELGRVD 92
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIP-----EeyggagLDYLAYALVAEELARAD 75
|
90 100 110
....*....|....*....|....*....|....*...
gi 1930971987 93 ASVATFIGVQSGLAMNSIAVAGSDEQQREWLPRMATGE 130
Cdd:pfam02771 76 ASVALALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
38-387 |
5.27e-27 |
|
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173842 [Multi-domain] Cd Length: 407 Bit Score: 110.94 E-value: 5.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 38 APIADAYWARAEFPMQVIAPLAELGmyGPGVPLVRQfensavyrgWAALEL-GRVDASVATFIGVQSglAMNSIAVAGSD 116
Cdd:cd01153 36 PPFKEALDAFAEAGWMALGVPEEYG--GQGLPITVY---------SALAEIfSRGDAPLMYASGTQG--AAATLLAHGTE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 117 EQQREWLPRMATGEIVGAFGLTEPYSGSDSAKgLRTTARREGD-EWVLDGEKRWIGN---ATFADVV--VIWAKDVADGQ 190
Cdd:cd01153 103 AQREKWIPRLAEGEWTGTMCLTEPDAGSDLGA-LRTKAVYQADgSWRINGVKRFISAgehDMSENIVhlVLARSEGAPPG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 191 VKG--------FLVTTDTAGFTATKIEDKIALRGVQNADIVMQDVRVP----ESRRLqnatsfRSTAEVLRLTRTEVAWQ 258
Cdd:cd01153 182 VKGlslflvpkFLDDGERNGVTVARIEEKMGLHGSPTCELVFDNAKGEligeEGMGL------AQMFAMMNGARLGVGTQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 259 AVGIAVGAYEAALAYARERIQFGKPIAA--------HQLVQDLLVKSLSNITASIALCTQASAMQDAGVGGDEH------ 324
Cdd:cd01153 256 GTGLAEAAYLNALAYAKERKQGGDLIKAapavtiihHPDVRRSLMTQKAYAEGSRALDLYTATVQDLAERKATEgedrka 335
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1930971987 325 -SALA-------KAFATAKMRETVAWCREVQGGNGIVLDKGVARFFADAEAIYSYEGTREVNTL-IVGRAIT 387
Cdd:cd01153 336 lSALAdlltpvvKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQALdLIGRKIV 407
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
18-386 |
2.03e-26 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 109.05 E-value: 2.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 18 LTEQERASLGQLRQYLEREVApiaDAYWARA----EFPMQVIAPLAELGMYGPGVPlvRQFENSAVYRGWAALELGRVDA 93
Cdd:PRK12341 5 LTEEQELLLASIRELITRNFP---EEYFRTCdengTYPREFMRALADNGISMLGVP--EEFGGTPADYVTQMLVLEEVSK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 94 SVATFIGVQSGLAMNSIAVAGSDEQQRE-WLPRMATGEIVGAFGLTEPYSGSDSAKgLRTTARREGDEWVLDGEKRWIGN 172
Cdd:PRK12341 80 CGAPAFLITNGQCIHSMRRFGSAEQLRKtAESTLETGDPAYALALTEPGAGSDNNS-ATTTYTRKNGKVYLNGQKTFITG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 173 ATFADVVVIWAKDV-ADGQVKGF---LVTTDTAGFTATKIEdKIALRGVQNADIVMQDVRVPESRRL-QNATSFRSTAEV 247
Cdd:PRK12341 159 AKEYPYMLVLARDPqPKDPKKAFtlwWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVgEEGMGFLNVMYN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 248 LRLTRTEVAWQAVGIAVGAYEAALAYARERIQFGKPIAAHQLVQDLLVKSLSNITASIALCTQASAMQDAGVGGDEHSAL 327
Cdd:PRK12341 238 FEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAAL 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1930971987 328 AKAFATAKMRETVAWCREVQGGNGIVLDKGVARFFADAEAIYSYEGTREVNTLIVGRAI 386
Cdd:PRK12341 318 AKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQI 376
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
241-386 |
1.13e-24 |
|
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: 98.48 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 241 FRSTAEVLRLTRTEVAWQAVGIAVGAYEAALAYARERIQFGKPIAAHQLVQDLLVKSLSNITASIALCTQASAMQDAGVG 320
Cdd:pfam00441 4 FRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAGGP 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1930971987 321 GDEHSALAKAFATAKMRETVAWCREVQGGNGIVLDKGVARFFADAEAIYSYEGTREVNTLIVGRAI 386
Cdd:pfam00441 84 DGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
30-388 |
1.15e-24 |
|
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: 103.97 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 30 RQYLEREVAPIADAYWARAEFPmqviaplAELGmyGPGVPLVRQfensAVYRGwaalELGRVDASVAtFIGVQSGLAMNS 109
Cdd:cd01152 34 REDRRRWQRALAAAGWAAPGWP-------KEYG--GRGASLMEQ----LIFRE----EMAAAGAPVP-FNQIGIDLAGPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 110 IAVAGSDEQQREWLPRMATGEIVGAFGLTEPYSGSDSAkGLRTTARREGDEWVLDGEKRWIGNATFADVVVIWAKdvADG 189
Cdd:cd01152 96 ILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLA-GLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVR--TDP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 190 QV---KG---FLVTTDTAGFTATKIedKIALRGVQNADIVMQDVRVPESRRL-QNATSFRSTAEVLRLTRTEVAwqavGI 262
Cdd:cd01152 173 EApkhRGisiLLVDMDSPGVTVRPI--RSINGGEFFNEVFLDDVRVPDANRVgEVNDGWKVAMTTLNFERVSIG----GS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 263 AVGAYEAALAYARERIQFGKPIAAHQLVQDLLVKSLSNITASIALCTQASAMQDAGVGGDEHSALAKAFATAKMRETVAW 342
Cdd:cd01152 247 AATFFELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFGSELAQELAEL 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1930971987 343 CREVQGGNGIVLDKG----VARFFAD------AEAIYSyeGTREVNTLIVGRAITG 388
Cdd:cd01152 327 ALELLGTAALLRDPApgaeLAGRWEAdylrsrATTIYG--GTSEIQRNIIAERLLG 380
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
99-386 |
2.60e-24 |
|
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: 103.60 E-value: 2.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 99 IGVQSGLAMNSIAVAG----SDEQQREWLPRMATGEI----VGAFGLTEPYSGSDSAKGLRTTARREGDEWVLDGEKrWI 170
Cdd:cd01154 107 AGLLCPLTMTDAAVYAlrkyGPEELKQYLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERSGGGVYRLNGHK-WF 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 171 GNATFADVVVIWAKDV-ADGQVKG---FLV-TTDTAG----FTATKIEDKIALRGVQNADIVMQDVrvpESRRL-QNATS 240
Cdd:cd01154 186 ASAPLADAALVLARPEgAPAGARGlslFLVpRLLEDGtrngYRIRRLKDKLGTRSVATGEVEFDDA---EAYLIgDEGKG 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 241 FRSTAEVLRLTRTEVAWQAVGIAVGAYEAALAYARERIQFGKPIAAHQLVQDLLVKSLSNITASIALCTQASAMQDAGVG 320
Cdd:cd01154 263 IYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAA 342
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1930971987 321 GDEHSALAKAFATAKMRETVAW--------CREVQGGNGIVLDKGVARFFADAEAIYSYEGTREVNTLIVGRAI 386
Cdd:cd01154 343 DKPVEAHMARLATPVAKLIACKraapvtseAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLRVL 416
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
134-224 |
8.23e-22 |
|
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: 88.88 E-value: 8.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 134 AFGLTEPYSGSDSAKGLRTTARREGDEWVLDGEKRWIGNATFADVVVIWAK---DVADGQVKGFLVTTDTAGFTATKIED 210
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGGGWVLNGTKWWITNAGIADLFLVLARtggDDRHGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....
gi 1930971987 211 KIALRGVQNADIVM 224
Cdd:pfam02770 81 KLGVRGLPTGELVF 94
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
107-385 |
2.11e-21 |
|
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: 94.76 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 107 MNSIAVAGSDEQQREWLPRMATGEIVGAFGLTEPYSGSDSAKGLRTTARREGDEWVLDGEKRWIGNATFAD--VVVIWAK 184
Cdd:cd01155 101 MEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDVASSDATNIECSIERDGDDYVINGRKWWSSGAGDPRckIAIVMGR 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 185 DVADG-----QVKGFLVTTDTAGftaTKIEDKIALRGVQNA-----DIVMQDVRVPESRR-LQNATSFRSTAEVLRLTRT 253
Cdd:cd01155 181 TDPDGaprhrQQSMILVPMDTPG---VTIIRPLSVFGYDDAphghaEITFDNVRVPASNLiLGEGRGFEIAQGRLGPGRI 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 254 EVAWQAVGIAVGAYEAALAYARERIQFGKPIAAHQLVQDLLVKSLSNITASIALCTQASAMQDAGVGGDEHS--ALAKAF 331
Cdd:cd01155 258 HHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTVGNKAARKeiAMIKVA 337
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1930971987 332 ATAKMRETVAWCREVQGGNGIVLDKGVARFFADAEAIYSYEGTREVNTLIVGRA 385
Cdd:cd01155 338 APRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARM 391
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
88-391 |
1.55e-19 |
|
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: 90.47 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 88 LGRVDASVATFIGVQSGLAMNSIAVAGSDEQQREWLPRMATGEIVGAFGLTEPYSGSDSaKGLRTTAR--REGDEWVLD- 164
Cdd:cd01150 91 LGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNL-QGLETTATydPLTQEFVINt 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 165 ----GEKRWIGN-ATFADVVVIWAKDVADGQ---VKGFLV---TTDT----AGFTATKIEDKIALRGVQNADIVMQDVRV 229
Cdd:cd01150 170 pdftATKWWPGNlGKTATHAVVFAQLITPGKnhgLHAFIVpirDPKThqplPGVTVGDIGPKMGLNGVDNGFLQFRNVRI 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 230 PESRRLqNATS------------------FRSTAEVLRLTRTEVAWQAVGIAVGAYEAALAYARERIQFGK-------PI 284
Cdd:cd01150 250 PRENLL-NRFGdvspdgtyvspfkdpnkrYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPkpsdpevQI 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 285 AAHQLVQDLLVKSLSnitASIAL-------------CTQASAMQDAGVGGDEH--SALAKAFATAKMRETVAWCREVQGG 349
Cdd:cd01150 329 LDYQLQQYRLFPQLA---AAYAFhfaakslvemyheIIKELLQGNSELLAELHalSAGLKAVATWTAAQGIQECREACGG 405
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1930971987 350 NGIVLDKGVARFFADAEAIYSYEGTREVNTLIVGRAITGQAA 391
Cdd:cd01150 406 HGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYA 447
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
52-377 |
9.16e-15 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 76.05 E-value: 9.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 52 MQVIAPLAELGMYgpgvPLVRQFENSAVYrgWAALE-LGRVDASVATFIGVQSGLAMNSIAVAGSDEQQREWLPRMATGE 130
Cdd:PLN02636 99 RQLTGLVREAGIR----PMKYLVEDPAKY--FAITEaVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLD 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 131 IVGAFGLTEPYSGSDsAKGLRTTAR--REGDEWVLD-----GEKRWIGNAT----FADVVVIW------AKDVADGQVKG 193
Cdd:PLN02636 173 YPGCFAMTELHHGSN-VQGLQTTATfdPLTDEFVINtpndgAIKWWIGNAAvhgkFATVFARLklpthdSKGVSDMGVHA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 194 FLV----TTDTAGFTATKIED---KIALRGVQNADIVMQDVRVPE----------SRRLQNATS-------FRSTAEVLR 249
Cdd:PLN02636 252 FIVpirdMKTHQVLPGVEIRDcghKVGLNGVDNGALRFRSVRIPRdnllnrfgdvSRDGKYTSSlptinkrFAATLGELV 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 250 LTRTEVAWQAVGIAVGAYEAALAYARERIQFGKP------IAAHQLVQDLLVKSLSNIT----ASIALCTQASAMQ---D 316
Cdd:PLN02636 332 GGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPkqpeisILDYQSQQHKLMPMLASTYafhfATEYLVERYSEMKkthD 411
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1930971987 317 AGVGGDEH--SALAKAFATAKMRETVAWCREVQGGNGIVldkGVARFFA---DAEAIYSYEGTREV 377
Cdd:PLN02636 412 DQLVADVHalSAGLKAYITSYTAKALSTCREACGGHGYA---AVNRFGSlrnDHDIFQTFEGDNTV 474
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
114-354 |
1.26e-12 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 69.46 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 114 GSDEQQREWLPRMATGEIVGAFGLTEPYSGSDSA----KGLRTTARREGDEWV---LDGEKRWIGNATFADVVVIWAK-- 184
Cdd:PRK09463 176 GTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGsipdTGVVCKGEWQGEEVLgmrLTWNKRYITLAPIATVLGLAFKly 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 185 D----VADGQVKGF---LVTTDTAGFtatkiedKIALR----GV--QNADIVMQDVRVPES-------------RRLQN- 237
Cdd:PRK09463 256 DpdglLGDKEDLGItcaLIPTDTPGV-------EIGRRhfplNVpfQNGPTRGKDVFIPLDyiiggpkmagqgwRMLMEc 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 238 -----ATSFRSTaevlrltrtevawqAVGIAVGAYEAALAYARERIQFGKPIAAHQLVQDllvkSLSNITASIALCTQAS 312
Cdd:PRK09463 329 lsvgrGISLPSN--------------STGGAKLAALATGAYARIRRQFKLPIGKFEGIEE----PLARIAGNAYLMDAAR 390
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1930971987 313 AMQDAGVGGDEH----SALAKAFATAKMRETVAWCREVQGGNGIVL 354
Cdd:PRK09463 391 TLTTAAVDLGEKpsvlSAIAKYHLTERGRQVINDAMDIHGGKGICL 436
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
94-386 |
3.26e-12 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 67.97 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 94 SVATFIGVQSGlAMNSIAVAGSDEQQREWLPRMATGEIVGAFGLTEPYSGSDSAKgLRTTARREGD-EWVLDGEKRWI-- 170
Cdd:PTZ00456 145 GFSMYPGLSIG-AANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQ-VKTKAEPSADgSYKITGTKIFIsa 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 171 GNATFAD--VVVIWA---------KDVADGQVKGFLVTTDTAGFTATKI-----EDKIALRGVQNADIVMQD-----VRV 229
Cdd:PTZ00456 223 GDHDLTEniVHIVLArlpnslpttKGLSLFLVPRHVVKPDGSLETAKNVkciglEKKMGIKGSSTCQLSFENsvgylIGE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 230 PESRRLQNATsFRSTAevlrltRTEVAWQAVGIAVGAYEAALAYARER----------------------------IQFG 281
Cdd:PTZ00456 303 PNAGMKQMFT-FMNTA------RVGTALEGVCHAELAFQNALRYARERrsmralsgtkepekpadriichanvrqnILFA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 282 KPIAAHQLVQDLLVKSLSNITASIALCTQASAMqdagvgGDE---HSALAKAFATAKMRETVAWCREVQGGNGIVLDKGV 358
Cdd:PTZ00456 376 KAVAEGGRALLLDVGRLLDIHAAAKDAATREAL------DHEigfYTPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGM 449
|
330 340
....*....|....*....|....*....
gi 1930971987 359 ARFFADAEAIYSYEGTREVNTL-IVGRAI 386
Cdd:PTZ00456 450 EQILRDARIGTLYEGTTGIQALdFIGRKV 478
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
114-354 |
1.07e-11 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 66.52 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 114 GSDEQQREWLPRMATGEIVGAFGLTEPYSGSDSA----KGLRTTARREGDEWV---LDGEKRWIGNATFADVVVIWAK-- 184
Cdd:PRK13026 175 GTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGaipdTGIVCRGEFEGEEVLglrLTWDKRYITLAPVATVLGLAFKlr 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 185 -------DVADGQVKGFLVTTDTAGFTATKIEDKIALRgVQNADIVMQDVRVPESRRL---QNATS-FRSTAEVLRLTRT 253
Cdd:PRK13026 255 dpdgllgDKKELGITCALIPTDHPGVEIGRRHNPLGMA-FMNGTTRGKDVFIPLDWIIggpDYAGRgWRMLVECLSAGRG 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 254 eVAWQAVGIAVG--AYEAALAYARERIQFGKPIAAHQLVQDllvkSLSNITASIALCTQASAMQDAGVggDEH------S 325
Cdd:PRK13026 334 -ISLPALGTASGhmATRTTGAYAYVRRQFGMPIGQFEGVQE----ALARIAGNTYLLEAARRLTTTGL--DLGvkpsvvT 406
|
250 260
....*....|....*....|....*....
gi 1930971987 326 ALAKAFATAKMRETVAWCREVQGGNGIVL 354
Cdd:PRK13026 407 AIAKYHMTELARDVVNDAMDIHAGKGIQL 435
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
84-384 |
5.51e-10 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 61.01 E-value: 5.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 84 AALELGRVDASVATFI-GVQSGLAMNSIAVAGSDEQQREWLPRMATGEIVGAFGLTEPYSGSDsAKGLRTTAR--REGDE 160
Cdd:PTZ00460 79 PNYYTPNLLCPQGTFIsTVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSD-VQNLETTATydKQTNE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 161 WVL-----DGEKRWIGNATF-ADVVVIWAKDVADGQVKG---FLVttdtagftatKIEDKIA---LRGVQNADI------ 222
Cdd:PTZ00460 158 FVIhtpsvEAVKFWPGELGFlCNFALVYAKLIVNGKNKGvhpFMV----------RIRDKEThkpLQGVEVGDIgpkmgy 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 223 --------VMQDVRVPESRRLQNATSFRSTAEVLRLTRTEVAWQAVGI------------AVGAYEAALAYARERIQFGK 282
Cdd:PTZ00460 228 avkdngflSFDHYRIPLDSLLARYIKVSEDGQVERQGNPKVSYASMMYmrnliidqyprfAAQALTVAIRYSIYRQQFTN 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 283 ------PIAAHQLVQDLLVKSLSNITASIALCTQASAM----------QDAGVGGDEHSAL--AKAFATAKMRETVAWCR 344
Cdd:PTZ00460 308 dnkqenSVLEYQTQQQKLLPLLAEFYACIFGGLKIKELvddnfnrvqkNDFSLLQLTHAILsaAKANYTYFVSNCAEWCR 387
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1930971987 345 EVQGGNGIVLDKGVARFFADAEAIYSYEGTREVNTLIVGR 384
Cdd:PTZ00460 388 LSCGGHGYAHYSGLPAIYFDMSPNITLEGENQIMYLQLAR 427
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
114-377 |
4.23e-09 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 58.27 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 114 GSDEQQREWLPRMATGEIVGAFGLTEPYSGSDSAKGLRTTARREGDEWVLDGEKRWIGNAT--FADVVVIWAKDVADG-- 189
Cdd:PLN02876 533 GNKEQQLEWLIPLLEGKIRSGFAMTEPQVASSDATNIECSIRRQGDSYVINGTKWWTSGAMdpRCRVLIVMGKTDFNApk 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 190 --QVKGFLVTTDTAGftaTKIEDKIALRGVQN-----ADIVMQDVRVPESR-RLQNATSFRSTAEVLRLTRTEVAWQAVG 261
Cdd:PLN02876 613 hkQQSMILVDIQTPG---VQIKRPLLVFGFDDaphghAEISFENVRVPAKNiLLGEGRGFEIAQGRLGPGRLHHCMRLIG 689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 262 IAVGAYEAALAYARERIQFGKPIAAHQLVQDLLVKSLSNITASIALCTQASAMQDagVGGDEHS----ALAKAFATAKMR 337
Cdd:PLN02876 690 AAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLD--RLGNKKArgiiAMAKVAAPNMAL 767
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1930971987 338 ETVAWCREVQGGNGIVLDKGVARFFADAEAIYSYEGTREV 377
Cdd:PLN02876 768 KVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEV 807
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
87-335 |
1.34e-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: 56.18 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 87 ELGRVDASVATFIGVQSGLAmNSIAVAGSDEQQREWLPRMATGEIVGAFGltEPYSGSDSAKGLRTTARrEGDEWVLDGE 166
Cdd:cd01163 61 ELAAADSNIAQALRAHFGFV-EALLLAGPEQFRKRWFGRVLNGWIFGNAV--SERGSVRPGTFLTATVR-DGGGYVLNGK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 167 KRWIGNATFADVVVIWAKDVADGQVkGFLVTTDTAGFTATKIEDKIALRGVQNADIVMQDVRVPE-------SRRLQNat 239
Cdd:cd01163 137 KFYSTGALFSDWVTVSALDEEGKLV-FAAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPdevlprpNAPDRG-- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 240 SFRSTAEVLRLTRTevawqAVGIAVGAYEAALAYARERiqfGKPIA------------AHQLVQDLLVKSLS--NITASI 305
Cdd:cd01163 214 TLLTAIYQLVLAAV-----LAGIARAALDDAVAYVRSR---TRPWIhsgaesarddpyVQQVVGDLAARLHAaeALVLQA 285
|
250 260 270
....*....|....*....|....*....|
gi 1930971987 306 ALCTQASAMQDAGVGGDEHSALAKAFATAK 335
Cdd:cd01163 286 ARALDAAAAAGTALTAEARGEAALAVAAAK 315
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
79-389 |
8.82e-08 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 54.01 E-value: 8.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 79 VYRGW-------------AALE-LGRVDASVATFIGVQSGLAMNSIAVAGSDEQQREWLPRMATGEIVGAFGLTEPYSGS 144
Cdd:PLN02312 119 VFRGWltetgpeaelrklALLEvIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGS 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 145 DsAKGLRT--TARREGDEWVLD-----GEKRWIGNAT-FADVVVIWAKDVADGQ---VKGFLVTT-DTAGFTA--TKIED 210
Cdd:PLN02312 199 N-VRGIETvtTYDPKTEEFVINtpcesAQKYWIGGAAnHATHTIVFSQLHINGKnegVHAFIAQIrDQDGNICpnIRIAD 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 211 ---KIALRGVQNADIVMQDVRVPEsRRLQNATS------------------FRSTAEVLRLTRTEVAWQAVGIAVGAYEA 269
Cdd:PLN02312 278 cghKIGLNGVDNGRIWFDNLRIPR-ENLLNSVAdvspdgkyvsaikdpdqrFGAFLAPLTSGRVTIAVSAIYSSKVGLAI 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 270 ALAYARERIQFGkpIAAHQlVQDLLVKSLSNITASIALCTQASAMQDAGVG--------GDEH--------SALAKAFAT 333
Cdd:PLN02312 357 AIRYSLSRRAFS--VTPNG-PEVLLLDYPSHQRRLLPLLAKTYAMSFAANDlkmiyvkrTPESnkaihvvsSGFKAVLTW 433
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1930971987 334 AKMReTVAWCREVQGGNGIVLDKGVARFFADAEAIYSYEGTREVNTLIVGRAITGQ 389
Cdd:PLN02312 434 HNMR-TLQECREACGGQGLKTENRVGQLKAEYDVQSTFEGDNNVLMQQVSKALLAE 488
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
255-376 |
9.31e-07 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 47.73 E-value: 9.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 255 VAWQAVGIAVGAYEAALAYARERIQ--FGKPIAAHQLVQDLLVKSLSNITASIALCTQASAMQDAGVGGDEH-------- 324
Cdd:pfam08028 2 IAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAAAGKPvtpalrae 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1930971987 325 SALAKAFATAKMRETVAWCREVQGGNGIVLDKGVARFFADAEAIYSYEGTRE 376
Cdd:pfam08028 82 ARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
97-225 |
1.37e-06 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 50.22 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 97 TFIGVQSGLAMNSIAVAGSDEQQREWLPRMATGEIVGAFGLTEPYSGSDsAKGLRTTAR--REGDEWV-----LDGEKRW 169
Cdd:PLN02443 97 GYTDLHWGMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSN-VQGLETTATfdPKTDEFVihsptLTSSKWW 175
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1930971987 170 IGN----ATFAdvvVIWAKDVADGQ---VKGFLVTTDTagftatkIEDKIALRGVQNADIVMQ 225
Cdd:PLN02443 176 PGGlgkvSTHA---VVYARLITNGKdhgIHGFIVQLRS-------LDDHSPLPGVTVGDIGMK 228
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
35-388 |
2.21e-05 |
|
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: 46.19 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 35 REVAPIADAYWARAE----FPMQVIAPLAELGMY---------GPGVPLVRQFEnsavyrgwAALELGRVDASVATfigV 101
Cdd:cd01159 4 EDLAPLIRERAPEAErarrLPDEVVRALREIGFFrmfvpkrygGLEGDFAEFAE--------AIATLAEACGSAAW---V 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 102 QSGLAMNSIAVAGSDEQQREwlprmatgEIVGAFGLTEpYSGSDSAKGlrtTARREGDEWVLDGEKRWIGNATFAD---V 178
Cdd:cd01159 73 ASIVATHSRMLAAFPPEAQE--------EVWGDGPDTL-LAGSYAPGG---RAERVDGGYRVSGTWPFASGCDHADwilV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 179 VVIWAKDVADGQVKGFLVTTdtAGFTATKIEDKIALRGVQNADIVMQDVRVPESRRLQNATSFRSTAEVLRLTRTEVAWQ 258
Cdd:cd01159 141 GAIVEDDDGGPLPRAFVVPR--AEYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLTAGDMMAGDGPGGSTPVYRMPLR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1930971987 259 ----------AVGIAVGAYEAALAYARERIQ---FGKPIAAHQLVQDLLVKSLSNITASIALCTQASAMQDAGVGGDEHS 325
Cdd:cd01159 219 qvfplsfaavSLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAELDAARAFLERATRDLWAHALAGGPI 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1930971987 326 A--------LAKAFATAKMRETVAWCREVQGGNGIVLDKGVARFFADAEAIYSYEGTR-EVNTLIVGRAITG 388
Cdd:cd01159 299 DveerarirRDAAYAAKLSAEAVDRLFHAAGGSALYTASPLQRIWRDIHAAAQHAALNpETAAEAYGRALLG 370
|
|
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