|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
53-461 |
0e+00 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 836.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 53 DIASAFPQATPASTFPTSVSDYFGLEDLLSPEDVALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIIPHLASLKIAGGTIK 132
Cdd:PLN02526 1 DVSVAFPQATPASIFPPSVSDYYQFDDLLTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 133 GYGCPGLSILSHALVGAEIARVDASCCTFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSL 212
Cdd:PLN02526 81 GYGCPGLSITASAIATAEVARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 213 NTTAVKVEGGWLLNGQKRWIGNATFADIVVVFARNTQTNQINGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIP 292
Cdd:PLN02526 161 NTTATKVEGGWILNGQKRWIGNSTFADVLVIFARNTTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 293 DEDRLTGINSFQDTNKVLAVSRIMVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWK 372
Cdd:PLN02526 241 DEDRLPGVNSFQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 373 LCKMYESGKMTPGQASLCKAWNTLRARETVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGREITGIA 452
Cdd:PLN02526 321 LCKLYESGKMTPGHASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREITGIA 400
|
....*....
gi 1373925884 453 SIKPSASGK 461
Cdd:PLN02526 401 SFKPAASTR 409
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
72-454 |
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: 565.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 72 SDYFGLEDLLSPEDVALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIIPHLASLKIAGGTIKGYGCPGLSILSHALVGAEI 151
Cdd:cd01151 4 EDPLNLDDLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIKGYGCAGLSSVAYGLIAREV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 152 ARVDASCCTFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRW 231
Cdd:cd01151 84 ERVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 232 IGNATFADIVVVFARNTQTNQINGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLTGINSFQDTNKVLA 311
Cdd:cd01151 164 ITNSPIADVFVVWARNDETGKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAEGLRGPFKCLN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 312 VSRIMVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQASLCK 391
Cdd:cd01151 244 NARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLK 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1373925884 392 AWNTLRARETVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGREITGIASI 454
Cdd:cd01151 324 RNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAITGIQAF 386
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
81-450 |
8.85e-114 |
|
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: 339.89 E-value: 8.85e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 81 LSPEDVALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIIPHLASLKIAGGTI-KGYGCPGLSILSHALVGAEIARVDASCC 159
Cdd:COG1960 5 LTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIpEEYGGLGLSLVELALVLEELARADASLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 160 TFALVHSSlCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNATFAD 239
Cdd:COG1960 85 LPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVAD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 240 IVVVFAR---NTQTNQINGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLTGIN-SFQDTNKVLAVSRI 315
Cdd:COG1960 164 VILVLARtdpAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGkGFKIAMSTLNAGRL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 316 MVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQASLCKAWNT 395
Cdd:COG1960 244 GLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLFAT 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1373925884 396 LRARETVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGREITG 450
Cdd:COG1960 324 EAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLG 378
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
83-448 |
1.99e-81 |
|
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: 1.99e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 83 PEDVALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIIPHLASLKIAGGTI-KGYGCPGLSILSHALVGAEIARVDASCCTF 161
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIpEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 162 ALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNATFADIV 241
Cdd:cd01158 81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 242 VVFAR---NTQTNQINGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLTGIN-SFQDTNKVLAVSRIMV 317
Cdd:cd01158 161 IVFAVtdpSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGeGFKIAMQTLDGGRIGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 318 AWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQASLCKAWNTLR 397
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1373925884 398 ARETVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGREI 448
Cdd:cd01158 321 AMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHL 371
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
87-446 |
1.96e-73 |
|
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: 234.49 E-value: 1.96e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 87 ALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIiphLASLKIAGGtikgygcpglsilshalvgaeiarvdascctfalvhs 166
Cdd:cd00567 5 ELRDSAREFAAEELEPYARERRETPEEPWEL---LAELGLLLG------------------------------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 167 slcMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNATFADIVVVFAR 246
Cdd:cd00567 45 ---AALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLAR 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 247 ----NTQTNQINGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLTGINS-FQDTNKVLAVSRIMVAWLP 321
Cdd:cd00567 122 tdeeGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGgFELAMKGLNVGRLLLAAVA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 322 IGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKM-TPGQASLCKAWNTLRARE 400
Cdd:cd00567 202 LGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDeARLEAAMAKLFATEAARE 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1373925884 401 TVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGR 446
Cdd:cd00567 282 VADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
81-448 |
6.89e-63 |
|
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: 208.42 E-value: 6.89e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 81 LSPEDVALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIIPHLASLKIAGGTI-KGYGCPGLSILSHALVGAEIARVDASCC 159
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITApEEYGGSGMGYLAHVIIMEEISRASGSVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 160 TFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNATFAD 239
Cdd:cd01156 82 LSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDAD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 240 IVVVFAR---NTQTNQINGFIVKKGTPGY-RATKIEnKIGLRIVQNGDIIMKDVFIPDEDRLTGINSfqdTNKVLA---- 311
Cdd:cd01156 162 TLVVYAKtdpSAGAHGITAFIVEKGMPGFsRAQKLD-KLGMRGSNTCELVFEDCEVPEENILGGENK---GVYVLMsgld 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 312 VSRIMVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQASLCK 391
Cdd:cd01156 238 YERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVI 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1373925884 392 AWNTLRArETVAL-GRELLGGNGILSDFLVAKAFCDIEpiyTYE---GTYDINTLVTGREI 448
Cdd:cd01156 318 LYAAEKA-TQVALdAIQILGGNGYINDYPTGRLLRDAK---LYEigaGTSEIRRMVIGREL 374
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
83-448 |
8.91e-56 |
|
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: 189.63 E-value: 8.91e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 83 PEDVALRKRVRRVMEEHVAPVVTKyWEKA-EFPFEIIPHLASLKIAG-GTIKGYGCPGLSILSHALVGAEIARVDASCCT 160
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHE-WEKAgEVPREVWRKAGEQGLLGvGFPEEYGGIGGDLLSAAVLWEELARAGGSGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 161 FaLVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNATFADI 240
Cdd:cd01160 80 L-SLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 241 VVVFARNTQTNQ----INGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLTGIN-SFQDTNKVLAVSRI 315
Cdd:cd01160 159 VIVVARTGGEARgaggISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENkGFYYLMQNLPQERL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 316 MVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQASLCKAWNT 395
Cdd:cd01160 239 LIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWAT 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1373925884 396 LRARETVALGRELLGGNGILSDFLVAKAFCD--IEPIYTyeGTYDINTLVTGREI 448
Cdd:cd01160 319 ELQNRVAYECVQLHGGWGYMREYPIARAYRDarVQPIYG--GTTEIMKELISRQM 371
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
81-450 |
4.02e-49 |
|
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: 172.24 E-value: 4.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 81 LSPEDVALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIIPHLASLKIAGGTIKG-YGCPGLSILSHALVGAEIARVDASCC 159
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDdVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 160 TFALVHSsLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNATFAD 239
Cdd:cd01162 81 AYISIHN-MCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 240 IVVVFARNTQTNQ--INGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLTGINS-FQDTNKVLAVSRIM 316
Cdd:cd01162 160 VYVVMARTGGEGPkgISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQgFGIAMAGLNGGRLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 317 VAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGkmTPGQASLC---KAW 393
Cdd:cd01162 240 IASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRG--DPDAVKLCamaKRF 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1373925884 394 NTLRARETVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGREITG 450
Cdd:cd01162 318 ATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLT 374
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
89-448 |
7.69e-45 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 161.58 E-value: 7.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 89 RKRVRRVMEEHVAPVVTKYWEKAEFPFEI--IPHLASLKIAGGTI-KGYGCPGLSILSHALVGAEIARVDASCCTFALVH 165
Cdd:PLN02519 34 KESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGITApEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAH 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 166 SSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNATFADIVVVFA 245
Cdd:PLN02519 114 SNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 246 RNTQT---NQINGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLTginsfQDTNKV------LAVSRIM 316
Cdd:PLN02519 194 KTDVAagsKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLG-----QEGKGVyvmmsgLDLERLV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 317 VAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQAS---LCKAW 393
Cdd:PLN02519 269 LAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAgviLCAAE 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1373925884 394 NTLRaretVAL-GRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGREI 448
Cdd:PLN02519 349 RATQ----VALqAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGREL 400
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
60-442 |
5.34e-43 |
|
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: 156.86 E-value: 5.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 60 QATPASTFPtsvsDYFGLEDLLSPEDVALRKRVRRVMEEHVAPVVTKYWEKaeFPFEIIPHLASLKIAGGTI-KGYGCPG 138
Cdd:cd01161 10 DIVTKQVFP----YPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEK--IPRKTLTQLKELGLFGLQVpEEYGGLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 139 LSILSHALVgAEIARVDASCCTFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVK 218
Cdd:cd01161 84 LNNTQYARL-AEIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 219 VEGG--WLLNGQKRWIGNATFADIVVVFARNTQTN-------QINGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDV 289
Cdd:cd01161 163 SEDGkhYVLNGSKIWITNGGIADIFTVFAKTEVKDatgsvkdKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 290 FIPDEDRLTGI-NSFQDTNKVLAVSRIMVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFL 368
Cdd:cd01161 243 KIPVENVLGEVgDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATES 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1373925884 369 LGWKLCKMYESGKMTPGQ--ASLCKAWNTLRARETVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTL 442
Cdd:cd01161 323 MAYMTSGNMDRGLKAEYQieAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRL 398
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
81-450 |
1.09e-42 |
|
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: 155.05 E-value: 1.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 81 LSPEDVALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIIPHLASLKIAGGTI-KGYGCPGLSILSHALVGAEIArvdaSCC 159
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIpEDCGGLGLGTFDTCLITEELA----YGC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 160 T---FALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNAT 236
Cdd:cd01157 77 TgvqTAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 237 FADIVVVFARNT------QTNQINGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLTGINS-FQDTNKV 309
Cdd:cd01157 157 KANWYFLLARSDpdpkcpASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAgFKIAMGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 310 LAVSRIMVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQASL 389
Cdd:cd01157 237 FDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASI 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1373925884 390 CKAWNTLRARETVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGREITG 450
Cdd:cd01157 317 AKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLG 377
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
82-191 |
1.61e-34 |
|
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: 124.88 E-value: 1.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 82 SPEDVALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIIPHLASLKIAGGTI-KGYGCPGLSILSHALVGAEIARVDASCCT 160
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIpEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|.
gi 1373925884 161 FALVHSSLCMSTIGMLGNEEQKQKYLPSLAR 191
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLAS 111
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
61-346 |
6.24e-32 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 126.21 E-value: 6.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 61 ATPASTFPTSVSDYFGLEDLlSPEDVALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIIPHLASLKIAGGTI-KGYGCPGL 139
Cdd:PTZ00461 18 WTAAATMTSASRAFMDLYNP-TPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVpEADGGAGM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 140 SILSHALVGAEIARVDASCCTFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKV 219
Cdd:PTZ00461 97 DAVAAVIIHHELSKYDPGFCLAYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 220 -EGGWLLNGQKRWIGNATFADIVVVFARntQTNQINGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLT 298
Cdd:PTZ00461 177 sNGNYVLNGSKIWITNGTVADVFLIYAK--VDGKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLG 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1373925884 299 GI-NSFQDTNKVLAVSRIMVAWLPIGVCMGVYDICYRYLQERKQFGAPL 346
Cdd:PTZ00461 255 EEgKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPI 303
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
81-448 |
1.60e-31 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 124.46 E-value: 1.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 81 LSPEDVALRKRVRRVMEEHVAPVVTKYW-EKAEFPFEIIPHLASLKIAG-GTIKGYGCPGLSILSHALVGAEIARvdaSC 158
Cdd:PRK12341 5 LTEEQELLLASIRELITRNFPEEYFRTCdENGTYPREFMRALADNGISMlGVPEEFGGTPADYVTQMLVLEEVSK---CG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 159 CTFALVHSSLCMSTIGMLGNEEQKQKYLPS-LARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNATF 237
Cdd:PRK12341 82 APAFLITNGQCIHSMRRFGSAEQLRKTAEStLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAKE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 238 ADIVVVFARNTQ----TNQINGFIVKKGTPGYRATKIEnKIGLRIVQNGDIIMKDVFIPDEDrLTGI--NSFQDTNKVLA 311
Cdd:PRK12341 162 YPYMLVLARDPQpkdpKKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESD-LVGEegMGFLNVMYNFE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 312 VSRIMVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQASLCK 391
Cdd:PRK12341 240 MERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAALAK 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1373925884 392 AWNTLRARETVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGREI 448
Cdd:PRK12341 320 LYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQI 376
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
109-448 |
5.56e-30 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 120.32 E-value: 5.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 109 EKAEFPFEIIPHLASLKIAGGTI-KGYGCPGLSILSHALVGAEIARVDASccTFALVHSSLCMSTIGMLGNEEQKQKYLP 187
Cdd:PRK03354 34 RDSVYPERFVKALADMGIDSLLIpEEHGGLDAGFVTLAAVWMELGRLGAP--TYVLYQLPGGFNTFLREGTQEQIDKIMA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 188 SLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNATFADIVVVFARNTQTNQINGF---IVKKGTPG 264
Cdd:PRK03354 112 FRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASPDKPVYtewFVDMSKPG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 265 YRATKIEnKIGLRIVQNGDIIMKDVFIPDEDrLTGI--NSFQDTNKVLAVSRIMVAWLPIGVCMGVYDICYRYLQERKQF 342
Cdd:PRK03354 192 IKVTKLE-KLGLRMDSCCEITFDDVELDEKD-MFGRegNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQF 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 343 GAPLAALQINQEKLVRM---LGNIQAMFL-LGWKlckmYESGKMTPGQASLCKAWNTLRARETVALGRELLGGNGILSDF 418
Cdd:PRK03354 270 GEAIGRFQLIQEKFAHMaikLNSMKNMLYeAAWK----ADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNH 345
|
330 340 350
....*....|....*....|....*....|
gi 1373925884 419 LVAKAFCDIEPIYTYEGTYDINTLVTGREI 448
Cdd:PRK03354 346 RISRFWRDLRVDRVSGGSDEMQILTLGRAV 375
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
83-439 |
1.20e-27 |
|
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: 113.60 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 83 PEDVALRKRVRRVMEEHVAPVVTKywEKAEFPFEI----IPHLASLKIAG----GTIKGYGCPGLSILSHALVGAEIARV 154
Cdd:cd01152 1 PSEEAFRAEVRAWLAAHLPPELRE--ESALGYREGredrRRWQRALAAAGwaapGWPKEYGGRGASLMEQLIFREEMAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 155 DASCcTFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGN 234
Cdd:cd01152 79 GAPV-PFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 235 ATFADIVVVFAR-NTQTNQING---FIVKKGTPGYRATKIENKIGlRIVQNgDIIMKDVFIPDEDRLTGINS-FQDTNKV 309
Cdd:cd01152 158 AHYADWAWLLVRtDPEAPKHRGisiLLVDMDSPGVTVRPIRSING-GEFFN-EVFLDDVRVPDANRVGEVNDgWKVAMTT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 310 LAVSRimvawlpigVCMGVYDICY-----RYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTP 384
Cdd:cd01152 236 LNFER---------VSIGGSAATFfelllARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPG 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1373925884 385 GQASLCKAWNTLRARETVALGRELLGGNGILSD----------FLVAKAFCDIEPIYTyeGTYDI 439
Cdd:cd01152 307 AEASIAKLFGSELAQELAELALELLGTAALLRDpapgaelagrWEADYLRSRATTIYG--GTSEI 369
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
310-448 |
1.69e-26 |
|
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: 104.26 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 310 LAVSRIMVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQASL 389
Cdd:pfam00441 11 LNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAGGPDGAEASM 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1373925884 390 CKAWNTLRARETVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGREI 448
Cdd:pfam00441 91 AKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
197-287 |
3.16e-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: 90.80 E-value: 3.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 197 CWALTEPAYGSDASSLNTTAVKVEGG-WLLNGQKRWIGNATFADIVVVFARNTQT---NQINGFIVKKGTPGYRATKIEN 272
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGGgWVLNGTKWWITNAGIADLFLVLARTGGDdrhGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 1373925884 273 KIGLRIVQNGDIIMK 287
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
87-442 |
1.69e-19 |
|
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: 90.51 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 87 ALRKRVRRVMEEHVAPVVtkyWEKAEFPfEIIPHLASLKIAGGTIKGYGCPgLSIlshalvgaeiarvdasccTFALVHs 166
Cdd:cd01154 66 AWHALMRRLIEEGVINIE---DGPAGEG-RRHVHFAAGYLLSDAAAGLLCP-LTM------------------TDAAVY- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 167 slcmsTIGMLGNEEQKQKYLPSLARFD----TIGCWaLTEPAYGSDASSLNTTAVKVEGG-WLLNGQKrWIGNATFADIV 241
Cdd:cd01154 122 -----ALRKYGPEELKQYLPGLLSDRYktglLGGTW-MTEKQGGSDLGANETTAERSGGGvYRLNGHK-WFASAPLADAA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 242 VVFAR----NTQTNQINGFIVKKGTP-----GYRATKIENKIGLRIVQNGDIIMKDV---FIPDEDRltGINSfqdTNKV 309
Cdd:cd01154 195 LVLARpegaPAGARGLSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDAeayLIGDEGK--GIYY---ILEM 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 310 LAVSRIMVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYE-SGKMTPGQA- 387
Cdd:cd01154 270 LNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDrAAADKPVEAh 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1373925884 388 ------SLCKAWNTLRARETVALGRELLGGNGILSDFLVAKAFCD--IEPIytYEGTYDINTL 442
Cdd:cd01154 350 marlatPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREaqVTPI--WEGTGNIQAL 410
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
125-449 |
2.56e-19 |
|
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: 89.76 E-value: 2.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 125 KIAGGTIKGYGCP----GLSiLSHALVGAeIARVDASCCTFALVHSSL--CMSTIGMLGNEEQKQKYLPSLARFDTIGCW 198
Cdd:cd01153 44 AFAEAGWMALGVPeeygGQG-LPITVYSA-LAEIFSRGDAPLMYASGTqgAAATLLAHGTEAQREKWIPRLAEGEWTGTM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 199 ALTEPAYGSDASSLNTTAVKVEGG-WLLNGQKRWIGN---ATFADIV-VVFAR----NTQTNQINGFIVKK----GTP-G 264
Cdd:cd01153 122 CLTEPDAGSDLGALRTKAVYQADGsWRINGVKRFISAgehDMSENIVhLVLARsegaPPGVKGLSLFLVPKflddGERnG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 265 YRATKIENKIGLRIVQNGDIIMKD---VFIPDEDRltGInsfQDTNKVLAVSRIMVAWLPIGVCMGVYDICYRYLQERKQ 341
Cdd:cd01153 202 VTVARIEEKMGLHGSPTCELVFDNakgELIGEEGM--GL---AQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 342 FGAPLAA---LQINQEKLVRMLGNIQAMFLLGWKLCKMY-------ESGKMTPGQAS------------LCKAWNTLRAR 399
Cdd:cd01153 277 GGDLIKAapaVTIIHHPDVRRSLMTQKAYAEGSRALDLYtatvqdlAERKATEGEDRkalsaladlltpVVKGFGSEAAL 356
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1373925884 400 ETVALGRELLGGNGILSDFLVAKAFCD--IEPIytYEGTYDINTL-VTGREIT 449
Cdd:cd01153 357 EAVSDAIQVHGGSGYTREYPIEQYYRDarITTI--YEGTTGIQALdLIGRKIV 407
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
153-435 |
7.48e-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: 89.31 E-value: 7.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 153 RVDASCCTFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAV--KVEGGWLLN---- 226
Cdd:cd01150 93 GYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATydPLTQEFVINtpdf 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 227 -GQKRWIGN-ATFADIVVVFAR---NTQTNQINGFIVK-------KGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDE 294
Cdd:cd01150 173 tATKWWPGNlGKTATHAVVFAQlitPGKNHGLHAFIVPirdpkthQPLPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRE 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 295 DRL----------TGINSFQDTNKVLAVSRIMVAWLPIGVCMGVYD-------ICYRYLQERKQFG-------APLAALQ 350
Cdd:cd01150 253 NLLnrfgdvspdgTYVSPFKDPNKRYGAMLGTRSGGRVGLIYDAAMslkkaatIAIRYSAVRRQFGpkpsdpeVQILDYQ 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 351 INQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQ-------------ASLcKAWNTLRARETVALGRELLGGNGILSD 417
Cdd:cd01150 333 LQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKELLQgnsellaelhalsAGL-KAVATWTAAQGIQECREACGGHGYLAM 411
|
330
....*....|....*...
gi 1373925884 418 FLVAKAFCDIEPIYTYEG 435
Cdd:cd01150 412 NRLPTLRDDNDPFCTYEG 429
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
164-413 |
3.18e-13 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 71.81 E-value: 3.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 164 VHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAV--KVEGGWLLN-----GQKRWIGNAT 236
Cdd:PLN02636 143 VQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATfdPLTDEFVINtpndgAIKWWIGNAA 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 237 F-ADIVVVFAR---------NTQTNQINGFIV-------KKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLtg 299
Cdd:PLN02636 223 VhGKFATVFARlklpthdskGVSDMGVHAFIVpirdmktHQVLPGVEIRDCGHKVGLNGVDNGALRFRSVRIPRDNLL-- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 300 iNSFQDT-------------NKVLAVS-------RIMVAWLPIGVCMGVYDICYRYLQERKQFGAP------LAALQINQ 353
Cdd:PLN02636 301 -NRFGDVsrdgkytsslptiNKRFAATlgelvggRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPkqpeisILDYQSQQ 379
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 354 EKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQ----------ASLcKAWNTLRARETVALGRELLGGNG 413
Cdd:PLN02636 380 HKLMPMLASTYAFHFATEYLVERYSEMKKTHDDqlvadvhalsAGL-KAYITSYTAKALSTCREACGGHG 448
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
117-414 |
3.79e-13 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 71.77 E-value: 3.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 117 IIPhlaslkiaggtiKGYGCPGLSILSHALVGAEIARVdascctfalvhSSLCMSTIG---------ML---GNEEQKQK 184
Cdd:PRK09463 127 IIP------------KEYGGLEFSAYAHSRVLQKLASR-----------SGTLAVTVMvpnslgpgeLLlhyGTDEQKDH 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 185 YLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGW--------LLNGQKRWIgnaTFADIVVVFARNTQTNQINGF 256
Cdd:PRK09463 184 YLPRLARGEEIPCFALTSPEAGSDAGSIPDTGVVCKGEWqgeevlgmRLTWNKRYI---TLAPIATVLGLAFKLYDPDGL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 257 I------------VKKGTPGYratkienKIGLR------IVQNGDIIMKDVFIPdedrLTGINSFQDT--------NKVL 310
Cdd:PRK09463 261 LgdkedlgitcalIPTDTPGV-------EIGRRhfplnvPFQNGPTRGKDVFIP----LDYIIGGPKMagqgwrmlMECL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 311 AVSR-IMvawLPiGVCMGVYDICYR----YLQERKQFGAPLAALQINQEKLVRMLGN---IQAMFLLGwklCKMYESGKm 382
Cdd:PRK09463 330 SVGRgIS---LP-SNSTGGAKLAALatgaYARIRRQFKLPIGKFEGIEEPLARIAGNaylMDAARTLT---TAAVDLGE- 401
|
330 340 350
....*....|....*....|....*....|...
gi 1373925884 383 TPGQAS-LCKAWNTLRARETVALGRELLGGNGI 414
Cdd:PRK09463 402 KPSVLSaIAKYHLTERGRQVINDAMDIHGGKGI 434
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
99-414 |
1.83e-12 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 69.60 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 99 HVAPVVTKYWEKAEFPFEIIPhlaslkiaggtiKGYGCPGLSILSHALVGAEIARVDASCCTFALVHSSLcmsTIGML-- 176
Cdd:PRK13026 108 DLPPEVWDYLKKEGFFALIIP------------KEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPNSL---GPGELlt 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 177 --GNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAV----KVEG----GWLLNGQKRWIgnaTFADIVVVFAR 246
Cdd:PRK13026 173 hyGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTGIvcrgEFEGeevlGLRLTWDKRYI---TLAPVATVLGL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 247 NTQTNQINGFIVKKGTPGYRATKIEN-----KIGLR------IVQNGDIIMKDVFIPdEDRLTG-----INSFQDTNKVL 310
Cdd:PRK13026 250 AFKLRDPDGLLGDKKELGITCALIPTdhpgvEIGRRhnplgmAFMNGTTRGKDVFIP-LDWIIGgpdyaGRGWRMLVECL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 311 AVSRIMVawLP-IGVCMGVydICYR----YLQERKQFGAPLAALQINQEKLVRMLGN---IQAMFLLgwkLCKMYESGKm 382
Cdd:PRK13026 329 SAGRGIS--LPaLGTASGH--MATRttgaYAYVRRQFGMPIGQFEGVQEALARIAGNtylLEAARRL---TTTGLDLGV- 400
|
330 340 350
....*....|....*....|....*....|...
gi 1373925884 383 TPGQAS-LCKAWNTLRARETVALGRELLGGNGI 414
Cdd:PRK13026 401 KPSVVTaIAKYHMTELARDVVNDAMDIHAGKGI 433
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
87-354 |
1.05e-10 |
|
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: 63.18 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 87 ALRKRVRRVMEEHVAP---VVTKYWEKAEFPFEIIPH-LASLKIAGGTI--------KGYGCPGLSILSHALVGAEIARv 154
Cdd:cd01155 5 ELRARVKAFMEEHVYPaeqEFLEYYAEGGDRWWTPPPiIEKLKAKAKAEglwnlflpEVSGLSGLTNLEYAYLAEETGR- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 155 dascCTFAlVHSSLC-------MSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYG-SDASSLNTTAVKVEGGWLLN 226
Cdd:cd01155 84 ----SFFA-PEVFNCqapdtgnMEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDVAsSDATNIECSIERDGDDYVIN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 227 GQKRWIGNATFAD--IVVVFAR-----NTQTNQINGFIVKKGTPGY---RATKI----ENKIGlrivqNGDIIMKDVFIP 292
Cdd:cd01155 159 GRKWWSSGAGDPRckIAIVMGRtdpdgAPRHRQQSMILVPMDTPGVtiiRPLSVfgydDAPHG-----HAEITFDNVRVP 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1373925884 293 DEDRLTGINS-FQDTNKVLAVSRIMVAWLPIGVC-MGVYDICYRYLQeRKQFGAPLAALQINQE 354
Cdd:cd01155 234 ASNLILGEGRgFEIAQGRLGPGRIHHCMRLIGAAeRALELMCQRAVS-REAFGKKLAQHGVVAH 296
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
160-435 |
3.15e-09 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 59.08 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 160 TFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAV-------KVEGGWLLNGQKRWI 232
Cdd:PLN02443 97 GYTDLHWGMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATfdpktdeFVIHSPTLTSSKWWP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 233 GN----ATFAdivVVFAR---NTQTNQINGFIVK-------KGTPGYRATKIENKIG---LRIVQNGDIIMKDVFIPDED 295
Cdd:PLN02443 177 GGlgkvSTHA---VVYARlitNGKDHGIHGFIVQlrslddhSPLPGVTVGDIGMKFGngaYNTMDNGFLRFDHVRIPRDQ 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 296 RLTGINSFQDTNKVLA--------------VSRIMVA----WLPIGVCMGVydicyRYLQERKQFGA---PLAALQIN-- 352
Cdd:PLN02443 254 MLMRLSKVTREGKYVQsdvprqlvygtmvyVRQTIVAdastALSRAVCIAT-----RYSAVRRQFGSqdgGPETQVIDyk 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 353 --QEKLVRMLGNIQAMFLLGWKLCKMY--------ESGKMTPGQASLC----KAWNTLRARETVALGRELLGGNGILSDF 418
Cdd:PLN02443 329 tqQSRLFPLLASAYAFRFVGEWLKWLYtdvtqrleANDFSTLPEAHACtaglKSLTTSATADGIEECRKLCGGHGYLCSS 408
|
330
....*....|....*..
gi 1373925884 419 LVAKAFCDIEPIYTYEG 435
Cdd:PLN02443 409 GLPELFAVYVPACTYEG 425
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
164-442 |
6.87e-09 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 58.25 E-value: 6.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 164 VHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAV--KVEGGWLLN-----GQKRWIGNAT 236
Cdd:PLN02312 155 VHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTydPKTEEFVINtpcesAQKYWIGGAA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 237 -FADIVVVFAR---NTQTNQINGFIVK----KGT--PGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLTGI------ 300
Cdd:PLN02312 235 nHATHTIVFSQlhiNGKNEGVHAFIAQirdqDGNicPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNSVadvspd 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 301 ----NSFQDTNK--------------VLAVSRIMVAwlPIGVCMGVydicyRYLQERKQFG-AP------LAALQINQEK 355
Cdd:PLN02312 315 gkyvSAIKDPDQrfgaflapltsgrvTIAVSAIYSS--KVGLAIAI-----RYSLSRRAFSvTPngpevlLLDYPSHQRR 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 356 LVRMLGNIQAMFLLGWKLCKMY-----ESGKMTPGQASLCKA---WNTLRareTVALGRELLGGNGILSDFLVA--KAFC 425
Cdd:PLN02312 388 LLPLLAKTYAMSFAANDLKMIYvkrtpESNKAIHVVSSGFKAvltWHNMR---TLQECREACGGQGLKTENRVGqlKAEY 464
|
330
....*....|....*..
gi 1373925884 426 DIEPiyTYEGtyDINTL 442
Cdd:PLN02312 465 DVQS--TFEG--DNNVL 477
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
160-446 |
1.66e-07 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 53.70 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 160 TFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAV--KVEGGWLLN-----GQKRWI 232
Cdd:PTZ00460 93 FISTVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATydKQTNEFVIHtpsveAVKFWP 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 233 GNATF-ADIVVVFAR---NTQTNQINGFIVK-------KGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLT--- 298
Cdd:PTZ00460 173 GELGFlCNFALVYAKlivNGKNKGVHPFMVRirdkethKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLAryi 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 299 -----GINSFQDTNKV----LAVSRIMVAWLPIGVCMGVYDICYRYLQERKQF----GAPLAAL--QINQEKLVRMLGNI 363
Cdd:PTZ00460 253 kvsedGQVERQGNPKVsyasMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQFtndnKQENSVLeyQTQQQKLLPLLAEF 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 364 QAMFLLGWKLCKMYES----------GKMTPGQASLC--KAWNTLRARETVALGRELLGGNGILSDFLVAKAFCDIEPIY 431
Cdd:PTZ00460 333 YACIFGGLKIKELVDDnfnrvqkndfSLLQLTHAILSaaKANYTYFVSNCAEWCRLSCGGHGYAHYSGLPAIYFDMSPNI 412
|
330
....*....|....*
gi 1373925884 432 TYEGTYDINTLVTGR 446
Cdd:PTZ00460 413 TLEGENQIMYLQLAR 427
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
121-340 |
1.37e-06 |
|
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: 50.40 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 121 LASLKIAG-GTI---KGYGCPGLSILSHALVGAEIARVDASCC-----TFALVHSSLcmstigMLGNEEQKQKYLPSLAR 191
Cdd:cd01163 28 VALLRQSGlGTLrvpKEYGGLGASLPDLYEVVRELAAADSNIAqalraHFGFVEALL------LAGPEQFRKRWFGRVLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 192 FDTIGCwALTEPAyGSDASSLNTTAVKVEGGWLLNGQKRWIGNATFADIVVVFARNTQTNQInGFIVKKGTPGYRATKIE 271
Cdd:cd01163 102 GWIFGN-AVSERG-SVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGKLV-FAAVPTDRPGITVVDDW 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1373925884 272 NKIGLRIVQNGDIIMKDVFIPDEDRLTGINSFQDTNKVLAVSRIMVAWLPIGVCMGVYDICYRYLQERK 340
Cdd:cd01163 179 DGFGQRLTASGTVTFDNVRVEPDEVLPRPNAPDRGTLLTAIYQLVLAAVLAGIARAALDDAVAYVRSRT 247
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
117-266 |
1.71e-06 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 50.26 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 117 IIPHLASLKIAggtiKGYGCPGLSILSHALVGAEIARVDASCCTFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIG 196
Cdd:PTZ00457 61 ILGNLYGARIA----TEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHSGFCTYLLSTVGSKELKGKYLTAMSDGTIMM 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 197 CWAlTEPAYGSDASSLNTTAV-KVEGGWLLNGQKRWIGNATFADIVVVFARNTQTNQING---------FIVKKGTPGYR 266
Cdd:PTZ00457 137 GWA-TEEGCGSDISMNTTKASlTDDGSYVLTGQKRCEFAASATHFLVLAKTLTQTAAEEGatevsrnsfFICAKDAKGVS 215
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
170-263 |
2.05e-06 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 50.25 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 170 MSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKV-EGGWLLNGQKRWI--GNATFAD--IVVVF 244
Cdd:PTZ00456 157 ANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSaDGSYKITGTKIFIsaGDHDLTEniVHIVL 236
|
90 100
....*....|....*....|...
gi 1373925884 245 AR--NTQ--TNQINGFIVKKGTP 263
Cdd:PTZ00456 237 ARlpNSLptTKGLSLFLVPRHVV 259
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
151-427 |
2.98e-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: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 151 IARVDASCCTFALVHSSLCMST--IGMLGNEEQkqkylpslARFdtigcWALTEPAYGSDASSLNTTAVKVEGGWLLNGQ 228
Cdd:cd01159 59 IATLAEACGSAAWVASIVATHSrmLAAFPPEAQ--------EEV-----WGDGPDTLLAGSYAPGGRAERVDGGYRVSGT 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 229 KRWIGNATFADIVVVfarntqtnqinGFIV--KKGTPGYRA-------TKIENK---IGLRIVQNGDIIMKDVFIPDEDR 296
Cdd:cd01159 126 WPFASGCDHADWILV-----------GAIVedDDGGPLPRAfvvpraeYEIVDTwhvVGLRGTGSNTVVVDDVFVPEHRT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925884 297 LTGINSFQDTNKVLAVSRIMVAWLP----------IGVCMGVYDICYRYLQERKQ---FGAPLAALQINQEKLVRMLGNI 363
Cdd:cd01159 195 LTAGDMMAGDGPGGSTPVYRMPLRQvfplsfaavsLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAEL 274
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1373925884 364 QAM--FLLG-----WKLCKmyESGKMTPGQASLCKAWNTLRARETVALGR---ELLGGNGILSDFLVAKAFCDI 427
Cdd:cd01159 275 DAAraFLERatrdlWAHAL--AGGPIDVEERARIRRDAAYAAKLSAEAVDrlfHAAGGSALYTASPLQRIWRDI 346
|
|
| |
