|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
101-509 |
0e+00 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 839.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 101 DIASAFPQATPASTFPTSVSDYFGLEDLLSPEDVALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIIPHLASLKIAGGTIK 180
Cdd:PLN02526 1 DVSVAFPQATPASIFPPSVSDYYQFDDLLTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 181 GYGCPGLSILSHALVGAEIARVDASCCTFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSL 260
Cdd:PLN02526 81 GYGCPGLSITASAIATAEVARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 261 NTTAVKVEGGWLLNGQKRWIGNATFADIVVVFARNTQTNQINGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIP 340
Cdd:PLN02526 161 NTTATKVEGGWILNGQKRWIGNSTFADVLVIFARNTTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 341 DEDRLTGINSFQDTNKVLAVSRIMVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWK 420
Cdd:PLN02526 241 DEDRLPGVNSFQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 421 LCKMYESGKMTPGQASLCKAWNTLRARETVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGREITGIA 500
Cdd:PLN02526 321 LCKLYESGKMTPGHASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREITGIA 400
|
....*....
gi 1373925878 501 SIKPSASGK 509
Cdd:PLN02526 401 SFKPAASTR 409
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
120-502 |
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 1373925878 120 SDYFGLEDLLSPEDVALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIIPHLASLKIAGGTIKGYGCPGLSILSHALVGAEI 199
Cdd:cd01151 4 EDPLNLDDLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIKGYGCAGLSSVAYGLIAREV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 200 ARVDASCCTFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRW 279
Cdd:cd01151 84 ERVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 280 IGNATFADIVVVFARNTQTNQINGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLTGINSFQDTNKVLA 359
Cdd:cd01151 164 ITNSPIADVFVVWARNDETGKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAEGLRGPFKCLN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 360 VSRIMVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQASLCK 439
Cdd:cd01151 244 NARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLK 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1373925878 440 AWNTLRARETVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGREITGIASI 502
Cdd:cd01151 324 RNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAITGIQAF 386
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
129-498 |
1.33e-113 |
|
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: 1.33e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 129 LSPEDVALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIIPHLASLKIAGGTI-KGYGCPGLSILSHALVGAEIARVDASCC 207
Cdd:COG1960 5 LTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIpEEYGGLGLSLVELALVLEELARADASLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 208 TFALVHSSlCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNATFAD 287
Cdd:COG1960 85 LPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVAD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 288 IVVVFAR---NTQTNQINGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLTGIN-SFQDTNKVLAVSRI 363
Cdd:COG1960 164 VILVLARtdpAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGkGFKIAMSTLNAGRL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 364 MVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQASLCKAWNT 443
Cdd:COG1960 244 GLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLFAT 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1373925878 444 LRARETVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGREITG 498
Cdd:COG1960 324 EAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLG 378
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
131-496 |
2.20e-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: 257.97 E-value: 2.20e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 131 PEDVALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIIPHLASLKIAGGTI-KGYGCPGLSILSHALVGAEIARVDASCCTF 209
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIpEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 210 ALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNATFADIV 289
Cdd:cd01158 81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 290 VVFAR---NTQTNQINGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLTGIN-SFQDTNKVLAVSRIMV 365
Cdd:cd01158 161 IVFAVtdpSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGeGFKIAMQTLDGGRIGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 366 AWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQASLCKAWNTLR 445
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1373925878 446 ARETVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGREI 496
Cdd:cd01158 321 AMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHL 371
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
135-494 |
3.36e-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: 235.26 E-value: 3.36e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 135 ALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIiphLASLKIAGGtikgygcpglsilshalvgaeiarvdascctfalvhs 214
Cdd:cd00567 5 ELRDSAREFAAEELEPYARERRETPEEPWEL---LAELGLLLG------------------------------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 215 slcMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNATFADIVVVFAR 294
Cdd:cd00567 45 ---AALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLAR 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 295 ----NTQTNQINGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLTGINS-FQDTNKVLAVSRIMVAWLP 369
Cdd:cd00567 122 tdeeGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGgFELAMKGLNVGRLLLAAVA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 370 IGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKM-TPGQASLCKAWNTLRARE 448
Cdd:cd00567 202 LGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDeARLEAAMAKLFATEAARE 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1373925878 449 TVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGR 494
Cdd:cd00567 282 VADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
129-496 |
2.22e-62 |
|
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: 2.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 129 LSPEDVALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIIPHLASLKIAGGTI-KGYGCPGLSILSHALVGAEIARVDASCC 207
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITApEEYGGSGMGYLAHVIIMEEISRASGSVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 208 TFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNATFAD 287
Cdd:cd01156 82 LSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDAD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 288 IVVVFAR---NTQTNQINGFIVKKGTPGY-RATKIEnKIGLRIVQNGDIIMKDVFIPDEDRLTGINSfqdTNKVLA---- 359
Cdd:cd01156 162 TLVVYAKtdpSAGAHGITAFIVEKGMPGFsRAQKLD-KLGMRGSNTCELVFEDCEVPEENILGGENK---GVYVLMsgld 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 360 VSRIMVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQASLCK 439
Cdd:cd01156 238 YERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVI 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1373925878 440 AWNTLRArETVAL-GRELLGGNGILSDFLVAKAFCDIEpiyTYE---GTYDINTLVTGREI 496
Cdd:cd01156 318 LYAAEKA-TQVALdAIQILGGNGYINDYPTGRLLRDAK---LYEigaGTSEIRRMVIGREL 374
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
131-496 |
2.35e-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: 190.02 E-value: 2.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 131 PEDVALRKRVRRVMEEHVAPVVTKyWEKA-EFPFEIIPHLASLKIAG-GTIKGYGCPGLSILSHALVGAEIARVDASCCT 208
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHE-WEKAgEVPREVWRKAGEQGLLGvGFPEEYGGIGGDLLSAAVLWEELARAGGSGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 209 FaLVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNATFADI 288
Cdd:cd01160 80 L-SLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 289 VVVFARNTQTNQ----INGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLTGIN-SFQDTNKVLAVSRI 363
Cdd:cd01160 159 VIVVARTGGEARgaggISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENkGFYYLMQNLPQERL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 364 MVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQASLCKAWNT 443
Cdd:cd01160 239 LIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWAT 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1373925878 444 LRARETVALGRELLGGNGILSDFLVAKAFCD--IEPIYTyeGTYDINTLVTGREI 496
Cdd:cd01160 319 ELQNRVAYECVQLHGGWGYMREYPIARAYRDarVQPIYG--GTTEIMKELISRQM 371
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
129-498 |
6.59e-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: 172.63 E-value: 6.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 129 LSPEDVALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIIPHLASLKIAGGTIKG-YGCPGLSILSHALVGAEIARVDASCC 207
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDdVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 208 TFALVHSsLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNATFAD 287
Cdd:cd01162 81 AYISIHN-MCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 288 IVVVFARNTQTNQ--INGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLTGINS-FQDTNKVLAVSRIM 364
Cdd:cd01162 160 VYVVMARTGGEGPkgISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQgFGIAMAGLNGGRLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 365 VAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGkmTPGQASLC---KAW 441
Cdd:cd01162 240 IASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRG--DPDAVKLCamaKRF 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1373925878 442 NTLRARETVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGREITG 498
Cdd:cd01162 318 ATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLT 374
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
137-496 |
1.05e-44 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 162.35 E-value: 1.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 137 RKRVRRVMEEHVAPVVTKYWEKAEFPFEI--IPHLASLKIAGGTI-KGYGCPGLSILSHALVGAEIARVDASCCTFALVH 213
Cdd:PLN02519 34 KESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGITApEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAH 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 214 SSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNATFADIVVVFA 293
Cdd:PLN02519 114 SNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 294 RNTQT---NQINGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLTginsfQDTNKV------LAVSRIM 364
Cdd:PLN02519 194 KTDVAagsKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLG-----QEGKGVyvmmsgLDLERLV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 365 VAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQAS---LCKAW 441
Cdd:PLN02519 269 LAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAgviLCAAE 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1373925878 442 NTLRaretVAL-GRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGREI 496
Cdd:PLN02519 349 RATQ----VALqAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGREL 400
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
129-498 |
9.03e-43 |
|
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which catalyze the alpha,beta dehydrogenation of the corresponding medium chain acyl-CoA by FAD, which becomes reduced. The reduced form of MCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. MCAD is a homotetramer.
Pssm-ID: 173846 [Multi-domain] Cd Length: 378 Bit Score: 156.21 E-value: 9.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 129 LSPEDVALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIIPHLASLKIAGGTI-KGYGCPGLSILSHALVGAEIARvdasCC 207
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIpEDCGGLGLGTFDTCLITEELAY----GC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 208 T---FALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNAT 284
Cdd:cd01157 77 TgvqTAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 285 FADIVVVFARNT------QTNQINGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLTGINS-FQDTNKV 357
Cdd:cd01157 157 KANWYFLLARSDpdpkcpASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAgFKIAMGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 358 LAVSRIMVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQASL 437
Cdd:cd01157 237 FDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASI 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1373925878 438 CKAWNTLRARETVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGREITG 498
Cdd:cd01157 317 AKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLG 377
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
108-490 |
1.26e-42 |
|
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: 1.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 108 QATPASTFPtsvsDYFGLEDLLSPEDVALRKRVRRVMEEHVAPVVTKYWEKaeFPFEIIPHLASLKIAGGTI-KGYGCPG 186
Cdd:cd01161 10 DIVTKQVFP----YPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEK--IPRKTLTQLKELGLFGLQVpEEYGGLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 187 LSILSHALVgAEIARVDASCCTFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVK 266
Cdd:cd01161 84 LNNTQYARL-AEIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 267 VEGG--WLLNGQKRWIGNATFADIVVVFARNTQTN-------QINGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDV 337
Cdd:cd01161 163 SEDGkhYVLNGSKIWITNGGIADIFTVFAKTEVKDatgsvkdKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 338 FIPDEDRLTGI-NSFQDTNKVLAVSRIMVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFL 416
Cdd:cd01161 243 KIPVENVLGEVgDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATES 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1373925878 417 LGWKLCKMYESGKMTPGQ--ASLCKAWNTLRARETVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTL 490
Cdd:cd01161 323 MAYMTSGNMDRGLKAEYQieAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRL 398
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
130-239 |
1.50e-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: 125.65 E-value: 1.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 130 SPEDVALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIIPHLASLKIAGGTI-KGYGCPGLSILSHALVGAEIARVDASCCT 208
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIpEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|.
gi 1373925878 209 FALVHSSLCMSTIGMLGNEEQKQKYLPSLAR 239
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLAS 111
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
109-394 |
9.51e-32 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 126.59 E-value: 9.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 109 ATPASTFPTSVSDYFGLEDLlSPEDVALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIIPHLASLKIAGGTI-KGYGCPGL 187
Cdd:PTZ00461 18 WTAAATMTSASRAFMDLYNP-TPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVpEADGGAGM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 188 SILSHALVGAEIARVDASCCTFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKV 267
Cdd:PTZ00461 97 DAVAAVIIHHELSKYDPGFCLAYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 268 -EGGWLLNGQKRWIGNATFADIVVVFARntQTNQINGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLT 346
Cdd:PTZ00461 177 sNGNYVLNGSKIWITNGTVADVFLIYAK--VDGKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLG 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1373925878 347 GI-NSFQDTNKVLAVSRIMVAWLPIGVCMGVYDICYRYLQERKQFGAPL 394
Cdd:PTZ00461 255 EEgKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPI 303
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
129-496 |
2.85e-31 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 124.46 E-value: 2.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 129 LSPEDVALRKRVRRVMEEHVAPVVTKYW-EKAEFPFEIIPHLASLKIAG-GTIKGYGCPGLSILSHALVGAEIARvdaSC 206
Cdd:PRK12341 5 LTEEQELLLASIRELITRNFPEEYFRTCdENGTYPREFMRALADNGISMlGVPEEFGGTPADYVTQMLVLEEVSK---CG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 207 CTFALVHSSLCMSTIGMLGNEEQKQKYLPS-LARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNATF 285
Cdd:PRK12341 82 APAFLITNGQCIHSMRRFGSAEQLRKTAEStLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAKE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 286 ADIVVVFARNTQ----TNQINGFIVKKGTPGYRATKIEnKIGLRIVQNGDIIMKDVFIPDEDrLTGI--NSFQDTNKVLA 359
Cdd:PRK12341 162 YPYMLVLARDPQpkdpKKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESD-LVGEegMGFLNVMYNFE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 360 VSRIMVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQASLCK 439
Cdd:PRK12341 240 MERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAALAK 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1373925878 440 AWNTLRARETVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGREI 496
Cdd:PRK12341 320 LYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQI 376
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
157-496 |
9.50e-30 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 120.32 E-value: 9.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 157 EKAEFPFEIIPHLASLKIAGGTI-KGYGCPGLSILSHALVGAEIARVDASccTFALVHSSLCMSTIGMLGNEEQKQKYLP 235
Cdd:PRK03354 34 RDSVYPERFVKALADMGIDSLLIpEEHGGLDAGFVTLAAVWMELGRLGAP--TYVLYQLPGGFNTFLREGTQEQIDKIMA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 236 SLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNATFADIVVVFARNTQTNQINGF---IVKKGTPG 312
Cdd:PRK03354 112 FRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASPDKPVYtewFVDMSKPG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 313 YRATKIEnKIGLRIVQNGDIIMKDVFIPDEDrLTGI--NSFQDTNKVLAVSRIMVAWLPIGVCMGVYDICYRYLQERKQF 390
Cdd:PRK03354 192 IKVTKLE-KLGLRMDSCCEITFDDVELDEKD-MFGRegNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQF 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 391 GAPLAALQINQEKLVRM---LGNIQAMFL-LGWKlckmYESGKMTPGQASLCKAWNTLRARETVALGRELLGGNGILSDF 466
Cdd:PRK03354 270 GEAIGRFQLIQEKFAHMaikLNSMKNMLYeAAWK----ADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNH 345
|
330 340 350
....*....|....*....|....*....|
gi 1373925878 467 LVAKAFCDIEPIYTYEGTYDINTLVTGREI 496
Cdd:PRK03354 346 RISRFWRDLRVDRVSGGSDEMQILTLGRAV 375
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
131-487 |
1.44e-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: 113.98 E-value: 1.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 131 PEDVALRKRVRRVMEEHVAPVVTKywEKAEFPFEI----IPHLASLKIAG----GTIKGYGCPGLSILSHALVGAEIARV 202
Cdd:cd01152 1 PSEEAFRAEVRAWLAAHLPPELRE--ESALGYREGredrRRWQRALAAAGwaapGWPKEYGGRGASLMEQLIFREEMAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 203 DASCcTFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGN 282
Cdd:cd01152 79 GAPV-PFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 283 ATFADIVVVFAR-NTQTNQING---FIVKKGTPGYRATKIENKIGlRIVQNgDIIMKDVFIPDEDRLTGINS-FQDTNKV 357
Cdd:cd01152 158 AHYADWAWLLVRtDPEAPKHRGisiLLVDMDSPGVTVRPIRSING-GEFFN-EVFLDDVRVPDANRVGEVNDgWKVAMTT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 358 LAVSRimvawlpigVCMGVYDICY-----RYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTP 432
Cdd:cd01152 236 LNFER---------VSIGGSAATFfelllARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPG 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1373925878 433 GQASLCKAWNTLRARETVALGRELLGGNGILSD----------FLVAKAFCDIEPIYTyeGTYDI 487
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 ... |
358-496 |
2.29e-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: 104.64 E-value: 2.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 358 LAVSRIMVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQASL 437
Cdd:pfam00441 11 LNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAGGPDGAEASM 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1373925878 438 CKAWNTLRARETVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGREI 496
Cdd:pfam00441 91 AKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
245-335 |
2.69e-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: 91.19 E-value: 2.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 245 CWALTEPAYGSDASSLNTTAVKVEGG-WLLNGQKRWIGNATFADIVVVFARNTQT---NQINGFIVKKGTPGYRATKIEN 320
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGGgWVLNGTKWWITNAGIADLFLVLARTGGDdrhGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 1373925878 321 KIGLRIVQNGDIIMK 335
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
135-490 |
1.88e-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: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 135 ALRKRVRRVMEEHVAPVVtkyWEKAEFPfEIIPHLASLKIAGGTIKGYGCPgLSIlshalvgaeiarvdasccTFALVHs 214
Cdd:cd01154 66 AWHALMRRLIEEGVINIE---DGPAGEG-RRHVHFAAGYLLSDAAAGLLCP-LTM------------------TDAAVY- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 215 slcmsTIGMLGNEEQKQKYLPSLARFD----TIGCWaLTEPAYGSDASSLNTTAVKVEGG-WLLNGQKrWIGNATFADIV 289
Cdd:cd01154 122 -----ALRKYGPEELKQYLPGLLSDRYktglLGGTW-MTEKQGGSDLGANETTAERSGGGvYRLNGHK-WFASAPLADAA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 290 VVFAR----NTQTNQINGFIVKKGTP-----GYRATKIENKIGLRIVQNGDIIMKDV---FIPDEDRltGINSfqdTNKV 357
Cdd:cd01154 195 LVLARpegaPAGARGLSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDAeayLIGDEGK--GIYY---ILEM 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 358 LAVSRIMVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYE-SGKMTPGQA- 435
Cdd:cd01154 270 LNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDrAAADKPVEAh 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1373925878 436 ------SLCKAWNTLRARETVALGRELLGGNGILSDFLVAKAFCD--IEPIytYEGTYDINTL 490
Cdd:cd01154 350 marlatPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREaqVTPI--WEGTGNIQAL 410
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
173-497 |
2.12e-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: 90.14 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 173 KIAGGTIKGYGCP----GLSiLSHALVGAeIARVDASCCTFALVHSSL--CMSTIGMLGNEEQKQKYLPSLARFDTIGCW 246
Cdd:cd01153 44 AFAEAGWMALGVPeeygGQG-LPITVYSA-LAEIFSRGDAPLMYASGTqgAAATLLAHGTEAQREKWIPRLAEGEWTGTM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 247 ALTEPAYGSDASSLNTTAVKVEGG-WLLNGQKRWIGN---ATFADIV-VVFAR----NTQTNQINGFIVKK----GTP-G 312
Cdd:cd01153 122 CLTEPDAGSDLGALRTKAVYQADGsWRINGVKRFISAgehDMSENIVhLVLARsegaPPGVKGLSLFLVPKflddGERnG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 313 YRATKIENKIGLRIVQNGDIIMKD---VFIPDEDRltGInsfQDTNKVLAVSRIMVAWLPIGVCMGVYDICYRYLQERKQ 389
Cdd:cd01153 202 VTVARIEEKMGLHGSPTCELVFDNakgELIGEEGM--GL---AQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 390 FGAPLAA---LQINQEKLVRMLGNIQAMFLLGWKLCKMY-------ESGKMTPGQAS------------LCKAWNTLRAR 447
Cdd:cd01153 277 GGDLIKAapaVTIIHHPDVRRSLMTQKAYAEGSRALDLYtatvqdlAERKATEGEDRkalsaladlltpVVKGFGSEAAL 356
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1373925878 448 ETVALGRELLGGNGILSDFLVAKAFCD--IEPIytYEGTYDINTL-VTGREIT 497
Cdd:cd01153 357 EAVSDAIQVHGGSGYTREYPIEQYYRDarITTI--YEGTTGIQALdLIGRKIV 407
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
201-483 |
1.04e-18 |
|
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: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 201 RVDASCCTFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAV--KVEGGWLLN---- 274
Cdd:cd01150 93 GYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATydPLTQEFVINtpdf 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 275 -GQKRWIGN-ATFADIVVVFAR---NTQTNQINGFIVK-------KGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDE 342
Cdd:cd01150 173 tATKWWPGNlGKTATHAVVFAQlitPGKNHGLHAFIVPirdpkthQPLPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRE 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 343 DRL----------TGINSFQDTNKVLAVSRIMVAWLPIGVCMGVYD-------ICYRYLQERKQFG-------APLAALQ 398
Cdd:cd01150 253 NLLnrfgdvspdgTYVSPFKDPNKRYGAMLGTRSGGRVGLIYDAAMslkkaatIAIRYSAVRRQFGpkpsdpeVQILDYQ 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 399 INQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQ-------------ASLcKAWNTLRARETVALGRELLGGNGILSD 465
Cdd:cd01150 333 LQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKELLQgnsellaelhalsAGL-KAVATWTAAQGIQECREACGGHGYLAM 411
|
330
....*....|....*...
gi 1373925878 466 FLVAKAFCDIEPIYTYEG 483
Cdd:cd01150 412 NRLPTLRDDNDPFCTYEG 429
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
212-461 |
4.02e-13 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 71.81 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 212 VHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAV--KVEGGWLLN-----GQKRWIGNAT 284
Cdd:PLN02636 143 VQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATfdPLTDEFVINtpndgAIKWWIGNAA 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 285 F-ADIVVVFAR---------NTQTNQINGFIV-------KKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLtg 347
Cdd:PLN02636 223 VhGKFATVFARlklpthdskGVSDMGVHAFIVpirdmktHQVLPGVEIRDCGHKVGLNGVDNGALRFRSVRIPRDNLL-- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 348 iNSFQDT-------------NKVLAVS-------RIMVAWLPIGVCMGVYDICYRYLQERKQFGAP------LAALQINQ 401
Cdd:PLN02636 301 -NRFGDVsrdgkytsslptiNKRFAATlgelvggRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPkqpeisILDYQSQQ 379
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 402 EKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQ----------ASLcKAWNTLRARETVALGRELLGGNG 461
Cdd:PLN02636 380 HKLMPMLASTYAFHFATEYLVERYSEMKKTHDDqlvadvhalsAGL-KAYITSYTAKALSTCREACGGHG 448
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
165-462 |
4.53e-13 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 71.77 E-value: 4.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 165 IIPhlaslkiaggtiKGYGCPGLSILSHALVGAEIARVdascctfalvhSSLCMSTIG---------ML---GNEEQKQK 232
Cdd:PRK09463 127 IIP------------KEYGGLEFSAYAHSRVLQKLASR-----------SGTLAVTVMvpnslgpgeLLlhyGTDEQKDH 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 233 YLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGW--------LLNGQKRWIgnaTFADIVVVFARNTQTNQINGF 304
Cdd:PRK09463 184 YLPRLARGEEIPCFALTSPEAGSDAGSIPDTGVVCKGEWqgeevlgmRLTWNKRYI---TLAPIATVLGLAFKLYDPDGL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 305 I------------VKKGTPGYratkienKIGLR------IVQNGDIIMKDVFIPdedrLTGINSFQDT--------NKVL 358
Cdd:PRK09463 261 LgdkedlgitcalIPTDTPGV-------EIGRRhfplnvPFQNGPTRGKDVFIP----LDYIIGGPKMagqgwrmlMECL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 359 AVSR-IMvawLPiGVCMGVYDICYR----YLQERKQFGAPLAALQINQEKLVRMLGN---IQAMFLLGwklCKMYESGKm 430
Cdd:PRK09463 330 SVGRgIS---LP-SNSTGGAKLAALatgaYARIRRQFKLPIGKFEGIEEPLARIAGNaylMDAARTLT---TAAVDLGE- 401
|
330 340 350
....*....|....*....|....*....|...
gi 1373925878 431 TPGQAS-LCKAWNTLRARETVALGRELLGGNGI 462
Cdd:PRK09463 402 KPSVLSaIAKYHLTERGRQVINDAMDIHGGKGI 434
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
147-462 |
1.88e-12 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 69.99 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 147 HVAPVVTKYWEKAEFPFEIIPhlaslkiaggtiKGYGCPGLSILSHALVGAEIARVDASCCTFALVHSSLcmsTIGML-- 224
Cdd:PRK13026 108 DLPPEVWDYLKKEGFFALIIP------------KEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPNSL---GPGELlt 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 225 --GNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAV----KVEG----GWLLNGQKRWIgnaTFADIVVVFAR 294
Cdd:PRK13026 173 hyGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTGIvcrgEFEGeevlGLRLTWDKRYI---TLAPVATVLGL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 295 NTQTNQINGFIVKKGTPGYRATKIEN-----KIGLR------IVQNGDIIMKDVFIPdEDRLTG-----INSFQDTNKVL 358
Cdd:PRK13026 250 AFKLRDPDGLLGDKKELGITCALIPTdhpgvEIGRRhnplgmAFMNGTTRGKDVFIP-LDWIIGgpdyaGRGWRMLVECL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 359 AVSRIMVawLP-IGVCMGVydICYR----YLQERKQFGAPLAALQINQEKLVRMLGN---IQAMFLLgwkLCKMYESGKm 430
Cdd:PRK13026 329 SAGRGIS--LPaLGTASGH--MATRttgaYAYVRRQFGMPIGQFEGVQEALARIAGNtylLEAARRL---TTTGLDLGV- 400
|
330 340 350
....*....|....*....|....*....|...
gi 1373925878 431 TPGQAS-LCKAWNTLRARETVALGRELLGGNGI 462
Cdd:PRK13026 401 KPSVVTaIAKYHMTELARDVVNDAMDIHAGKGI 433
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
135-402 |
1.25e-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: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 135 ALRKRVRRVMEEHVAP---VVTKYWEKAEFPFEIIPH-LASLKIAGGTI--------KGYGCPGLSILSHALVGAEIARv 202
Cdd:cd01155 5 ELRARVKAFMEEHVYPaeqEFLEYYAEGGDRWWTPPPiIEKLKAKAKAEglwnlflpEVSGLSGLTNLEYAYLAEETGR- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 203 dascCTFAlVHSSLC-------MSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYG-SDASSLNTTAVKVEGGWLLN 274
Cdd:cd01155 84 ----SFFA-PEVFNCqapdtgnMEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDVAsSDATNIECSIERDGDDYVIN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 275 GQKRWIGNATFAD--IVVVFAR-----NTQTNQINGFIVKKGTPGY---RATKI----ENKIGlrivqNGDIIMKDVFIP 340
Cdd:cd01155 159 GRKWWSSGAGDPRckIAIVMGRtdpdgAPRHRQQSMILVPMDTPGVtiiRPLSVfgydDAPHG-----HAEITFDNVRVP 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1373925878 341 DEDRLTGINS-FQDTNKVLAVSRIMVAWLPIGVC-MGVYDICYRYLQeRKQFGAPLAALQINQE 402
Cdd:cd01155 234 ASNLILGEGRgFEIAQGRLGPGRIHHCMRLIGAAeRALELMCQRAVS-REAFGKKLAQHGVVAH 296
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
208-483 |
3.79e-09 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 59.08 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 208 TFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAV-------KVEGGWLLNGQKRWI 280
Cdd:PLN02443 97 GYTDLHWGMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATfdpktdeFVIHSPTLTSSKWWP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 281 GN----ATFAdivVVFAR---NTQTNQINGFIVK-------KGTPGYRATKIENKIG---LRIVQNGDIIMKDVFIPDED 343
Cdd:PLN02443 177 GGlgkvSTHA---VVYARlitNGKDHGIHGFIVQlrslddhSPLPGVTVGDIGMKFGngaYNTMDNGFLRFDHVRIPRDQ 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 344 RLTGINSFQDTNKVLA--------------VSRIMVA----WLPIGVCMGVydicyRYLQERKQFGA---PLAALQIN-- 400
Cdd:PLN02443 254 MLMRLSKVTREGKYVQsdvprqlvygtmvyVRQTIVAdastALSRAVCIAT-----RYSAVRRQFGSqdgGPETQVIDyk 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 401 --QEKLVRMLGNIQAMFLLGWKLCKMY--------ESGKMTPGQASLC----KAWNTLRARETVALGRELLGGNGILSDF 466
Cdd:PLN02443 329 tqQSRLFPLLASAYAFRFVGEWLKWLYtdvtqrleANDFSTLPEAHACtaglKSLTTSATADGIEECRKLCGGHGYLCSS 408
|
330
....*....|....*..
gi 1373925878 467 LVAKAFCDIEPIYTYEG 483
Cdd:PLN02443 409 GLPELFAVYVPACTYEG 425
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
212-490 |
8.23e-09 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 58.25 E-value: 8.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 212 VHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAV--KVEGGWLLN-----GQKRWIGNAT 284
Cdd:PLN02312 155 VHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTydPKTEEFVINtpcesAQKYWIGGAA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 285 -FADIVVVFAR---NTQTNQINGFIVK----KGT--PGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLTGI------ 348
Cdd:PLN02312 235 nHATHTIVFSQlhiNGKNEGVHAFIAQirdqDGNicPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNSVadvspd 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 349 ----NSFQDTNK--------------VLAVSRIMVAwlPIGVCMGVydicyRYLQERKQFG-AP------LAALQINQEK 403
Cdd:PLN02312 315 gkyvSAIKDPDQrfgaflapltsgrvTIAVSAIYSS--KVGLAIAI-----RYSLSRRAFSvTPngpevlLLDYPSHQRR 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 404 LVRMLGNIQAMFLLGWKLCKMY-----ESGKMTPGQASLCKA---WNTLRareTVALGRELLGGNGILSDFLVA--KAFC 473
Cdd:PLN02312 388 LLPLLAKTYAMSFAANDLKMIYvkrtpESNKAIHVVSSGFKAvltWHNMR---TLQECREACGGQGLKTENRVGqlKAEY 464
|
330
....*....|....*..
gi 1373925878 474 DIEPiyTYEGtyDINTL 490
Cdd:PLN02312 465 DVQS--TFEG--DNNVL 477
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
208-494 |
1.97e-07 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 53.70 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 208 TFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAV--KVEGGWLLN-----GQKRWI 280
Cdd:PTZ00460 93 FISTVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATydKQTNEFVIHtpsveAVKFWP 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 281 GNATF-ADIVVVFAR---NTQTNQINGFIVK-------KGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLT--- 346
Cdd:PTZ00460 173 GELGFlCNFALVYAKlivNGKNKGVHPFMVRirdkethKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLAryi 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 347 -----GINSFQDTNKV----LAVSRIMVAWLPIGVCMGVYDICYRYLQERKQF----GAPLAAL--QINQEKLVRMLGNI 411
Cdd:PTZ00460 253 kvsedGQVERQGNPKVsyasMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQFtndnKQENSVLeyQTQQQKLLPLLAEF 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 412 QAMFLLGWKLCKMYES----------GKMTPGQASLC--KAWNTLRARETVALGRELLGGNGILSDFLVAKAFCDIEPIY 479
Cdd:PTZ00460 333 YACIFGGLKIKELVDDnfnrvqkndfSLLQLTHAILSaaKANYTYFVSNCAEWCRLSCGGHGYAHYSGLPAIYFDMSPNI 412
|
330
....*....|....*
gi 1373925878 480 TYEGTYDINTLVTGR 494
Cdd:PTZ00460 413 TLEGENQIMYLQLAR 427
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
169-388 |
1.60e-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: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 169 LASLKIAG-GTI---KGYGCPGLSILSHALVGAEIARVDASCC-----TFALVHSSLcmstigMLGNEEQKQKYLPSLAR 239
Cdd:cd01163 28 VALLRQSGlGTLrvpKEYGGLGASLPDLYEVVRELAAADSNIAqalraHFGFVEALL------LAGPEQFRKRWFGRVLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 240 FDTIGCwALTEPAyGSDASSLNTTAVKVEGGWLLNGQKRWIGNATFADIVVVFARNTQTNQInGFIVKKGTPGYRATKIE 319
Cdd:cd01163 102 GWIFGN-AVSERG-SVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGKLV-FAAVPTDRPGITVVDDW 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1373925878 320 NKIGLRIVQNGDIIMKDVFIPDEDRLTGINSFQDTNKVLAVSRIMVAWLPIGVCMGVYDICYRYLQERK 388
Cdd:cd01163 179 DGFGQRLTASGTVTFDNVRVEPDEVLPRPNAPDRGTLLTAIYQLVLAAVLAGIARAALDDAVAYVRSRT 247
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
165-314 |
1.68e-06 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 50.65 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 165 IIPHLASLKIAggtiKGYGCPGLSILSHALVGAEIARVDASCCTFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIG 244
Cdd:PTZ00457 61 ILGNLYGARIA----TEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHSGFCTYLLSTVGSKELKGKYLTAMSDGTIMM 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 245 CWAlTEPAYGSDASSLNTTAV-KVEGGWLLNGQKRWIgNATFADIVVVFARN-TQTNQING---------FIVKKGTPGY 313
Cdd:PTZ00457 137 GWA-TEEGCGSDISMNTTKASlTDDGSYVLTGQKRCE-FAASATHFLVLAKTlTQTAAEEGatevsrnsfFICAKDAKGV 214
|
.
gi 1373925878 314 R 314
Cdd:PTZ00457 215 S 215
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
218-311 |
1.97e-06 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 50.64 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 218 MSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKV-EGGWLLNGQKRWI--GNATFAD--IVVVF 292
Cdd:PTZ00456 157 ANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSaDGSYKITGTKIFIsaGDHDLTEniVHIVL 236
|
90 100
....*....|....*....|...
gi 1373925878 293 AR--NTQ--TNQINGFIVKKGTP 311
Cdd:PTZ00456 237 ARlpNSLptTKGLSLFLVPRHVV 259
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
197-475 |
2.34e-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: 46.57 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 197 AEIARVDAScctFALVHSSLCMST--IGMLGNEEQkqkylpslARFdtigcWALTEPAYGSDASSLNTTAVKVEGGWLLN 274
Cdd:cd01159 60 ATLAEACGS---AAWVASIVATHSrmLAAFPPEAQ--------EEV-----WGDGPDTLLAGSYAPGGRAERVDGGYRVS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 275 GQKRWIGNATFADIVVVfarntqtnqinGFIV--KKGTPGYRA-------TKIENK---IGLRIVQNGDIIMKDVFIPDE 342
Cdd:cd01159 124 GTWPFASGCDHADWILV-----------GAIVedDDGGPLPRAfvvpraeYEIVDTwhvVGLRGTGSNTVVVDDVFVPEH 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925878 343 DRLTGINSFQDTNKVLAVSRIMVAWLP----------IGVCMGVYDICYRYLQERKQ---FGAPLAALQINQEKLVRMLG 409
Cdd:cd01159 193 RTLTAGDMMAGDGPGGSTPVYRMPLRQvfplsfaavsLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAA 272
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1373925878 410 NIQAM--FLLG-----WKLCKmyESGKMTPGQASLCKAWNTLRARETVALGR---ELLGGNGILSDFLVAKAFCDI 475
Cdd:cd01159 273 ELDAAraFLERatrdlWAHAL--AGGPIDVEERARIRRDAAYAAKLSAEAVDrlfHAAGGSALYTASPLQRIWRDI 346
|
|
| |
