|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
90-498 |
0e+00 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 837.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 90 DIASAFPQATPASTFPTSVSDYFGLEDLLSPEDVALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIIPHLASLKIAGGTIK 169
Cdd:PLN02526 1 DVSVAFPQATPASIFPPSVSDYYQFDDLLTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 170 GYGCPGLSILSHALVGAEIARVDASCCTFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSL 249
Cdd:PLN02526 81 GYGCPGLSITASAIATAEVARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 250 NTTAVKVEGGWLLNGQKRWIGNATFADIVVVFARNTQTNQINGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIP 329
Cdd:PLN02526 161 NTTATKVEGGWILNGQKRWIGNSTFADVLVIFARNTTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 330 DEDRLTGINSFQDTNKVLAVSRIMVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWK 409
Cdd:PLN02526 241 DEDRLPGVNSFQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 410 LCKMYESGKMTPGQASLCKAWNTLRARETVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGREITGIA 489
Cdd:PLN02526 321 LCKLYESGKMTPGHASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREITGIA 400
|
....*....
gi 1373925882 490 SIKPSASGK 498
Cdd:PLN02526 401 SFKPAASTR 409
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
109-491 |
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 1373925882 109 SDYFGLEDLLSPEDVALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIIPHLASLKIAGGTIKGYGCPGLSILSHALVGAEI 188
Cdd:cd01151 4 EDPLNLDDLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIKGYGCAGLSSVAYGLIAREV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 189 ARVDASCCTFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRW 268
Cdd:cd01151 84 ERVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 269 IGNATFADIVVVFARNTQTNQINGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLTGINSFQDTNKVLA 348
Cdd:cd01151 164 ITNSPIADVFVVWARNDETGKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAEGLRGPFKCLN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 349 VSRIMVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQASLCK 428
Cdd:cd01151 244 NARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLK 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1373925882 429 AWNTLRARETVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGREITGIASI 491
Cdd:cd01151 324 RNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAITGIQAF 386
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
118-487 |
8.35e-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: 341.43 E-value: 8.35e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 118 LSPEDVALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIIPHLASLKIAGGTI-KGYGCPGLSILSHALVGAEIARVDASCC 196
Cdd:COG1960 5 LTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIpEEYGGLGLSLVELALVLEELARADASLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 197 TFALVHSSlCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNATFAD 276
Cdd:COG1960 85 LPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVAD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 277 IVVVFAR---NTQTNQINGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLTGIN-SFQDTNKVLAVSRI 352
Cdd:COG1960 164 VILVLARtdpAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGkGFKIAMSTLNAGRL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 353 MVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQASLCKAWNT 432
Cdd:COG1960 244 GLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLFAT 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1373925882 433 LRARETVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGREITG 487
Cdd:COG1960 324 EAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLG 378
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
120-485 |
2.47e-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: 257.58 E-value: 2.47e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 120 PEDVALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIIPHLASLKIAGGTI-KGYGCPGLSILSHALVGAEIARVDASCCTF 198
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIpEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 199 ALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNATFADIV 278
Cdd:cd01158 81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 279 VVFAR---NTQTNQINGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLTGIN-SFQDTNKVLAVSRIMV 354
Cdd:cd01158 161 IVFAVtdpSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGeGFKIAMQTLDGGRIGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 355 AWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQASLCKAWNTLR 434
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1373925882 435 ARETVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGREI 485
Cdd:cd01158 321 AMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHL 371
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
124-483 |
2.04e-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: 235.64 E-value: 2.04e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 124 ALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIiphLASLKIAGGtikgygcpglsilshalvgaeiarvdascctfalvhs 203
Cdd:cd00567 5 ELRDSAREFAAEELEPYARERRETPEEPWEL---LAELGLLLG------------------------------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 204 slcMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNATFADIVVVFAR 283
Cdd:cd00567 45 ---AALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLAR 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 284 ----NTQTNQINGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLTGINS-FQDTNKVLAVSRIMVAWLP 358
Cdd:cd00567 122 tdeeGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGgFELAMKGLNVGRLLLAAVA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 359 IGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKM-TPGQASLCKAWNTLRARE 437
Cdd:cd00567 202 LGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDeARLEAAMAKLFATEAARE 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1373925882 438 TVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGR 483
Cdd:cd00567 282 VADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
118-485 |
1.71e-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: 1.71e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 118 LSPEDVALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIIPHLASLKIAGGTI-KGYGCPGLSILSHALVGAEIARVDASCC 196
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITApEEYGGSGMGYLAHVIIMEEISRASGSVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 197 TFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNATFAD 276
Cdd:cd01156 82 LSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDAD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 277 IVVVFAR---NTQTNQINGFIVKKGTPGY-RATKIEnKIGLRIVQNGDIIMKDVFIPDEDRLTGINSfqdTNKVLA---- 348
Cdd:cd01156 162 TLVVYAKtdpSAGAHGITAFIVEKGMPGFsRAQKLD-KLGMRGSNTCELVFEDCEVPEENILGGENK---GVYVLMsgld 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 349 VSRIMVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQASLCK 428
Cdd:cd01156 238 YERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVI 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1373925882 429 AWNTLRArETVAL-GRELLGGNGILSDFLVAKAFCDIEpiyTYE---GTYDINTLVTGREI 485
Cdd:cd01156 318 LYAAEKA-TQVALdAIQILGGNGYINDYPTGRLLRDAK---LYEigaGTSEIRRMVIGREL 374
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
120-485 |
1.86e-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: 1.86e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 120 PEDVALRKRVRRVMEEHVAPVVTKyWEKA-EFPFEIIPHLASLKIAG-GTIKGYGCPGLSILSHALVGAEIARVDASCCT 197
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHE-WEKAgEVPREVWRKAGEQGLLGvGFPEEYGGIGGDLLSAAVLWEELARAGGSGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 198 FaLVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNATFADI 277
Cdd:cd01160 80 L-SLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 278 VVVFARNTQTNQ----INGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLTGIN-SFQDTNKVLAVSRI 352
Cdd:cd01160 159 VIVVARTGGEARgaggISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENkGFYYLMQNLPQERL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 353 MVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQASLCKAWNT 432
Cdd:cd01160 239 LIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWAT 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1373925882 433 LRARETVALGRELLGGNGILSDFLVAKAFCD--IEPIYTyeGTYDINTLVTGREI 485
Cdd:cd01160 319 ELQNRVAYECVQLHGGWGYMREYPIARAYRDarVQPIYG--GTTEIMKELISRQM 371
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
118-487 |
5.32e-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: 5.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 118 LSPEDVALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIIPHLASLKIAGGTIKG-YGCPGLSILSHALVGAEIARVDASCC 196
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDdVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 197 TFALVHSsLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNATFAD 276
Cdd:cd01162 81 AYISIHN-MCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 277 IVVVFARNTQTNQ--INGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLTGINS-FQDTNKVLAVSRIM 353
Cdd:cd01162 160 VYVVMARTGGEGPkgISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQgFGIAMAGLNGGRLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 354 VAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGkmTPGQASLC---KAW 430
Cdd:cd01162 240 IASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRG--DPDAVKLCamaKRF 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1373925882 431 NTLRARETVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGREITG 487
Cdd:cd01162 318 ATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLT 374
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
126-485 |
1.10e-44 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 161.97 E-value: 1.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 126 RKRVRRVMEEHVAPVVTKYWEKAEFPFEI--IPHLASLKIAGGTI-KGYGCPGLSILSHALVGAEIARVDASCCTFALVH 202
Cdd:PLN02519 34 KESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGITApEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAH 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 203 SSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNATFADIVVVFA 282
Cdd:PLN02519 114 SNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 283 RNTQT---NQINGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLTginsfQDTNKV------LAVSRIM 353
Cdd:PLN02519 194 KTDVAagsKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLG-----QEGKGVyvmmsgLDLERLV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 354 VAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQAS---LCKAW 430
Cdd:PLN02519 269 LAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAgviLCAAE 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1373925882 431 NTLRaretVAL-GRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGREI 485
Cdd:PLN02519 349 RATQ----VALqAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGREL 400
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
97-479 |
1.05e-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: 1.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 97 QATPASTFPtsvsDYFGLEDLLSPEDVALRKRVRRVMEEHVAPVVTKYWEKaeFPFEIIPHLASLKIAGGTI-KGYGCPG 175
Cdd:cd01161 10 DIVTKQVFP----YPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEK--IPRKTLTQLKELGLFGLQVpEEYGGLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 176 LSILSHALVgAEIARVDASCCTFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVK 255
Cdd:cd01161 84 LNNTQYARL-AEIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 256 VEGG--WLLNGQKRWIGNATFADIVVVFARNTQTN-------QINGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDV 326
Cdd:cd01161 163 SEDGkhYVLNGSKIWITNGGIADIFTVFAKTEVKDatgsvkdKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 327 FIPDEDRLTGI-NSFQDTNKVLAVSRIMVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFL 405
Cdd:cd01161 243 KIPVENVLGEVgDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATES 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1373925882 406 LGWKLCKMYESGKMTPGQ--ASLCKAWNTLRARETVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTL 479
Cdd:cd01161 323 MAYMTSGNMDRGLKAEYQieAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRL 398
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
118-487 |
1.26e-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: 155.82 E-value: 1.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 118 LSPEDVALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIIPHLASLKIAGGTI-KGYGCPGLSILSHALVGAEIARvdasCC 196
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIpEDCGGLGLGTFDTCLITEELAY----GC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 197 T---FALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNAT 273
Cdd:cd01157 77 TgvqTAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 274 FADIVVVFARNT------QTNQINGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLTGINS-FQDTNKV 346
Cdd:cd01157 157 KANWYFLLARSDpdpkcpASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAgFKIAMGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 347 LAVSRIMVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQASL 426
Cdd:cd01157 237 FDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASI 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1373925882 427 CKAWNTLRARETVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGREITG 487
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 ... |
119-228 |
1.60e-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: 1.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 119 SPEDVALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIIPHLASLKIAGGTI-KGYGCPGLSILSHALVGAEIARVDASCCT 197
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIpEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|.
gi 1373925882 198 FALVHSSLCMSTIGMLGNEEQKQKYLPSLAR 228
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLAS 111
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
98-383 |
8.39e-32 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 126.59 E-value: 8.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 98 ATPASTFPTSVSDYFGLEDLlSPEDVALRKRVRRVMEEHVAPVVTKYWEKAEFPFEIIPHLASLKIAGGTI-KGYGCPGL 176
Cdd:PTZ00461 18 WTAAATMTSASRAFMDLYNP-TPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVpEADGGAGM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 177 SILSHALVGAEIARVDASCCTFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKV 256
Cdd:PTZ00461 97 DAVAAVIIHHELSKYDPGFCLAYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 257 -EGGWLLNGQKRWIGNATFADIVVVFARntQTNQINGFIVKKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLT 335
Cdd:PTZ00461 177 sNGNYVLNGSKIWITNGTVADVFLIYAK--VDGKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLG 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1373925882 336 GI-NSFQDTNKVLAVSRIMVAWLPIGVCMGVYDICYRYLQERKQFGAPL 383
Cdd:PTZ00461 255 EEgKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPI 303
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
118-485 |
2.53e-31 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 124.46 E-value: 2.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 118 LSPEDVALRKRVRRVMEEHVAPVVTKYW-EKAEFPFEIIPHLASLKIAG-GTIKGYGCPGLSILSHALVGAEIARvdaSC 195
Cdd:PRK12341 5 LTEEQELLLASIRELITRNFPEEYFRTCdENGTYPREFMRALADNGISMlGVPEEFGGTPADYVTQMLVLEEVSK---CG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 196 CTFALVHSSLCMSTIGMLGNEEQKQKYLPS-LARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNATF 274
Cdd:PRK12341 82 APAFLITNGQCIHSMRRFGSAEQLRKTAEStLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAKE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 275 ADIVVVFARNTQ----TNQINGFIVKKGTPGYRATKIEnKIGLRIVQNGDIIMKDVFIPDEDrLTGI--NSFQDTNKVLA 348
Cdd:PRK12341 162 YPYMLVLARDPQpkdpKKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESD-LVGEegMGFLNVMYNFE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 349 VSRIMVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQASLCK 428
Cdd:PRK12341 240 MERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAALAK 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1373925882 429 AWNTLRARETVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGREI 485
Cdd:PRK12341 320 LYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQI 376
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
146-485 |
8.50e-30 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 120.32 E-value: 8.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 146 EKAEFPFEIIPHLASLKIAGGTI-KGYGCPGLSILSHALVGAEIARVDASccTFALVHSSLCMSTIGMLGNEEQKQKYLP 224
Cdd:PRK03354 34 RDSVYPERFVKALADMGIDSLLIpEEHGGLDAGFVTLAAVWMELGRLGAP--TYVLYQLPGGFNTFLREGTQEQIDKIMA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 225 SLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGNATFADIVVVFARNTQTNQINGF---IVKKGTPG 301
Cdd:PRK03354 112 FRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASPDKPVYtewFVDMSKPG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 302 YRATKIEnKIGLRIVQNGDIIMKDVFIPDEDrLTGI--NSFQDTNKVLAVSRIMVAWLPIGVCMGVYDICYRYLQERKQF 379
Cdd:PRK03354 192 IKVTKLE-KLGLRMDSCCEITFDDVELDEKD-MFGRegNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQF 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 380 GAPLAALQINQEKLVRM---LGNIQAMFL-LGWKlckmYESGKMTPGQASLCKAWNTLRARETVALGRELLGGNGILSDF 455
Cdd:PRK03354 270 GEAIGRFQLIQEKFAHMaikLNSMKNMLYeAAWK----ADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNH 345
|
330 340 350
....*....|....*....|....*....|
gi 1373925882 456 LVAKAFCDIEPIYTYEGTYDINTLVTGREI 485
Cdd:PRK03354 346 RISRFWRDLRVDRVSGGSDEMQILTLGRAV 375
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
120-476 |
1.33e-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: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 120 PEDVALRKRVRRVMEEHVAPVVTKywEKAEFPFEI----IPHLASLKIAG----GTIKGYGCPGLSILSHALVGAEIARV 191
Cdd:cd01152 1 PSEEAFRAEVRAWLAAHLPPELRE--ESALGYREGredrRRWQRALAAAGwaapGWPKEYGGRGASLMEQLIFREEMAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 192 DASCcTFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGWLLNGQKRWIGN 271
Cdd:cd01152 79 GAPV-PFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 272 ATFADIVVVFAR-NTQTNQING---FIVKKGTPGYRATKIENKIGlRIVQNgDIIMKDVFIPDEDRLTGINS-FQDTNKV 346
Cdd:cd01152 158 AHYADWAWLLVRtDPEAPKHRGisiLLVDMDSPGVTVRPIRSING-GEFFN-EVFLDDVRVPDANRVGEVNDgWKVAMTT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 347 LAVSRimvawlpigVCMGVYDICY-----RYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTP 421
Cdd:cd01152 236 LNFER---------VSIGGSAATFfelllARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPG 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1373925882 422 GQASLCKAWNTLRARETVALGRELLGGNGILSD----------FLVAKAFCDIEPIYTyeGTYDI 476
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 ... |
347-485 |
1.68e-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: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 347 LAVSRIMVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQASL 426
Cdd:pfam00441 11 LNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAGGPDGAEASM 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1373925882 427 CKAWNTLRARETVALGRELLGGNGILSDFLVAKAFCDIEPIYTYEGTYDINTLVTGREI 485
Cdd:pfam00441 91 AKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
234-324 |
2.99e-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: 2.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 234 CWALTEPAYGSDASSLNTTAVKVEGG-WLLNGQKRWIGNATFADIVVVFARNTQT---NQINGFIVKKGTPGYRATKIEN 309
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGGgWVLNGTKWWITNAGIADLFLVLARTGGDdrhGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 1373925882 310 KIGLRIVQNGDIIMK 324
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
124-479 |
1.54e-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: 90.89 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 124 ALRKRVRRVMEEHVAPVVtkyWEKAEFPfEIIPHLASLKIAGGTIKGYGCPgLSIlshalvgaeiarvdasccTFALVHs 203
Cdd:cd01154 66 AWHALMRRLIEEGVINIE---DGPAGEG-RRHVHFAAGYLLSDAAAGLLCP-LTM------------------TDAAVY- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 204 slcmsTIGMLGNEEQKQKYLPSLARFD----TIGCWaLTEPAYGSDASSLNTTAVKVEGG-WLLNGQKrWIGNATFADIV 278
Cdd:cd01154 122 -----ALRKYGPEELKQYLPGLLSDRYktglLGGTW-MTEKQGGSDLGANETTAERSGGGvYRLNGHK-WFASAPLADAA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 279 VVFAR----NTQTNQINGFIVKKGTP-----GYRATKIENKIGLRIVQNGDIIMKDV---FIPDEDRltGINSfqdTNKV 346
Cdd:cd01154 195 LVLARpegaPAGARGLSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDAeayLIGDEGK--GIYY---ILEM 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 347 LAVSRIMVAWLPIGVCMGVYDICYRYLQERKQFGAPLAALQINQEKLVRMLGNIQAMFLLGWKLCKMYE-SGKMTPGQA- 424
Cdd:cd01154 270 LNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDrAAADKPVEAh 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1373925882 425 ------SLCKAWNTLRARETVALGRELLGGNGILSDFLVAKAFCD--IEPIytYEGTYDINTL 479
Cdd:cd01154 350 marlatPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREaqVTPI--WEGTGNIQAL 410
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
162-486 |
2.01e-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: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 162 KIAGGTIKGYGCP----GLSiLSHALVGAeIARVDASCCTFALVHSSL--CMSTIGMLGNEEQKQKYLPSLARFDTIGCW 235
Cdd:cd01153 44 AFAEAGWMALGVPeeygGQG-LPITVYSA-LAEIFSRGDAPLMYASGTqgAAATLLAHGTEAQREKWIPRLAEGEWTGTM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 236 ALTEPAYGSDASSLNTTAVKVEGG-WLLNGQKRWIGN---ATFADIV-VVFAR----NTQTNQINGFIVKK----GTP-G 301
Cdd:cd01153 122 CLTEPDAGSDLGALRTKAVYQADGsWRINGVKRFISAgehDMSENIVhLVLARsegaPPGVKGLSLFLVPKflddGERnG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 302 YRATKIENKIGLRIVQNGDIIMKD---VFIPDEDRltGInsfQDTNKVLAVSRIMVAWLPIGVCMGVYDICYRYLQERKQ 378
Cdd:cd01153 202 VTVARIEEKMGLHGSPTCELVFDNakgELIGEEGM--GL---AQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 379 FGAPLAA---LQINQEKLVRMLGNIQAMFLLGWKLCKMY-------ESGKMTPGQAS------------LCKAWNTLRAR 436
Cdd:cd01153 277 GGDLIKAapaVTIIHHPDVRRSLMTQKAYAEGSRALDLYtatvqdlAERKATEGEDRkalsaladlltpVVKGFGSEAAL 356
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1373925882 437 ETVALGRELLGGNGILSDFLVAKAFCD--IEPIytYEGTYDINTL-VTGREIT 486
Cdd:cd01153 357 EAVSDAIQVHGGSGYTREYPIEQYYRDarITTI--YEGTTGIQALdLIGRKIV 407
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
190-472 |
9.71e-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: 9.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 190 RVDASCCTFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAV--KVEGGWLLN---- 263
Cdd:cd01150 93 GYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATydPLTQEFVINtpdf 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 264 -GQKRWIGN-ATFADIVVVFAR---NTQTNQINGFIVK-------KGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDE 331
Cdd:cd01150 173 tATKWWPGNlGKTATHAVVFAQlitPGKNHGLHAFIVPirdpkthQPLPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRE 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 332 DRL----------TGINSFQDTNKVLAVSRIMVAWLPIGVCMGVYD-------ICYRYLQERKQFG-------APLAALQ 387
Cdd:cd01150 253 NLLnrfgdvspdgTYVSPFKDPNKRYGAMLGTRSGGRVGLIYDAAMslkkaatIAIRYSAVRRQFGpkpsdpeVQILDYQ 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 388 INQEKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQ-------------ASLcKAWNTLRARETVALGRELLGGNGILSD 454
Cdd:cd01150 333 LQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKELLQgnsellaelhalsAGL-KAVATWTAAQGIQECREACGGHGYLAM 411
|
330
....*....|....*...
gi 1373925882 455 FLVAKAFCDIEPIYTYEG 472
Cdd:cd01150 412 NRLPTLRDDNDPFCTYEG 429
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
201-450 |
3.83e-13 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 71.81 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 201 VHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAV--KVEGGWLLN-----GQKRWIGNAT 273
Cdd:PLN02636 143 VQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATfdPLTDEFVINtpndgAIKWWIGNAA 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 274 F-ADIVVVFAR---------NTQTNQINGFIV-------KKGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLtg 336
Cdd:PLN02636 223 VhGKFATVFARlklpthdskGVSDMGVHAFIVpirdmktHQVLPGVEIRDCGHKVGLNGVDNGALRFRSVRIPRDNLL-- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 337 iNSFQDT-------------NKVLAVS-------RIMVAWLPIGVCMGVYDICYRYLQERKQFGAP------LAALQINQ 390
Cdd:PLN02636 301 -NRFGDVsrdgkytsslptiNKRFAATlgelvggRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPkqpeisILDYQSQQ 379
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 391 EKLVRMLGNIQAMFLLGWKLCKMYESGKMTPGQ----------ASLcKAWNTLRARETVALGRELLGGNG 450
Cdd:PLN02636 380 HKLMPMLASTYAFHFATEYLVERYSEMKKTHDDqlvadvhalsAGL-KAYITSYTAKALSTCREACGGHG 448
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
154-451 |
4.02e-13 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 71.77 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 154 IIPhlaslkiaggtiKGYGCPGLSILSHALVGAEIARVdascctfalvhSSLCMSTIG---------ML---GNEEQKQK 221
Cdd:PRK09463 127 IIP------------KEYGGLEFSAYAHSRVLQKLASR-----------SGTLAVTVMvpnslgpgeLLlhyGTDEQKDH 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 222 YLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKVEGGW--------LLNGQKRWIgnaTFADIVVVFARNTQTNQINGF 293
Cdd:PRK09463 184 YLPRLARGEEIPCFALTSPEAGSDAGSIPDTGVVCKGEWqgeevlgmRLTWNKRYI---TLAPIATVLGLAFKLYDPDGL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 294 I------------VKKGTPGYratkienKIGLR------IVQNGDIIMKDVFIPdedrLTGINSFQDT--------NKVL 347
Cdd:PRK09463 261 LgdkedlgitcalIPTDTPGV-------EIGRRhfplnvPFQNGPTRGKDVFIP----LDYIIGGPKMagqgwrmlMECL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 348 AVSR-IMvawLPiGVCMGVYDICYR----YLQERKQFGAPLAALQINQEKLVRMLGN---IQAMFLLGwklCKMYESGKm 419
Cdd:PRK09463 330 SVGRgIS---LP-SNSTGGAKLAALatgaYARIRRQFKLPIGKFEGIEEPLARIAGNaylMDAARTLT---TAAVDLGE- 401
|
330 340 350
....*....|....*....|....*....|...
gi 1373925882 420 TPGQAS-LCKAWNTLRARETVALGRELLGGNGI 451
Cdd:PRK09463 402 KPSVLSaIAKYHLTERGRQVINDAMDIHGGKGI 434
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
136-451 |
1.67e-12 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 69.99 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 136 HVAPVVTKYWEKAEFPFEIIPhlaslkiaggtiKGYGCPGLSILSHALVGAEIARVDASCCTFALVHSSLcmsTIGML-- 213
Cdd:PRK13026 108 DLPPEVWDYLKKEGFFALIIP------------KEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPNSL---GPGELlt 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 214 --GNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAV----KVEG----GWLLNGQKRWIgnaTFADIVVVFAR 283
Cdd:PRK13026 173 hyGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTGIvcrgEFEGeevlGLRLTWDKRYI---TLAPVATVLGL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 284 NTQTNQINGFIVKKGTPGYRATKIEN-----KIGLR------IVQNGDIIMKDVFIPdEDRLTG-----INSFQDTNKVL 347
Cdd:PRK13026 250 AFKLRDPDGLLGDKKELGITCALIPTdhpgvEIGRRhnplgmAFMNGTTRGKDVFIP-LDWIIGgpdyaGRGWRMLVECL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 348 AVSRIMVawLP-IGVCMGVydICYR----YLQERKQFGAPLAALQINQEKLVRMLGN---IQAMFLLgwkLCKMYESGKm 419
Cdd:PRK13026 329 SAGRGIS--LPaLGTASGH--MATRttgaYAYVRRQFGMPIGQFEGVQEALARIAGNtylLEAARRL---TTTGLDLGV- 400
|
330 340 350
....*....|....*....|....*....|...
gi 1373925882 420 TPGQAS-LCKAWNTLRARETVALGRELLGGNGI 451
Cdd:PRK13026 401 KPSVVTaIAKYHMTELARDVVNDAMDIHAGKGI 433
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
124-391 |
1.20e-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: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 124 ALRKRVRRVMEEHVAP---VVTKYWEKAEFPFEIIPH-LASLKIAGGTI--------KGYGCPGLSILSHALVGAEIARv 191
Cdd:cd01155 5 ELRARVKAFMEEHVYPaeqEFLEYYAEGGDRWWTPPPiIEKLKAKAKAEglwnlflpEVSGLSGLTNLEYAYLAEETGR- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 192 dascCTFAlVHSSLC-------MSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYG-SDASSLNTTAVKVEGGWLLN 263
Cdd:cd01155 84 ----SFFA-PEVFNCqapdtgnMEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDVAsSDATNIECSIERDGDDYVIN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 264 GQKRWIGNATFAD--IVVVFAR-----NTQTNQINGFIVKKGTPGY---RATKI----ENKIGlrivqNGDIIMKDVFIP 329
Cdd:cd01155 159 GRKWWSSGAGDPRckIAIVMGRtdpdgAPRHRQQSMILVPMDTPGVtiiRPLSVfgydDAPHG-----HAEITFDNVRVP 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1373925882 330 DEDRLTGINS-FQDTNKVLAVSRIMVAWLPIGVC-MGVYDICYRYLQeRKQFGAPLAALQINQE 391
Cdd:cd01155 234 ASNLILGEGRgFEIAQGRLGPGRIHHCMRLIGAAeRALELMCQRAVS-REAFGKKLAQHGVVAH 296
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
197-472 |
3.64e-09 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 59.08 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 197 TFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAV-------KVEGGWLLNGQKRWI 269
Cdd:PLN02443 97 GYTDLHWGMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATfdpktdeFVIHSPTLTSSKWWP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 270 GN----ATFAdivVVFAR---NTQTNQINGFIVK-------KGTPGYRATKIENKIG---LRIVQNGDIIMKDVFIPDED 332
Cdd:PLN02443 177 GGlgkvSTHA---VVYARlitNGKDHGIHGFIVQlrslddhSPLPGVTVGDIGMKFGngaYNTMDNGFLRFDHVRIPRDQ 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 333 RLTGINSFQDTNKVLA--------------VSRIMVA----WLPIGVCMGVydicyRYLQERKQFGA---PLAALQIN-- 389
Cdd:PLN02443 254 MLMRLSKVTREGKYVQsdvprqlvygtmvyVRQTIVAdastALSRAVCIAT-----RYSAVRRQFGSqdgGPETQVIDyk 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 390 --QEKLVRMLGNIQAMFLLGWKLCKMY--------ESGKMTPGQASLC----KAWNTLRARETVALGRELLGGNGILSDF 455
Cdd:PLN02443 329 tqQSRLFPLLASAYAFRFVGEWLKWLYtdvtqrleANDFSTLPEAHACtaglKSLTTSATADGIEECRKLCGGHGYLCSS 408
|
330
....*....|....*..
gi 1373925882 456 LVAKAFCDIEPIYTYEG 472
Cdd:PLN02443 409 GLPELFAVYVPACTYEG 425
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
201-479 |
7.92e-09 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 58.25 E-value: 7.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 201 VHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAV--KVEGGWLLN-----GQKRWIGNAT 273
Cdd:PLN02312 155 VHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTydPKTEEFVINtpcesAQKYWIGGAA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 274 -FADIVVVFAR---NTQTNQINGFIVK----KGT--PGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLTGI------ 337
Cdd:PLN02312 235 nHATHTIVFSQlhiNGKNEGVHAFIAQirdqDGNicPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNSVadvspd 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 338 ----NSFQDTNK--------------VLAVSRIMVAwlPIGVCMGVydicyRYLQERKQFG-AP------LAALQINQEK 392
Cdd:PLN02312 315 gkyvSAIKDPDQrfgaflapltsgrvTIAVSAIYSS--KVGLAIAI-----RYSLSRRAFSvTPngpevlLLDYPSHQRR 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 393 LVRMLGNIQAMFLLGWKLCKMY-----ESGKMTPGQASLCKA---WNTLRareTVALGRELLGGNGILSDFLVA--KAFC 462
Cdd:PLN02312 388 LLPLLAKTYAMSFAANDLKMIYvkrtpESNKAIHVVSSGFKAvltWHNMR---TLQECREACGGQGLKTENRVGqlKAEY 464
|
330
....*....|....*..
gi 1373925882 463 DIEPiyTYEGtyDINTL 479
Cdd:PLN02312 465 DVQS--TFEG--DNNVL 477
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
197-483 |
1.90e-07 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 53.70 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 197 TFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAV--KVEGGWLLN-----GQKRWI 269
Cdd:PTZ00460 93 FISTVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATydKQTNEFVIHtpsveAVKFWP 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 270 GNATF-ADIVVVFAR---NTQTNQINGFIVK-------KGTPGYRATKIENKIGLRIVQNGDIIMKDVFIPDEDRLT--- 335
Cdd:PTZ00460 173 GELGFlCNFALVYAKlivNGKNKGVHPFMVRirdkethKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLAryi 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 336 -----GINSFQDTNKV----LAVSRIMVAWLPIGVCMGVYDICYRYLQERKQF----GAPLAAL--QINQEKLVRMLGNI 400
Cdd:PTZ00460 253 kvsedGQVERQGNPKVsyasMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQFtndnKQENSVLeyQTQQQKLLPLLAEF 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 401 QAMFLLGWKLCKMYES----------GKMTPGQASLC--KAWNTLRARETVALGRELLGGNGILSDFLVAKAFCDIEPIY 468
Cdd:PTZ00460 333 YACIFGGLKIKELVDDnfnrvqkndfSLLQLTHAILSaaKANYTYFVSNCAEWCRLSCGGHGYAHYSGLPAIYFDMSPNI 412
|
330
....*....|....*
gi 1373925882 469 TYEGTYDINTLVTGR 483
Cdd:PTZ00460 413 TLEGENQIMYLQLAR 427
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
158-377 |
1.54e-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: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 158 LASLKIAG-GTI---KGYGCPGLSILSHALVGAEIARVDASCC-----TFALVHSSLcmstigMLGNEEQKQKYLPSLAR 228
Cdd:cd01163 28 VALLRQSGlGTLrvpKEYGGLGASLPDLYEVVRELAAADSNIAqalraHFGFVEALL------LAGPEQFRKRWFGRVLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 229 FDTIGCwALTEPAyGSDASSLNTTAVKVEGGWLLNGQKRWIGNATFADIVVVFARNTQTNQInGFIVKKGTPGYRATKIE 308
Cdd:cd01163 102 GWIFGN-AVSERG-SVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGKLV-FAAVPTDRPGITVVDDW 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1373925882 309 NKIGLRIVQNGDIIMKDVFIPDEDRLTGINSFQDTNKVLAVSRIMVAWLPIGVCMGVYDICYRYLQERK 377
Cdd:cd01163 179 DGFGQRLTASGTVTFDNVRVEPDEVLPRPNAPDRGTLLTAIYQLVLAAVLAGIARAALDDAVAYVRSRT 247
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
154-303 |
1.77e-06 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 50.65 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 154 IIPHLASLKIAggtiKGYGCPGLSILSHALVGAEIARVDASCCTFALVHSSLCMSTIGMLGNEEQKQKYLPSLARFDTIG 233
Cdd:PTZ00457 61 ILGNLYGARIA----TEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHSGFCTYLLSTVGSKELKGKYLTAMSDGTIMM 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 234 CWAlTEPAYGSDASSLNTTAV-KVEGGWLLNGQKRWIgNATFADIVVVFARN-TQTNQING---------FIVKKGTPGY 302
Cdd:PTZ00457 137 GWA-TEEGCGSDISMNTTKASlTDDGSYVLTGQKRCE-FAASATHFLVLAKTlTQTAAEEGatevsrnsfFICAKDAKGV 214
|
.
gi 1373925882 303 R 303
Cdd:PTZ00457 215 S 215
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
207-300 |
2.02e-06 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 50.25 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 207 MSTIGMLGNEEQKQKYLPSLARFDTIGCWALTEPAYGSDASSLNTTAVKV-EGGWLLNGQKRWI--GNATFAD--IVVVF 281
Cdd:PTZ00456 157 ANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSaDGSYKITGTKIFIsaGDHDLTEniVHIVL 236
|
90 100
....*....|....*....|...
gi 1373925882 282 AR--NTQ--TNQINGFIVKKGTP 300
Cdd:PTZ00456 237 ARlpNSLptTKGLSLFLVPRHVV 259
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
186-464 |
2.58e-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: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 186 AEIARVDAScctFALVHSSLCMST--IGMLGNEEQkqkylpslARFdtigcWALTEPAYGSDASSLNTTAVKVEGGWLLN 263
Cdd:cd01159 60 ATLAEACGS---AAWVASIVATHSrmLAAFPPEAQ--------EEV-----WGDGPDTLLAGSYAPGGRAERVDGGYRVS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 264 GQKRWIGNATFADIVVVfarntqtnqinGFIV--KKGTPGYRA-------TKIENK---IGLRIVQNGDIIMKDVFIPDE 331
Cdd:cd01159 124 GTWPFASGCDHADWILV-----------GAIVedDDGGPLPRAfvvpraeYEIVDTwhvVGLRGTGSNTVVVDDVFVPEH 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1373925882 332 DRLTGINSFQDTNKVLAVSRIMVAWLP----------IGVCMGVYDICYRYLQERKQ---FGAPLAALQINQEKLVRMLG 398
Cdd:cd01159 193 RTLTAGDMMAGDGPGGSTPVYRMPLRQvfplsfaavsLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAA 272
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1373925882 399 NIQAM--FLLG-----WKLCKmyESGKMTPGQASLCKAWNTLRARETVALGR---ELLGGNGILSDFLVAKAFCDI 464
Cdd:cd01159 273 ELDAAraFLERatrdlWAHAL--AGGPIDVEERARIRRDAAYAAKLSAEAVDrlfHAAGGSALYTASPLQRIWRDI 346
|
|
| |
