|
Name |
Accession |
Description |
Interval |
E-value |
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
36-408 |
0e+00 |
|
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: 687.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 36 ETHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCASTGVI 115
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 116 MSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASAT 195
Cdd:cd01158 81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 196 VVFASTDRSRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRIGI 275
Cdd:cd01158 161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 276 ASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAKLAASEA 355
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1168286 356 ATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLLR 408
Cdd:cd01158 321 AMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
33-411 |
4.65e-179 |
|
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: 503.60 E-value: 4.65e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 33 ELPETHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCAST 112
Cdd:COG1960 4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 113 GVIMSVNNSLyLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEA 192
Cdd:COG1960 84 ALPVGVHNGA-AEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 193 SATVVFASTDRSRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGR 272
Cdd:COG1960 163 DVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 273 IGIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAKLAA 352
Cdd:COG1960 243 LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLFA 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1168286 353 SEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLLRSYR 411
Cdd:COG1960 323 TEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
34-403 |
1.51e-125 |
|
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: 367.51 E-value: 1.51e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 34 LPETHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCASTG 113
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 114 VIMSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEAS 193
Cdd:cd01156 82 LSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDAD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 194 ATVVFASTDRSRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRI 273
Cdd:cd01156 162 TLVVYAKTDPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYERL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 274 GIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAKLAAS 353
Cdd:cd01156 242 VLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILYAA 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1168286 354 EAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIA 403
Cdd:cd01156 322 EKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIG 371
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
36-403 |
1.20e-122 |
|
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: 358.52 E-value: 1.20e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 36 ETHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAmdvpeelsgagldylaysialeeisrgcastgvi 115
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLLGAA---------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 116 msvnnslylgPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASAT 195
Cdd:cd00567 47 ----------LLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 196 VVFASTDRS-RQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRIG 274
Cdd:cd00567 117 IVLARTDEEgPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 275 IASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDN-KKPFTKESAMAKLAAS 353
Cdd:cd00567 197 LAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQgPDEARLEAAMAKLFAT 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1168286 354 EAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIA 403
Cdd:cd00567 277 EAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
34-408 |
1.42e-119 |
|
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: 352.52 E-value: 1.42e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 34 LPETHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCASTG 113
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 114 VIMSVNNsLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEAS 193
Cdd:cd01162 81 AYISIHN-MCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 194 ATVVFASTDRSRQnKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRI 273
Cdd:cd01162 160 VYVVMARTGGEGP-KGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 274 GIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKP-FTKESAMAKLAA 352
Cdd:cd01162 239 NIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPdAVKLCAMAKRFA 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1168286 353 SEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLLR 408
Cdd:cd01162 319 TDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLT 374
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
33-410 |
1.20e-109 |
|
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: 328.27 E-value: 1.20e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 33 ELPETHQMLRQTCRDFAEKELVPiaAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGcAST 112
Cdd:cd01161 26 EQTEELNMLVGPVEKFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMD-LGF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 113 GVIMSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAR--EEGDSWVLNGTKAWITNSW 190
Cdd:cd01161 103 SVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVlsEDGKHYVLNGSKIWITNGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 191 EASATVVFASTDRSRQN----KGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQ 266
Cdd:cd01161 183 IADIFTVFAKTEVKDATgsvkDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMN 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 267 TLDMGRIGIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDN--KKPFTKE 344
Cdd:cd01161 263 ILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRglKAEYQIE 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168286 345 SAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLLRSY 410
Cdd:cd01161 343 AAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQHA 408
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
34-407 |
3.14e-106 |
|
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: 318.38 E-value: 3.14e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 34 LPETHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCasTG 113
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGC--TG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 114 VIMSVN-NSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEA 192
Cdd:cd01157 79 VQTAIEaNSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 193 SATVVFASTD---RSRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLD 269
Cdd:cd01157 159 NWYFLLARSDpdpKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 270 MGRIGIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAK 349
Cdd:cd01157 239 KTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAK 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1168286 350 LAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLL 407
Cdd:cd01157 319 AFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
36-407 |
1.10e-104 |
|
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: 314.44 E-value: 1.10e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 36 ETHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISR-GCASTGV 114
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARaGGSGPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 115 imSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASA 194
Cdd:cd01160 81 --SLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 195 TVVFASTDR-SRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRI 273
Cdd:cd01160 159 VIVVARTGGeARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 274 GIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAKLAAS 353
Cdd:cd01160 239 LIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWAT 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1168286 354 EAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLL 407
Cdd:cd01160 319 ELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
12-408 |
1.77e-99 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 302.18 E-value: 1.77e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 12 SLGRALRARDWRRLHTVYQSVELPETHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQ--VKKMGELGLLAMDVPEELS 89
Cdd:PLN02519 4 SAAKARRRGLARRFSSSSSSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGITAPEEYG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 90 GAGLDYLAYSIALEEISRGCASTGVIMSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTT 169
Cdd:PLN02519 84 GLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 170 AREEGDSWVLNGTKAWITNSWEASATVVFASTDRSRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIP 249
Cdd:PLN02519 164 AERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 250 KENLLGEPGMGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTW 329
Cdd:PLN02519 244 EENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVY 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168286 330 RAAMLKDNKKPFTKESAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLLR 408
Cdd:PLN02519 324 SVARDCDNGKVDRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFK 402
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
34-403 |
2.80e-95 |
|
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: 290.80 E-value: 2.80e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 34 LPETHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAMdVPEELSGAGLDYLAYSIALEEISR---GCA 110
Cdd:cd01151 13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGA-TIKGYGCAGLSSVAYGLIAREVERvdsGYR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 111 STgviMSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSW 190
Cdd:cd01151 92 SF---MSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 191 EASATVVFASTDRSRQNKGisaFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLgePGM-GFKIAMQTLD 269
Cdd:cd01151 169 IADVFVVWARNDETGKIRG---FILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL--PGAeGLRGPFKCLN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 270 MGRIGIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAK 349
Cdd:cd01151 244 NARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLK 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1168286 350 LAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIA 403
Cdd:cd01151 324 RNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILG 377
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
35-411 |
1.55e-74 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 238.30 E-value: 1.55e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 35 PEtHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCASTGV 114
Cdd:PTZ00461 39 PE-HAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 115 IMSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGD-SWVLNGTKAWITNSWEAS 193
Cdd:PTZ00461 118 AYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGTVAD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 194 ATVVFASTDRSrqnkgISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRI 273
Cdd:PTZ00461 198 VFLIYAKVDGK-----ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 274 GIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAmlkDNKKPFTKE---SAMAKL 350
Cdd:PTZ00461 273 TLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVS---HNVHPGNKNrlgSDAAKL 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1168286 351 AASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLLRSYR 411
Cdd:PTZ00461 350 FATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLKGLK 410
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
46-411 |
2.95e-73 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 233.85 E-value: 2.95e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 46 RDFAEKELvpiaAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCASTGVImsvNNSLYLG 125
Cdd:PRK12341 22 RNFPEEYF----RTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCGAPAFLI---TNGQCIH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 126 PILKFGSSQQKQQWI-TPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASATVVFASTDRS 204
Cdd:PRK12341 95 SMRRFGSAEQLRKTAeSTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAKEYPYMLVLARDPQP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 205 R-QNKGISAFLVPMPTPGLTLGKKEdKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRIGIASQALGIA 283
Cdd:PRK12341 175 KdPKKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFEMERLINAARSLGFA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 284 QASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAKLAASEAATAISHQA 363
Cdd:PRK12341 254 ECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAALAKLYCARTAMEVIDDA 333
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1168286 364 IQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQrLVIAGH-LLRSYR 411
Cdd:PRK12341 334 IQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIM-IYIAGRqILKDYQ 381
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
44-408 |
9.75e-65 |
|
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: 212.64 E-value: 9.75e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 44 TCRDFAEKELVPIAAQLDKE--------HLFPT---SQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCAST 112
Cdd:cd01153 4 EVARLAENVLAPLNADGDREgpvfddgrVVVPPpfkEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 113 GVIMSVNNSLYLgpILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGD-SWVLNGTKAWITNSWE 191
Cdd:cd01153 84 MYASGTQGAAAT--LLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGEH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 192 ASAT----VVFAST-DRSRQNKGISAFLVP-----MPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPkenLLGEPGMGF 261
Cdd:cd01153 162 DMSEnivhLVLARSeGAPPGVKGLSLFLVPkflddGERNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 262 KIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRHAFGAPL--------TKLQNIQFKLADMALALESARLLTWRAAM 333
Cdd:cd01153 239 AQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIkaapavtiIHHPDVRRSLMTQKAYAEGSRALDLYTAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 334 LKD--NKKPFTKESA------------MAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQR 399
Cdd:cd01153 319 VQDlaERKATEGEDRkalsaladlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQA 398
|
....*....
gi 1168286 400 LVIAGHLLR 408
Cdd:cd01153 399 LDLIGRKIV 407
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
29-403 |
1.35e-59 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 199.31 E-value: 1.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 29 YQSVEL--PEtHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAMDVpEELSGAGLDYLAYSIALEEIS 106
Cdd:PLN02526 23 YQFDDLltPE-EQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTI-KGYGCPGLSITASAIATAEVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 107 RGCASTGVIMSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWI 186
Cdd:PLN02526 101 RVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 187 TNSWEASATVVFAstdRSRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLgePGM-GFKIAM 265
Cdd:PLN02526 181 GNSTFADVLVIFA---RNTTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRL--PGVnSFQDTN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 266 QTLDMGRIGIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKES 345
Cdd:PLN02526 256 KVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHA 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1168286 346 AMAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIA 403
Cdd:PLN02526 336 SLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTG 393
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
58-411 |
6.66e-59 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 196.59 E-value: 6.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 58 AQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCASTGVIMSVNNSLylGPILKFGSSQQKQ 137
Cdd:PRK03354 30 AECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPTYVLYQLPGGF--NTFLREGTQEQID 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 138 QWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASATVVFASTDRSRQNKGISAFLVPM 217
Cdd:PRK03354 108 KIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASPDKPVYTEWFVDM 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 218 PTPGLTLGKKEdKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENR 297
Cdd:PRK03354 188 SKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 298 HAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAKLAASEAATAISHQAIQILGGMGYVTEMP 377
Cdd:PRK03354 267 VQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHR 346
|
330 340 350
....*....|....*....|....*....|....
gi 1168286 378 AERYYRDARITEIYEGTSEIQRLVIAGHLLRSYR 411
Cdd:PRK03354 347 ISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQYR 380
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
258-403 |
1.13e-55 |
|
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: 180.53 E-value: 1.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 258 GMGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDN 337
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168286 338 KKPFTKESAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIA 403
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
71-407 |
1.16e-54 |
|
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: 185.63 E-value: 1.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 71 VKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCASTGVIMSVNNSLylGP-ILKFGSSQQKQQWITPFTNGDKI 149
Cdd:cd01152 41 QRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIGIDLA--GPtILAYGTDEQKRRFLPPILSGEEI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 150 GCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASATVVFASTD-RSRQNKGISAFLVPMPTPGLTLGKKE 228
Cdd:cd01152 119 WCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDpEAPKHRGISILLVDMDSPGVTVRPIR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 229 DKLGirASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRIGIASQAlGIAQASLDCAVKYAENRhafGAPLTKLQ 308
Cdd:cd01152 199 SING--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIGGSA-ATFFELLLARLLLLTRD---GRPLIDDP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 309 NIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAKLAASEAATAISHQAIQILGG---MGYVTEMPA-----ER 380
Cdd:cd01152 273 LVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFGSELAQELAELALELLGTaalLRDPAPGAElagrwEA 352
|
330 340
....*....|....*....|....*..
gi 1168286 381 YYRDARITEIYEGTSEIQRLVIAGHLL 407
Cdd:cd01152 353 DYLRSRATTIYGGTSEIQRNIIAERLL 379
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
39-403 |
2.30e-50 |
|
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: 174.50 E-value: 2.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 39 QMLRQTCRDF-------AEKELVPIAAQLDKEHLFPTSQVKKMGE----LGLLAMDVPEELSGAGLDYLAYSIALEEISR 107
Cdd:cd01155 4 QELRARVKAFmeehvypAEQEFLEYYAEGGDRWWTPPPIIEKLKAkakaEGLWNLFLPEVSGLSGLTNLEYAYLAEETGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 108 --------GCAS--TGViMSVnnslylgpILKFGSSQQKQQWITPFTNGDKIGCFALSEPG-NGSDAGAASTTAREEGDS 176
Cdd:cd01155 84 sffapevfNCQApdTGN-MEV--------LHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 177 WVLNGTKAWITNSWEASATVV-------FASTDRSRQNkgiSAFLVPMPTPGLTLgkkedklgIRASST----------A 239
Cdd:cd01155 155 YVINGRKWWSSGAGDPRCKIAivmgrtdPDGAPRHRQQ---SMILVPMDTPGVTI--------IRPLSVfgyddaphghA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 240 NLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMAL 319
Cdd:cd01155 224 EITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 320 ALESARLLTWRAAMLKDNK--KPFTKESAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEI 397
Cdd:cd01155 304 EIEQARLLVLKAAHMIDTVgnKAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEV 383
|
....*.
gi 1168286 398 QRLVIA 403
Cdd:cd01155 384 HLRSIA 389
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
35-147 |
4.41e-47 |
|
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: 156.85 E-value: 4.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 35 PETHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCASTGV 114
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|...
gi 1168286 115 IMSVNNSLYLGPILKFGSSQQKQQWITPFTNGD 147
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
137-400 |
4.35e-45 |
|
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: 161.00 E-value: 4.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 137 QQWITPFTNGD-----KIGCFaLSEPGNGSDAGAASTTA-REEGDSWVLNGTKaWITNSWEASATVVFASTDRSRQN-KG 209
Cdd:cd01154 132 KQYLPGLLSDRyktglLGGTW-MTEKQGGSDLGANETTAeRSGGGVYRLNGHK-WFASAPLADAALVLARPEGAPAGaRG 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 210 ISAFLVPMPTPGLTLGKKE-----DKLGIRASSTANLIFEDCripKENLLGEPGMGFKIAMQTLDMGRIGIASQALGIAQ 284
Cdd:cd01154 210 LSLFLVPRLLEDGTRNGYRirrlkDKLGTRSVATGEVEFDDA---EAYLIGDEGKGIYYILEMLNISRLDNAVAALGIMR 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 285 ASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAM--------AKLAASEAA 356
Cdd:cd01154 287 RALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKPVEAHmarlatpvAKLIACKRA 366
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1168286 357 TAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRL 400
Cdd:cd01154 367 APVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQAL 410
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
48-400 |
9.92e-31 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 124.21 E-value: 9.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 48 FAEKELVPIAAQLDKE--HLFPTSQV----------KKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISrgCASTGVI 115
Cdd:PTZ00456 70 LATQTLLPLYESSDSEgcVLLKDGNVttpkgfkeayQALKAGGWTGISEPEEYGGQALPLSVGFITRELMA--TANWGFS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 116 MSVNNSL-YLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGD-SWVLNGTKAWIT----NS 189
Cdd:PTZ00456 148 MYPGLSIgAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISagdhDL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 190 WEASATVVFASTDRSR-QNKGISAFLVP--MPTPGLTLGKK--------EDKLGIRASSTANLIFEDcriPKENLLGEPG 258
Cdd:PTZ00456 228 TENIVHIVLARLPNSLpTTKGLSLFLVPrhVVKPDGSLETAknvkciglEKKMGIKGSSTCQLSFEN---SVGYLIGEPN 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 259 MGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRHAFGA---------PLTKL-------QNIQFKLA----DMA 318
Cdd:PTZ00456 305 AGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRSMRAlsgtkepekPADRIichanvrQNILFAKAvaegGRA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 319 LALESARLL---------TWRAAMlkDNKKPFTkeSAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITE 389
Cdd:PTZ00456 385 LLLDVGRLLdihaaakdaATREAL--DHEIGFY--TPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGT 460
|
410
....*....|.
gi 1168286 390 IYEGTSEIQRL 400
Cdd:PTZ00456 461 LYEGTTGIQAL 471
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
151-244 |
6.14e-30 |
|
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: 111.22 E-value: 6.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 151 CFALSEPGNGSDAGA-ASTTAREEGDSWVLNGTKAWITNSWEASATVVFASTDRSRQNKGISAFLVPMPTPGLTLGKKED 229
Cdd:pfam02770 1 AFALTEPGAGSDVASlKTTAADGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 1168286 230 KLGIRASSTANLIFE 244
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
86-403 |
1.43e-29 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 121.44 E-value: 1.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 86 EELSGAGLDYLAYSIALEEISR----------GCASTGViMSVnnslylgpILKFGSSQQKQQWITPFTNGDKIGCFALS 155
Cdd:PLN02876 487 DQLLGAGLSNLEYGYLCEIMGRsvwapqvfncGAPDTGN-MEV--------LLRYGNKEQQLEWLIPLLEGKIRSGFAMT 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 156 EPG-NGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASATV--VFASTDRSR-QNKGISAFLVPMPTPGLTLGKKEDKL 231
Cdd:PLN02876 558 EPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPRCRVliVMGKTDFNApKHKQQSMILVDIQTPGVQIKRPLLVF 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 232 GIRAS--STANLIFEDCRIPKEN-LLGEpGMGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQ 308
Cdd:PLN02876 638 GFDDAphGHAEISFENVRVPAKNiLLGE-GRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHG 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 309 NIQFKLADMALALESARLLTWRAAMLKD---NKKPfTKESAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDA 385
Cdd:PLN02876 717 SFLSDLAKCRVELEQTRLLVLEAADQLDrlgNKKA-RGIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATA 795
|
330
....*....|....*...
gi 1168286 386 RITEIYEGTSEIQRLVIA 403
Cdd:PLN02876 796 RTLRIADGPDEVHLGTIA 813
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
21-371 |
1.52e-29 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 121.22 E-value: 1.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 21 DWRRLHTvYQSVELPETHQmlrqtcrDFAEKELVPIAAQLDKehlFPTSQVKK---------MGELGLLAMDVPEELSGA 91
Cdd:PRK13026 66 DWQKLHS-YPKPTLTAEEQ-------AFIDNEVETLLTMLDD---WDIVQNRKdlppevwdyLKKEGFFALIIPKEYGGK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 92 GLDYLAYSIALEEISRGCASTGVIMSVNNSLylGP---ILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAAST 168
Cdd:PRK13026 135 GFSAYANSTIVSKIATRSVSAAVTVMVPNSL--GPgelLTHYGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPD 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 169 TA-----REEGDSWV---LNGTKAWITNSweASATVV---FASTD-----RSRQNKGISAFLVPMPTPGLTLGKKEDKLG 232
Cdd:PRK13026 213 TGivcrgEFEGEEVLglrLTWDKRYITLA--PVATVLglaFKLRDpdgllGDKKELGITCALIPTDHPGVEIGRRHNPLG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 233 IRasstanliF-------EDCRIPKENLLGEP---GMGFKIAMQTLDMGRiGIASQALGIAQASLdcAVK----YAENRH 298
Cdd:PRK13026 291 MA--------FmngttrgKDVFIPLDWIIGGPdyaGRGWRMLVECLSAGR-GISLPALGTASGHM--ATRttgaYAYVRR 359
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168286 299 AFGAPLTKLQNIQFKLADMA---LALESARLLTwrAAMLKDNKKPfTKESAMAKLAASEAATAISHQAIQILGGMG 371
Cdd:PRK13026 360 QFGMPIGQFEGVQEALARIAgntYLLEAARRLT--TTGLDLGVKP-SVVTAIAKYHMTELARDVVNDAMDIHAGKG 432
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
70-412 |
2.98e-23 |
|
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: 102.02 E-value: 2.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 70 QVKKMGELGLlamDVPEElsgagldYLAYSIALEEISrgcASTGVIMSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKI 149
Cdd:cd01150 69 DVERMGELMA---DDPEK-------MLALTNSLGGYD---LSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEII 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 150 GCFALSEPGNGSDAGAASTTAR--EEGDSWVLN-----GTKAWITN-SWEASATVVFASTDRSRQNKGISAFLVPM---- 217
Cdd:cd01150 136 GCFAQTELGHGSNLQGLETTATydPLTQEFVINtpdftATKWWPGNlGKTATHAVVFAQLITPGKNHGLHAFIVPIrdpk 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 218 ---PTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLG----------------EPGMGFKIAMQTLDMGRIGIASQ 278
Cdd:cd01150 216 thqPLPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNrfgdvspdgtyvspfkDPNKRYGAMLGTRSGGRVGLIYD 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 279 ALGIAQASLDCAVKYAENRHAFG-------APLTKLQNIQFKLADMalaLESARLLTWRAAMLKDNKKPFTKESAMAK-- 349
Cdd:cd01150 296 AAMSLKKAATIAIRYSAVRRQFGpkpsdpeVQILDYQLQQYRLFPQ---LAAAYAFHFAAKSLVEMYHEIIKELLQGNse 372
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168286 350 -------LAASEAATAISH--QAIQIL----GGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLLRSYRS 412
Cdd:cd01150 373 llaelhaLSAGLKAVATWTaaQGIQECreacGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQ 448
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
52-386 |
8.19e-23 |
|
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: 98.93 E-value: 8.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 52 ELVPIAAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCASTGVIMSvNNSLYLGPILKFG 131
Cdd:cd01163 9 RIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALR-AHFGFVEALLLAG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 132 SSQQKQQWITPFTNGDKIGCfALSEPGnGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASATVVFASTDRSRQnkgiS 211
Cdd:cd01163 88 PEQFRKRWFGRVLNGWIFGN-AVSERG-SVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGKL----V 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 212 AFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLdMGRIGIASQALGIAQASLDCAV 291
Cdd:cd01163 162 FAAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPNAPDRGTLLTA-IYQLVLAAVLAGIARAALDDAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 292 KYAENR-----HAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDN--KKPFTKE----------SAMAKLAASE 354
Cdd:cd01163 241 AYVRSRtrpwiHSGAESARDDPYVQQVVGDLAARLHAAEALVLQAARALDAaaAAGTALTaeargeaalaVAAAKVVVTR 320
|
330 340 350
....*....|....*....|....*....|..
gi 1168286 355 AATAISHQAIQILGGMGYVTEMPAERYYRDAR 386
Cdd:cd01163 321 LALDATSRLFEVGGASATAREHNLDRHWRNAR 352
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
21-371 |
1.21e-21 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 97.19 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 21 DWRRLHTvYQSVELPETHQM-----LRQTCR---DFA----EKELVPIAAQLDKEHlfptsqvkkmgelGLLAMDVPEEL 88
Cdd:PRK09463 67 DWKKLLN-YPKPTLTAEEQAfldgpVEELCRmvnDWQitheLADLPPEVWQFIKEH-------------GFFGMIIPKEY 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 89 SGAGLDYLAYSIALEEISRGCASTGVIMSVNNSLylGP---ILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGA 165
Cdd:PRK09463 133 GGLEFSAYAHSRVLQKLASRSGTLAVTVMVPNSL--GPgelLLHYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGS 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 166 ASTTA-----REEGDSWV---LNGTKAWITNSweASATVV---FASTDR-----SRQNKGISAFLVPMPTPGLTLGKKED 229
Cdd:PRK09463 211 IPDTGvvckgEWQGEEVLgmrLTWNKRYITLA--PIATVLglaFKLYDPdgllgDKEDLGITCALIPTDTPGVEIGRRHF 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 230 KLGIRasstanliF-------EDCRIPKENLLGEP---GMGFKIAMQTLDMGR-IGIASQALGIAQASLDCAVKYAENRH 298
Cdd:PRK09463 289 PLNVP--------FqngptrgKDVFIPLDYIIGGPkmaGQGWRMLMECLSVGRgISLPSNSTGGAKLAALATGAYARIRR 360
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1168286 299 AFGAPLTKLQNIQFKLADM---ALALESARLLTWRAAMLKDnkKPFTKeSAMAKLAASEAA-TAISHqAIQILGGMG 371
Cdd:PRK09463 361 QFKLPIGKFEGIEEPLARIagnAYLMDAARTLTTAAVDLGE--KPSVL-SAIAKYHLTERGrQVIND-AMDIHGGKG 433
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
274-396 |
1.15e-19 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 84.32 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 274 GIASQALGIAQASLDCAVKYAENR--HAFGAPLTKLQNIQFKLADMALALESARLLTWRAA----MLKDNKKPFT----K 343
Cdd:pfam08028 1 GIAAAALGAARAALAEFTERARGRvrAYFGVPLAEDPATQLALAEAAARIDAARLLLERAAarieAAAAAGKPVTpalrA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1168286 344 ESAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSE 396
Cdd:pfam08028 81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
137-397 |
3.03e-17 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 83.65 E-value: 3.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 137 QQWITPFTN----------GDKIGCF---ALSEPGNGSDAGAASTTA-REEGDSWVLNGTKaWITNSWEASATVVFASTD 202
Cdd:PRK11561 154 QDWLTPLLSdrydshllpgGQKRGLLigmGMTEKQGGSDVLSNTTRAeRLADGSYRLVGHK-WFFSVPQSDAHLVLAQAK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 203 rsrqnKGISAFLVPMPTP-----GLTLGKKEDKLGIRASSTANLIFEDCripKENLLGEPGMGFKiamQTLDMG---RIG 274
Cdd:PRK11561 233 -----GGLSCFFVPRFLPdgqrnAIRLERLKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIR---LILKMGgmtRFD 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 275 IASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDnKKPFTKESAMAKLAASE 354
Cdd:PRK11561 302 CALGSHGLMRRAFSVAIYHAHQRQVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWD-RRADAKEALWARLFTPA 380
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1168286 355 AATAISHQ-------AIQILGGMGYVTEMPAERYYRDARITEIYEGTSEI 397
Cdd:PRK11561 381 AKFVICKRgipfvaeAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNI 430
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
111-411 |
2.07e-15 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 78.36 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 111 STGVIMSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREE--GDSWVLN-----GTK 183
Cdd:PLN02636 136 SLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDplTDEFVINtpndgAIK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 184 AWITNSW-EASATVVFA-----STD-RSRQNKGISAFLVPMPT-------PGLTLGKKEDKLGIRASSTANLIFEDCRIP 249
Cdd:PLN02636 216 WWIGNAAvHGKFATVFArlklpTHDsKGVSDMGVHAFIVPIRDmkthqvlPGVEIRDCGHKVGLNGVDNGALRFRSVRIP 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 250 KENLLGEPG----------------MGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRHAFGAP------LTKL 307
Cdd:PLN02636 296 RDNLLNRFGdvsrdgkytsslptinKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPkqpeisILDY 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 308 QNIQFKLADM-----ALALESARLLTWRAAMLKDNKKPFTKEsaMAKLAASEAATAISHQAIQI------LGGMGYVTEM 376
Cdd:PLN02636 376 QSQQHKLMPMlastyAFHFATEYLVERYSEMKKTHDDQLVAD--VHALSAGLKAYITSYTAKALstcreaCGGHGYAAVN 453
|
330 340 350
....*....|....*....|....*....|....*
gi 1168286 377 PAERYYRDARITEIYEGTSEIQRLVIAGHLLRSYR 411
Cdd:PLN02636 454 RFGSLRNDHDIFQTFEGDNTVLLQQVAADLLKQYK 488
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
111-300 |
1.34e-14 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 75.58 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 111 STGVIMSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAAST--TAREEGDSWVLN-----GTK 183
Cdd:PLN02312 148 SLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETvtTYDPKTEEFVINtpcesAQK 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 184 AWITNSWE-ASATVVFASTDRSRQNKGISAFLVPMPT------PGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLG- 255
Cdd:PLN02312 228 YWIGGAANhATHTIVFSQLHINGKNEGVHAFIAQIRDqdgnicPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNs 307
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 256 ---------------EPGMGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRHAF 300
Cdd:PLN02312 308 vadvspdgkyvsaikDPDQRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 367
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
52-386 |
1.43e-13 |
|
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: 71.61 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 52 ELVPI----AAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCASTGVIMSVNN--SLYLG 125
Cdd:cd01159 5 DLAPLirerAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIVAthSRMLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 126 pilKFGSSQQKQQWitpftngdkigcfalsepGNGSDAGAAST-----TAREEGDSWVLNGTKAWITNSWEASATVVFAS 200
Cdd:cd01159 85 ---AFPPEAQEEVW------------------GDGPDTLLAGSyapggRAERVDGGYRVSGTWPFASGCDHADWILVGAI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 201 TDRSRQNKGISAFLVPMptPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGM------GFKIA---MQTLDMG 271
Cdd:cd01159 144 VEDDDGGPLPRAFVVPR--AEYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLTAGDMmagdgpGGSTPvyrMPLRQVF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 272 RIGIASQALGIAQASLDCAVKYAENR---HAFGAPLTKLQNIQFKLADMALALESARLL---TWRAAM--LKDNKKPFTK 343
Cdd:cd01159 222 PLSFAAVSLGAAEGALAEFLELAGKRvrqYGAAVKMAEAPITQLRLAEAAAELDAARAFlerATRDLWahALAGGPIDVE 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1168286 344 ESAMAKLAASEAATaISHQAIQIL----GGMGYVTEMPAERYYRDAR 386
Cdd:cd01159 302 ERARIRRDAAYAAK-LSAEAVDRLfhaaGGSALYTASPLQRIWRDIH 347
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
126-300 |
4.89e-12 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 67.56 E-value: 4.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 126 PILKF-GSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAR--EEGDSWVLNGTKAWITNSWE------ASATV 196
Cdd:PTZ00460 104 PAFQVlGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATydKQTNEFVIHTPSVEAVKFWPgelgflCNFAL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 197 VFASTDRSRQNKGISAFLVPM-------PTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLL--------------- 254
Cdd:PTZ00460 184 VYAKLIVNGKNKGVHPFMVRIrdkethkPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLaryikvsedgqverq 263
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1168286 255 GEPGMGFKIAMqtldMGRIGIASQALGIAQASLDCAVKYAENRHAF 300
Cdd:PTZ00460 264 GNPKVSYASMM----YMRNLIIDQYPRFAAQALTVAIRYSIYRQQF 305
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
131-254 |
1.79e-10 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 62.93 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168286 131 GSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAR--EEGDSWVLN-----GTKAWITNSWEASA-TVVFASTD 202
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATfdPKTDEFVIHsptltSSKWWPGGLGKVSThAVVYARLI 193
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168286 203 RSRQNKGISAFLVP-------MPTPGLTLGKKEDKLGIRASSTAN---LIFEDCRIPKENLL 254
Cdd:PLN02443 194 TNGKDHGIHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQML 255
|
|
| |
