|
Name |
Accession |
Description |
Interval |
E-value |
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
38-410 |
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: 687.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 38 ETHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCASTGVI 117
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 118 MSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASAT 197
Cdd:cd01158 81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 198 VVFASTDRSRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRIGI 277
Cdd:cd01158 161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 278 ASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAKLAASEA 357
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 11968090 358 ATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLLR 410
Cdd:cd01158 321 AMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
35-413 |
6.67e-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: 503.22 E-value: 6.67e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 35 ELPETHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCAST 114
Cdd:COG1960 4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 115 GVIMSVNNSLyLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEA 194
Cdd:COG1960 84 ALPVGVHNGA-AEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 195 SATVVFASTDRSRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGR 274
Cdd:COG1960 163 DVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 275 IGIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAKLAA 354
Cdd:COG1960 243 LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLFA 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 11968090 355 SEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLLRSYR 413
Cdd:COG1960 323 TEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
36-405 |
2.33e-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: 367.12 E-value: 2.33e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 36 LPETHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCASTG 115
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 116 VIMSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEAS 195
Cdd:cd01156 82 LSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDAD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 196 ATVVFASTDRSRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRI 275
Cdd:cd01156 162 TLVVYAKTDPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYERL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 276 GIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAKLAAS 355
Cdd:cd01156 242 VLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILYAA 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 11968090 356 EAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIA 405
Cdd:cd01156 322 EKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIG 371
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
38-405 |
1.52e-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: 358.13 E-value: 1.52e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 38 ETHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAmdvpeelsgagldylaysialeeisrgcastgvi 117
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLLGAA---------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 118 msvnnslylgPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASAT 197
Cdd:cd00567 47 ----------LLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 198 VVFASTDRS-RQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRIG 276
Cdd:cd00567 117 IVLARTDEEgPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 277 IASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDN-KKPFTKESAMAKLAAS 355
Cdd:cd00567 197 LAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQgPDEARLEAAMAKLFAT 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 11968090 356 EAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIA 405
Cdd:cd00567 277 EAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
36-410 |
2.25e-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: 352.13 E-value: 2.25e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 36 LPETHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCASTG 115
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 116 VIMSVNNsLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEAS 195
Cdd:cd01162 81 AYISIHN-MCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 196 ATVVFASTDRSRQnKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRI 275
Cdd:cd01162 160 VYVVMARTGGEGP-KGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 276 GIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKP-FTKESAMAKLAA 354
Cdd:cd01162 239 NIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPdAVKLCAMAKRFA 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 11968090 355 SEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLLR 410
Cdd:cd01162 319 TDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLT 374
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
35-412 |
1.92e-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: 327.89 E-value: 1.92e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 35 ELPETHQMLRQTCRDFAEKELVPiaAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGcAST 114
Cdd:cd01161 26 EQTEELNMLVGPVEKFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMD-LGF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 115 GVIMSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAR--EEGDSWVLNGTKAWITNSW 192
Cdd:cd01161 103 SVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVlsEDGKHYVLNGSKIWITNGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 193 EASATVVFASTDRSRQN----KGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQ 268
Cdd:cd01161 183 IADIFTVFAKTEVKDATgsvkDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMN 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 269 TLDMGRIGIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDN--KKPFTKE 346
Cdd:cd01161 263 ILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRglKAEYQIE 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11968090 347 SAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLLRSY 412
Cdd:cd01161 343 AAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQHA 408
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
36-409 |
5.24e-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: 317.99 E-value: 5.24e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 36 LPETHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCasTG 115
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGC--TG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 116 VIMSVN-NSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEA 194
Cdd:cd01157 79 VQTAIEaNSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 195 SATVVFASTD---RSRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLD 271
Cdd:cd01157 159 NWYFLLARSDpdpKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 272 MGRIGIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAK 351
Cdd:cd01157 239 KTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAK 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 11968090 352 LAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLL 409
Cdd:cd01157 319 AFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
38-409 |
1.63e-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: 314.05 E-value: 1.63e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 38 ETHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISR-GCASTGV 116
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARaGGSGPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 117 imSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASA 196
Cdd:cd01160 81 --SLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 197 TVVFASTDR-SRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRI 275
Cdd:cd01160 159 VIVVARTGGeARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 276 GIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAKLAAS 355
Cdd:cd01160 239 LIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWAT 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 11968090 356 EAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLL 409
Cdd:cd01160 319 ELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
13-410 |
1.36e-99 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 302.57 E-value: 1.36e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 13 GSLGRALRARDWRRLHTVYQSVELPETHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQ--VKKMGELGLLAMDVPEEL 90
Cdd:PLN02519 3 LSAAKARRRGLARRFSSSSSSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGITAPEEY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 91 SGAGLDYLAYSIALEEISRGCASTGVIMSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAAST 170
Cdd:PLN02519 83 GGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKC 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 171 TAREEGDSWVLNGTKAWITNSWEASATVVFASTDRSRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRI 250
Cdd:PLN02519 163 KAERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 251 PKENLLGEPGMGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLT 330
Cdd:PLN02519 243 PEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 331 WRAAMLKDNKKPFTKESAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLLR 410
Cdd:PLN02519 323 YSVARDCDNGKVDRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFK 402
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
36-405 |
4.23e-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: 290.41 E-value: 4.23e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 36 LPETHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAMdVPEELSGAGLDYLAYSIALEEISR---GCA 112
Cdd:cd01151 13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGA-TIKGYGCAGLSSVAYGLIAREVERvdsGYR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 113 STgviMSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSW 192
Cdd:cd01151 92 SF---MSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 193 EASATVVFASTDRSRQNKGisaFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLgePGM-GFKIAMQTLD 271
Cdd:cd01151 169 IADVFVVWARNDETGKIRG---FILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL--PGAeGLRGPFKCLN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 272 MGRIGIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAK 351
Cdd:cd01151 244 NARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLK 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 11968090 352 LAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIA 405
Cdd:cd01151 324 RNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILG 377
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
37-413 |
1.92e-74 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 237.91 E-value: 1.92e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 37 PEtHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCASTGV 116
Cdd:PTZ00461 39 PE-HAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 117 IMSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGD-SWVLNGTKAWITNSWEAS 195
Cdd:PTZ00461 118 AYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGTVAD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 196 ATVVFASTDRSrqnkgISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRI 275
Cdd:PTZ00461 198 VFLIYAKVDGK-----ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 276 GIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAmlkDNKKPFTKE---SAMAKL 352
Cdd:PTZ00461 273 TLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVS---HNVHPGNKNrlgSDAAKL 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 11968090 353 AASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLLRSYR 413
Cdd:PTZ00461 350 FATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLKGLK 410
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
48-413 |
2.56e-73 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 234.24 E-value: 2.56e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 48 RDFAEKELvpiaAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCASTGVImsvNNSLYLG 127
Cdd:PRK12341 22 RNFPEEYF----RTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCGAPAFLI---TNGQCIH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 128 PILKFGSSQQKQQWI-TPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASATVVFASTDRS 206
Cdd:PRK12341 95 SMRRFGSAEQLRKTAeSTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAKEYPYMLVLARDPQP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 207 R-QNKGISAFLVPMPTPGLTLGKKEdKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRIGIASQALGIA 285
Cdd:PRK12341 175 KdPKKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFEMERLINAARSLGFA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 286 QASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAKLAASEAATAISHQA 365
Cdd:PRK12341 254 ECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAALAKLYCARTAMEVIDDA 333
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 11968090 366 IQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQrLVIAGH-LLRSYR 413
Cdd:PRK12341 334 IQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIM-IYIAGRqILKDYQ 381
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
46-410 |
1.32e-64 |
|
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: 212.25 E-value: 1.32e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 46 TCRDFAEKELVPIAAQLDKE--------HLFPT---SQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCAST 114
Cdd:cd01153 4 EVARLAENVLAPLNADGDREgpvfddgrVVVPPpfkEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 115 GVIMSVNNSLYLgpILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGD-SWVLNGTKAWITNSWE 193
Cdd:cd01153 84 MYASGTQGAAAT--LLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGEH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 194 ASAT----VVFAST-DRSRQNKGISAFLVP-----MPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPkenLLGEPGMGF 263
Cdd:cd01153 162 DMSEnivhLVLARSeGAPPGVKGLSLFLVPkflddGERNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 264 KIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRHAFGAPL--------TKLQNIQFKLADMALALESARLLTWRAAM 335
Cdd:cd01153 239 AQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIkaapavtiIHHPDVRRSLMTQKAYAEGSRALDLYTAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 336 LKD--NKKPFTKESA------------MAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQR 401
Cdd:cd01153 319 VQDlaERKATEGEDRkalsaladlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQA 398
|
....*....
gi 11968090 402 LVIAGHLLR 410
Cdd:cd01153 399 LDLIGRKIV 407
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
31-405 |
1.62e-59 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 199.31 E-value: 1.62e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 31 YQSVEL--PEtHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAMDVpEELSGAGLDYLAYSIALEEIS 108
Cdd:PLN02526 23 YQFDDLltPE-EQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTI-KGYGCPGLSITASAIATAEVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 109 RGCASTGVIMSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWI 188
Cdd:PLN02526 101 RVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 189 TNSWEASATVVFAstdRSRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLgePGM-GFKIAM 267
Cdd:PLN02526 181 GNSTFADVLVIFA---RNTTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRL--PGVnSFQDTN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 268 QTLDMGRIGIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKES 347
Cdd:PLN02526 256 KVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHA 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 11968090 348 AMAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIA 405
Cdd:PLN02526 336 SLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTG 393
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
60-413 |
6.59e-59 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 196.59 E-value: 6.59e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 60 AQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCASTGVIMSVNNSLylGPILKFGSSQQKQ 139
Cdd:PRK03354 30 AECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPTYVLYQLPGGF--NTFLREGTQEQID 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 140 QWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASATVVFASTDRSRQNKGISAFLVPM 219
Cdd:PRK03354 108 KIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASPDKPVYTEWFVDM 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 220 PTPGLTLGKKEdKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENR 299
Cdd:PRK03354 188 SKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 300 HAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAKLAASEAATAISHQAIQILGGMGYVTEMP 379
Cdd:PRK03354 267 VQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHR 346
|
330 340 350
....*....|....*....|....*....|....
gi 11968090 380 AERYYRDARITEIYEGTSEIQRLVIAGHLLRSYR 413
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 ... |
260-405 |
1.07e-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: 1.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 260 GMGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDN 339
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11968090 340 KKPFTKESAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIA 405
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
73-409 |
2.05e-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: 184.86 E-value: 2.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 73 VKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCASTGVIMSVNNSLylGP-ILKFGSSQQKQQWITPFTNGDKI 151
Cdd:cd01152 41 QRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIGIDLA--GPtILAYGTDEQKRRFLPPILSGEEI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 152 GCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASATVVFASTD-RSRQNKGISAFLVPMPTPGLTLGKKE 230
Cdd:cd01152 119 WCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDpEAPKHRGISILLVDMDSPGVTVRPIR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 231 DKLGirASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRIGIASQAlGIAQASLDCAVKYAENRhafGAPLTKLQ 310
Cdd:cd01152 199 SING--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIGGSA-ATFFELLLARLLLLTRD---GRPLIDDP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 311 NIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAKLAASEAATAISHQAIQILGG---MGYVTEMPA-----ER 382
Cdd:cd01152 273 LVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFGSELAQELAELALELLGTaalLRDPAPGAElagrwEA 352
|
330 340
....*....|....*....|....*..
gi 11968090 383 YYRDARITEIYEGTSEIQRLVIAGHLL 409
Cdd:cd01152 353 DYLRSRATTIYGGTSEIQRNIIAERLL 379
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
41-405 |
2.17e-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: 2.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 41 QMLRQTCRDF-------AEKELVPIAAQLDKEHLFPTSQVKKMGE----LGLLAMDVPEELSGAGLDYLAYSIALEEISR 109
Cdd:cd01155 4 QELRARVKAFmeehvypAEQEFLEYYAEGGDRWWTPPPIIEKLKAkakaEGLWNLFLPEVSGLSGLTNLEYAYLAEETGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 110 --------GCAS--TGViMSVnnslylgpILKFGSSQQKQQWITPFTNGDKIGCFALSEPG-NGSDAGAASTTAREEGDS 178
Cdd:cd01155 84 sffapevfNCQApdTGN-MEV--------LHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 179 WVLNGTKAWITNSWEASATVV-------FASTDRSRQNkgiSAFLVPMPTPGLTLgkkedklgIRASST----------A 241
Cdd:cd01155 155 YVINGRKWWSSGAGDPRCKIAivmgrtdPDGAPRHRQQ---SMILVPMDTPGVTI--------IRPLSVfgyddaphghA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 242 NLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMAL 321
Cdd:cd01155 224 EITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 322 ALESARLLTWRAAMLKDNK--KPFTKESAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEI 399
Cdd:cd01155 304 EIEQARLLVLKAAHMIDTVgnKAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEV 383
|
....*.
gi 11968090 400 QRLVIA 405
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 ... |
37-149 |
5.08e-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: 5.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 37 PETHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCASTGV 116
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|...
gi 11968090 117 IMSVNNSLYLGPILKFGSSQQKQQWITPFTNGD 149
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
139-402 |
4.55e-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: 4.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 139 QQWITPFTNGD-----KIGCFaLSEPGNGSDAGAASTTA-REEGDSWVLNGTKaWITNSWEASATVVFASTDRSRQN-KG 211
Cdd:cd01154 132 KQYLPGLLSDRyktglLGGTW-MTEKQGGSDLGANETTAeRSGGGVYRLNGHK-WFASAPLADAALVLARPEGAPAGaRG 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 212 ISAFLVPMPTPGLTLGKKE-----DKLGIRASSTANLIFEDCripKENLLGEPGMGFKIAMQTLDMGRIGIASQALGIAQ 286
Cdd:cd01154 210 LSLFLVPRLLEDGTRNGYRirrlkDKLGTRSVATGEVEFDDA---EAYLIGDEGKGIYYILEMLNISRLDNAVAALGIMR 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 287 ASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAM--------AKLAASEAA 358
Cdd:cd01154 287 RALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKPVEAHmarlatpvAKLIACKRA 366
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 11968090 359 TAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRL 402
Cdd:cd01154 367 APVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQAL 410
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
50-402 |
1.20e-30 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 123.82 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 50 FAEKELVPIAAQLDKE--HLFPTSQV----------KKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISrgCASTGVI 117
Cdd:PTZ00456 70 LATQTLLPLYESSDSEgcVLLKDGNVttpkgfkeayQALKAGGWTGISEPEEYGGQALPLSVGFITRELMA--TANWGFS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 118 MSVNNSL-YLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGD-SWVLNGTKAWIT----NS 191
Cdd:PTZ00456 148 MYPGLSIgAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISagdhDL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 192 WEASATVVFASTDRSR-QNKGISAFLVP--MPTPGLTLGKK--------EDKLGIRASSTANLIFEDcriPKENLLGEPG 260
Cdd:PTZ00456 228 TENIVHIVLARLPNSLpTTKGLSLFLVPrhVVKPDGSLETAknvkciglEKKMGIKGSSTCQLSFEN---SVGYLIGEPN 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 261 MGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRHAFGA---------PLTKL-------QNIQFKLA----DMA 320
Cdd:PTZ00456 305 AGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRSMRAlsgtkepekPADRIichanvrQNILFAKAvaegGRA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 321 LALESARLL---------TWRAAMlkDNKKPFTkeSAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITE 391
Cdd:PTZ00456 385 LLLDVGRLLdihaaakdaATREAL--DHEIGFY--TPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGT 460
|
410
....*....|.
gi 11968090 392 IYEGTSEIQRL 402
Cdd:PTZ00456 461 LYEGTTGIQAL 471
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
153-246 |
8.00e-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: 110.83 E-value: 8.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 153 CFALSEPGNGSDAGA-ASTTAREEGDSWVLNGTKAWITNSWEASATVVFASTDRSRQNKGISAFLVPMPTPGLTLGKKED 231
Cdd:pfam02770 1 AFALTEPGAGSDVASlKTTAADGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 11968090 232 KLGIRASSTANLIFE 246
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
88-405 |
1.46e-29 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 121.44 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 88 EELSGAGLDYLAYSIALEEISR----------GCASTGViMSVnnslylgpILKFGSSQQKQQWITPFTNGDKIGCFALS 157
Cdd:PLN02876 487 DQLLGAGLSNLEYGYLCEIMGRsvwapqvfncGAPDTGN-MEV--------LLRYGNKEQQLEWLIPLLEGKIRSGFAMT 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 158 EPG-NGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASATV--VFASTDRSR-QNKGISAFLVPMPTPGLTLGKKEDKL 233
Cdd:PLN02876 558 EPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPRCRVliVMGKTDFNApKHKQQSMILVDIQTPGVQIKRPLLVF 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 234 GIRAS--STANLIFEDCRIPKEN-LLGEpGMGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQ 310
Cdd:PLN02876 638 GFDDAphGHAEISFENVRVPAKNiLLGE-GRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHG 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 311 NIQFKLADMALALESARLLTWRAAMLKD---NKKPfTKESAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDA 387
Cdd:PLN02876 717 SFLSDLAKCRVELEQTRLLVLEAADQLDrlgNKKA-RGIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATA 795
|
330
....*....|....*...
gi 11968090 388 RITEIYEGTSEIQRLVIA 405
Cdd:PLN02876 796 RTLRIADGPDEVHLGTIA 813
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
23-373 |
1.53e-29 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 121.22 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 23 DWRRLHTvYQSVELPETHQmlrqtcrDFAEKELVPIAAQLDKehlFPTSQVKK---------MGELGLLAMDVPEELSGA 93
Cdd:PRK13026 66 DWQKLHS-YPKPTLTAEEQ-------AFIDNEVETLLTMLDD---WDIVQNRKdlppevwdyLKKEGFFALIIPKEYGGK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 94 GLDYLAYSIALEEISRGCASTGVIMSVNNSLylGP---ILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAAST 170
Cdd:PRK13026 135 GFSAYANSTIVSKIATRSVSAAVTVMVPNSL--GPgelLTHYGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPD 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 171 TA-----REEGDSWV---LNGTKAWITNSweASATVV---FASTD-----RSRQNKGISAFLVPMPTPGLTLGKKEDKLG 234
Cdd:PRK13026 213 TGivcrgEFEGEEVLglrLTWDKRYITLA--PVATVLglaFKLRDpdgllGDKKELGITCALIPTDHPGVEIGRRHNPLG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 235 IRasstanliF-------EDCRIPKENLLGEP---GMGFKIAMQTLDMGRiGIASQALGIAQASLdcAVK----YAENRH 300
Cdd:PRK13026 291 MA--------FmngttrgKDVFIPLDWIIGGPdyaGRGWRMLVECLSAGR-GISLPALGTASGHM--ATRttgaYAYVRR 359
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11968090 301 AFGAPLTKLQNIQFKLADMA---LALESARLLTwrAAMLKDNKKPfTKESAMAKLAASEAATAISHQAIQILGGMG 373
Cdd:PRK13026 360 QFGMPIGQFEGVQEALARIAgntYLLEAARRLT--TTGLDLGVKP-SVVTAIAKYHMTELARDVVNDAMDIHAGKG 432
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
72-414 |
2.84e-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: 2.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 72 QVKKMGELGLlamDVPEElsgagldYLAYSIALEEISrgcASTGVIMSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKI 151
Cdd:cd01150 69 DVERMGELMA---DDPEK-------MLALTNSLGGYD---LSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEII 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 152 GCFALSEPGNGSDAGAASTTAR--EEGDSWVLN-----GTKAWITN-SWEASATVVFASTDRSRQNKGISAFLVPM---- 219
Cdd:cd01150 136 GCFAQTELGHGSNLQGLETTATydPLTQEFVINtpdftATKWWPGNlGKTATHAVVFAQLITPGKNHGLHAFIVPIrdpk 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 220 ---PTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLG----------------EPGMGFKIAMQTLDMGRIGIASQ 280
Cdd:cd01150 216 thqPLPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNrfgdvspdgtyvspfkDPNKRYGAMLGTRSGGRVGLIYD 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 281 ALGIAQASLDCAVKYAENRHAFG-------APLTKLQNIQFKLADMalaLESARLLTWRAAMLKDNKKPFTKESAMAK-- 351
Cdd:cd01150 296 AAMSLKKAATIAIRYSAVRRQFGpkpsdpeVQILDYQLQQYRLFPQ---LAAAYAFHFAAKSLVEMYHEIIKELLQGNse 372
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11968090 352 -------LAASEAATAISH--QAIQIL----GGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLLRSYRS 414
Cdd:cd01150 373 llaelhaLSAGLKAVATWTaaQGIQECreacGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQ 448
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
54-388 |
1.27e-22 |
|
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: 98.55 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 54 ELVPIAAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCASTGVIMSvNNSLYLGPILKFG 133
Cdd:cd01163 9 RIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALR-AHFGFVEALLLAG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 134 SSQQKQQWITPFTNGDKIGCfALSEPGnGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASATVVFASTDRSRQnkgiS 213
Cdd:cd01163 88 PEQFRKRWFGRVLNGWIFGN-AVSERG-SVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGKL----V 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 214 AFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLdMGRIGIASQALGIAQASLDCAV 293
Cdd:cd01163 162 FAAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPNAPDRGTLLTA-IYQLVLAAVLAGIARAALDDAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 294 KYAENR-----HAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDN--KKPFTKE----------SAMAKLAASE 356
Cdd:cd01163 241 AYVRSRtrpwiHSGAESARDDPYVQQVVGDLAARLHAAEALVLQAARALDAaaAAGTALTaeargeaalaVAAAKVVVTR 320
|
330 340 350
....*....|....*....|....*....|..
gi 11968090 357 AATAISHQAIQILGGMGYVTEMPAERYYRDAR 388
Cdd:cd01163 321 LALDATSRLFEVGGASATAREHNLDRHWRNAR 352
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
23-373 |
1.37e-21 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 97.19 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 23 DWRRLHTvYQSVELPETHQM-----LRQTCR---DFA----EKELVPIAAQLDKEHlfptsqvkkmgelGLLAMDVPEEL 90
Cdd:PRK09463 67 DWKKLLN-YPKPTLTAEEQAfldgpVEELCRmvnDWQitheLADLPPEVWQFIKEH-------------GFFGMIIPKEY 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 91 SGAGLDYLAYSIALEEISRGCASTGVIMSVNNSLylGP---ILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGA 167
Cdd:PRK09463 133 GGLEFSAYAHSRVLQKLASRSGTLAVTVMVPNSL--GPgelLLHYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGS 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 168 ASTTA-----REEGDSWV---LNGTKAWITNSweASATVV---FASTDR-----SRQNKGISAFLVPMPTPGLTLGKKED 231
Cdd:PRK09463 211 IPDTGvvckgEWQGEEVLgmrLTWNKRYITLA--PIATVLglaFKLYDPdgllgDKEDLGITCALIPTDTPGVEIGRRHF 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 232 KLGIRasstanliF-------EDCRIPKENLLGEP---GMGFKIAMQTLDMGR-IGIASQALGIAQASLDCAVKYAENRH 300
Cdd:PRK09463 289 PLNVP--------FqngptrgKDVFIPLDYIIGGPkmaGQGWRMLMECLSVGRgISLPSNSTGGAKLAALATGAYARIRR 360
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11968090 301 AFGAPLTKLQNIQFKLADM---ALALESARLLTWRAAMLKDnkKPFTKeSAMAKLAASEAA-TAISHqAIQILGGMG 373
Cdd:PRK09463 361 QFKLPIGKFEGIEEPLARIagnAYLMDAARTLTTAAVDLGE--KPSVL-SAIAKYHLTERGrQVIND-AMDIHGGKG 433
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
276-398 |
1.11e-19 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 84.32 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 276 GIASQALGIAQASLDCAVKYAENR--HAFGAPLTKLQNIQFKLADMALALESARLLTWRAA----MLKDNKKPFT----K 345
Cdd:pfam08028 1 GIAAAALGAARAALAEFTERARGRvrAYFGVPLAEDPATQLALAEAAARIDAARLLLERAAarieAAAAAGKPVTpalrA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 11968090 346 ESAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSE 398
Cdd:pfam08028 81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
139-399 |
3.08e-17 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 83.65 E-value: 3.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 139 QQWITPFTN----------GDKIGCF---ALSEPGNGSDAGAASTTA-REEGDSWVLNGTKaWITNSWEASATVVFASTD 204
Cdd:PRK11561 154 QDWLTPLLSdrydshllpgGQKRGLLigmGMTEKQGGSDVLSNTTRAeRLADGSYRLVGHK-WFFSVPQSDAHLVLAQAK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 205 rsrqnKGISAFLVPMPTP-----GLTLGKKEDKLGIRASSTANLIFEDCripKENLLGEPGMGFKiamQTLDMG---RIG 276
Cdd:PRK11561 233 -----GGLSCFFVPRFLPdgqrnAIRLERLKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIR---LILKMGgmtRFD 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 277 IASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDnKKPFTKESAMAKLAASE 356
Cdd:PRK11561 302 CALGSHGLMRRAFSVAIYHAHQRQVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWD-RRADAKEALWARLFTPA 380
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 11968090 357 AATAISHQ-------AIQILGGMGYVTEMPAERYYRDARITEIYEGTSEI 399
Cdd:PRK11561 381 AKFVICKRgipfvaeAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNI 430
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
113-413 |
2.16e-15 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 77.98 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 113 STGVIMSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREE--GDSWVLN-----GTK 185
Cdd:PLN02636 136 SLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDplTDEFVINtpndgAIK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 186 AWITNSW-EASATVVFA-----STD-RSRQNKGISAFLVPMPT-------PGLTLGKKEDKLGIRASSTANLIFEDCRIP 251
Cdd:PLN02636 216 WWIGNAAvHGKFATVFArlklpTHDsKGVSDMGVHAFIVPIRDmkthqvlPGVEIRDCGHKVGLNGVDNGALRFRSVRIP 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 252 KENLLGEPG----------------MGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRHAFGAP------LTKL 309
Cdd:PLN02636 296 RDNLLNRFGdvsrdgkytsslptinKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPkqpeisILDY 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 310 QNIQFKLADM-----ALALESARLLTWRAAMLKDNKKPFTKEsaMAKLAASEAATAISHQAIQI------LGGMGYVTEM 378
Cdd:PLN02636 376 QSQQHKLMPMlastyAFHFATEYLVERYSEMKKTHDDQLVAD--VHALSAGLKAYITSYTAKALstcreaCGGHGYAAVN 453
|
330 340 350
....*....|....*....|....*....|....*
gi 11968090 379 PAERYYRDARITEIYEGTSEIQRLVIAGHLLRSYR 413
Cdd:PLN02636 454 RFGSLRNDHDIFQTFEGDNTVLLQQVAADLLKQYK 488
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
113-302 |
1.38e-14 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 75.58 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 113 STGVIMSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAAST--TAREEGDSWVLN-----GTK 185
Cdd:PLN02312 148 SLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETvtTYDPKTEEFVINtpcesAQK 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 186 AWITNSWE-ASATVVFASTDRSRQNKGISAFLVPMPT------PGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLG- 257
Cdd:PLN02312 228 YWIGGAANhATHTIVFSQLHINGKNEGVHAFIAQIRDqdgnicPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNs 307
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 258 ---------------EPGMGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRHAF 302
Cdd:PLN02312 308 vadvspdgkyvsaikDPDQRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 367
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
54-388 |
1.75e-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: 71.23 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 54 ELVPI----AAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCASTGVIMSVNN--SLYLG 127
Cdd:cd01159 5 DLAPLirerAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIVAthSRMLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 128 pilKFGSSQQKQQWitpftngdkigcfalsepGNGSDAGAAST-----TAREEGDSWVLNGTKAWITNSWEASATVVFAS 202
Cdd:cd01159 85 ---AFPPEAQEEVW------------------GDGPDTLLAGSyapggRAERVDGGYRVSGTWPFASGCDHADWILVGAI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 203 TDRSRQNKGISAFLVPMptPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGM------GFKIA---MQTLDMG 273
Cdd:cd01159 144 VEDDDGGPLPRAFVVPR--AEYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLTAGDMmagdgpGGSTPvyrMPLRQVF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 274 RIGIASQALGIAQASLDCAVKYAENR---HAFGAPLTKLQNIQFKLADMALALESARLL---TWRAAM--LKDNKKPFTK 345
Cdd:cd01159 222 PLSFAAVSLGAAEGALAEFLELAGKRvrqYGAAVKMAEAPITQLRLAEAAAELDAARAFlerATRDLWahALAGGPIDVE 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 11968090 346 ESAMAKLAASEAATaISHQAIQIL----GGMGYVTEMPAERYYRDAR 388
Cdd:cd01159 302 ERARIRRDAAYAAK-LSAEAVDRLfhaaGGSALYTASPLQRIWRDIH 347
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
128-302 |
4.96e-12 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 67.56 E-value: 4.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 128 PILKF-GSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAR--EEGDSWVLNGTKAWITNSWE------ASATV 198
Cdd:PTZ00460 104 PAFQVlGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATydKQTNEFVIHTPSVEAVKFWPgelgflCNFAL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 199 VFASTDRSRQNKGISAFLVPM-------PTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLL--------------- 256
Cdd:PTZ00460 184 VYAKLIVNGKNKGVHPFMVRIrdkethkPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLaryikvsedgqverq 263
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 11968090 257 GEPGMGFKIAMqtldMGRIGIASQALGIAQASLDCAVKYAENRHAF 302
Cdd:PTZ00460 264 GNPKVSYASMM----YMRNLIIDQYPRFAAQALTVAIRYSIYRQQF 305
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
133-256 |
1.81e-10 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 62.93 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11968090 133 GSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAR--EEGDSWVLN-----GTKAWITNSWEASA-TVVFASTD 204
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATfdPKTDEFVIHsptltSSKWWPGGLGKVSThAVVYARLI 193
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 11968090 205 RSRQNKGISAFLVP-------MPTPGLTLGKKEDKLGIRASSTAN---LIFEDCRIPKENLL 256
Cdd:PLN02443 194 TNGKDHGIHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQML 255
|
|
| |
