|
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: 684.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 36 ETHQMLRQTCRDFAEKELVPIAAQLDREHLFPTAQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRACASTGVI 115
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 116 MSVNNSLYLGPILKFGSAQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASAT 195
Cdd:cd01158 81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 196 VVFASTDRSRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRIGI 275
Cdd:cd01158 161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 276 ASQALGIAQASLDCAVKYAENRNAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAKLAASEA 355
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 74199397 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 |
4.55e-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: 4.55e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 33 ELPETHQMLRQTCRDFAEKELVPIAAQLDREHLFPTAQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRACAST 112
Cdd:COG1960 4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 113 GVIMSVNNSLyLGPILKFGSAQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEA 192
Cdd:COG1960 84 ALPVGVHNGA-AEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 193 SATVVFASTDRSRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGR 272
Cdd:COG1960 163 DVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 273 IGIASQALGIAQASLDCAVKYAENRNAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAKLAA 352
Cdd:COG1960 243 LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLFA 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 74199397 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 |
3.54e-127 |
|
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: 371.74 E-value: 3.54e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 34 LPETHQMLRQTCRDFAEKELVPIAAQLDREHLFPTAQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRACASTG 113
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 114 VIMSVNNSLYLGPILKFGSAQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEAS 193
Cdd:cd01156 82 LSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDAD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 194 ATVVFASTDRSRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRI 273
Cdd:cd01156 162 TLVVYAKTDPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYERL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 274 GIASQALGIAQASLDCAVKYAENRNAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAKLAAS 353
Cdd:cd01156 242 VLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILYAA 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 74199397 354 EAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIA 403
Cdd:cd01156 322 EKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIG 371
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
36-403 |
6.60e-123 |
|
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: 358.91 E-value: 6.60e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 36 ETHQMLRQTCRDFAEKELVPIAAQLDREHLFPTAQVKKMGELGLLAmdvpeelsgagldylaysialeeisracastgvi 115
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLLGAA---------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 116 msvnnslylgPILKFGSAQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASAT 195
Cdd:cd00567 47 ----------LLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 196 VVFASTDRS-RQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRIG 274
Cdd:cd00567 117 IVLARTDEEgPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 275 IASQALGIAQASLDCAVKYAENRNAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDN-KKPFTKESAMAKLAAS 353
Cdd:cd00567 197 LAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQgPDEARLEAAMAKLFAT 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 74199397 354 EAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIA 403
Cdd:cd00567 277 EAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
34-408 |
2.29e-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: 351.75 E-value: 2.29e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 34 LPETHQMLRQTCRDFAEKELVPIAAQLDREHLFPTAQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRACASTG 113
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 114 VIMSVNNsLYLGPILKFGSAQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEAS 193
Cdd:cd01162 81 AYISIHN-MCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 194 ATVVFASTDRSRQnKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRI 273
Cdd:cd01162 160 VYVVMARTGGEGP-KGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 274 GIASQALGIAQASLDCAVKYAENRNAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKP-FTKESAMAKLAA 352
Cdd:cd01162 239 NIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPdAVKLCAMAKRFA 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 74199397 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 |
1.78e-110 |
|
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: 330.58 E-value: 1.78e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 33 ELPETHQMLRQTCRDFAEKELVPiaAQLDREHLFPTAQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRAcAST 112
Cdd:cd01161 26 EQTEELNMLVGPVEKFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMD-LGF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 113 GVIMSVNNSLYLGPILKFGSAQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAR--EEGDSWVLNGTKAWITNSW 190
Cdd:cd01161 103 SVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVlsEDGKHYVLNGSKIWITNGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 191 EASATVVFASTDRSRQN----KGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQ 266
Cdd:cd01161 183 IADIFTVFAKTEVKDATgsvkDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMN 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 267 TLDMGRIGIASQALGIAQASLDCAVKYAENRNAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDN--KKPFTKE 344
Cdd:cd01161 263 ILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRglKAEYQIE 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74199397 345 SAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLLRSY 410
Cdd:cd01161 343 AAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQHA 408
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
36-407 |
3.44e-105 |
|
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: 315.59 E-value: 3.44e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 36 ETHQMLRQTCRDFAEKELVPIAAQLDREHLFPTAQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRACAStGVI 115
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGS-GPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 116 MSVNNSLYLGPILKFGSAQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASAT 195
Cdd:cd01160 80 LSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 196 VVFASTDR-SRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRIG 274
Cdd:cd01160 160 IVVARTGGeARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 275 IASQALGIAQASLDCAVKYAENRNAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAKLAASE 354
Cdd:cd01160 240 IAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATE 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 74199397 355 AATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLL 407
Cdd:cd01160 320 LQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
34-407 |
6.91e-105 |
|
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: 314.91 E-value: 6.91e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 34 LPETHQMLRQTCRDFAEKELVPIAAQLDREHLFPTAQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRACasTG 113
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGC--TG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 114 VIMSVN-NSLYLGPILKFGSAQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEA 192
Cdd:cd01157 79 VQTAIEaNSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 193 SATVVFASTD---RSRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLD 269
Cdd:cd01157 159 NWYFLLARSDpdpKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 270 MGRIGIASQALGIAQASLDCAVKYAENRNAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAK 349
Cdd:cd01157 239 KTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAK 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 74199397 350 LAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLL 407
Cdd:cd01157 319 AFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
13-408 |
1.01e-99 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 302.57 E-value: 1.01e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 13 LRRALGVRDWRRLHTVY----QSVELPETHQMLRQTCRDFAEKELVPIAAQLDREHLFPTAQ--VKKMGELGLLAMDVPE 86
Cdd:PLN02519 1 MLLSAAKARRRGLARRFssssSSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGITAPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 87 ELSGAGLDYLAYSIALEEISRACASTGVIMSVNNSLYLGPILKFGSAQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAA 166
Cdd:PLN02519 81 EYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 167 STTAREEGDSWVLNGTKAWITNSWEASATVVFASTDRSRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDC 246
Cdd:PLN02519 161 KCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 247 RIPKENLLGEPGMGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRNAFGAPLTKLQNIQFKLADMALALESARL 326
Cdd:PLN02519 241 FVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 327 LTWRAAMLKDNKKPFTKESAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHL 406
Cdd:PLN02519 321 YVYSVARDCDNGKVDRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGREL 400
|
..
gi 74199397 407 LR 408
Cdd:PLN02519 401 FK 402
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
34-403 |
5.65e-97 |
|
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: 295.04 E-value: 5.65e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 34 LPETHQMLRQTCRDFAEKELVPIAAQLDREHLFPTAQVKKMGELGLLAMdVPEELSGAGLDYLAYSIALEEISRACASTG 113
Cdd:cd01151 13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGA-TIKGYGCAGLSSVAYGLIAREVERVDSGYR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 114 VIMSVNNSLYLGPILKFGSAQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEAS 193
Cdd:cd01151 92 SFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 194 ATVVFASTDRSRQNKGisaFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLgePGM-GFKIAMQTLDMGR 272
Cdd:cd01151 172 VFVVWARNDETGKIRG---FILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL--PGAeGLRGPFKCLNNAR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 273 IGIASQALGIAQASLDCAVKYAENRNAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAKLAA 352
Cdd:cd01151 247 YGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLKRNN 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 74199397 353 SEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIA 403
Cdd:cd01151 327 CGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILG 377
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
35-411 |
6.06e-75 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 239.07 E-value: 6.06e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 35 PEtHQMLRQTCRDFAEKELVPIAAQLDREHLFPTAQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRACASTGV 114
Cdd:PTZ00461 39 PE-HAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 115 IMSVNNSLYLGPILKFGSAQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGD-SWVLNGTKAWITNSWEAS 193
Cdd:PTZ00461 118 AYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGTVAD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 194 ATVVFASTDRSrqnkgISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRI 273
Cdd:PTZ00461 198 VFLIYAKVDGK-----ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 274 GIASQALGIAQASLDCAVKYAENRNAFGAPLTKLQNIQFKLADMALALESARLLTWRAAmlkDNKKPFTKE---SAMAKL 350
Cdd:PTZ00461 273 TLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVS---HNVHPGNKNrlgSDAAKL 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74199397 351 AASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLLRSYR 411
Cdd:PTZ00461 350 FATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLKGLK 410
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
46-411 |
5.20e-74 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 235.78 E-value: 5.20e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 46 RDFAEKELvpiaAQLDREHLFPTAQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRACASTGVImsvNNSLYLG 125
Cdd:PRK12341 22 RNFPEEYF----RTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCGAPAFLI---TNGQCIH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 126 PILKFGSAQQKQQWI-TPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASATVVFASTDRS 204
Cdd:PRK12341 95 SMRRFGSAEQLRKTAeSTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAKEYPYMLVLARDPQP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 205 R-QNKGISAFLVPMPTPGLTLGKKEdKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRIGIASQALGIA 283
Cdd:PRK12341 175 KdPKKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFEMERLINAARSLGFA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 284 QASLDCAVKYAENRNAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAKLAASEAATAISHQA 363
Cdd:PRK12341 254 ECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAALAKLYCARTAMEVIDDA 333
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 74199397 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 |
8.95e-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: 8.95e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 44 TCRDFAEKELVPIAAQLDRE--------HLFPTA---QVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRACAST 112
Cdd:cd01153 4 EVARLAENVLAPLNADGDREgpvfddgrVVVPPPfkeALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 113 GVIMSVNNSLYLgpILKFGSAQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGD-SWVLNGTKAWITNSWE 191
Cdd:cd01153 84 MYASGTQGAAAT--LLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGEH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 192 ASAT----VVFAST-DRSRQNKGISAFLVP-----MPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPkenLLGEPGMGF 261
Cdd:cd01153 162 DMSEnivhLVLARSeGAPPGVKGLSLFLVPkflddGERNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 262 KIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRNAFGAPL--------TKLQNIQFKLADMALALESARLLTWRAAM 333
Cdd:cd01153 239 AQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIkaapavtiIHHPDVRRSLMTQKAYAEGSRALDLYTAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 334 LKD--NKKPFTKESA------------MAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQR 399
Cdd:cd01153 319 VQDlaERKATEGEDRkalsaladlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQA 398
|
....*....
gi 74199397 400 LVIAGHLLR 408
Cdd:cd01153 399 LDLIGRKIV 407
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
58-411 |
6.45e-60 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 199.29 E-value: 6.45e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 58 AQLDREHLFPTAQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRACASTGVIMSVNNSLylGPILKFGSAQQKQ 137
Cdd:PRK03354 30 AECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPTYVLYQLPGGF--NTFLREGTQEQID 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 138 QWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASATVVFASTDRSRQNKGISAFLVPM 217
Cdd:PRK03354 108 KIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASPDKPVYTEWFVDM 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 218 PTPGLTLGKKEdKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENR 297
Cdd:PRK03354 188 SKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 298 NAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAKLAASEAATAISHQAIQILGGMGYVTEMP 377
Cdd:PRK03354 267 VQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHR 346
|
330 340 350
....*....|....*....|....*....|....
gi 74199397 378 AERYYRDARITEIYEGTSEIQRLVIAGHLLRSYR 411
Cdd:PRK03354 347 ISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQYR 380
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
29-403 |
1.16e-59 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 199.31 E-value: 1.16e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 29 YQSVEL--PEtHQMLRQTCRDFAEKELVPIAAQLDREHLFPTAQVKKMGELGLLAMDVpEELSGAGLDYLAYSIALEEIS 106
Cdd:PLN02526 23 YQFDDLltPE-EQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTI-KGYGCPGLSITASAIATAEVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 107 RACASTGVIMSVNNSLYLGPILKFGSAQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWI 186
Cdd:PLN02526 101 RVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 187 TNSWEASATVVFAstdRSRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLgePGM-GFKIAM 265
Cdd:PLN02526 181 GNSTFADVLVIFA---RNTTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRL--PGVnSFQDTN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 266 QTLDMGRIGIASQALGIAQASLDCAVKYAENRNAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKES 345
Cdd:PLN02526 256 KVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHA 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 74199397 346 AMAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIA 403
Cdd:PLN02526 336 SLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTG 393
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
258-403 |
8.57e-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: 178.22 E-value: 8.57e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 258 GMGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRNAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDN 337
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74199397 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 |
8.99e-55 |
|
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: 8.99e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 71 VKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRACASTGVIMSVNNSLylGP-ILKFGSAQQKQQWITPFTNGDKI 149
Cdd:cd01152 41 QRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIGIDLA--GPtILAYGTDEQKRRFLPPILSGEEI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 150 GCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASATVVFASTD-RSRQNKGISAFLVPMPTPGLTLGKKE 228
Cdd:cd01152 119 WCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDpEAPKHRGISILLVDMDSPGVTVRPIR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 229 DKLGirASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRIGIASQAlGIAQASLDCAVKYAenrNAFGAPLTKLQ 308
Cdd:cd01152 199 SING--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIGGSA-ATFFELLLARLLLL---TRDGRPLIDDP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 309 NIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAMAKLAASEAATAISHQAIQILGG---MGYVTEMPA-----ER 380
Cdd:cd01152 273 LVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFGSELAQELAELALELLGTaalLRDPAPGAElagrwEA 352
|
330 340
....*....|....*....|....*..
gi 74199397 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 |
9.74e-52 |
|
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: 177.97 E-value: 9.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 39 QMLRQTCRDF-------AEKELVPIAAQLDREHLFPTAQVKKMGE----LGLLAMDVPEELSGAGLDYLAYSIALEEISR 107
Cdd:cd01155 4 QELRARVKAFmeehvypAEQEFLEYYAEGGDRWWTPPPIIEKLKAkakaEGLWNLFLPEVSGLSGLTNLEYAYLAEETGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 108 A--------CAS--TGViMSVnnslylgpILKFGSAQQKQQWITPFTNGDKIGCFALSEPG-NGSDAGAASTTAREEGDS 176
Cdd:cd01155 84 SffapevfnCQApdTGN-MEV--------LHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 177 WVLNGTKAWITNSWEASATVV-------FASTDRSRQNkgiSAFLVPMPTPGLTLgkkedklgIRASST----------A 239
Cdd:cd01155 155 YVINGRKWWSSGAGDPRCKIAivmgrtdPDGAPRHRQQ---SMILVPMDTPGVTI--------IRPLSVfgyddaphghA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 240 NLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRNAFGAPLTKLQNIQFKLADMAL 319
Cdd:cd01155 224 EITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 320 ALESARLLTWRAAMLKDNK--KPFTKESAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEI 397
Cdd:cd01155 304 EIEQARLLVLKAAHMIDTVgnKAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEV 383
|
....*.
gi 74199397 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 |
3.76e-48 |
|
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: 159.55 E-value: 3.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 35 PETHQMLRQTCRDFAEKELVPIAAQLDREHLFPTAQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRACASTGV 114
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|...
gi 74199397 115 IMSVNNSLYLGPILKFGSAQQKQQWITPFTNGD 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 |
3.74e-44 |
|
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: 158.69 E-value: 3.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 137 QQWITPFTNGD-----KIGCFaLSEPGNGSDAGAASTTA-REEGDSWVLNGTKaWITNSWEASATVVFASTDRSRQN-KG 209
Cdd:cd01154 132 KQYLPGLLSDRyktglLGGTW-MTEKQGGSDLGANETTAeRSGGGVYRLNGHK-WFASAPLADAALVLARPEGAPAGaRG 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 210 ISAFLVPMPTPGLTLGKKE-----DKLGIRASSTANLIFEDCripKENLLGEPGMGFKIAMQTLDMGRIGIASQALGIAQ 284
Cdd:cd01154 210 LSLFLVPRLLEDGTRNGYRirrlkDKLGTRSVATGEVEFDDA---EAYLIGDEGKGIYYILEMLNISRLDNAVAALGIMR 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 285 ASLDCAVKYAENRNAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDNKKPFTKESAM--------AKLAASEAA 356
Cdd:cd01154 287 RALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKPVEAHmarlatpvAKLIACKRA 366
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 74199397 357 TAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSEIQRL 400
Cdd:cd01154 367 APVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQAL 410
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
48-400 |
8.11e-32 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 127.29 E-value: 8.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 48 FAEKELVPIAAQLDRE--HLFPTAQV----------KKMGELGLLAMDVPEELSGAGLDYLAYSIALEEIsrACASTGVI 115
Cdd:PTZ00456 70 LATQTLLPLYESSDSEgcVLLKDGNVttpkgfkeayQALKAGGWTGISEPEEYGGQALPLSVGFITRELM--ATANWGFS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 116 MSVNNSL-YLGPILKFGSAQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGD-SWVLNGTKAWIT----NS 189
Cdd:PTZ00456 148 MYPGLSIgAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISagdhDL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 190 WEASATVVFASTDRSR-QNKGISAFLVP--MPTPGLTLGKK--------EDKLGIRASSTANLIFEDcriPKENLLGEPG 258
Cdd:PTZ00456 228 TENIVHIVLARLPNSLpTTKGLSLFLVPrhVVKPDGSLETAknvkciglEKKMGIKGSSTCQLSFEN---SVGYLIGEPN 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 259 MGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRNAFGA---------PLTKL-------QNIQFKLA----DMA 318
Cdd:PTZ00456 305 AGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRSMRAlsgtkepekPADRIichanvrQNILFAKAvaegGRA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 319 LALESARLL---------TWRAAMlkDNKKPFTkeSAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITE 389
Cdd:PTZ00456 385 LLLDVGRLLdihaaakdaATREAL--DHEIGFY--TPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGT 460
|
410
....*....|.
gi 74199397 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 |
6.95e-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: 6.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 151 CFALSEPGNGSDAGA-ASTTAREEGDSWVLNGTKAWITNSWEASATVVFASTDRSRQNKGISAFLVPMPTPGLTLGKKED 229
Cdd:pfam02770 1 AFALTEPGAGSDVASlKTTAADGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 74199397 230 KLGIRASSTANLIFE 244
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
86-403 |
4.73e-29 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 119.90 E-value: 4.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 86 EELSGAGLDYLAYSIALEEISRACASTGVI---------MSVnnslylgpILKFGSAQQKQQWITPFTNGDKIGCFALSE 156
Cdd:PLN02876 487 DQLLGAGLSNLEYGYLCEIMGRSVWAPQVFncgapdtgnMEV--------LLRYGNKEQQLEWLIPLLEGKIRSGFAMTE 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 157 PG-NGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASATV--VFASTDRSR-QNKGISAFLVPMPTPGLTLGKKEDKLG 232
Cdd:PLN02876 559 PQvASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPRCRVliVMGKTDFNApKHKQQSMILVDIQTPGVQIKRPLLVFG 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 233 IRAS--STANLIFEDCRIPKEN-LLGEpGMGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRNAFGAPLTKLQN 309
Cdd:PLN02876 639 FDDAphGHAEISFENVRVPAKNiLLGE-GRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGS 717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 310 IQFKLADMALALESARLLTWRAAMLKD---NKKPfTKESAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDAR 386
Cdd:PLN02876 718 FLSDLAKCRVELEQTRLLVLEAADQLDrlgNKKA-RGIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATAR 796
|
330
....*....|....*..
gi 74199397 387 ITEIYEGTSEIQRLVIA 403
Cdd:PLN02876 797 TLRIADGPDEVHLGTIA 813
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
21-371 |
6.07e-28 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 116.21 E-value: 6.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 21 DWRRLHTvYQSVELPETHQmlrqtcrDFAEKELVPIAAQLD-------REHLFPTAQvKKMGELGLLAMDVPEELSGAGL 93
Cdd:PRK13026 66 DWQKLHS-YPKPTLTAEEQ-------AFIDNEVETLLTMLDdwdivqnRKDLPPEVW-DYLKKEGFFALIIPKEYGGKGF 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 94 DYLAYSIALEEISRACASTGVIMSVNNSLylGP---ILKFGSAQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTA 170
Cdd:PRK13026 137 SAYANSTIVSKIATRSVSAAVTVMVPNSL--GPgelLTHYGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 171 -----REEGDSWV---LNGTKAWITNSweASATVV---FASTD-----RSRQNKGISAFLVPMPTPGLTLGKKEDKLGIR 234
Cdd:PRK13026 215 ivcrgEFEGEEVLglrLTWDKRYITLA--PVATVLglaFKLRDpdgllGDKKELGITCALIPTDHPGVEIGRRHNPLGMA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 235 asstanliF-------EDCRIPKENLLGEP---GMGFKIAMQTLDMGRiGIASQALGIAQASLdcAVK----YAENRNAF 300
Cdd:PRK13026 293 --------FmngttrgKDVFIPLDWIIGGPdyaGRGWRMLVECLSAGR-GISLPALGTASGHM--ATRttgaYAYVRRQF 361
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74199397 301 GAPLTKLQNIQFKLADMA---LALESARLLTwrAAMLKDNKKPfTKESAMAKLAASEAATAISHQAIQILGGMG 371
Cdd:PRK13026 362 GMPIGQFEGVQEALARIAgntYLLEAARRLT--TTGLDLGVKP-SVVTAIAKYHMTELARDVVNDAMDIHAGKG 432
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
52-386 |
1.97e-24 |
|
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: 103.56 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 52 ELVPIAAQLDREHLFPTAQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRACASTGVIMSvNNSLYLGPILKFG 131
Cdd:cd01163 9 RIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALR-AHFGFVEALLLAG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 132 SAQQKQQWITPFTNGDKIGCfALSEPGnGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASATVVFASTDRSRQnkgiS 211
Cdd:cd01163 88 PEQFRKRWFGRVLNGWIFGN-AVSERG-SVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEGKL----V 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 212 AFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLdMGRIGIASQALGIAQASLDCAV 291
Cdd:cd01163 162 FAAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPNAPDRGTLLTA-IYQLVLAAVLAGIARAALDDAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 292 KYAEN--RNAFGAPLTKLQN---IQFKLADMALALESARLLTWRAAMLKDN--KKPFTKE----------SAMAKLAASE 354
Cdd:cd01163 241 AYVRSrtRPWIHSGAESARDdpyVQQVVGDLAARLHAAEALVLQAARALDAaaAAGTALTaeargeaalaVAAAKVVVTR 320
|
330 340 350
....*....|....*....|....*....|..
gi 74199397 355 AATAISHQAIQILGGMGYVTEMPAERYYRDAR 386
Cdd:cd01163 321 LALDATSRLFEVGGASATAREHNLDRHWRNAR 352
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
70-412 |
8.51e-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: 100.48 E-value: 8.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 70 QVKKMGELGLlamDVPEElsgagldYLAYSIALEEISracASTGVIMSVNNSLYLGPILKFGSAQQKQQWITPFTNGDKI 149
Cdd:cd01150 69 DVERMGELMA---DDPEK-------MLALTNSLGGYD---LSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEII 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 150 GCFALSEPGNGSDAGAASTTAR--EEGDSWVLN-----GTKAWITN-SWEASATVVFASTDRSRQNKGISAFLVPM---- 217
Cdd:cd01150 136 GCFAQTELGHGSNLQGLETTATydPLTQEFVINtpdftATKWWPGNlGKTATHAVVFAQLITPGKNHGLHAFIVPIrdpk 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 218 ---PTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLG----------------EPGMGFKIAMQTLDMGRIGIASQ 278
Cdd:cd01150 216 thqPLPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNrfgdvspdgtyvspfkDPNKRYGAMLGTRSGGRVGLIYD 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 279 ALGIAQASLDCAVKYAENRNAFG-------APLTKLQNIQFKLADMalaLESARLLTWRAAMLKDNKKPFTKESAMAK-- 349
Cdd:cd01150 296 AAMSLKKAATIAIRYSAVRRQFGpkpsdpeVQILDYQLQQYRLFPQ---LAAAYAFHFAAKSLVEMYHEIIKELLQGNse 372
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74199397 350 -------LAASEAATAISH--QAIQIL----GGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLLRSYRS 412
Cdd:cd01150 373 llaelhaLSAGLKAVATWTaaQGIQECreacGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQ 448
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
78-371 |
8.67e-21 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 94.88 E-value: 8.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 78 GLLAMDVPEELSGAGLDYLAYSIALEEISRACASTGVIMSVNNSLylGP---ILKFGSAQQKQQWITPFTNGDKIGCFAL 154
Cdd:PRK09463 122 GFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTVMVPNSL--GPgelLLHYGTDEQKDHYLPRLARGEEIPCFAL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 155 SEPGNGSDAGAASTTA-----REEGDSWV---LNGTKAWITNSweASATVV---FASTDR-----SRQNKGISAFLVPMP 218
Cdd:PRK09463 200 TSPEAGSDAGSIPDTGvvckgEWQGEEVLgmrLTWNKRYITLA--PIATVLglaFKLYDPdgllgDKEDLGITCALIPTD 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 219 TPGLTLGKKEDKLGIRasstanliF-------EDCRIPKENLLGEP---GMGFKIAMQTLDMGR-IGIASQALGIAQASL 287
Cdd:PRK09463 278 TPGVEIGRRHFPLNVP--------FqngptrgKDVFIPLDYIIGGPkmaGQGWRMLMECLSVGRgISLPSNSTGGAKLAA 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 288 DCAVKYAENRNAFGAPLTKLQNIQFKLADM---ALALESARLLTWRAAMLKDnkKPFTKeSAMAKLAASEAA-TAISHqA 363
Cdd:PRK09463 350 LATGAYARIRRQFKLPIGKFEGIEEPLARIagnAYLMDAARTLTTAAVDLGE--KPSVL-SAIAKYHLTERGrQVIND-A 425
|
....*...
gi 74199397 364 IQILGGMG 371
Cdd:PRK09463 426 MDIHGGKG 433
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
274-396 |
2.55e-19 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 83.55 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 274 GIASQALGIAQASLDCAVKYAENR--NAFGAPLTKLQNIQFKLADMALALESARLLTWRAA----MLKDNKKPFT----K 343
Cdd:pfam08028 1 GIAAAALGAARAALAEFTERARGRvrAYFGVPLAEDPATQLALAEAAARIDAARLLLERAAarieAAAAAGKPVTpalrA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 74199397 344 ESAMAKLAASEAATAISHQAIQILGGMGYVTEMPAERYYRDARITEIYEGTSE 396
Cdd:pfam08028 81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
137-397 |
9.37e-17 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 82.11 E-value: 9.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 137 QQWITPFTN----------GDKIGCF---ALSEPGNGSDAGAASTTA-REEGDSWVLNGTKaWITNSWEASATVVFASTD 202
Cdd:PRK11561 154 QDWLTPLLSdrydshllpgGQKRGLLigmGMTEKQGGSDVLSNTTRAeRLADGSYRLVGHK-WFFSVPQSDAHLVLAQAK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 203 rsrqnKGISAFLVPMPTP-----GLTLGKKEDKLGIRASSTANLIFEDCripKENLLGEPGMGFKiamQTLDMG---RIG 274
Cdd:PRK11561 233 -----GGLSCFFVPRFLPdgqrnAIRLERLKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIR---LILKMGgmtRFD 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 275 IASQALGIAQASLDCAVKYAENRNAFGAPLTKLQNIQFKLADMALALESARLLTWRAAMLKDnKKPFTKESAMAKLAASE 354
Cdd:PRK11561 302 CALGSHGLMRRAFSVAIYHAHQRQVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWD-RRADAKEALWARLFTPA 380
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 74199397 355 AATAISHQ-------AIQILGGMGYVTEMPAERYYRDARITEIYEGTSEI 397
Cdd:PRK11561 381 AKFVICKRgipfvaeAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNI 430
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
98-411 |
2.05e-15 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 78.36 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 98 YSIALEEISRACASTGVIMSVNNSLYLGPILKFGSAQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREE--GD 175
Cdd:PLN02636 123 YFAITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDplTD 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 176 SWVLN-----GTKAWITNSW-EASATVVFA-----STD-RSRQNKGISAFLVPMPT-------PGLTLGKKEDKLGIRAS 236
Cdd:PLN02636 203 EFVINtpndgAIKWWIGNAAvHGKFATVFArlklpTHDsKGVSDMGVHAFIVPIRDmkthqvlPGVEIRDCGHKVGLNGV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 237 STANLIFEDCRIPKENLLGEPG----------------MGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRNAF 300
Cdd:PLN02636 283 DNGALRFRSVRIPRDNLLNRFGdvsrdgkytsslptinKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQF 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 301 GAP------LTKLQNIQFKLADM-----ALALESARLLTWRAAMLKDNKKPFTKEsaMAKLAASEAATAISHQAIQI--- 366
Cdd:PLN02636 363 GPPkqpeisILDYQSQQHKLMPMlastyAFHFATEYLVERYSEMKKTHDDQLVAD--VHALSAGLKAYITSYTAKALstc 440
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 74199397 367 ---LGGMGYVTEMPAERYYRDARITEIYEGTSEIQRLVIAGHLLRSYR 411
Cdd:PLN02636 441 reaCGGHGYAAVNRFGSLRNDHDIFQTFEGDNTVLLQQVAADLLKQYK 488
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
111-300 |
1.59e-14 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 75.58 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 111 STGVIMSVNNSLYLGPILKFGSAQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAAST--TAREEGDSWVLN-----GTK 183
Cdd:PLN02312 148 SLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETvtTYDPKTEEFVINtpcesAQK 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 184 AWITNSWE-ASATVVFASTDRSRQNKGISAFLVPMPT------PGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLG- 255
Cdd:PLN02312 228 YWIGGAANhATHTIVFSQLHINGKNEGVHAFIAQIRDqdgnicPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNs 307
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 256 ---------------EPGMGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRNAF 300
Cdd:PLN02312 308 vadvspdgkyvsaikDPDQRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 367
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
52-386 |
3.90e-14 |
|
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: 73.15 E-value: 3.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 52 ELVPI----AAQLDREHLFPTAQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRACASTGVIMSVNN--SLYLG 125
Cdd:cd01159 5 DLAPLirerAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIVAthSRMLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 126 pilKFGSAQQKQQWitpftngdkigcfalsepGNGSDAGAAST-----TAREEGDSWVLNGTKAWITNSWEASATVVFAS 200
Cdd:cd01159 85 ---AFPPEAQEEVW------------------GDGPDTLLAGSyapggRAERVDGGYRVSGTWPFASGCDHADWILVGAI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 201 TDRSRQNKGISAFLVPMptPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGM------GFKIA---MQTLDMG 271
Cdd:cd01159 144 VEDDDGGPLPRAFVVPR--AEYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLTAGDMmagdgpGGSTPvyrMPLRQVF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 272 RIGIASQALGIAQASLDCAVKYAENR---NAFGAPLTKLQNIQFKLADMALALESARLL---TWRAAM--LKDNKKPFTK 343
Cdd:cd01159 222 PLSFAAVSLGAAEGALAEFLELAGKRvrqYGAAVKMAEAPITQLRLAEAAAELDAARAFlerATRDLWahALAGGPIDVE 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 74199397 344 ESAMAKLAASEAATaISHQAIQIL----GGMGYVTEMPAERYYRDAR 386
Cdd:cd01159 302 ERARIRRDAAYAAK-LSAEAVDRLfhaaGGSALYTASPLQRIWRDIH 347
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
126-300 |
8.47e-12 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 66.79 E-value: 8.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 126 PILKF-GSAQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAR--EEGDSWVLNGTKAWITNSWE------ASATV 196
Cdd:PTZ00460 104 PAFQVlGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATydKQTNEFVIHTPSVEAVKFWPgelgflCNFAL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 197 VFASTDRSRQNKGISAFLVPM-------PTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLL--------------- 254
Cdd:PTZ00460 184 VYAKLIVNGKNKGVHPFMVRIrdkethkPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLaryikvsedgqverq 263
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 74199397 255 GEPGMGFKIAMqtldMGRIGIASQALGIAQASLDCAVKYAENRNAF 300
Cdd:PTZ00460 264 GNPKVSYASMM----YMRNLIIDQYPRFAAQALTVAIRYSIYRQQF 305
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
131-254 |
2.33e-10 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 62.55 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74199397 131 GSAQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAR--EEGDSWVLN-----GTKAWITNSWEASA-TVVFASTD 202
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATfdPKTDEFVIHsptltSSKWWPGGLGKVSThAVVYARLI 193
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74199397 203 RSRQNKGISAFLVP-------MPTPGLTLGKKEDKLGIRASSTAN---LIFEDCRIPKENLL 254
Cdd:PLN02443 194 TNGKDHGIHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQML 255
|
|
| |
