|
Name |
Accession |
Description |
Interval |
E-value |
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
10-385 |
7.28e-152 |
|
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: 433.88 E-value: 7.28e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 10 WTDDEIRFREEVRAFGQKEIAPVADEIDK-GPYPRDLIRKIGQAGYMGVHHEKEVGGSARGLSYEIIVAEELSSINGGLD 88
Cdd:COG1960 5 LTEEQRALRDEVREFAEEEIAPEAREWDReGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 89 MArMASATLYGMPVSKFGTDEQKKKYLTPIIKGEKIGCIGITEPDVGSDTAGMKTKAEKDGDEWVLNGEKKFITNGSVAD 168
Cdd:COG1960 85 LP-VGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVAD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 169 YMCAFAITDPSVKAKnGMSAFIVDTKSDGFSVVQDHELLGMKSARVSWLKFEDVRILSDMLLGEPGQGFHILMDELDSER 248
Cdd:COG1960 164 VILVLARTDPAAGHR-GISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 249 TAIAAEAIGYARTPYEIAVKYSNEREQFGRPIRAFEGVSFKISDMAMKLEAGRALTLMAARAYDRDENITKLASIAKLFT 328
Cdd:COG1960 243 LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKLFA 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 998177658 329 TESAIQITNDAIQILGGAGYTTDYPIERFFRDARLMTIGGGTAEILRFLIQREVFKE 385
Cdd:COG1960 323 TEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGR 379
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
12-384 |
8.24e-141 |
|
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: 405.50 E-value: 8.24e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 12 DDEIRFREEVRAFGQKEIAPVADEID-KGPYPRDLIRKIGQAGYMGVHHEKEVGGSarGLSYE--IIVAEELSSINGGLD 88
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDeKGEFPREVIKEMAELGLMGIPIPEEYGGA--GLDFLayAIAIEELAKVDASVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 89 MARMASATLYGMPVSKFGTDEQKKKYLTPIIKGEKIGCIGITEPDVGSDTAGMKTKAEKDGDEWVLNGEKKFITNGSVAD 168
Cdd:cd01158 79 VIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 169 YMCAFAITDPSVKAKnGMSAFIVDTKSDGFSVVQDHELLGMKSARVSWLKFEDVRILSDMLLGEPGQGFHILMDELDSER 248
Cdd:cd01158 159 FYIVFAVTDPSKGYR-GITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 249 TAIAAEAIGYARTPYEIAVKYSNEREQFGRPIRAFEGVSFKISDMAMKLEAGRALTLMAARAYDRDENITKLASIAKLFT 328
Cdd:cd01158 238 IGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFA 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 998177658 329 TESAIQITNDAIQILGGAGYTTDYPIERFFRDARLMTIGGGTAEILRFLIQREVFK 384
Cdd:cd01158 318 SEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
11-384 |
6.46e-120 |
|
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: 352.48 E-value: 6.46e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 11 TDDEIRFREEVRAFGQKEIAPVADEIDKGPY-PRDLIRKIGQAGYMGVHHEKEVGGSARGLSYEIIVAEELSSINGGLDM 89
Cdd:cd01156 3 DDEIEMLRQSVREFAQKEIAPLAAKIDRDNEfPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 90 ARMASATLYGMPVSKFGTDEQKKKYLTPIIKGEKIGCIGITEPDVGSDTAGMKTKAEKDGDEWVLNGEKKFITNGSVADY 169
Cdd:cd01156 83 SYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDADT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 170 MCAFAITDPSVKAKnGMSAFIVDTKSDGFSVVQDHELLGMKSARVSWLKFEDVRILSDMLLGEPGQGFHILMDELDSERT 249
Cdd:cd01156 163 LVVYAKTDPSAGAH-GITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYERL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 250 AIAAEAIGYARTPYEIAVKYSNEREQFGRPIRAFEGVSFKISDMAMKLEAGRALTLMAARAYDRDENITKLASIAKLFTT 329
Cdd:cd01156 242 VLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILYAA 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 998177658 330 ESAIQITNDAIQILGGAGYTTDYPIERFFRDARLMTIGGGTAEILRFLIQREVFK 384
Cdd:cd01156 322 EKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
16-380 |
1.83e-117 |
|
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: 344.27 E-value: 1.83e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 16 RFREEVRAFGQKEIAPVADEIDKGPypRDLIRKIGQAGYMGVHHekevggsarglsyeiivaeelssinggldmarmasa 95
Cdd:cd00567 5 ELRDSAREFAAEELEPYARERRETP--EEPWELLAELGLLLGAA------------------------------------ 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 96 tlygmPVSKFGTDEQKKKYLTPIIKGEKIGCIGITEPDVGSDTAGMKTKAEKDGDEWVLNGEKKFITNGSVADYMCAFAI 175
Cdd:cd00567 47 -----LLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLAR 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 176 TDPSVKAKNGMSAFIVDTKSDGFSVVQDHELLGMKSARVSWLKFEDVRILSDMLLGEPGQGFHILMDELDSERTAIAAEA 255
Cdd:cd00567 122 TDEEGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLLAAVA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 256 IGYARTPYEIAVKYSNEREQFGRPIRAFEGVSFKISDMAMKLEAGRALTLMAARAYDRDE-NITKLASIAKLFTTESAIQ 334
Cdd:cd00567 202 LGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPdEARLEAAMAKLFATEAARE 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 998177658 335 ITNDAIQILGGAGYTTDYPIERFFRDARLMTIGGGTAEILRFLIQR 380
Cdd:cd00567 282 VADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
17-382 |
1.84e-103 |
|
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: 310.59 E-value: 1.84e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 17 FREEVRAFGQKEIAPVADEIDK-GPYPRDLIRKIGQAGYMGVHHEKEVGGSARGLSYEIIVAEELSSiNGGLDMARMASA 95
Cdd:cd01160 6 FRDVVRRFFAKEVAPFHHEWEKaGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELAR-AGGSGPGLSLHT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 96 TLYGMPVSKFGTDEQKKKYLTPIIKGEKIGCIGITEPDVGSDTAGMKTKAEKDGDEWVLNGEKKFITNGSVADYMCAFAI 175
Cdd:cd01160 85 DIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVIVVAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 176 TDPSVKAKNGMSAFIVDTKSDGFSVVQDHELLGMKSARVSWLKFEDVRILSDMLLGEPGQGFHILMDELDSERTAIAAEA 255
Cdd:cd01160 165 TGGEARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAAGA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 256 IGYARTPYEIAVKYSNEREQFGRPIRAFEGVSFKISDMAMKLEAGRALTLMAARAYDRDENITKLASIAKLFTTESAIQI 335
Cdd:cd01160 245 LAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATELQNRV 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 998177658 336 TNDAIQILGGAGYTTDYPIERFFRDARLMTIGGGTAEILRFLIQREV 382
Cdd:cd01160 325 AYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQM 371
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
6-385 |
1.12e-90 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 278.68 E-value: 1.12e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 6 SSTLWTDDEIRFREEVRAFGQKEIAPVADEIDKG---PYPRDLIRKIGQAGYMGVHHEKEVGGSARGLSYEIIVAEELSS 82
Cdd:PLN02519 22 SSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATnsfPKDVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 83 INGGLDMARMASATLYGMPVSKFGTDEQKKKYLTPIIKGEKIGCIGITEPDVGSDTAGMKTKAEKDGDEWVLNGEKKFIT 162
Cdd:PLN02519 102 ASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 163 NGSVADYMCAFAITDPSVKAKnGMSAFIVDTKSDGFSVVQDHELLGMKSARVSWLKFEDVRILSDMLLGEPGQGFHILMD 242
Cdd:PLN02519 182 NGPVAQTLVVYAKTDVAAGSK-GITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 243 ELDSERTAIAAEAIGYARTPYEIAVKYSNEREQFGRPIRAFEGVSFKISDMAMKLEAGRALTLMAARAYDRDENITKLAS 322
Cdd:PLN02519 261 GLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCA 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 998177658 323 IAKLFTTESAIQITNDAIQILGGAGYTTDYPIERFFRDARLMTIGGGTAEILRFLIQREVFKE 385
Cdd:PLN02519 341 GVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
11-383 |
8.04e-89 |
|
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: 273.31 E-value: 8.04e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 11 TDDEIRFREEVRAFGQKEIAPVADEIDK-GPYPRDLIRKIGQAGYMGVHHEKEVGGSARGLSYEIIVAEELSSINGGLDM 89
Cdd:cd01157 2 TEQQKEFQETARKFAREEIIPVAAEYDKsGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 90 ARMASaTLYGMPVSKFGTDEQKKKYLTPIIKGEKIGCIGITEPDVGSDTAGMKTKAEKDGDEWVLNGEKKFITNGSVADY 169
Cdd:cd01157 82 AIEAN-SLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 170 MCAFAITDPSVK--AKNGMSAFIVDTKSDGFSVVQDHELLGMKSARVSWLKFEDVRILSDMLLGEPGQGFHILMDELDSE 247
Cdd:cd01157 161 YFLLARSDPDPKcpASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 248 RTAIAAEAIGYARTPYEIAVKYSNEREQFGRPIRAFEGVSFKISDMAMKLEAGRALTLMAARAYDRDENITKLASIAKLF 327
Cdd:cd01157 241 RPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAF 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 998177658 328 TTESAIQITNDAIQILGGAGYTTDYPIERFFRDARLMTIGGGTAEILRFLIQREVF 383
Cdd:cd01157 321 AADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
11-385 |
4.58e-85 |
|
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: 263.53 E-value: 4.58e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 11 TDDEIRFREEVRAFGQKEIAPVADEID-KGPYPRDLIRKIGQAGYMGVHHEKEVGGSARGLSYEIIVAEELS----SING 85
Cdd:cd01162 2 NEEQRAIQEVARAFAAKEMAPHAADWDqKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALStgcvSTAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 86 GLDMARMASatlyGMpVSKFGTDEQKKKYLTPIIKGEKIGCIGITEPDVGSDTAGMKTKAEKDGDEWVLNGEKKFITNGS 165
Cdd:cd01162 82 YISIHNMCA----WM-IDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 166 VADYMCAFAITDPsvKAKNGMSAFIVDTKSDGFSVVQDHELLGMKSARVSWLKFEDVRILSDMLLGEPGQGFHILMDELD 245
Cdd:cd01162 157 DSDVYVVMARTGG--EGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 246 SERTAIAAEAIGYARTPYEIAVKYSNEREQFGRPIRAFEGVSFKISDMAMKLEAGRALTLMAARAYDR-DENITKLASIA 324
Cdd:cd01162 235 GGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRgDPDAVKLCAMA 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 998177658 325 KLFTTESAIQITNDAIQILGGAGYTTDYPIERFFRDARLMTIGGGTAEILRFLIQREVFKE 385
Cdd:cd01162 315 KRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
11-378 |
4.44e-75 |
|
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: 238.91 E-value: 4.44e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 11 TDDEIRFREEV-----RAFGQKEIAPVADEIDKgpYPRDLIRKIGQAGYMGVHHEKEVGGSARGLSYEIIVAEELSsING 85
Cdd:cd01161 24 TEEQTEELNMLvgpveKFFEEVNDPAKNDQLEK--IPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVG-MDL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 86 GLDMARMASATLYGMPVSKFGTDEQKKKYLTPIIKGEKIGCIGITEPDVGSDTAGMKTKAEK--DGDEWVLNGEKKFITN 163
Cdd:cd01161 101 GFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLseDGKHYVLNGSKIWITN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 164 GSVADYMCAFAIT---DPSVKAKNGMSAFIVDTKSDGFSVVQDHELLGMKSARVSWLKFEDVRILSDMLLGEPGQGFHIL 240
Cdd:cd01161 181 GGIADIFTVFAKTevkDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 241 MDELDSERTAIAAEAIGYARTPYEIAVKYSNEREQFGRPIRAFEGVSFKISDMAMKLEAGRALTLMAARAYDR----DEN 316
Cdd:cd01161 261 MNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRglkaEYQ 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 998177658 317 ITklASIAKLFTTESAIQITNDAIQILGGAGYTTDYPIERFFRDARLMTIGGGTAEILRFLI 378
Cdd:cd01161 341 IE--AAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFI 400
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
4-382 |
1.29e-72 |
|
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: 231.86 E-value: 1.29e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 4 YLSSTLWTDDEIRFREEVRAFGQKEIAP-VADEIDKGPYPRDLIRKIGQAGYMGVHHeKEVGGSarGLSYEI--IVAEEL 80
Cdd:cd01151 7 LNLDDLLTEEERAIRDTAREFCQEELAPrVLEAYREEKFDRKIIEEMGELGLLGATI-KGYGCA--GLSSVAygLIAREV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 81 SSINGGLDMARMASATLYGMPVSKFGTDEQKKKYLTPIIKGEKIGCIGITEPDVGSDTAGMKTKAEKDGDEWVLNGEKKF 160
Cdd:cd01151 84 ERVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 161 ITNGSVADYMCAFAITDpsvkAKNGMSAFIVDTKSDGFSVVQDHELLGMKSARVSWLKFEDVRILSDMLLgePG-QGFHI 239
Cdd:cd01151 164 ITNSPIADVFVVWARND----ETGKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL--PGaEGLRG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 240 LMDELDSERTAIAAEAIGYARTPYEIAVKYSNEREQFGRPIRAFEGVSFKISDMAMKLEAGRALTLMAARAYDRDENITK 319
Cdd:cd01151 238 PFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPE 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 998177658 320 LASIAKLFTTESAIQITNDAIQILGGAGYTTDYPIERFFRDARLMTIGGGTAEILRFLIQREV 382
Cdd:cd01151 318 QISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAI 380
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
11-386 |
4.14e-72 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 231.36 E-value: 4.14e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 11 TDDEIRFREEVRAFGQKEIAPVADEID-KGPYPRDLIRKIGQAGYMGVHHEKEVGGSARGLSYEIIVAEELSSINGGLDM 89
Cdd:PTZ00461 38 TPEHAALRETVAKFSREVVDKHAREDDiNMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 90 ARMASATLYgmpVSKF---GTDEQKKKYLTPIIKGEKIGCIGITEPDVGSDTAGMKTKAEKDGDE-WVLNGEKKFITNGS 165
Cdd:PTZ00461 118 AYLAHSMLF---VNNFyysASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGnYVLNGSKIWITNGT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 166 VADYMCAFAitdpsvKAKNGMSAFIVDTKSDGFSVVQDHELLGMKSARVSWLKFEDVRILSDMLLGEPGQGFHILMDELD 245
Cdd:PTZ00461 195 VADVFLIYA------KVDGKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 246 SERTAIAAEAIGYARTPYEIAVKYSNEREQFGRPIRAFEGVSFKISDMAMKLEAGRALTLMAARAYDRDENITKLASIAK 325
Cdd:PTZ00461 269 LERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAK 348
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 998177658 326 LFTTESAIQITNDAIQILGGAGYTTDYPIERFFRDARLMTIGGGTAEILRFLIQREVFKEF 386
Cdd:PTZ00461 349 LFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLKGL 409
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
12-383 |
7.11e-70 |
|
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: 224.53 E-value: 7.11e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 12 DDEIRFREEVRAFGQKEIAPVADEIDKGPYP------RDLIRKIGQAGYMGVHHEKEVGGSARGLSYEIIVAEELSsING 85
Cdd:cd01152 1 PSEEAFRAEVRAWLAAHLPPELREESALGYRegredrRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMA-AAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 86 GLDMARMASATLYGMPVSKFGTDEQKKKYLTPIIKGEKIGCIGITEPDVGSDTAGMKTKAEKDGDEWVLNGEKKFITNGS 165
Cdd:cd01152 80 APVPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 166 VADYMCAFAITDPSVKAKNGMSAFIVDTKSDGFSVVQDHELLGmkSARVSWLKFEDVRILSDMLLGEPGQGFHILMDELD 245
Cdd:cd01152 160 YADWAWLLVRTDPEAPKHRGISILLVDMDSPGVTVRPIRSING--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 246 SERTAIAaeaiGYARTPYEIAVKYSNEREQFGRPIRAFEGVSFKISDMAMKLEAGRALTLMAARAYDRDENITKLASIAK 325
Cdd:cd01152 238 FERVSIG----GSAATFFELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAK 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 998177658 326 LFTTESAIQITNDAIQILG--------GAGYTTDYPIERFFRDARLMTIGGGTAEILRFLIQREVF 383
Cdd:cd01152 314 LFGSELAQELAELALELLGtaallrdpAPGAELAGRWEADYLRSRATTIYGGTSEIQRNIIAERLL 379
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
37-386 |
4.39e-62 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 204.19 E-value: 4.39e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 37 DKGPYPRDLIRKIGQAGY--MGVhhEKEVGGSARGLSYEIIVAEELSSiNGGLDMARMASATLYGMpvSKFGTDEQKKK- 113
Cdd:PRK12341 34 ENGTYPREFMRALADNGIsmLGV--PEEFGGTPADYVTQMLVLEEVSK-CGAPAFLITNGQCIHSM--RRFGSAEQLRKt 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 114 YLTPIIKGEKIGCIGITEPDVGSDTAGMKTKAEKDGDEWVLNGEKKFITNGSVADYMCAFAITDPSVKAKNGMSAFIVDT 193
Cdd:PRK12341 109 AESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAKEYPYMLVLARDPQPKDPKKAFTLWWVDS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 194 KSDGFSVVQDHELlGMKSARVSWLKFEDVRILSDMLLGEPGQGFHILMDELDSERTAIAAEAIGYARTPYEIAVKYSNER 273
Cdd:PRK12341 189 SKPGIKINPLHKI-GWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 274 EQFGRPIRAFEGVSFKISDMAMKLEAGRALTLMAARAYDRDENITKLASIAKLFTTESAIQITNDAIQILGGAGYTTDYP 353
Cdd:PRK12341 268 IQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEAR 347
|
330 340 350
....*....|....*....|....*....|...
gi 998177658 354 IERFFRDARLMTIGGGTAEILRFLIQREVFKEF 386
Cdd:PRK12341 348 VSRFWRDVRCERIGGGTDEIMIYIAGRQILKDY 380
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
19-373 |
3.26e-57 |
|
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: 192.22 E-value: 3.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 19 EEVRAFGQKEIAPVADEIDKGP---------YP---RDLIRKIGQAGYMGVHHEKEVGGSARGLSYEIIVAEELSSINGG 86
Cdd:cd01153 3 EEVARLAENVLAPLNADGDREGpvfddgrvvVPppfKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 87 LDMARM---ASATLYgmpvsKFGTDEQKKKYLTPIIKGEKIGCIGITEPDVGSDTAGMKTKAEKDGD-EWVLNGEKKFIT 162
Cdd:cd01153 83 LMYASGtqgAAATLL-----AHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFIS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 163 NGSVADYM----CAFAITDPSVKAKNGMSAFIV-----DTKSDGFSVVQDHELLGMKSARVSWLKFEDVRILsdmLLGEP 233
Cdd:cd01153 158 AGEHDMSEnivhLVLARSEGAPPGVKGLSLFLVpkfldDGERNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 234 GQGFHILMDELDSERTAIAAEAIGYARTPYEIAVKYSNEREQFGRPIRAFEGVsFKI-------SDMAMKL--EAGRALT 304
Cdd:cd01153 235 GMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAPAV-TIIhhpdvrrSLMTQKAyaEGSRALD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 305 LMAARAYD------RDENITKLAS--------IAKLFTTESAIQITNDAIQILGGAGYTTDYPIERFFRDARLMTIGGGT 370
Cdd:cd01153 314 LYTATVQDlaerkaTEGEDRKALSaladlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGT 393
|
...
gi 998177658 371 AEI 373
Cdd:cd01153 394 TGI 396
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
234-380 |
4.52e-50 |
|
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: 165.51 E-value: 4.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 234 GQGFHILMDELDSERTAIAAEAIGYARTPYEIAVKYSNEREQFGRPIRAFEGVSFKISDMAMKLEAGRALTLMAARAYDR 313
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 998177658 314 DENITKLASIAKLFTTESAIQITNDAIQILGGAGYTTDYPIERFFRDARLMTIGGGTAEILRFLIQR 380
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIAR 147
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
41-386 |
1.44e-45 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 160.77 E-value: 1.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 41 YPRDLIRKIGQAGYMGVHHEKEVGGSARGLSYEIIVAEELssinggldmARMASAT--LYGMP-----VSKFGTDEQKKK 113
Cdd:PRK03354 38 YPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMEL---------GRLGAPTyvLYQLPggfntFLREGTQEQIDK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 114 YLTPIIKGEKIGCIGITEPDVGSDTAGMKTKAEKDGDEWVLNGEKKFITNGSVADYMCAFAiTDPSVKAKNGMSAFIVDT 193
Cdd:PRK03354 109 IMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVVMA-RDGASPDKPVYTEWFVDM 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 194 KSDGFSVVQDHELlGMKSARVSWLKFEDVRILSDMLLGEPGQGFHILMDELDSERTAIAAEAIGYARTPYEIAVKYSNER 273
Cdd:PRK03354 188 SKPGIKVTKLEKL-GLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 274 EQFGRPIRAFEGVSFKISDMAMKLEAGRALTLMAARAYDRDENITKLASIAKLFTTESAIQITNDAIQILGGAGYTTDYP 353
Cdd:PRK03354 267 VQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHR 346
|
330 340 350
....*....|....*....|....*....|...
gi 998177658 354 IERFFRDARLMTIGGGTAEILRFLIQREVFKEF 386
Cdd:PRK03354 347 ISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQY 379
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
104-373 |
3.01e-41 |
|
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: 149.85 E-value: 3.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 104 KFGTDEQKKKYLTPIIKGEKIGCIGITEPDVGS-DTAGMKTKAEKDGDEWVLNGEKKFITNGSvaDYMCAFAI----TDP 178
Cdd:cd01155 106 RYGSEEQKKQWLEPLLDGKIRSAFAMTEPDVASsDATNIECSIERDGDDYVINGRKWWSSGAG--DPRCKIAIvmgrTDP 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 179 SVKAKNGM-SAFIVDTKSDGFSVVQDHELLGMKSARVSW--LKFEDVRI-LSDMLLGEpGQGFHILMDELDSERTAIAAE 254
Cdd:cd01155 184 DGAPRHRQqSMILVPMDTPGVTIIRPLSVFGYDDAPHGHaeITFDNVRVpASNLILGE-GRGFEIAQGRLGPGRIHHCMR 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 255 AIGYARTPYEIAVKYSNEREQFGRPIRAFEGVSFKISDMAMKLEAGRALTLMAARAYDRDENITKLASIA--KLFTTESA 332
Cdd:cd01155 263 LIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTVGNKAARKEIAmiKVAAPRMA 342
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 998177658 333 IQITNDAIQILGGAGYTTDYPIERFFRDARLMTIGGGTAEI 373
Cdd:cd01155 343 LKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEV 383
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
3-382 |
2.89e-39 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 145.00 E-value: 2.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 3 DYLS-STLWTDDEIRFREEVRAFGQKEIAPVADEI-DKGPYPRDLIRKIGQAGYmgvhhekeVGGSARG--------LSY 72
Cdd:PLN02526 21 DYYQfDDLLTPEEQALRKRVRECMEKEVAPIMTEYwEKAEFPFHIIPKLGSLGI--------AGGTIKGygcpglsiTAS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 73 EIIVAEeLSSINGGLDMARMASATLYGMPVSKFGTDEQKKKYLTPIIKGEKIGCIGITEPDVGSDTAGMKTKAEKDGDEW 152
Cdd:PLN02526 93 AIATAE-VARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGW 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 153 VLNGEKKFITNGSVADYMCAFAiTDPSVKAKNGmsaFIVDTKSDGFSVVQDHELLGMKSARVSWLKFEDVRILSDMLLge 232
Cdd:PLN02526 172 ILNGQKRWIGNSTFADVLVIFA-RNTTTNQING---FIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRL-- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 233 PG-QGFHILMDELDSERTAIAAEAIGYARTPYEIAVKYSNEREQFGRPIRAFEGVSFKISDMAMKLEAGRALTLMAARAY 311
Cdd:PLN02526 246 PGvNSFQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLY 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 998177658 312 DRDENITKLASIAKLFTTESAIQITNDAIQILGGAGYTTDYPIERFFRDARLMTIGGGTAEILRFLIQREV 382
Cdd:PLN02526 326 ESGKMTPGHASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREI 396
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
11-122 |
1.78e-33 |
|
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: 120.65 E-value: 1.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 11 TDDEIRFREEVRAFGQKEIAPVADEID-KGPYPRDLIRKIGQAGYMGVHHEKEVGGSARGLSYEIIVAEELSSINGGLDM 89
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDeEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|...
gi 998177658 90 ARMASATLYGMPVSKFGTDEQKKKYLTPIIKGE 122
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
92-374 |
2.95e-33 |
|
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: 128.64 E-value: 2.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 92 MASATLYGMpvSKFGTDEQKKKYLTPIIKGEK---IGCIGITEPDVGSDTAGMKTKAEKD-GDEWVLNGEKKFiTNGSVA 167
Cdd:cd01154 115 MTDAAVYAL--RKYGPEELKQYLPGLLSDRYKtglLGGTWMTEKQGGSDLGANETTAERSgGGVYRLNGHKWF-ASAPLA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 168 DYMCAFAITDPSVKAKNGMSAFIV-----DTKSDGFSVVQDHELLGMKSARVSWLKFEDVrilSDMLLGEPGQGFHILMD 242
Cdd:cd01154 192 DAALVLARPEGAPAGARGLSLFLVprlleDGTRNGYRIRRLKDKLGTRSVATGEVEFDDA---EAYLIGDEGKGIYYILE 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 243 ELDSERTAIAAEAIGYARTPYEIAVKYSNEREQFGRPIRAFEGVSFKISDMAMKLEAGRALTLMAARAYDR-------DE 315
Cdd:cd01154 269 MLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRaaadkpvEA 348
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 316 NITKLAS-IAKLFTTESAIQITNDAIQILGGAGYTTDYPIERFFRDARLMTIGGGTAEIL 374
Cdd:cd01154 349 HMARLATpVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQ 408
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
53-384 |
5.09e-27 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 113.04 E-value: 5.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 53 GYMGVHHEKEVGGSARGLSYEIIVAEELSSINGGLDM----ARMASATLygmpvSKFGTDEQKKKYLTPIIKGEKIGCIG 128
Cdd:PTZ00456 112 GWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMypglSIGAANTL-----MAWGSEEQKEQYLTKLVSGEWSGTMC 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 129 ITEPDVGSDTAGMKTKAEKDGD-EWVLNGEKKFITNGSvADYM-----CAFAITDPSVKAKNGMSAFIVD---TKSDGfS 199
Cdd:PTZ00456 187 LTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISAGD-HDLTenivhIVLARLPNSLPTTKGLSLFLVPrhvVKPDG-S 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 200 VVQDHEL--------LGMKSARVSWLKFEDVrilSDMLLGEPGQGFHILMDELDSERTAIAAEAIGYARTPYEIAVKYSN 271
Cdd:PTZ00456 265 LETAKNVkciglekkMGIKGSSTCQLSFENS---VGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYAR 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 272 EReqfgRPIRAFEGVSFK-------ISDMAMKL---------EAGRALTLMAARAYD-------------RDENITKLAS 322
Cdd:PTZ00456 342 ER----RSMRALSGTKEPekpadriICHANVRQnilfakavaEGGRALLLDVGRLLDihaaakdaatreaLDHEIGFYTP 417
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 998177658 323 IAKLFTTESAIQITNDAIQILGGAGYTTDYPIERFFRDARLMTIGGGTAEILRF-LIQREVFK 384
Cdd:PTZ00456 418 IAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALdFIGRKVLS 480
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
104-373 |
6.58e-25 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 106.80 E-value: 6.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 104 KFGTDEQKKKYLTPIIKGEKIGCIGITEPDVGS-DTAGMKTKAEKDGDEWVLNGeKKFITNGSVaDYMCAFAI----TDP 178
Cdd:PLN02876 531 RYGNKEQQLEWLIPLLEGKIRSGFAMTEPQVASsDATNIECSIRRQGDSYVING-TKWWTSGAM-DPRCRVLIvmgkTDF 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 179 SVKAKNGMSAFIVDTKSDGFSVVQDHELLGMKSARV--SWLKFEDVRI-LSDMLLGEpGQGFHILMDELDSERTAIAAEA 255
Cdd:PLN02876 609 NAPKHKQQSMILVDIQTPGVQIKRPLLVFGFDDAPHghAEISFENVRVpAKNILLGE-GRGFEIAQGRLGPGRLHHCMRL 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 256 IGYARTPYEIAVKYSNEREQFGRPIrAFEGvSFkISDMA---MKLEAGRALTLMAARAYDRDENitKLA----SIAKLFT 328
Cdd:PLN02876 688 IGAAERGMQLMVQRALSRKAFGKLI-AQHG-SF-LSDLAkcrVELEQTRLLVLEAADQLDRLGN--KKArgiiAMAKVAA 762
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 998177658 329 TESAIQITNDAIQILGGAGYTTDYPIERFFRDARLMTIGGGTAEI 373
Cdd:PLN02876 763 PNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEV 807
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
126-220 |
1.75e-24 |
|
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: 96.20 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 126 CIGITEPDVGSDTAGMKTKA-EKDGDEWVLNGEKKFITNGSVADYMCAFAITDPsVKAKNGMSAFIVDTKSDGFSVVQDH 204
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGG-DDRHGGISLFLVPKDAPGVSVRRIE 79
|
90
....*....|....*.
gi 998177658 205 ELLGMKSARVSWLKFE 220
Cdd:pfam02770 80 TKLGVRGLPTGELVFD 95
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
103-347 |
1.61e-21 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 96.56 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 103 SKFGTDEQKKKYLTPIIKGEKIGCIGITEPDVGSDTAGMK-----TKAEKDGDEWV---LNGEKKFITNGSVADYM-CAF 173
Cdd:PRK13026 172 THYGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPdtgivCRGEFEGEEVLglrLTWDKRYITLAPVATVLgLAF 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 174 AITDPS----VKAKNGMSAFIVDTKSDGFSVVQDHELLGMksarvswlKF-------EDVRILSDMLLGEP---GQGFHI 239
Cdd:PRK13026 252 KLRDPDgllgDKKELGITCALIPTDHPGVEIGRRHNPLGM--------AFmngttrgKDVFIPLDWIIGGPdyaGRGWRM 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 240 LMDELDSERtAIAAEAIGYARTpyEIAVK----YSNEREQFGRPIRAFEGVSFKISDMAMK---LEAGRALTlmaARAYD 312
Cdd:PRK13026 324 LVECLSAGR-GISLPALGTASG--HMATRttgaYAYVRRQFGMPIGQFEGVQEALARIAGNtylLEAARRLT---TTGLD 397
|
250 260 270
....*....|....*....|....*....|....*
gi 998177658 313 RDENITKLASIAKLFTTESAIQITNDAIQILGGAG 347
Cdd:PRK13026 398 LGVKPSVVTAIAKYHMTELARDVVNDAMDIHAGKG 432
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
104-347 |
3.61e-21 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 95.65 E-value: 3.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 104 KFGTDEQKKKYLTPIIKGEKIGCIGITEPDVGSDTAGMK-----TKAEKDGDEWV---LNGEKKFITNGSVADYM-CAFA 174
Cdd:PRK09463 174 HYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPdtgvvCKGEWQGEEVLgmrLTWNKRYITLAPIATVLgLAFK 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 175 ITDPsvkakNGMsafIVDTKSDGFSVV---QDHEllGMKSARVSW----------LKFEDVRILSDMLLGEP---GQGFH 238
Cdd:PRK09463 254 LYDP-----DGL---LGDKEDLGITCAlipTDTP--GVEIGRRHFplnvpfqngpTRGKDVFIPLDYIIGGPkmaGQGWR 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 239 ILMDELDSERtAIA--AEAIGYARTPYEIAVKYSNEREQFGRPIRAFEGVSFKISDMAMK---LEAGRALTlmaARAYDR 313
Cdd:PRK09463 324 MLMECLSVGR-GISlpSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNaylMDAARTLT---TAAVDL 399
|
250 260 270
....*....|....*....|....*....|....
gi 998177658 314 DENITKLASIAKLFTTESAIQITNDAIQILGGAG 347
Cdd:PRK09463 400 GEKPSVLSAIAKYHLTERGRQVINDAMDIHGGKG 433
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
29-365 |
9.29e-19 |
|
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: 86.99 E-value: 9.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 29 IAPVADEIDKGPYPRDLIRK--------IGQAGYMGVHHEKEVGGSarGLSYEIIVA--EELSSINGGLDMARMASatlY 98
Cdd:cd01163 3 ARPLAARIAEGAAERDRQRGlpyeevalLRQSGLGTLRVPKEYGGL--GASLPDLYEvvRELAAADSNIAQALRAH---F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 99 GMP--VSKFGTDEQKKKYLTPIIKGEKIGCigiTEPDVGSDTAGMK-TKAEKDGDEWVLNGEKKFITNGSVADYMCAFAi 175
Cdd:cd01163 78 GFVeaLLLAGPEQFRKRWFGRVLNGWIFGN---AVSERGSVRPGTFlTATVRDGGGYVLNGKKFYSTGALFSDWVTVSA- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 176 TDPSVKAkngmSAFIVDTKSDGFSVVQDHELLGMKSARVSWLKFEDVRILSDMLLGEPGQGfhilmdELDSERTAI---- 251
Cdd:cd01163 154 LDEEGKL----VFAAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPNAP------DRGTLLTAIyqlv 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 252 -AAEAIGYARTPYEIAVKYSNEReqfGRPI------RAFEG--VSFKISDMAMKLEAGRALTLMAARAYDR----DENIT 318
Cdd:cd01163 224 lAAVLAGIARAALDDAVAYVRSR---TRPWihsgaeSARDDpyVQQVVGDLAARLHAAEALVLQAARALDAaaaaGTALT 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 998177658 319 KLASI--------AKLFTTESAIQITNDAIQILGGAGYTTDYPIERFFRDARLMT 365
Cdd:cd01163 301 AEARGeaalavaaAKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNARTHT 355
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
251-362 |
3.26e-18 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 80.08 E-value: 3.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 251 IAAEAIGYARTPYEIAVKYSNEREQ--FGRPIRAFEGVSFKISDMAMKLEAGRALTLMAA-RAYDR-------DENITKL 320
Cdd:pfam08028 2 IAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAaRIEAAaaagkpvTPALRAE 81
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 998177658 321 ASIAKLFTTESAIQITNDAIQILGGAGYTTDYPIERFFRDAR 362
Cdd:pfam08028 82 ARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIH 123
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
120-374 |
7.97e-15 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 75.94 E-value: 7.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 120 KGEKIGcIGITEPDVGSDTAGMKTKAEK-DGDEWVLNGEKKFItngSV--ADYMCAFAitdpsvKAKNGMSAFIV----- 191
Cdd:PRK11561 176 RGLLIG-MGMTEKQGGSDVLSNTTRAERlADGSYRLVGHKWFF---SVpqSDAHLVLA------QAKGGLSCFFVprflp 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 192 DTKSDGFSVVQDHELLGMKSARVSWLKFEDVrilSDMLLGEPGQGF-HIL----MDELDSertaiAAEAIGYARTPYEIA 266
Cdd:PRK11561 246 DGQRNAIRLERLKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIrLILkmggMTRFDC-----ALGSHGLMRRAFSVA 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 267 VKYSNEREQFGRPIRAFEGVSFKISDMAMKLEAGRALTLMAARAYDRDENItKLASIAKLFT-------TESAIQITNDA 339
Cdd:PRK11561 318 IYHAHQRQVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDRRADA-KEALWARLFTpaakfviCKRGIPFVAEA 396
|
250 260 270
....*....|....*....|....*....|....*
gi 998177658 340 IQILGGAGYTTDYPIERFFRDARLMTIGGGTAEIL 374
Cdd:PRK11561 397 MEVLGGIGYCEESELPRLYREMPVNSIWEGSGNIM 431
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
55-279 |
2.27e-13 |
|
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: 71.59 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 55 MGVHHEKEVGGSARGLSYEIIVAEELSSINGGLDMARMASATLYGMPVSKF-------GTDEQKKKYLTPIIKGEKIGCI 127
Cdd:cd01150 59 YEELKRKAKTDVERMGELMADDPEKMLALTNSLGGYDLSLGAKLGLHLGLFgnaiknlGTDEHQDYWLQGANNLEIIGCF 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 128 GITEPDVGSDTAGMKTKAEKD--GDEWVLN-----GEKKFITN-GSVADYMCAFA--ITDpsvkAKN-GMSAFIVDTKS- 195
Cdd:cd01150 139 AQTELGHGSNLQGLETTATYDplTQEFVINtpdftATKWWPGNlGKTATHAVVFAqlITP----GKNhGLHAFIVPIRDp 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 196 DGFSV-----VQD-HELLGMKSARVSWLKFEDVRI-LSDML---------------LGEPGQGFHILMDELDSERTAIAA 253
Cdd:cd01150 215 KTHQPlpgvtVGDiGPKMGLNGVDNGFLQFRNVRIpRENLLnrfgdvspdgtyvspFKDPNKRYGAMLGTRSGGRVGLIY 294
|
250 260
....*....|....*....|....*.
gi 998177658 254 EAIGYARTPYEIAVKYSNEREQFGRP 279
Cdd:cd01150 295 DAAMSLKKAATIAIRYSAVRRQFGPK 320
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
76-279 |
2.98e-11 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 64.88 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 76 VAEELSSINGGLDMARMASATLYGMPVSKFGTDEQKKKYLTPIIKGEKIGCIGITEPDVGSDTAGMKTKAEKD--GDEWV 153
Cdd:PLN02636 126 ITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDplTDEFV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 154 LN-----GEKKFITNGSV-ADYMCAFA-ITDPSVKAKN----GMSAFIVDTKSdgfsvVQDHELL------------GMK 210
Cdd:PLN02636 206 INtpndgAIKWWIGNAAVhGKFATVFArLKLPTHDSKGvsdmGVHAFIVPIRD-----MKTHQVLpgveirdcghkvGLN 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 211 SARVSWLKFEDVRILSDMLLGEPG----------------QGFHILMDELDSERTAIAAEAIGYARTPYEIAVKYSNERE 274
Cdd:PLN02636 281 GVDNGALRFRSVRIPRDNLLNRFGdvsrdgkytsslptinKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQ 360
|
....*
gi 998177658 275 QFGRP 279
Cdd:PLN02636 361 QFGPP 365
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
106-277 |
1.92e-08 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 56.38 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 106 GTDEQKKKYLTPIIKGEKIGCIGITEPDVGSDTAGMKTKAEKD--GDEWVLNGEKKFITN------GSVADYMCAFA--I 175
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDpkTDEFVIHSPTLTSSKwwpgglGKVSTHAVVYArlI 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 176 TDpsvKAKNGMSAFIVDTKSdgfsvVQDHELL--------GMK-------SARVSWLKFEDVRILSDMLL---------G 231
Cdd:PLN02443 194 TN---GKDHGIHGFIVQLRS-----LDDHSPLpgvtvgdiGMKfgngaynTMDNGFLRFDHVRIPRDQMLmrlskvtreG 265
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 998177658 232 E------PGQGFHILMDELdseRTAIAAEAIGYARTPYEIAVKYSNEREQFG 277
Cdd:PLN02443 266 KyvqsdvPRQLVYGTMVYV---RQTIVADASTALSRAVCIATRYSAVRRQFG 314
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
97-276 |
1.36e-04 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 43.99 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 97 LYGMPVSKFGTDEQKKKYLTPIIKGEKIGCIGITEPDVGSDTAGMKTKAEKD--GDEWVLN----GEKKFITNGSVADYM 170
Cdd:PLN02312 159 LWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDpkTEEFVINtpceSAQKYWIGGAANHAT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 171 CAFAITDPSVKAKN-GMSAFIVDTKSDGFSV-----VQD--HE--LLGMKSARVsWlkFEDVRILSDMLLG--------- 231
Cdd:PLN02312 239 HTIVFSQLHINGKNeGVHAFIAQIRDQDGNIcpnirIADcgHKigLNGVDNGRI-W--FDNLRIPRENLLNsvadvspdg 315
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 998177658 232 -------EPGQGFHILMDELDSERTAIAAEAIGYARTPYEIAVKYSNEREQF 276
Cdd:PLN02312 316 kyvsaikDPDQRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 367
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
94-276 |
7.21e-04 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 41.75 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 94 SATLYGMPVSKF---GTDEQKKKYLTPIIKGEKIGCIGITEPDVGSDTAGMKTKA--EKDGDEWVLN-----------GE 157
Cdd:PTZ00460 95 STVHFAMVIPAFqvlGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTAtyDKQTNEFVIHtpsveavkfwpGE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 998177658 158 KKFITNgsvadYMCAFAitDPSVKAKN-GMSAFIVDTKSD-------GFSVVQDHELLGMKSARVSWLKFEDVRILSDML 229
Cdd:PTZ00460 175 LGFLCN-----FALVYA--KLIVNGKNkGVHPFMVRIRDKethkplqGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSL 247
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 998177658 230 L---------------GEPGQGFHILMdeldSERTAIAAEAIGYARTPYEIAVKYSNEREQF 276
Cdd:PTZ00460 248 LaryikvsedgqverqGNPKVSYASMM----YMRNLIIDQYPRFAAQALTVAIRYSIYRQQF 305
|
|
| |
