|
Name |
Accession |
Description |
Interval |
E-value |
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
10-390 |
0e+00 |
|
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: 750.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 10 DLGEDIEMLRESVRSWAQAELAPRAGEIDRTDQFPMDAWKKMGDLGVLGITVAEEYGGANMGYLAHMIAMEEISRASASV 89
Cdd:cd01156 1 GLDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 90 GLSYGAHSNLCVNQIHRNGTAAQKAKYLPKLVSGEWIGALAMSEPNAGSDVVSMKLRADFKGDRFVLNGTKMWITNGPDC 169
Cdd:cd01156 81 ALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 170 DVLVVYAKTEPDLGARGMTAFIVEKGMKGFSVAQKLDKLGMRGSHTGELVFQDVEVPVENILGAENGGAKVLMSGLDYER 249
Cdd:cd01156 161 DTLVVYAKTDPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 250 AVLSGGPVGIMQACMDVVTPYIHDRKQFGQSIGEFQLIQGKVADMYTTLQAARSYLYTVGKNLDALGTDhvrqvRKDCAA 329
Cdd:cd01156 241 LVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMD-----PKDAAG 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054981763 330 VILYTAEKATWMAGESVQILGGNGYINEYPVGRLWRDAKLYEIGAGTSEIRRMLIGRELFA 390
Cdd:cd01156 316 VILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
5-391 |
0e+00 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 583.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 5 PGLKFDlgEDIEMLRESVRSWAQAELAPRAGEIDRTDQFPMDA--WKKMGDLGVLGITVAEEYGGANMGYLAHMIAMEEI 82
Cdd:PLN02519 22 SSLLFD--DTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 83 SRASASVGLSYGAHSNLCVNQIHRNGTAAQKAKYLPKLVSGEWIGALAMSEPNAGSDVVSMKLRADFKGDRFVLNGTKMW 162
Cdd:PLN02519 100 SRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMW 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 163 ITNGPDCDVLVVYAKTEPDLGARGMTAFIVEKGMKGFSVAQKLDKLGMRGSHTGELVFQDVEVPVENILGAENGGAKVLM 242
Cdd:PLN02519 180 CTNGPVAQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 243 SGLDYERAVLSGGPVGIMQACMDVVTPYIHDRKQFGQSIGEFQLIQGKVADMYTTLQAARSYLYTVGKNLDALGTDhvrq 322
Cdd:PLN02519 260 SGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVD---- 335
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054981763 323 vRKDCAAVILYTAEKATWMAGESVQILGGNGYINEYPVGRLWRDAKLYEIGAGTSEIRRMLIGRELFAE 391
Cdd:PLN02519 336 -RKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
9-391 |
2.62e-165 |
|
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: 468.17 E-value: 2.62e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 9 FDLGEDIEMLRESVRSWAQAELAPRAGEIDRTDQFPMDAWKKMGDLGVLGITVAEEYGGANMGYLAHMIAMEEISRASAS 88
Cdd:COG1960 3 FELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 89 VGLSYGAHsNLCVNQIHRNGTAAQKAKYLPKLVSGEWIGALAMSEPNAGSDVVSMKLRADFKGDRFVLNGTKMWITNGPD 168
Cdd:COG1960 83 LALPVGVH-NGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 169 CDVLVVYAKTEPDLGARGMTAFIVEKGMKGFSVAQKLDKLGMRGSHTGELVFQDVEVPVENILGAENGGAKVLMSGLDYE 248
Cdd:COG1960 162 ADVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 249 RAVLSGGPVGIMQACMDVVTPYIHDRKQFGQSIGEFQLIQGKVADMYTTLQAARSYLYTVGKNLDAlgtdhVRQVRKDCA 328
Cdd:COG1960 242 RLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDA-----GEDAALEAA 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054981763 329 AVILYTAEKATWMAGESVQILGGNGYINEYPVGRLWRDAKLYEIGAGTSEIRRMLIGRELFAE 391
Cdd:COG1960 317 MAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGR 379
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
13-390 |
2.00e-146 |
|
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: 419.75 E-value: 2.00e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 13 EDIEMLRESVRSWAQAELAPRAGEIDRTDQFPMDAWKKMGDLGVLGITVAEEYGGANMGYLAHMIAMEEISRASASVGLS 92
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 93 YGAHSNLCVNQIHRNGTAAQKAKYLPKLVSGEWIGALAMSEPNAGSDVVSMKLRADFKGDRFVLNGTKMWITNGPDCDVL 172
Cdd:cd01158 81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 173 VVYAKTEPDLGARGMTAFIVEKGMKGFSVAQKLDKLGMRGSHTGELVFQDVEVPVENILGAENGGAKVLMSGLDYERAVL 252
Cdd:cd01158 161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 253 SGGPVGIMQACMDVVTPYIHDRKQFGQSIGEFQLIQGKVADMYTTLQAARSYLYTVGKNLDAlGTDHVrqvrKDCAAVIL 332
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDN-GEPFI----KEAAMAKL 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1054981763 333 YTAEKATWMAGESVQILGGNGYINEYPVGRLWRDAKLYEIGAGTSEIRRMLIGRELFA 390
Cdd:cd01158 316 FASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
13-386 |
1.54e-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: 344.65 E-value: 1.54e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 13 EDIEMLRESVRSWAQAELAPRAGEIDRTDQFPMDAWKKMGDLGVlgitvaeeygganmgylahmiameeisrasasvgls 92
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLLG------------------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 93 ygahsnlcVNQIHRNGTAAQKAKYLPKLVSGEWIGALAMSEPNAGSDVVSMKLRADFKGDRFVLNGTKMWITNGPDCDVL 172
Cdd:cd00567 45 --------AALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 173 VVYAKTEP-DLGARGMTAFIVEKGMKGFSVAQKLDKLGMRGSHTGELVFQDVEVPVENILGAENGGAKVLMSGLDYERAV 251
Cdd:cd00567 117 IVLARTDEeGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 252 LSGGPVGIMQACMDVVTPYIHDRKQFGQSIGEFQLIQGKVADMYTTLQAARSYLYTVGKNLDAlgtdHVRQVRKDCAAVI 331
Cdd:cd00567 197 LAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQ----GPDEARLEAAMAK 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1054981763 332 LYTAEKATWMAGESVQILGGNGYINEYPVGRLWRDAKLYEIGAGTSEIRRMLIGR 386
Cdd:cd00567 273 LFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
17-391 |
1.13e-103 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 312.26 E-value: 1.13e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 17 MLRESVRSWAQAELAPRAGEIDRTDQFPMDAWKKMGDLGVLGITVAEEYGGANMGYLAHMIAMEEISRASASVGLSYGAH 96
Cdd:PTZ00461 43 ALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLAH 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 97 SNLCVNQIHRNGTAAQKAKYLPKLVSGEWIGALAMSEPNAGSDVVSMKLRADFKGD-RFVLNGTKMWITNGPDCDVLVVY 175
Cdd:PTZ00461 123 SMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGTVADVFLIY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 176 AKTEPDLgargmTAFIVEKGMKGFSVAQKLDKLGMRGSHTGELVFQDVEVPVENILGAENGGAKVLMSGLDYERAVLSGG 255
Cdd:PTZ00461 203 AKVDGKI-----TAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 256 PVGIMQACMDVVTPYIHDRKQFGQSIGEFQLIQGKVADMYTTLQAARSYLYTVGKNL-----DALGTDhvrqvrkdcaAV 330
Cdd:PTZ00461 278 AVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVhpgnkNRLGSD----------AA 347
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054981763 331 ILYTAEKATWMAGESVQILGGNGYINEYPVGRLWRDAKLYEIGAGTSEIRRMLIGRELFAE 391
Cdd:PTZ00461 348 KLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLKG 408
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
13-388 |
1.64e-101 |
|
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: 305.58 E-value: 1.64e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 13 EDIEMLRESVRSWAQAELAPRAGEIDRTDQFPMDAWKKMGDLGVLGITVAEEYGGANMGYLAHMIAMEEISRASASvGLS 92
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGS-GPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 93 YGAHSNLCVNQIHRNGTAAQKAKYLPKLVSGEWIGALAMSEPNAGSDVVSMKLRADFKGDRFVLNGTKMWITNGPDCDVL 172
Cdd:cd01160 80 LSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 173 VVYAKTEPDL-GARGMTAFIVEKGMKGFSVAQKLDKLGMRGSHTGELVFQDVEVPVENILGAENGGAKVLMSGLDYERAV 251
Cdd:cd01160 160 IVVARTGGEArGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 252 LSGGPVGIMQACMDVVTPYIHDRKQFGQSIGEFQLIQGKVADMYTTLQAARSYlytvgknLDALGTDHVrQVRKDCAavi 331
Cdd:cd01160 240 IAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAF-------LDNCAWRHE-QGRLDVA--- 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054981763 332 lyTAEKATWMAGE--------SVQILGGNGYINEYPVGRLWRDAKLYEIGAGTSEIRRMLIGREL 388
Cdd:cd01160 309 --EASMAKYWATElqnrvayeCVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQM 371
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
6-384 |
1.55e-96 |
|
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: 293.99 E-value: 1.55e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 6 GLKFDLGEDIEMLRESVRSWAQAELAPRagEIDRTDQFPMDAWKKMGDLGVLGITVAEEYGGANMGYLAHMIAMEEISRA 85
Cdd:cd01161 22 VLTEEQTEELNMLVGPVEKFFEEVNDPA--KNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 86 sASVGLSYGAHSNLCVNQIHRNGTAAQKAKYLPKLVSGEWIGALAMSEPNAGSDVVSMKLRADFK--GDRFVLNGTKMWI 163
Cdd:cd01161 100 -LGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSedGKHYVLNGSKIWI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 164 TNGPDCDVLVVYAKTE---PDLGAR-GMTAFIVEKGMKGFSVAQKLDKLGMRGSHTGELVFQDVEVPVENILGAENGGAK 239
Cdd:cd01161 179 TNGGIADIFTVFAKTEvkdATGSVKdKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 240 VLMSGLDYERAVLSGGPVGIMQACMDVVTPYIHDRKQFGQSIGEFQLIQGKVADMYTTLQAARSYLYTVGKNLDALGTdh 319
Cdd:cd01161 259 VAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLK-- 336
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054981763 320 vRQVRKDCAAVILYTAEKATWMAGESVQILGGNGYINEYPVGRLWRDAKLYEIGAGTSEIRRMLI 384
Cdd:cd01161 337 -AEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFI 400
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
11-391 |
2.59e-93 |
|
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: 284.72 E-value: 2.59e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 11 LGEDIEMLRESVRSWAQAELAPRAGEIDRTDQFPMDAWKKMGDLGVLGITVAEEYGGANMGYLAHMIAMEEISRASASVG 90
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 91 lSYGAHSNLCVNQIHRNGTAAQKAKYLPKLVSGEWIGALAMSEPNAGSDVVSMKLRADFKGDRFVLNGTKMWITNGPDCD 170
Cdd:cd01162 81 -AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 171 VLVVYAKTEPDlGARGMTAFIVEKGMKGFSVAQKLDKLGMRGSHTGELVFQDVEVPVENILGAENGGAKVLMSGLDYERA 250
Cdd:cd01162 160 VYVVMARTGGE-GPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 251 VLSGGPVGIMQACMDVVTPYIHDRKQFGQSIGEFQLIQGKVADMYTTLQAARSYLYTVGKNLDALGTDHVrqvrKDCAAV 330
Cdd:cd01162 239 NIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAV----KLCAMA 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054981763 331 ILYTAEKATWMAGESVQILGGNGYINEYPVGRLWRDAKLYEIGAGTSEIRRMLIGRELFAE 391
Cdd:cd01162 315 KRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
11-387 |
1.35e-92 |
|
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: 283.10 E-value: 1.35e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 11 LGEDIEMLRESVRSWAQAELAPRAGEIDRTDQFPMDAWKKMGDLGVLGITVaEEYGGANMGYLAHMIAMEEISRASASVG 90
Cdd:cd01151 13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATI-KGYGCAGLSSVAYGLIAREVERVDSGYR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 91 LSYGAHSNLCVNQIHRNGTAAQKAKYLPKLVSGEWIGALAMSEPNAGSDVVSMKLRADFKGDRFVLNGTKMWITNGPDCD 170
Cdd:cd01151 92 SFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 171 VLVVYAKTEPDLGARGmtaFIVEKGMKGFSVAQKLDKLGMRGSHTGELVFQDVEVPVENILGAENGgakvlMSG----LD 246
Cdd:cd01151 172 VFVVWARNDETGKIRG---FILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAEG-----LRGpfkcLN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 247 YERAVLSGGPVGIMQACMDVVTPYIHDRKQFGQSIGEFQLIQGKVADMYTTLQAARSYLYTVGKNLDA--LGTDHVRQVR 324
Cdd:cd01151 244 NARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQgkATPEQISLLK 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054981763 325 KDCAAVILYTAEKATwmagesvQILGGNGYINEYPVGRLWRDAK---LYEigaGTSEIRRMLIGRE 387
Cdd:cd01151 324 RNNCGKALEIARTAR-------EMLGGNGISDEYHIIRHMVNLEsvnTYE---GTHDIHALILGRA 379
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
11-389 |
2.80e-80 |
|
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: 251.35 E-value: 2.80e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 11 LGEDIEMLRESVRSWAQAELAPRAGEIDRTDQFPMDAWKKMGDLGVLGITVAEEYGGANMGYLAHMIAMEEISRASASVG 90
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 91 LSYGAHSnLCVNQIHRNGTAAQKAKYLPKLVSGEWIGALAMSEPNAGSDVVSMKLRADFKGDRFVLNGTKMWITNGPDCD 170
Cdd:cd01157 81 TAIEANS-LGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKAN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 171 VLVVYAKTEPDLGA---RGMTAFIVEKGMKGFSVAQKLDKLGMRGSHTGELVFQDVEVPVENILGAENGGAKVLMSGLDY 247
Cdd:cd01157 160 WYFLLARSDPDPKCpasKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 248 ERAVLSGGPVGIMQACMDVVTPYIHDRKQFGQSIGEFQLIQGKVADMYTTLQAARSYLYTVGKNLDAlgtdhvrQVRKDC 327
Cdd:cd01157 240 TRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDS-------GRRNTY 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054981763 328 AAVI--LYTAEKATWMAGESVQILGGNGYINEYPVGRLWRDAKLYEIGAGTSEIRRMLIGRELF 389
Cdd:cd01157 313 YASIakAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
9-388 |
8.12e-62 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 203.42 E-value: 8.12e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 9 FDLGEDIEMLRESVRswaqaELAPRAG------EIDRTDQFPMDAWKKMGDLGVLGITVAEEYGGANMGYLAHMIAMEEI 82
Cdd:PRK12341 3 FSLTEEQELLLASIR-----ELITRNFpeeyfrTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 83 SRASASVglsYGAHSNLCVNQIHRNGTAAQKAK-YLPKLVSGEWIGALAMSEPNAGSDVVSMKLRADFKGDRFVLNGTKM 161
Cdd:PRK12341 78 SKCGAPA---FLITNGQCIHSMRRFGSAEQLRKtAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 162 WITNGPDCDVLVVYAK-TEPDLGARGMTAFIVEKGMKGFSVaQKLDKLGMRGSHTGELVFQDVEVPVENILGAENGGAKV 240
Cdd:PRK12341 155 FITGAKEYPYMLVLARdPQPKDPKKAFTLWWVDSSKPGIKI-NPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 241 LMSGLDYERAVLSGGPVGIMQACMDVVTPYIHDRKQFGQSIGEFQLIQGKVADMYTTLQAARSYLYTVgknldALGTDHV 320
Cdd:PRK12341 234 VMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKV-----AWQADNG 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054981763 321 RQVRKDCAAVILYTAEKATWMAGESVQILGGNGYINEYPVGRLWRDAKLYEIGAGTSEIRRMLIGREL 388
Cdd:PRK12341 309 QSLRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQI 376
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
13-124 |
1.39e-53 |
|
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: 173.42 E-value: 1.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 13 EDIEMLRESVRSWAQAELAPRAGEIDRTDQFPMDAWKKMGDLGVLGITVAEEYGGANMGYLAHMIAMEEISRASASVGLS 92
Cdd:pfam02771 2 EEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVALA 81
|
90 100 110
....*....|....*....|....*....|..
gi 1054981763 93 YGAHSNLCVNQIHRNGTAAQKAKYLPKLVSGE 124
Cdd:pfam02771 82 LSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
18-388 |
8.97e-50 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 172.73 E-value: 8.97e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 18 LRESVRSWAQAELAPRAGEIDRTDQFPMDAWKKMGDLGVLGITVaEEYGGANMGYLAHMIAMEEISRASASVGLSYGAHS 97
Cdd:PLN02526 36 LRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTI-KGYGCPGLSITASAIATAEVARVDASCSTFILVHS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 98 NLCVNQIHRNGTAAQKAKYLPKLVSGEWIGALAMSEPNAGSDVVSMKLRADFKGDRFVLNGTKMWITNGPDCDVLVVYAK 177
Cdd:PLN02526 115 SLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFADVLVIFAR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 178 tepDLGARGMTAFIVEKGMKGFSVAQKLDKLGMRGSHTGELVFQDVEVPVENILGAENGGAKVLMSgLDYERAVLSGGPV 257
Cdd:PLN02526 195 ---NTTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNSFQDTNKV-LAVSRVMVAWQPI 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 258 GIMQACMDVVTPYIHDRKQFGQSIGEFQLIQGKVADMYTTLQAarsyLYTVGKNLdalgtdhvrqvrkdCAaviLYTAEK 337
Cdd:PLN02526 271 GISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQA----MFLVGWRL--------------CK---LYESGK 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1054981763 338 AT---------W---MAGESV----QILGGNGYINEYPVGRLWRDAKLYEIGAGTSEIRRMLIGREL 388
Cdd:PLN02526 330 MTpghaslgkaWitkKARETValgrELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREI 396
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
7-387 |
3.56e-49 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 170.40 E-value: 3.56e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 7 LKFDLGEDIEMLRESVRSWAQAE-LAPRAGEIDRTDQFPMDAWKKMGDLGVLGITVAEEYGGANMGYLAHMIAMEEISRA 85
Cdd:PRK03354 1 MDFNLNDEQELFVAGIRELMASEnWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 86 SASVGLSYGAHSNLcvNQIHRNGTAAQKAKYLPKLVSGEWIGALAMSEPNAGSDVVSMKLRADFKGDRFVLNGTKMWITN 165
Cdd:PRK03354 81 GAPTYVLYQLPGGF--NTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 166 GPDCDVLVVYAKTEPDLGARGMTAFIVEKGMKGFSVaQKLDKLGMRGSHTGELVFQDVEVPVENILGAENGGAKVLMSGL 245
Cdd:PRK03354 159 SAYTPYIVVMARDGASPDKPVYTEWFVDMSKPGIKV-TKLEKLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 246 DYERAVLSGGPVGIMQACMDVVTPYIHDRKQFGQSIGEFQLIQGKVADMYTTLQAARSYLYTVgknldALGTDHVRQVRK 325
Cdd:PRK03354 238 DHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEA-----AWKADNGTITSG 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1054981763 326 DCAAVILYTAEKATWMAGESVQILGGNGYINEYPVGRLWRDAKLYEIGAGTSEIRRMLIGRE 387
Cdd:PRK03354 313 DAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRA 374
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
46-388 |
1.67e-46 |
|
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: 164.10 E-value: 1.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 46 DAWKKMGDLGVLGITVAEEYGGANMGYLAHMIAMEEISRASASVGLSYGAHSnlCVNQIHRNGTAAQKAKYLPKLVSGEW 125
Cdd:cd01153 40 EALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMYASGTQG--AAATLLAHGTEAQREKWIPRLAEGEW 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 126 IGALAMSEPNAGSDVVSMKLRADFKGD-RFVLNGTKMWITNG----PDCDVLVVYAKTE-PDLGARGMTAFIVEK----- 194
Cdd:cd01153 118 TGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGehdmSENIVHLVLARSEgAPPGVKGLSLFLVPKflddg 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 195 GMKGFSVAQKLDKLGMRGSHTGELVFQDVEVPvenILGAENGGAKVLMSGLDYERAVLSGGPVGIMQACMDVVTPYIHDR 274
Cdd:cd01153 198 ERNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKER 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 275 KQFGQSIGEF-QLIQGKVADMYTTLQAARSY--------LYTVGKNLDALGTDHVRQVRKDCAAV--IL------YTAEK 337
Cdd:cd01153 275 KQGGDLIKAApAVTIIHHPDVRRSLMTQKAYaegsraldLYTATVQDLAERKATEGEDRKALSALadLLtpvvkgFGSEA 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1054981763 338 ATWMAGESVQILGGNGYINEYPVGRLWRDAKLYEIGAGTSEIRRM-LIGREL 388
Cdd:cd01153 355 ALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQALdLIGRKI 406
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
235-388 |
2.88e-42 |
|
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: 145.09 E-value: 2.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 235 NGGAKVLMSGLDYERAVLSGGPVGIMQACMDVVTPYIHDRKQFGQSIGEFQLIQGKVADMYTTLQAARSYLYTVGKNLDA 314
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1054981763 315 LGTDhvrqvRKDCAAVILYTAEKATWMAGESVQILGGNGYINEYPVGRLWRDAKLYEIGAGTSEIRRMLIGREL 388
Cdd:pfam00441 81 GGPD-----GAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
16-389 |
8.52e-41 |
|
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: 148.26 E-value: 8.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 16 EMLRESVRSWAQAELAP-----RAGEIDRTDQFPMDAWKKMGDLGVLGITVAEEYGGANMGYLAHMIAMEEISRASASV- 89
Cdd:cd01152 4 EAFRAEVRAWLAAHLPPelreeSALGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 90 GLSYGAHsnLCVNQIHRNGTAAQKAKYLPKLVSGEWIGALAMSEPNAGSDVVSMKLRADFKGDRFVLNGTKMWITNGPDC 169
Cdd:cd01152 84 FNQIGID--LAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 170 DVLVVYAKTEPDLGA-RGMTAFIVEKGMKGFSVAQKLDKLGmrGSHTGELVFQDVEVPVENILGAENGGAKVLMSGLDYE 248
Cdd:cd01152 162 DWAWLLVRTDPEAPKhRGISILLVDMDSPGVTVRPIRSING--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 249 RAVLSGGPvgIMQACMDVVTPYIHDRKQFGQSigEFQLIQGKVADMYTTLQAARSYLYTVGKNLDALGTDHVRqvrkdcA 328
Cdd:cd01152 240 RVSIGGSA--ATFFELLLARLLLLTRDGRPLI--DDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAE------A 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 329 AVI-LYTAEKATWMAGESVQILGGNGYI----NEYPVGRLWRDAKLYE----IGAGTSEIRRMLIGRELF 389
Cdd:cd01152 310 SIAkLFGSELAQELAELALELLGTAALLrdpaPGAELAGRWEADYLRSrattIYGGTSEIQRNIIAERLL 379
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
115-379 |
2.39e-32 |
|
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: 125.95 E-value: 2.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 115 KYLPKLVSGE----WIGALAMSEPNAGSDVVSMKLRADF-KGDRFVLNGTKmWITNGPDCDVLVVYAKTE-PDLGARGMT 188
Cdd:cd01154 133 QYLPGLLSDRyktgLLGGTWMTEKQGGSDLGANETTAERsGGGVYRLNGHK-WFASAPLADAALVLARPEgAPAGARGLS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 189 AFIV----EKGMK-GFSVAQKLDKLGMRGSHTGELVFQDVEVpveNILGAENGGAKVLMSGLDYERAVLSGGPVGIMQAC 263
Cdd:cd01154 212 LFLVprllEDGTRnGYRIRRLKDKLGTRSVATGEVEFDDAEA---YLIGDEGKGIYYILEMLNISRLDNAVAALGIMRRA 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 264 MDVVTPYIHDRKQFGQSIGEFQLIQGKVADMYTTLQAARSYLYTVGKNLDALGTDHVRQ---VRKDCAAVILYTAEKATW 340
Cdd:cd01154 289 LSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKPVEahmARLATPVAKLIACKRAAP 368
|
250 260 270
....*....|....*....|....*....|....*....
gi 1054981763 341 MAGESVQILGGNGYINEYPVGRLWRDAKLYEIGAGTSEI 379
Cdd:cd01154 369 VTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNI 407
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
128-220 |
4.09e-32 |
|
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: 116.61 E-value: 4.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 128 ALAMSEPNAGSDVVSMKLRA-DFKGDRFVLNGTKMWITNGPDCDVLVVYAKTEPDLGARGMTAFIVEKGMKGFSVAQKLD 206
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....
gi 1054981763 207 KLGMRGSHTGELVF 220
Cdd:pfam02770 81 KLGVRGLPTGELVF 94
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
104-386 |
1.03e-27 |
|
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: 112.87 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 104 IHRNGTAAQKAKYLPKLVSGEWIGALAMSEPN-AGSDVVSMKLRADFKGDRFVLNGTKMWITNG--PDCDVLVVYAKTEP 180
Cdd:cd01155 104 LHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRKWWSSGAgdPRCKIAIVMGRTDP 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 181 DLGARGM--TAFIVEKGMKGFSVAQKLDKLGMRGSHTG--ELVFQDVEVPVENILGAENGGAKVLMSGLdyeravlsgGP 256
Cdd:cd01155 184 DGAPRHRqqSMILVPMDTPGVTIIRPLSVFGYDDAPHGhaEITFDNVRVPASNLILGEGRGFEIAQGRL---------GP 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 257 ---------VGIMQACMDVVTPYIHDRKQFGQSIGEFQLIQGKVADMYTTLQAARSYLYTVGKNLDALGTdhvRQVRKDC 327
Cdd:cd01155 255 grihhcmrlIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTVGN---KAARKEI 331
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1054981763 328 AAVILYTAEKATWMAGESVQILGGNGYINEYPVGRLWRDAKLYEIGAGTSEIRRMLIGR 386
Cdd:cd01155 332 AMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIAR 390
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
46-388 |
3.76e-22 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 98.40 E-value: 3.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 46 DAWKKMGDLGVLGITVAEEYGGANMGYLAHMIAMEEISRASASV----GLSYGAhsnlcVNQIHRNGTAAQKAKYLPKLV 121
Cdd:PTZ00456 103 EAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFsmypGLSIGA-----ANTLMAWGSEEQKEQYLTKLV 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 122 SGEWIGALAMSEPNAGSDVVSMKLRADFKGD-RFVLNGTKMWITNGpDCD-----VLVVYAKTEPDL-GARGMTAFIVEK 194
Cdd:PTZ00456 178 SGEWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISAG-DHDlteniVHIVLARLPNSLpTTKGLSLFLVPR 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 195 GM----------KGFSVAQKLDKLGMRGSHTGELVFQDvevPVENILGAENGGAKVLMSGLDYERAVLSGGPVGIMQACM 264
Cdd:PTZ00456 257 HVvkpdgsletaKNVKCIGLEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAF 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 265 DVVTPYIHDRKQFGQSIGEFQ-------LI-QGKVADMYTTLQA----ARSYLYTVGKNLDALG--TDHVRQVRKDCAAV 330
Cdd:PTZ00456 334 QNALRYARERRSMRALSGTKEpekpadrIIcHANVRQNILFAKAvaegGRALLLDVGRLLDIHAaaKDAATREALDHEIG 413
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1054981763 331 ILYTAEKA---TW---MAGESVQILGGNGYINEYPVGRLWRDAKLYEIGAGTSEIRRM-LIGREL 388
Cdd:PTZ00456 414 FYTPIAKGcltEWgveAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALdFIGRKV 478
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
88-362 |
2.63e-18 |
|
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: 86.61 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 88 SVGLSYGAHSNLCVNQIHRNGTAAQKAKYLPKLVSGEWIGALAMSEPNAGSDVVSMKLRADF--KGDRFVLN-----GTK 160
Cdd:cd01150 97 SLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYdpLTQEFVINtpdftATK 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 161 MWITN-GPDCDVLVVYAKTEPDLGARGMTAFIVE-------KGMKGFSVAQKLDKLGMRGSHTGELVFQDVEVPVENILg 232
Cdd:cd01150 177 WWPGNlGKTATHAVVFAQLITPGKNHGLHAFIVPirdpkthQPLPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLL- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 233 aeNGGAKVLMSGLdYER-------------AVLSGGPVGIMQA-------CMDVVTPYIHDRKQFGQ-------SIGEFQ 285
Cdd:cd01150 256 --NRFGDVSPDGT-YVSpfkdpnkrygamlGTRSGGRVGLIYDaamslkkAATIAIRYSAVRRQFGPkpsdpevQILDYQ 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 286 LIQGKVADmyttlQAARSYLY-TVGKNLDALGTDHVRQVRKDCAAV-----ILYTAEKA--TWMAGESVQIL----GGNG 353
Cdd:cd01150 333 LQQYRLFP-----QLAAAYAFhFAAKSLVEMYHEIIKELLQGNSELlaelhALSAGLKAvaTWTAAQGIQECreacGGHG 407
|
330
....*....|.
gi 1054981763 354 YI--NEYPVGR 362
Cdd:cd01150 408 YLamNRLPTLR 418
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
28-368 |
1.87e-17 |
|
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: 83.14 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 28 AELAPRAGEIDRTDQFPMDAWKKMGDLGVLGITVAEEYGGANMGY--LAHMIAmeEISRASASVGLSYGAHSNLcVNQIH 105
Cdd:cd01163 8 ARIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLpdLYEVVR--ELAAADSNIAQALRAHFGF-VEALL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 106 RNGTAAQKAKYLPKLVSGEWIGAlAMSE---PNAGSDVVsmklRADFKGDRFVLNGTKMWITNGPDCDVLVVYAKTEPDl 182
Cdd:cd01163 85 LAGPEQFRKRWFGRVLNGWIFGN-AVSErgsVRPGTFLT----ATVRDGGGYVLNGKKFYSTGALFSDWVTVSALDEEG- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 183 garGMTAFIVEKGMKGFSVAQKLDKLGMRGSHTGELVFQDVEVPVENILGAENgGAKVLMSGLDYERAVLSGGPVGIMQA 262
Cdd:cd01163 159 ---KLVFAAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPN-APDRGTLLTAIYQLVLAAVLAGIARA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 263 CMDVVTPYIHDRKQ------FGQSIGEFQLIQgKVADMYTTLQAARSYLYTVGKNLDALGTDHVRQVRKDCAAVILYTAE 336
Cdd:cd01163 235 ALDDAVAYVRSRTRpwihsgAESARDDPYVQQ-VVGDLAARLHAAEALVLQAARALDAAAAAGTALTAEARGEAALAVAA 313
|
330 340 350
....*....|....*....|....*....|....*....
gi 1054981763 337 ------KATWMAGESV-QILGGNGYINEYPVGRLWRDAK 368
Cdd:cd01163 314 akvvvtRLALDATSRLfEVGGASATAREHNLDRHWRNAR 352
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
106-379 |
2.36e-16 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 80.99 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 106 RNGTAAQKAKYLPKLVSGEWIGALAMSEPN-AGSDVVSMKLRADFKGDRFVLNGTKMWiTNG---PDCDVLVVYAKTEPD 181
Cdd:PLN02876 531 RYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWW-TSGamdPRCRVLIVMGKTDFN 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 182 LGARGMTAFI-VEKGMKGFSVAQKLDKLGMRGSHTG--ELVFQDVEVPVENILGAENGGAKVLMSGLDYERAVLSGGPVG 258
Cdd:PLN02876 610 APKHKQQSMIlVDIQTPGVQIKRPLLVFGFDDAPHGhaEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIG 689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 259 IMQACMDVVTPYIHDRKQFGQSIGEFQLIQGKVADMYTTLQAARSYLYTVGKNLDALGTDHVRQVRKDCAAVILYTAEKA 338
Cdd:PLN02876 690 AAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDRLGNKKARGIIAMAKVAAPNMALKV 769
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1054981763 339 TWMAgesVQILGGNGYINEYPVGRLWRDAKLYEIGAGTSEI 379
Cdd:PLN02876 770 LDMA---MQVHGAAGVSSDTVLAHLWATARTLRIADGPDEV 807
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
44-302 |
2.53e-16 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 80.77 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 44 PMDAWKKMGDLGVLGITVAEEYGGANMGYLAHMIAMEEISRASASVGLSYGAHSNLCVNQ-IHRNGTAAQKAKYLPKLVS 122
Cdd:PRK13026 110 PPEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPNSLGPGElLTHYGTQEQKDYWLPRLAD 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 123 GEWIGALAMSEPNAGSDVVSMK-----LRADFKGDR---FVLNGTKMWITNGPDCDVLVVYAKTE-PD--LGAR---GMT 188
Cdd:PRK13026 190 GTEIPCFALTGPEAGSDAGAIPdtgivCRGEFEGEEvlgLRLTWDKRYITLAPVATVLGLAFKLRdPDglLGDKkelGIT 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 189 AFIVEKGMKGFSVAQKLDKLGMR---GSHTGELVFqdveVPVENILGAENG---GAKVLMSGLDYERAV-LSGGPVGIMQ 261
Cdd:PRK13026 270 CALIPTDHPGVEIGRRHNPLGMAfmnGTTRGKDVF----IPLDWIIGGPDYagrGWRMLVECLSAGRGIsLPALGTASGH 345
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1054981763 262 ACMDVVTPYIHDRKQFGQSIGEFQLIQGKVADM--YT-TLQAAR 302
Cdd:PRK13026 346 MATRTTGAYAYVRRQFGMPIGQFEGVQEALARIagNTyLLEAAR 389
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
44-304 |
5.21e-16 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 79.86 E-value: 5.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 44 PMDAWKKMGDLGVLGITVAEEYGGANMGYLAHMIAMEEISR----ASASVGL--SYGAHSNLcvnqIHRnGTAAQKAKYL 117
Cdd:PRK09463 111 PPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASrsgtLAVTVMVpnSLGPGELL----LHY-GTDEQKDHYL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 118 PKLVSGEWIGALAMSEPNAGSDVVSMK-----LRADFKGDRFV---LNGTKMWITNGPDCDVLVVYAKTE-PD--LGAR- 185
Cdd:PRK09463 186 PRLARGEEIPCFALTSPEAGSDAGSIPdtgvvCKGEWQGEEVLgmrLTWNKRYITLAPIATVLGLAFKLYdPDglLGDKe 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 186 --GMTAFIVEKGMKGFSVAQKLDKLG---MRGSHTGELVFqdveVPVENILGAENG---GAKVLMSGLDYERAV-LSGGP 256
Cdd:PRK09463 266 dlGITCALIPTDTPGVEIGRRHFPLNvpfQNGPTRGKDVF----IPLDYIIGGPKMagqGWRMLMECLSVGRGIsLPSNS 341
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1054981763 257 VGIMQACMDVVTPYIHDRKQFGQSIGEFQLIQGKVADM--YTTLQ-AARSY 304
Cdd:PRK09463 342 TGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIagNAYLMdAARTL 392
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
29-367 |
8.02e-16 |
|
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: 78.16 E-value: 8.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 29 ELAPRAGEIDRTDQFPMDAWKKMGDLGVLGITVAEEYGGANMGYLAHMIAMEEISRASASVG---LSYGAHSNLcvnqih 105
Cdd:cd01159 9 LIRERAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAwvaSIVATHSRM------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 106 rngtaaqkAKYLPKLVSGEWIGalamSEPNAGSDVVSMKL-RADFKGDRFVLNGTKMWITNGPDCDVLVVYAKTEPDLGA 184
Cdd:cd01159 83 --------LAAFPPEAQEEVWG----DGPDTLLAGSYAPGgRAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDDGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 185 RGMTAFIVEKgmKGFSVAQKLDKLGMRGSHTGELVFQDVEVPVENIL--GAENGGAKVLMSGLDYERAVLSGGP------ 256
Cdd:cd01159 151 PLPRAFVVPR--AEYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLtaGDMMAGDGPGGSTPVYRMPLRQVFPlsfaav 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 257 -VGIMQACMDVVTPYIHDRKQ---FGQSIGEFQLIQGKVADMYTTLQAARSYLYTVGKNLDALG-------TDHVRQVRK 325
Cdd:cd01159 229 sLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAELDAARAFLERATRDLWAHAlaggpidVEERARIRR 308
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1054981763 326 DCAAVILYTAEKATWMAGESvqilGGNGYINEYPVGRLWRDA 367
Cdd:cd01159 309 DAAYAAKLSAEAVDRLFHAA----GGSALYTASPLQRIWRDI 346
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
58-313 |
2.43e-10 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 61.82 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 58 GITVAEEYGGANMGYLAHMIAMEEISRASASVGLSYGAHSNLCVNQIHRNGTAAQKAKYLPKLVSGEWIGALAMSEPNaG 137
Cdd:PTZ00457 67 GARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHSGFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWATEEGC-G 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 138 SDVVSMKLRADFKGD-RFVLNGTKMWItNGPDCDVLVVYAKT-------EPDLGARGMTAFIVEKGMKGFSVaqkldklg 209
Cdd:PTZ00457 146 SDISMNTTKASLTDDgSYVLTGQKRCE-FAASATHFLVLAKTltqtaaeEGATEVSRNSFFICAKDAKGVSV-------- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 210 mrgsHTGELVFQDveVPVENILGAENGGAKVLMSGLDYERAVLSGGPVGIMQACMdvvtpyihdrKQFGQSIGEfQLIQG 289
Cdd:PTZ00457 217 ----NGDSVVFEN--TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVV----------QELRGSNAE-EGATD 279
|
250 260
....*....|....*....|....
gi 1054981763 290 KVADMYTTLQAARSYLYTVGKNLD 313
Cdd:PTZ00457 280 TVASFACAMYAMESTLYALTANLD 303
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
79-354 |
2.54e-10 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 62.18 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 79 MEEISRASASVGLSYGAHSNLCVNQIHRNGTAAQKAKYLPKLVSGEWIGALAMSEPNAGSDVVSMKLRADFK--GDRFVL 156
Cdd:PLN02636 127 TEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDplTDEFVI 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 157 N-----GTKMWITNGP-DCDVLVVYAKTE-PDLGARGMT-----AFIVE-KGMKGFSVAQKLD------KLGMRGSHTGE 217
Cdd:PLN02636 207 NtpndgAIKWWIGNAAvHGKFATVFARLKlPTHDSKGVSdmgvhAFIVPiRDMKTHQVLPGVEirdcghKVGLNGVDNGA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 218 LVFQDVEVPVENILG-----AENGGAKVLMSGLDYE-----------RAVLSGGPVGIMQACMDVVTPYIHDRKQFGQ-- 279
Cdd:PLN02636 287 LRFRSVRIPRDNLLNrfgdvSRDGKYTSSLPTINKRfaatlgelvggRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPpk 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 280 ----SIGEFQLIQGKVADMYTTLQA---ARSYLYTVgknLDALGTDHVRQVRKDCAA--------VILYTAeKATWMAGE 344
Cdd:PLN02636 367 qpeiSILDYQSQQHKLMPMLASTYAfhfATEYLVER---YSEMKKTHDDQLVADVHAlsaglkayITSYTA-KALSTCRE 442
|
330
....*....|
gi 1054981763 345 SVqilGGNGY 354
Cdd:PLN02636 443 AC---GGHGY 449
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
123-379 |
1.15e-09 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 59.77 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 123 GEWIGaLAMSEPNAGSDVVSMKLRAD-FKGDRFVLNGTKmWITNGPDCDVLVVYAKTEpdlgaRGMTAFIVEK----GMK 197
Cdd:PRK11561 177 GLLIG-MGMTEKQGGSDVLSNTTRAErLADGSYRLVGHK-WFFSVPQSDAHLVLAQAK-----GGLSCFFVPRflpdGQR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 198 GFSVAQKL-DKLGMRGSHTGELVFQDVevpVENILGAENGGAKVLMSGLDYERAVLSGGPVGIMQACMDVVTPYIHDRKQ 276
Cdd:PRK11561 250 NAIRLERLkDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQRQV 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 277 FGQSIGEFQLIQGKVADMYTTLQAARSYLYTVGKNLDALGTDHvrqvrkDCAAVILYT--AEKATWMAG-----ESVQIL 349
Cdd:PRK11561 327 FGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDRRADAK------EALWARLFTpaAKFVICKRGipfvaEAMEVL 400
|
250 260 270
....*....|....*....|....*....|
gi 1054981763 350 GGNGYINEYPVGRLWRDAKLYEIGAGTSEI 379
Cdd:PRK11561 401 GGIGYCEESELPRLYREMPVNSIWEGSGNI 430
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
257-378 |
1.43e-09 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 55.81 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 257 VGIMQACMDVVTPYIHDRKQ--FGQSIGEFQLIQGKVADMYTTLQAARSYLYTVG---KNLDALGTDHVRQVRKDCAAVI 331
Cdd:pfam08028 7 LGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAariEAAAAAGKPVTPALRAEARRAA 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1054981763 332 LYTAEKATWMAGESVQILGGNGYINEYPVGRLWRDAKLYEIGAGTSE 378
Cdd:pfam08028 87 AFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
93-291 |
1.99e-06 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 49.84 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 93 YGAHSNLCVNQIHRNGTAAQKAKYLPKLVSGEWIGALAMSEPNAGSDVVSMKLRADF--KGDRFVLN-----GTKMWITN 165
Cdd:PTZ00460 95 STVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYdkQTNEFVIHtpsveAVKFWPGE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 166 -GPDCDVLVVYAKTEPDLGARGMTAFIVE-------KGMKGFSVAQKLDKLGMRGSHTGELVFQDVEVPVENILG----- 232
Cdd:PTZ00460 175 lGFLCNFALVYAKLIVNGKNKGVHPFMVRirdkethKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLAryikv 254
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1054981763 233 ------AENGGAKVLMSGLDYERAVLSGGPVGIMQACMDVVTPYIHDRKQF----GQ--SIGEFQLIQGKV 291
Cdd:PTZ00460 255 sedgqvERQGNPKVSYASMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQFtndnKQenSVLEYQTQQQKL 325
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
96-356 |
1.45e-05 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 47.14 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 96 HSNLCVNQIHRNGTAAQKAKYLPKLVSGEWIGALAMSEPNAGSDVVSMKLRADF--KGDRFVLN-----GTKMWITN-GP 167
Cdd:PLN02443 102 HWGMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFdpKTDEFVIHsptltSSKWWPGGlGK 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 168 DCDVLVVYAKTEPDLGARGMTAFIVE-------KGMKGFSVAQKLDKLGMRGSHT---GELVFQDVEVPVENILGAEngg 237
Cdd:PLN02443 182 VSTHAVVYARLITNGKDHGIHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTmdnGFLRFDHVRIPRDQMLMRL--- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 238 AKVLMSG----LDYERAVLSGGPVGIMQACMD-----------VVTPYIHDRKQFGQSIG--EFQLIQGKVAD--MYTTL 298
Cdd:PLN02443 259 SKVTREGkyvqSDVPRQLVYGTMVYVRQTIVAdastalsravcIATRYSAVRRQFGSQDGgpETQVIDYKTQQsrLFPLL 338
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054981763 299 QAARSYLYtVGKNLDALGTDHVRQVRKD----------CAAVILYTAEKATWMAGESVQIL-GGNGYIN 356
Cdd:PLN02443 339 ASAYAFRF-VGEWLKWLYTDVTQRLEANdfstlpeahaCTAGLKSLTTSATADGIEECRKLcGGHGYLC 406
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
88-244 |
1.75e-03 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 40.53 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 88 SVGLSYGAHSNLCVNQIHRNGTAAQKAKYLPKLVSGEWIGALAMSEPNAGSDVVSMKLRA--DFKGDRFVLN-----GTK 160
Cdd:PLN02312 148 SLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTtyDPKTEEFVINtpcesAQK 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054981763 161 MWITNGPD-CDVLVVYAKTEPDLGARGMTAFIVE------KGMKGFSVAQKLDKLGMRGSHTGELVFQDVEVPVENILga 233
Cdd:PLN02312 228 YWIGGAANhATHTIVFSQLHINGKNEGVHAFIAQirdqdgNICPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLL-- 305
|
170
....*....|.
gi 1054981763 234 eNGGAKVLMSG 244
Cdd:PLN02312 306 -NSVADVSPDG 315
|
|
| |
