SitesBLAST
Comparing Echvi_0738 FitnessBrowser__Cola:Echvi_0738 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
Q96329 Acyl-coenzyme A oxidase 4, peroxisomal; AOX 4; G6p; Short-chain acyl-CoA oxidase; AtCX4; AtG6; SAOX; EC 1.3.3.6 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
48% identity, 86% coverage: 63:451/452 of query aligns to 41:428/436 of Q96329
2ix5A Short chain specific acyl-coa oxidase from arabidopsis thaliana, acx4 in complex with acetoacetyl-coa (see paper)
48% identity, 86% coverage: 63:451/452 of query aligns to 25:412/415 of 2ix5A
- active site: L158 (= L196), T159 (= T197), S271 (≠ T310), E392 (= E431), R404 (= R443)
- binding acetoacetyl-coenzyme a: S165 (= S203), A167 (≠ V205), S168 (≠ A206), F261 (= F300), L268 (= L307), R272 (= R311), E392 (= E431), G393 (= G432), R404 (= R443)
- binding flavin-adenine dinucleotide: L158 (= L196), T159 (= T197), G164 (= G202), S165 (= S203), W189 (= W228), N239 (= N278), R297 (= R336), F300 (= F339), L304 (≠ I343), F307 (= F346), L309 (= L348), N310 (≠ V349), E365 (= E404), L366 (= L405), G368 (= G407), G369 (= G408), Y391 (= Y430), T394 (= T433), D396 (≠ E435), I397 (= I436)
2ix6A Short chain specific acyl-coa oxidase from arabidopsis thaliana, acx4 (see paper)
48% identity, 86% coverage: 63:451/452 of query aligns to 25:412/416 of 2ix6A
- active site: L158 (= L196), T159 (= T197), S271 (≠ T310), E392 (= E431), R404 (= R443)
- binding flavin-adenine dinucleotide: T159 (= T197), G164 (= G202), S165 (= S203), W189 (= W228), N239 (= N278), R297 (= R336), F300 (= F339), L304 (≠ I343), F307 (= F346), N310 (≠ V349), E365 (= E404), L366 (= L405), G369 (= G408), I372 (= I411), Y391 (= Y430), T394 (= T433), D396 (≠ E435)
2ebaA Crystal structure of the putative glutaryl-coa dehydrogenase from thermus thermophilus
41% identity, 85% coverage: 69:451/452 of query aligns to 3:380/380 of 2ebaA
- active site: L131 (= L196), T132 (= T197), A239 (≠ T310), E360 (= E431), R372 (= R443)
- binding flavin-adenine dinucleotide: L131 (= L196), T132 (= T197), G136 (≠ V201), G137 (= G202), S138 (= S203), W161 (= W228), T163 (≠ G230), R265 (= R336), L272 (≠ I343), K275 (≠ F346), D333 (≠ E404), I334 (≠ L405), G337 (= G408), T355 (≠ A426), T358 (≠ S429), Y359 (= Y430), T362 (= T433)
3sf6A Crystal structure of glutaryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
37% identity, 85% coverage: 69:451/452 of query aligns to 6:386/387 of 3sf6A
- active site: L134 (= L196), T135 (= T197), A245 (≠ T310), E366 (= E431), Q378 (≠ R443)
- binding dihydroflavine-adenine dinucleotide: F132 (= F194), L134 (= L196), T135 (= T197), G140 (= G202), S141 (= S203), W165 (= W228), I166 (= I229), T167 (≠ G230), S361 (≠ A426), T364 (≠ S429), Y365 (= Y430), T368 (= T433), E370 (= E435), M371 (≠ I436)
3swoA Crystal structure of a glutaryl-coa dehydrogenase from mycobacterium smegmatis in complex with fadh2 (see paper)
34% identity, 85% coverage: 69:451/452 of query aligns to 8:387/388 of 3swoA
- active site: L135 (= L196), T136 (= T197), A246 (≠ T310), E367 (= E431), K379 (≠ R443)
- binding dihydroflavine-adenine dinucleotide: F133 (= F194), L135 (= L196), T136 (= T197), G141 (= G202), S142 (= S203), W166 (= W228), I167 (= I229), T168 (≠ G230), R272 (= R336), V274 (≠ Q338), F275 (= F339), L279 (≠ I343), Y282 (≠ F346), T340 (≠ E404), L341 (= L405), G344 (= G408), I347 (= I411), T365 (≠ S429), Y366 (= Y430), T369 (= T433), E371 (= E435), M372 (≠ I436)
2r0nA The effect of a glu370asp mutation in glutaryl-coa dehydrogenase on proton transfer to the dienolate intermediate (see paper)
36% identity, 85% coverage: 69:452/452 of query aligns to 6:389/390 of 2r0nA
- active site: L133 (= L196), T134 (= T197), A247 (≠ T310), E368 (= E431), R380 (= R443)
- binding flavin-adenine dinucleotide: F131 (= F194), L133 (= L196), T134 (= T197), G139 (= G202), S140 (= S203), W166 (= W228), I167 (= I229), T168 (≠ G230), Y367 (= Y430), T370 (= T433), D372 (≠ E435)
- binding 3-thiaglutaryl-CoA: R92 (≠ S155), S93 (≠ T156), V97 (= V160), P142 (≠ V205), G238 (≠ K301), F241 (≠ S304), L244 (= L307), N245 (≠ R308), P318 (≠ D381), Y367 (= Y430), E368 (= E431), I377 (= I440)
1sirA The crystal structure and mechanism of human glutaryl-coa dehydrogenase (see paper)
36% identity, 85% coverage: 69:452/452 of query aligns to 6:389/390 of 1sirA
- active site: L133 (= L196), T134 (= T197), A247 (≠ T310), E368 (= E431), R380 (= R443)
- binding flavin-adenine dinucleotide: F131 (= F194), L133 (= L196), T134 (= T197), G139 (= G202), S140 (= S203), W166 (= W228), I167 (= I229), T168 (≠ G230), Y367 (= Y430), T370 (= T433)
- binding s-4-nitrobutyryl-coa: S93 (≠ T156), S140 (= S203), F241 (≠ S304), G242 (≠ E305), L244 (= L307), N245 (≠ R308), R248 (= R311), P318 (≠ D381), Y367 (= Y430), E368 (= E431), R380 (= R443)
2r0mA The effect of a glu370asp mutation in glutaryl-coa dehydrogenase on proton transfer to the dienolate intermediate (see paper)
36% identity, 85% coverage: 69:452/452 of query aligns to 6:389/390 of 2r0mA
- active site: L133 (= L196), T134 (= T197), A247 (≠ T310), D368 (≠ E431), R380 (= R443)
- binding 4-nitrobutanoic acid: L101 (= L164), Y367 (= Y430), D368 (≠ E431)
- binding flavin-adenine dinucleotide: F131 (= F194), L133 (= L196), T134 (= T197), G139 (= G202), S140 (= S203), W166 (= W228), I167 (= I229), T168 (≠ G230), L210 (= L273), Y367 (= Y430), T370 (= T433)
3gncA Crystal structure of glutaryl-coa dehydrogenase from burkholderia pseudomallei with fragment 6421 (see paper)
33% identity, 84% coverage: 73:450/452 of query aligns to 12:380/380 of 3gncA
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
34% identity, 78% coverage: 91:441/452 of query aligns to 18:372/378 of 5ol2F
- active site: L124 (= L196), T125 (= T197), G241 (≠ T310)
- binding calcium ion: E29 (= E102), E33 (≠ K106), R35 (≠ H108)
- binding coenzyme a persulfide: L238 (= L307), R242 (= R311), E362 (= E431), G363 (= G432)
- binding flavin-adenine dinucleotide: F122 (= F194), L124 (= L196), T125 (= T197), P127 (= P199), T131 (≠ S203), F155 (≠ W228), I156 (= I229), T157 (≠ G230), E198 (= E268), R267 (= R336), F270 (= F339), L274 (≠ I343), F277 (= F346), Q335 (≠ E404), L336 (= L405), G338 (= G407), G339 (= G408), Y361 (= Y430), T364 (= T433), E366 (= E435)
Sites not aligning to the query:
3eonC 2.55a crystal structure of native glutaryl-coa dehydrogenase from burkholderia pseudomallei in complex with a small molecule (see paper)
32% identity, 84% coverage: 73:450/452 of query aligns to 11:382/382 of 3eonC
3gqtC Crystal structure of glutaryl-coa dehydrogenase from burkholderia pseudomallei with fragment (1,4-dimethyl-1,2,3,4- tetrahydroquinoxalin-6-yl)methylamine (see paper)
32% identity, 84% coverage: 73:451/452 of query aligns to 11:385/385 of 3gqtC
- active site: L135 (= L196), T136 (= T197), A250 (≠ T310), E365 (= E431), R377 (= R443)
- binding 1-(1,4-dimethyl-1,2,3,4-tetrahydroquinoxalin-6-yl)methanamine: W166 (= W228), K210 (= K270), L213 (= L273), T218 (≠ N278), Y364 (= Y430)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
33% identity, 83% coverage: 73:445/452 of query aligns to 1:377/380 of 4l1fA
- active site: L125 (= L196), T126 (= T197), G242 (≠ T310), E363 (= E431), R375 (= R443)
- binding coenzyme a persulfide: T132 (≠ S203), H179 (≠ K251), F232 (= F300), M236 (≠ S304), E237 (= E305), L239 (= L307), D240 (≠ R308), R243 (= R311), Y362 (= Y430), E363 (= E431), G364 (= G432), R375 (= R443)
- binding flavin-adenine dinucleotide: F123 (= F194), L125 (= L196), T126 (= T197), G131 (= G202), T132 (≠ S203), F156 (≠ W228), I157 (= I229), T158 (≠ G230), R268 (= R336), Q270 (= Q338), F271 (= F339), I275 (= I343), F278 (= F346), L281 (≠ V349), Q336 (≠ E404), I337 (≠ L405), G340 (= G408), I358 (≠ A426), Y362 (= Y430), T365 (= T433), Q367 (≠ E435)
- binding 1,3-propandiol: L5 (= L77), Q10 (= Q82)
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
33% identity, 82% coverage: 77:448/452 of query aligns to 7:378/384 of 1jqiA
- active site: G377 (= G447)
- binding acetoacetyl-coenzyme a: L95 (= L164), F125 (= F194), S134 (= S203), F234 (= F300), M238 (≠ S304), Q239 (≠ E305), L241 (= L307), D242 (≠ R308), R245 (= R311), Y364 (= Y430), E365 (= E431), G366 (= G432)
- binding flavin-adenine dinucleotide: F125 (= F194), L127 (= L196), S128 (≠ T197), G133 (= G202), S134 (= S203), W158 (= W228), T160 (≠ G230), R270 (= R336), F273 (= F339), L280 (≠ F346), Q338 (≠ E404), I339 (≠ L405), G342 (= G408), I360 (≠ A426), T367 (= T433), E369 (= E435), I370 (= I436)
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
33% identity, 82% coverage: 77:448/452 of query aligns to 34:405/412 of P15651
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
32% identity, 87% coverage: 57:448/452 of query aligns to 11:405/412 of P16219
- G90 (≠ I122) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (vs. gap) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 194:203, 60% identical) binding in other chain
- R171 (≠ K214) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ WIG 228:230) binding in other chain
- A192 (≠ S235) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (≠ Q249) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R336) binding
- Q308 (= Q347) binding in other chain
- R325 (≠ Q364) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ T392) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ ELFGG 404:408) binding
- R380 (= R419) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ TKE 433:435) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
33% identity, 82% coverage: 77:448/452 of query aligns to 7:378/385 of 7y0bA
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[[4-[(3S)-oxolan-3-yl]oxyphenyl]methyl]phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: M343 (≠ N409), T347 (≠ L413), E348 (= E414)
- binding flavin-adenine dinucleotide: F125 (= F194), L127 (= L196), S128 (≠ T197), G133 (= G202), S134 (= S203), W158 (= W228), T160 (≠ G230), R270 (= R336), F273 (= F339), L280 (≠ F346), V282 (≠ L348), Q338 (≠ E404), I339 (≠ L405), G342 (= G408), I360 (≠ A426), Y364 (= Y430), T367 (= T433), E369 (= E435), I370 (= I436), L373 (= L439)
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
33% identity, 82% coverage: 77:448/452 of query aligns to 4:375/381 of 8sgsA
- binding coenzyme a: S131 (= S203), A133 (= A206), N177 (≠ D247), F231 (= F300), M235 (≠ S304), L238 (= L307), I312 (≠ D381), E362 (= E431), G363 (= G432)
- binding flavin-adenine dinucleotide: F122 (= F194), L124 (= L196), S125 (≠ T197), G130 (= G202), S131 (= S203), W155 (= W228), T157 (≠ G230), R267 (= R336), F270 (= F339), L274 (≠ I343), L277 (≠ F346), Q335 (≠ E404), I336 (≠ L405), G338 (= G407), G339 (= G408), I357 (≠ A426), I360 (≠ S429), Y361 (= Y430), T364 (= T433), E366 (= E435)
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
33% identity, 82% coverage: 77:448/452 of query aligns to 10:381/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (= F194), L130 (= L196), S131 (≠ T197), G136 (= G202), S137 (= S203), W161 (= W228), T163 (≠ G230), T214 (≠ N278), R273 (= R336), F276 (= F339), L280 (≠ I343), L283 (≠ F346), V285 (≠ L348), Q341 (≠ E404), I342 (≠ L405), G345 (= G408), I363 (≠ A426), Y367 (= Y430), T370 (= T433), E372 (= E435), L376 (= L439)
Query Sequence
>Echvi_0738 FitnessBrowser__Cola:Echvi_0738
MKNLLQSFSSIKSLIKNIDFAKLNQLSQKVDLNEMVGIVSQMSESDLAKMMKMMKGGGKK
RELPPVNGDFYSLEKTLPPHEQEIVAKVRDFMEKEVRPIANEYWNKGHFPMHIIPKMAEL
GIAGLTYKGYGCPGHSALLEGFLAMEMARVDTSISTFFGVQSGLAMGSIYVCGSEEQKQE
WLPKMQKMDVIGAFGLTEPKVGSGVAGGLTTTCKREGDEWVINGQKKWIGNATFSDITVI
WARDLDDQQVKGFIVRKDNPGFHPEKIENKMALRTVQNALITMKDCRVPESDRLQNANSF
KDTSEILRLTRAGVAWQAVGCGRGAYEAALRYTNERKQFGRPIAGFQLVQDLLVTMLGDL
TAMQTMVYRLSKMQDAGELKDEHASLAKVFCTLRMRTIVDHSRELFGGNGILLEYDIARF
VADAEAIYSYEGTKEINSLIVGRAITGHSAFV
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory