SitesBLAST
Comparing WP_205630629.1 NCBI__GCF_001484605.1:WP_205630629.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
3dufA Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
39% identity, 87% coverage: 29:349/369 of query aligns to 37:359/365 of 3dufA
- active site: S62 (≠ A54), I139 (= I131), R264 (= R255), H268 (= H259), T269 (= T260), Y278 (= Y268)
- binding magnesium ion: D170 (= D162), N199 (= N191), F201 (≠ W193)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1r)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: Y99 (= Y91), R100 (= R92), I141 (= I133), G169 (= G161), D170 (= D162), G171 (= G163), N199 (= N191), F201 (≠ W193), A202 (= A194), H268 (= H259)
1w85A The crystal structure of pyruvate dehydrogenase e1 bound to the peripheral subunit binding domain of e2 (see paper)
38% identity, 87% coverage: 29:349/369 of query aligns to 37:353/358 of 1w85A
- active site: S62 (≠ A54), I139 (= I131), R264 (= R255), H268 (= H259), T269 (= T260)
- binding magnesium ion: D170 (= D162), N199 (= N191), F201 (≠ W193)
- binding thiamine diphosphate: Y99 (= Y91), R100 (= R92), I139 (= I131), I141 (= I133), G169 (= G161), D170 (= D162), G171 (= G163), G172 (≠ A164), N199 (= N191), A202 (= A194), I203 (= I195), H268 (= H259)
3dv0A Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
37% identity, 87% coverage: 29:349/369 of query aligns to 37:344/349 of 3dv0A
- active site: S62 (≠ A54), I139 (= I131), R264 (= R255), H268 (= H259)
- binding magnesium ion: D170 (= D162), N199 (= N191), F201 (≠ W193)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: Y99 (= Y91), R100 (= R92), I141 (= I133), G169 (= G161), D170 (= D162), G171 (= G163), N199 (= N191), F201 (≠ W193), A202 (= A194), I203 (= I195), R264 (= R255)
3dv0E Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
36% identity, 87% coverage: 29:349/369 of query aligns to 37:339/344 of 3dv0E
- active site: S62 (≠ A54), I139 (= I131), R264 (= R255)
- binding magnesium ion: G169 (= G161), D170 (= D162), Q197 (≠ S189), N199 (= N191)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: Y99 (= Y91), R100 (= R92), I139 (= I131), I141 (= I133), G169 (= G161), D170 (= D162), G171 (= G163), N199 (= N191), F201 (≠ W193), A202 (= A194), I203 (= I195)
1w88A The crystal structure of pyruvate dehydrogenase e1(d180n,e183q) bound to the peripheral subunit binding domain of e2 (see paper)
35% identity, 87% coverage: 29:349/369 of query aligns to 36:335/340 of 1w88A
- active site: S61 (≠ A54), I138 (= I131), R263 (= R267)
- binding magnesium ion: D169 (= D162), N198 (= N191), F200 (≠ W193)
- binding thiamine diphosphate: Y98 (= Y91), R99 (= R92), I140 (= I133), G168 (= G161), D169 (= D162), G170 (= G163), A201 (= A194), I202 (= I195)
P12694 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial; Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain; BCKDE1A; BCKDH E1-alpha; EC 1.2.4.4 from Homo sapiens (Human) (see 14 papers)
34% identity, 93% coverage: 17:358/369 of query aligns to 87:436/445 of P12694
- Y158 (= Y91) binding thiamine diphosphate
- R159 (= R92) binding thiamine diphosphate; to W: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs769688327
- Q190 (≠ R112) to K: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- S206 (≠ A127) binding K(+)
- S207 (≠ T128) binding thiamine diphosphate
- P208 (= P129) binding K(+)
- T211 (≠ A135) binding K(+); to M: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123503
- Q212 (= Q136) binding K(+)
- E238 (≠ D162) binding Mg(2+)
- G239 (= G163) binding thiamine diphosphate
- A240 (= A164) binding thiamine diphosphate
- G249 (≠ A173) to S: in MSUD1A; no effect on solubility; no effect on mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852874
- A253 (= A177) to T: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs199599175
- A254 (= A178) to D: in MSUD1A; uncertain significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs373713279
- R265 (≠ S189) binding thiamine diphosphate; to W: in MSUD1A; uncertain significance; no effect on solubility; no effect on mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852873
- N267 (= N191) binding Mg(2+); to S: in MSUD1A; uncertain significance; no effect on solubility; no effect on mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; decreased affinity for the cofactor thiamine diphosphate; decreased 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs1568508047
- Y269 (≠ W193) binding Mg(2+)
- A285 (= A208) to P: in MSUD1A; no effect on solubility; no effect on mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123508
- G290 (= G213) to R: in MSUD1A; no effect on solubility; no effect on mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; decreased 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852871
- R297 (= R220) to H: in MSUD1A; uncertain significance; decreased affinity for the cofactor thiamine diphosphate; decreased 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs200137189
- T310 (= T233) to R: in MSUD1A; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852875
- I326 (= I249) to T: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- H336 (= H259) binding thiamine diphosphate
- S337 (≠ T260) modified: Phosphoserine; by BCKDK; mutation to A: Substantially decreases the stability of the BCKD complex.
- S347 (≠ D270) mutation to A: Does not affect the stability of the BCKD complex.
- F409 (= F331) to C: in MSUD1A; decreased solubility; loss of mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852872
- Y413 (= Y335) to C: in MSUD1A; uncertain significance; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123508
Sites not aligning to the query:
- 1:45 modified: transit peptide, Mitochondrion
- 438 Y → N: in MSUD1A; decreased solubility; loss of mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852870
P11960 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial; Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain; BCKDE1A; BCKDH E1-alpha; EC 1.2.4.4 from Rattus norvegicus (Rat) (see paper)
34% identity, 93% coverage: 17:358/369 of query aligns to 83:432/441 of P11960
- S333 (≠ T260) modified: Phosphoserine; by BCKDK
2bffA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
34% identity, 93% coverage: 17:358/369 of query aligns to 37:383/392 of 2bffA
- active site: E71 (≠ A54), S157 (≠ T128), R282 (= R255), H286 (= H259), S287 (≠ T260), Y295 (= Y268)
- binding manganese (ii) ion: E188 (≠ D162), N217 (= N191), Y219 (≠ W193)
- binding 2-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-2-oxo-2,3-dihydro-1,3-thiazol-5-yl}ethyl trihydrogendiphosphate: Q107 (≠ S90), Y108 (= Y91), R109 (= R92), L159 (≠ I133), G187 (= G161), E188 (≠ D162), G189 (= G163), A190 (= A164), R215 (≠ S189), N217 (= N191), Y219 (≠ W193), A220 (= A194), I221 (= I195), H286 (= H259)
2bewA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
34% identity, 93% coverage: 17:358/369 of query aligns to 37:381/390 of 2bewA
- active site: E71 (≠ A54), S157 (≠ T128), R282 (= R255), H286 (= H259), S287 (≠ T260), Y295 (= Y268)
- binding manganese (ii) ion: E188 (≠ D162), N217 (= N191), Y219 (≠ W193), A220 (= A194)
- binding c2-1-hydroxyphenyl-thiamin diphosphate: M82 (≠ P65), Q107 (≠ S90), Y108 (= Y91), R109 (= R92), L159 (≠ I133), G187 (= G161), E188 (≠ D162), G189 (= G163), A190 (= A164), R215 (≠ S189), N217 (= N191), Y219 (≠ W193), A220 (= A194), I221 (= I195), H286 (= H259)
2bevA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
34% identity, 93% coverage: 17:358/369 of query aligns to 37:381/390 of 2bevA
- active site: E71 (≠ A54), S157 (≠ T128), R282 (= R255), H286 (= H259), S287 (≠ T260), Y295 (= Y268)
- binding manganese (ii) ion: E188 (≠ D162), N217 (= N191), Y219 (≠ W193), A220 (= A194)
- binding c2-1-hydroxy-2-methyl-butyl-thiamin diphosphate: F80 (≠ L63), Q107 (≠ S90), Y108 (= Y91), R109 (= R92), S157 (≠ T128), L159 (≠ I133), G187 (= G161), E188 (≠ D162), G189 (= G163), A190 (= A164), R215 (≠ S189), N217 (= N191), Y219 (≠ W193), A220 (= A194), I221 (= I195), H286 (= H259)
2beuA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
34% identity, 93% coverage: 17:358/369 of query aligns to 37:381/390 of 2beuA
- active site: E71 (≠ A54), S157 (≠ T128), R282 (= R255), H286 (= H259), S287 (≠ T260), Y295 (= Y268)
- binding manganese (ii) ion: E188 (≠ D162), N217 (= N191), Y219 (≠ W193), A220 (= A194)
- binding c2-1-hydroxy-3-methyl-propyl-thiamin diphosphate: Q107 (≠ S90), Y108 (= Y91), R109 (= R92), S157 (≠ T128), L159 (≠ I133), G187 (= G161), E188 (≠ D162), G189 (= G163), A190 (= A164), R215 (≠ S189), N217 (= N191), Y219 (≠ W193), A220 (= A194), I221 (= I195), H286 (= H259)
1wciA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
34% identity, 93% coverage: 17:358/369 of query aligns to 37:379/388 of 1wciA
- active site: E71 (≠ A54), S157 (≠ T128), R282 (= R255), H286 (= H259), S287 (≠ T260), Y295 (= Y268)
- binding manganese (ii) ion: E188 (≠ D162), N217 (= N191), Y219 (≠ W193), A220 (= A194)
- binding c2-1-hydroxy-3-methyl-butyl-thiamin: Q107 (≠ S90), Y108 (= Y91), R109 (= R92), L159 (≠ I133), G187 (= G161), E188 (≠ D162), G189 (= G163), A190 (= A164), R215 (≠ S189), N217 (= N191), Y219 (≠ W193), A220 (= A194), I221 (= I195), H286 (= H259)
1dtwA Human branched-chain alpha-keto acid dehydrogenase (see paper)
33% identity, 93% coverage: 17:358/369 of query aligns to 36:373/382 of 1dtwA