SitesBLAST
Comparing WP_076581700.1 NCBI__GCF_001971705.1:WP_076581700.1 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)
41% identity, 79% coverage: 35:331/375 of query aligns to 36:330/365 of 3dufA
- active site: S62 (= S61), I139 (= I137), R264 (= R266), H268 (= H270), T269 (= T271), Y278 (= Y279)
- binding magnesium ion: D170 (= D168), N199 (= N197), F201 (≠ W199)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1r)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: Y99 (= Y98), R100 (= R99), I141 (= I139), G169 (= G167), D170 (= D168), G171 (= G169), N199 (= N197), F201 (≠ W199), A202 (= A200), H268 (= H270)
1w85A The crystal structure of pyruvate dehydrogenase e1 bound to the peripheral subunit binding domain of e2 (see paper)
40% identity, 79% coverage: 35:331/375 of query aligns to 36:324/358 of 1w85A
- active site: S62 (= S61), I139 (= I137), R264 (= R266), H268 (= H270), T269 (= T271)
- binding magnesium ion: D170 (= D168), N199 (= N197), F201 (≠ W199)
- binding thiamine diphosphate: Y99 (= Y98), R100 (= R99), I139 (= I137), I141 (= I139), G169 (= G167), D170 (= D168), G171 (= G169), G172 (≠ S170), N199 (= N197), A202 (= A200), I203 (= I201), H268 (= H270)
3dv0A Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
39% identity, 79% coverage: 35:331/375 of query aligns to 36:315/349 of 3dv0A
- active site: S62 (= S61), I139 (= I137), R264 (= R266), H268 (= H270)
- binding magnesium ion: D170 (= D168), N199 (= N197), F201 (≠ W199)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: Y99 (= Y98), R100 (= R99), I141 (= I139), G169 (= G167), D170 (= D168), G171 (= G169), N199 (= N197), F201 (≠ W199), A202 (= A200), I203 (= I201), R264 (= R266)
3dv0E Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
39% identity, 79% coverage: 35:331/375 of query aligns to 36:310/344 of 3dv0E
- active site: S62 (= S61), I139 (= I137), R264 (= R266)
- binding magnesium ion: G169 (= G167), D170 (= D168), Q197 (≠ N195), N199 (= N197)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: Y99 (= Y98), R100 (= R99), I139 (= I137), I141 (= I139), G169 (= G167), D170 (= D168), G171 (= G169), N199 (= N197), F201 (≠ W199), A202 (= A200), I203 (= I201)
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, 95% coverage: 18:373/375 of query aligns to 77:441/445 of P12694
- Y158 (= Y98) binding thiamine diphosphate
- R159 (= R99) binding thiamine diphosphate; to W: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs769688327
- Q190 (vs. gap) to K: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- S206 (≠ N136) binding K(+)
- S207 (≠ I137) binding thiamine diphosphate
- P208 (≠ S138) binding K(+)
- T211 (≠ G141) binding K(+); to M: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123503
- Q212 (≠ H142) binding K(+)
- E238 (≠ D168) binding Mg(2+)
- G239 (= G169) binding thiamine diphosphate
- A240 (≠ S170) binding thiamine diphosphate
- G249 (≠ A179) 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 (= A183) to T: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs199599175
- A254 (≠ G184) to D: in MSUD1A; uncertain significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs373713279
- R265 (≠ N195) 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 (= N197) 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 (≠ W199) binding Mg(2+)
- A285 (= A215) 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 (≠ A220) 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 (≠ Q227) to H: in MSUD1A; uncertain significance; decreased affinity for the cofactor thiamine diphosphate; decreased 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs200137189
- T310 (= T240) to R: in MSUD1A; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852875
- I326 (= I260) to T: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- H336 (= H270) binding thiamine diphosphate
- S337 (≠ T271) modified: Phosphoserine; by BCKDK; mutation to A: Substantially decreases the stability of the BCKD complex.
- S347 (≠ D281) mutation to A: Does not affect the stability of the BCKD complex.
- F409 (= F341) 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 (= Y345) 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
- Y438 (≠ E370) to N: in MSUD1A; decreased solubility; loss of mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852870
Sites not aligning to the query:
- 1:45 modified: transit peptide, Mitochondrion
1w88A The crystal structure of pyruvate dehydrogenase e1(d180n,e183q) bound to the peripheral subunit binding domain of e2 (see paper)
38% identity, 79% coverage: 35:331/375 of query aligns to 35:306/340 of 1w88A
- active site: S61 (= S61), I138 (= I137), R263 (= R266)
- binding magnesium ion: D169 (= D168), N198 (= N197), F200 (≠ W199)
- binding thiamine diphosphate: Y98 (= Y98), R99 (= R99), I140 (= I139), G168 (= G167), D169 (= D168), G170 (= G169), A201 (= A200), I202 (= I201)
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, 95% coverage: 18:373/375 of query aligns to 73:437/441 of P11960
- S333 (≠ T271) modified: Phosphoserine; by BCKDK
2bffA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
34% identity, 95% coverage: 18:373/375 of query aligns to 27:388/392 of 2bffA
- active site: E71 (≠ S61), S157 (≠ I137), R282 (= R266), H286 (= H270), S287 (≠ T271), Y295 (= Y279)
- binding manganese (ii) ion: E188 (≠ D168), N217 (= N197), Y219 (≠ W199)
- 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 (= Q97), Y108 (= Y98), R109 (= R99), L159 (≠ I139), G187 (= G167), E188 (≠ D168), G189 (= G169), A190 (≠ S170), R215 (≠ N195), N217 (= N197), Y219 (≠ W199), A220 (= A200), I221 (= I201), H286 (= H270)
Q5SLR4 2-oxoisovalerate dehydrogenase subunit alpha; Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain; BCKDH E1-alpha; EC 1.2.4.4 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
39% identity, 95% coverage: 5:360/375 of query aligns to 2:364/367 of Q5SLR4
- F66 (≠ T70) binding substrate
- YYR 94:96 (≠ QYR 97:99) binding thiamine diphosphate
- Y95 (= Y98) binding substrate
- MPEH 128:131 (vs. gap) binding substrate
- S144 (≠ I137) binding substrate
- SPI 144:146 (≠ ISI 137:139) binding thiamine diphosphate
- 174:180 (vs. 167:173, 86% identical) binding thiamine diphosphate
- D175 (= D168) binding Mg(2+)
- N204 (= N197) binding Mg(2+)
- NFYAI 204:208 (≠ NQWAI 197:201) binding thiamine diphosphate
- Y206 (≠ W199) binding Mg(2+)
- H273 (= H270) binding thiamine diphosphate
1umdA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methyl-2-oxopentanoate as an intermediate (see paper)
39% identity, 93% coverage: 11:360/375 of query aligns to 3:359/362 of 1umdA
- active site: I52 (≠ S61), S139 (≠ I137), R264 (= R266), H268 (= H270), S269 (≠ T271), Y277 (= Y279)
- binding 2-oxo-4-methylpentanoic acid: F61 (≠ T70), Y90 (= Y98), S139 (≠ I137)
- binding magnesium ion: D170 (= D168), N199 (= N197), Y201 (≠ W199)
- binding thiamine diphosphate: Y89 (≠ Q97), Y90 (= Y98), R91 (= R99), P140 (≠ S138), I141 (= I139), G169 (= G167), D170 (= D168), G171 (= G169), N199 (= N197), Y201 (≠ W199), A202 (= A200), I203 (= I201), H268 (= H270)
1umcA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methylpentanoate (see paper)
39% identity, 93% coverage: 11:360/375 of query aligns to 3:359/362 of 1umcA
- active site: I52 (≠ S61), S139 (≠ I137), R264 (= R266), H268 (= H270), S269 (≠ T271), Y277 (= Y279)
- binding 4-methyl valeric acid: Y90 (= Y98), H126 (vs. gap)
- binding magnesium ion: D170 (= D168), N199 (= N197), Y201 (≠ W199)
- binding thiamine diphosphate: Y89 (≠ Q97), Y90 (= Y98), R91 (= R99), I141 (= I139), G169 (= G167), D170 (= D168), G171 (= G169), N199 (= N197), Y201 (≠ W199), I203 (= I201), H268 (= H270)
1umbA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 in holo-form (see paper)
39% identity, 93% coverage: 11:360/375 of query aligns to 3:359/362 of 1umbA
- active site: I52 (≠ S61), S139 (≠ I137), R264 (= R266), H268 (= H270), S269 (≠ T271), Y277 (= Y279)
- binding magnesium ion: D170 (= D168), N199 (= N197), Y201 (≠ W199)
- binding thiamine diphosphate: Y89 (≠ Q97), Y90 (= Y98), R91 (= R99), P140 (≠ S138), I141 (= I139), G169 (= G167), D170 (= D168), G171 (= G169), N199 (= N197), Y201 (≠ W199), A202 (= A200), I203 (= I201), H268 (= H270)
2bewA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
33% identity, 95% coverage: 18:373/375 of query aligns to 27:386/390 of 2bewA