SitesBLAST
Comparing RR42_RS33045 FitnessBrowser__Cup4G11:RR42_RS33045 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)
38% identity, 89% coverage: 30:346/355 of query aligns to 38:355/365 of 3dufA
- active site: S62 (≠ A54), I139 (≠ V131), R264 (= R256), H268 (= H260), T269 (= T261), Y278 (= Y269)
- 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 (= H260)
1w85A The crystal structure of pyruvate dehydrogenase e1 bound to the peripheral subunit binding domain of e2 (see paper)
37% identity, 89% coverage: 30:346/355 of query aligns to 38:349/358 of 1w85A
- active site: S62 (≠ A54), I139 (≠ V131), R264 (= R256), H268 (= H260), T269 (= T261)
- binding magnesium ion: D170 (= D162), N199 (= N191), F201 (≠ W193)
- binding thiamine diphosphate: Y99 (= Y91), R100 (= R92), I139 (≠ V131), I141 (= I133), G169 (= G161), D170 (= D162), G171 (= G163), G172 (= G164), N199 (= N191), A202 (= A194), I203 (= I195), H268 (= H260)
3dv0A Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
37% identity, 89% coverage: 30:346/355 of query aligns to 38:340/349 of 3dv0A
- active site: S62 (≠ A54), I139 (≠ V131), R264 (= R256), H268 (= H260)
- 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 (= R256)
3dv0E Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
36% identity, 89% coverage: 30:346/355 of query aligns to 38:335/344 of 3dv0E
- active site: S62 (≠ A54), I139 (≠ V131), R264 (= R256)
- binding magnesium ion: G169 (= G161), D170 (= D162), Q197 (≠ N189), N199 (= N191)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: Y99 (= Y91), R100 (= R92), I139 (≠ V131), 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, 89% coverage: 30:346/355 of query aligns to 37:331/340 of 1w88A
- active site: S61 (≠ A54), I138 (≠ V131), R263 (= R256)
- 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)
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)
37% identity, 97% coverage: 6:348/355 of query aligns to 10:361/367 of Q5SLR4
1umdA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methyl-2-oxopentanoate as an intermediate (see paper)
37% identity, 97% coverage: 6:348/355 of query aligns to 5:356/362 of 1umdA
- active site: I52 (≠ A54), S139 (≠ V131), R264 (= R256), H268 (= H260), S269 (≠ T261), Y277 (= Y269)
- binding 2-oxo-4-methylpentanoic acid: F61 (≠ T63), Y90 (= Y91), S139 (≠ V131)
- binding magnesium ion: D170 (= D162), N199 (= N191), Y201 (≠ W193)
- binding thiamine diphosphate: Y89 (≠ S90), Y90 (= Y91), R91 (= R92), P140 (= P132), I141 (= I133), G169 (= G161), D170 (= D162), G171 (= G163), N199 (= N191), Y201 (≠ W193), A202 (= A194), I203 (= I195), H268 (= H260)
1umcA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methylpentanoate (see paper)
37% identity, 97% coverage: 6:348/355 of query aligns to 5:356/362 of 1umcA
- active site: I52 (≠ A54), S139 (≠ V131), R264 (= R256), H268 (= H260), S269 (≠ T261), Y277 (= Y269)
- binding 4-methyl valeric acid: Y90 (= Y91), H126 (≠ A123)
- binding magnesium ion: D170 (= D162), N199 (= N191), Y201 (≠ W193)
- binding thiamine diphosphate: Y89 (≠ S90), Y90 (= Y91), R91 (= R92), I141 (= I133), G169 (= G161), D170 (= D162), G171 (= G163), N199 (= N191), Y201 (≠ W193), I203 (= I195), H268 (= H260)
1umbA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 in holo-form (see paper)
37% identity, 97% coverage: 6:348/355 of query aligns to 5:356/362 of 1umbA
- active site: I52 (≠ A54), S139 (≠ V131), R264 (= R256), H268 (= H260), S269 (≠ T261), Y277 (= Y269)
- binding magnesium ion: D170 (= D162), N199 (= N191), Y201 (≠ W193)
- binding thiamine diphosphate: Y89 (≠ S90), Y90 (= Y91), R91 (= R92), P140 (= P132), I141 (= I133), G169 (= G161), D170 (= D162), G171 (= G163), N199 (= N191), Y201 (≠ W193), A202 (= A194), I203 (= I195), H268 (= H260)
1qs0A Crystal structure of pseudomonas putida 2-oxoisovalerate dehydrogenase (branched-chain alpha-keto acid dehydrogenase, e1b) (see paper)
33% identity, 96% coverage: 6:346/355 of query aligns to 46:403/407 of 1qs0A
- active site: V95 (≠ A54), G181 (vs. gap), R307 (= R256), H311 (= H260), S312 (≠ T261), Y320 (= Y269)
- binding magnesium ion: D212 (= D162), N241 (= N191), W243 (= W193)
- binding thiamine diphosphate: Y132 (= Y91), R133 (= R92), L183 (≠ I133), G211 (= G161), D212 (= D162), G213 (= G163), A214 (≠ G164), N241 (= N191), W243 (= W193), A244 (= A194), I245 (= I195), H311 (= H260)
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)
31% identity, 94% coverage: 15:346/355 of query aligns to 82:423/445 of P12694
- Y158 (= Y91) binding
- R159 (= R92) binding ; 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 (≠ C130) binding
- S207 (≠ V131) binding
- P208 (= P132) binding
- T211 (≠ N135) binding ; to M: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123503
- Q212 (= Q136) binding
- E238 (≠ D162) binding
- G239 (= G163) binding
- A240 (≠ G164) binding
- G249 (= G173) 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 (≠ G178) to D: in MSUD1A; uncertain significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity
- R265 (≠ N189) binding ; 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 ; 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
- Y269 (≠ W193) binding
- A285 (= A209) 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 (≠ A214) 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 (≠ Q221) to H: in MSUD1A; uncertain significance; decreased affinity for the cofactor thiamine diphosphate; decreased 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs200137189
- T310 (= T234) to R: in MSUD1A; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852875
- I326 (= I250) to T: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- H336 (= H260) binding
- S337 (≠ T261) modified: Phosphoserine; by BCKDK; mutation to A: Substantially decreases the stability of the BCKD complex.
- S347 (≠ D271) mutation to A: Does not affect the stability of the BCKD complex.
- F409 (= F332) 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 (= Y336) 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
2bewA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
31% identity, 94% coverage: 15:346/355 of query aligns to 32:368/390 of 2bewA
- active site: E71 (≠ A54), S157 (≠ V131), R282 (= R256), H286 (= H260), S287 (≠ T261), Y295 (= Y269)
- binding manganese (ii) ion: E188 (≠ D162), N217 (= N191), Y219 (≠ W193), A220 (= A194)
- binding c2-1-hydroxyphenyl-thiamin diphosphate: M82 (≠ A65), Q107 (≠ S90), Y108 (= Y91), R109 (= R92), L159 (≠ I133), G187 (= G161), E188 (≠ D162), G189 (= G163), A190 (≠ G164), R215 (≠ N189), N217 (= N191), Y219 (≠ W193), A220 (= A194), I221 (= I195), H286 (= H260)
2bevA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
31% identity, 94% coverage: 15:346/355 of query aligns to 32:368/390 of 2bevA
- active site: E71 (≠ A54), S157 (≠ V131), R282 (= R256), H286 (= H260), S287 (≠ T261), Y295 (= Y269)
- binding manganese (ii) ion: E188 (≠ D162), N217 (= N191), Y219 (≠ W193), A220 (= A194)
- binding c2-1-hydroxy-2-methyl-butyl-thiamin diphosphate: F80 (≠ T63), Q107 (≠ S90), Y108 (= Y91), R109 (= R92), S157 (≠ V131), L159 (≠ I133), G187 (= G161), E188 (≠ D162), G189 (= G163), A190 (≠ G164), R215 (≠ N189), N217 (= N191), Y219 (≠ W193), A220 (= A194), I221 (= I195), H286 (= H260)
2beuA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
31% identity, 94% coverage: 15:346/355 of query aligns to 32:368/390 of 2beuA
- active site: E71 (≠ A54), S157 (≠ V131), R282 (= R256), H286 (= H260), S287 (≠ T261), Y295 (= Y269)
- 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 (≠ V131), L159 (≠ I133), G187 (= G161), E188 (≠ D162), G189 (= G163), A190 (≠ G164), R215 (≠ N189), N217 (= N191), Y219 (≠ W193), A220 (= A194), I221 (= I195), H286 (= H260)
1wciA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
31% identity, 94% coverage: 15:346/355 of query aligns to 32:366/388 of 1wciA
- active site: E71 (≠ A54), S157 (≠ V131), R282 (= R256), H286 (= H260), S287 (≠ T261), Y295 (= Y269)
- 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 (≠ G164), R215 (≠ N189), N217 (= N191), Y219 (≠ W193), A220 (= A194), I221 (= I195), H286 (= H260)
2bffA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
31% identity, 94% coverage: 15:346/355 of query aligns to 32:370/392 of 2bffA
- active site: E71 (≠ A54), S157 (≠ V131), R282 (= R256), H286 (= H260), S287 (≠ T261), Y295 (= Y269)
- 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 (≠ G164), R215 (≠ N189), N217 (= N191), Y219 (≠ W193), A220 (= A194), I221 (= I195), H286 (= H260)
1dtwA Human branched-chain alpha-keto acid dehydrogenase (see paper)
31% identity, 94% coverage: 15:346/355 of query aligns to 31:360/382 of 1dtwA
- active site: E70 (≠ A54), S156 (≠ V131), R281 (= R256), H285 (= H260), S286 (≠ T261), Y294 (= Y269)
- binding potassium ion: S155 (≠ C130), S156 (≠ V131), P157 (= P132), T160 (≠ N135), Q161 (= Q136)
- binding magnesium ion: E187 (≠ D162), N216 (= N191), Y218 (≠ W193)
- binding thiamine diphosphate: Q106 (≠ S90), Y107 (= Y91), R108 (= R92), L158 (≠ I133), G186 (= G161), E187 (≠ D162), G188 (= G163), A189 (≠ G164), R214 (≠ N189), N216 (= N191), Y218 (≠ W193), A219 (= A194), I220 (= I195), H285 (= H260)
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)
31% identity, 95% coverage: 15:352/355 of query aligns to 78:425/441 of P11960
- S333 (≠ T261) modified: Phosphoserine; by BCKDK
1v1mA Crosstalk between cofactor binding and the phosphorylation loop conformation in the bckd machine (see paper)
29% identity, 95% coverage: 15:352/355 of query aligns to 32:356/372 of 1v1mA
- active site: E71 (≠ A54), S157 (≠ V131), R282 (= R256)
- binding manganese (ii) ion: E188 (≠ D162), N217 (= N191), Y219 (≠ W193)
- binding thiamine diphosphate: R109 (= R92), L159 (≠ I133), G187 (= G161), E188 (≠ D162), G189 (= G163), A190 (≠ G164), R215 (≠ N189), N217 (= N191), Y219 (≠ W193), A220 (= A194), I221 (= I195)
P16387 Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial; Pyruvate dehydrogenase complex component E1 alpha; PDHE1-A; EC 1.2.4.1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
29% identity, 89% coverage: 21:336/355 of query aligns to 58:391/420 of P16387
- S313 (≠ T261) modified: Phosphoserine; by PDK1 and PDK2
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
Query Sequence
>RR42_RS33045 FitnessBrowser__Cup4G11:RR42_RS33045
MATVATFDIEYTQFLDPQGEPTQALPAFALDPEALLPLYRAMVLTRQFDLKAIALQRTGQ
IGTFASALGQEAVGVGVASAMRAQDVLVPSYRDHAAQFQRGVSMTESLLYWGGDERGNAF
AAAPHDFANCVPIGNQVCHAAGIAYAMKLRREPRATVCLLGDGGTSKGDFYEGMNMAGAW
HAPLVLVVNNNQWAISMPRSQQTAARTLAQKAIAAGIPGLQVDGNDVVAVRQVTLDALER
ARGGGGATLIEAITYRLGDHTTADDASRYRDSEQVRQHWLLEPVARLRNYLLRLGAWDAP
REDALAKDCAAQVAAAVQAYLATPLPETAAMFDCLYASLPKALAGQVATAHRFAP
Or try a new SitesBLAST search
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