SitesBLAST
Comparing Ga0059261_2273 FitnessBrowser__Korea:Ga0059261_2273 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)
1qs0A Crystal structure of pseudomonas putida 2-oxoisovalerate dehydrogenase (branched-chain alpha-keto acid dehydrogenase, e1b) (see paper)
58% identity, 94% coverage: 12:414/429 of query aligns to 5:407/407 of 1qs0A
- active site: V95 (≠ R102), G181 (= G188), R307 (= R314), H311 (= H318), S312 (= S319), Y320 (= Y327)
- binding magnesium ion: D212 (≠ E219), N241 (= N248), W243 (= W250)
- binding thiamine diphosphate: Y132 (= Y139), R133 (= R140), L183 (= L190), G211 (= G218), D212 (≠ E219), G213 (= G220), A214 (≠ S221), N241 (= N248), W243 (= W250), A244 (= A251), I245 (= I252), H311 (= H318)
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)
39% identity, 83% coverage: 60:414/429 of query aligns to 78:427/445 of P12694
- Y158 (= Y139) binding thiamine diphosphate
- R159 (= R140) binding thiamine diphosphate; to W: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs769688327
- Q190 (= Q171) to K: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- S206 (= S187) binding K(+)
- S207 (≠ G188) binding thiamine diphosphate
- P208 (≠ N189) binding K(+)
- T211 (= T192) binding K(+); to M: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123503
- Q212 (= Q193) binding K(+)
- E238 (= E219) binding Mg(2+)
- G239 (= G220) binding thiamine diphosphate
- A240 (≠ S221) binding thiamine diphosphate
- G249 (≠ A230) 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 (= A234) to T: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs199599175
- A254 (≠ T235) to D: in MSUD1A; uncertain significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs373713279
- R265 (≠ V246) 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 (= N248) 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 (≠ W250) binding Mg(2+)
- A285 (= A267) 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 (= G272) 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 (= R279) to H: in MSUD1A; uncertain significance; decreased affinity for the cofactor thiamine diphosphate; decreased 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs200137189
- T310 (= T292) to R: in MSUD1A; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852875
- I326 (= I308) to T: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- H336 (= H318) binding thiamine diphosphate
- S337 (= S319) modified: Phosphoserine; by BCKDK; mutation to A: Substantially decreases the stability of the BCKD complex.
- S347 (= S329) mutation to A: Does not affect the stability of the BCKD complex.
- F409 (= F396) 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 (≠ F400) 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)
39% identity, 83% coverage: 60:414/429 of query aligns to 74:423/441 of P11960
- S333 (= S319) modified: Phosphoserine; by BCKDK
2bffA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
39% identity, 83% coverage: 60:414/429 of query aligns to 28:374/392 of 2bffA
- active site: E71 (≠ R102), S157 (≠ G188), R282 (= R314), H286 (= H318), S287 (= S319), Y295 (= Y327)
- binding manganese (ii) ion: E188 (= E219), N217 (= N248), Y219 (≠ W250)
- 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 (≠ S138), Y108 (= Y139), R109 (= R140), L159 (= L190), G187 (= G218), E188 (= E219), G189 (= G220), A190 (≠ S221), R215 (≠ V246), N217 (= N248), Y219 (≠ W250), A220 (= A251), I221 (= I252), H286 (= H318)
2bewA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
39% identity, 83% coverage: 60:414/429 of query aligns to 28:372/390 of 2bewA
- active site: E71 (≠ R102), S157 (≠ G188), R282 (= R314), H286 (= H318), S287 (= S319), Y295 (= Y327)
- binding manganese (ii) ion: E188 (= E219), N217 (= N248), Y219 (≠ W250), A220 (= A251)
- binding c2-1-hydroxyphenyl-thiamin diphosphate: M82 (= M113), Q107 (≠ S138), Y108 (= Y139), R109 (= R140), L159 (= L190), G187 (= G218), E188 (= E219), G189 (= G220), A190 (≠ S221), R215 (≠ V246), N217 (= N248), Y219 (≠ W250), A220 (= A251), I221 (= I252), H286 (= H318)
2bevA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
39% identity, 83% coverage: 60:414/429 of query aligns to 28:372/390 of 2bevA
- active site: E71 (≠ R102), S157 (≠ G188), R282 (= R314), H286 (= H318), S287 (= S319), Y295 (= Y327)
- binding manganese (ii) ion: E188 (= E219), N217 (= N248), Y219 (≠ W250), A220 (= A251)
- binding c2-1-hydroxy-2-methyl-butyl-thiamin diphosphate: F80 (= F111), Q107 (≠ S138), Y108 (= Y139), R109 (= R140), S157 (≠ G188), L159 (= L190), G187 (= G218), E188 (= E219), G189 (= G220), A190 (≠ S221), R215 (≠ V246), N217 (= N248), Y219 (≠ W250), A220 (= A251), I221 (= I252), H286 (= H318)
2beuA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
39% identity, 83% coverage: 60:414/429 of query aligns to 28:372/390 of 2beuA
- active site: E71 (≠ R102), S157 (≠ G188), R282 (= R314), H286 (= H318), S287 (= S319), Y295 (= Y327)
- binding manganese (ii) ion: E188 (= E219), N217 (= N248), Y219 (≠ W250), A220 (= A251)
- binding c2-1-hydroxy-3-methyl-propyl-thiamin diphosphate: Q107 (≠ S138), Y108 (= Y139), R109 (= R140), S157 (≠ G188), L159 (= L190), G187 (= G218), E188 (= E219), G189 (= G220), A190 (≠ S221), R215 (≠ V246), N217 (= N248), Y219 (≠ W250), A220 (= A251), I221 (= I252), H286 (= H318)
1wciA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
39% identity, 83% coverage: 60:414/429 of query aligns to 28:370/388 of 1wciA
- active site: E71 (≠ R102), S157 (≠ G188), R282 (= R314), H286 (= H318), S287 (= S319), Y295 (= Y327)
- binding manganese (ii) ion: E188 (= E219), N217 (= N248), Y219 (≠ W250), A220 (= A251)
- binding c2-1-hydroxy-3-methyl-butyl-thiamin: Q107 (≠ S138), Y108 (= Y139), R109 (= R140), L159 (= L190), G187 (= G218), E188 (= E219), G189 (= G220), A190 (≠ S221), R215 (≠ V246), N217 (= N248), Y219 (≠ W250), A220 (= A251), I221 (= I252), H286 (= H318)
1dtwA Human branched-chain alpha-keto acid dehydrogenase (see paper)
38% identity, 83% coverage: 60:414/429 of query aligns to 27:364/382 of 1dtwA
- active site: E70 (≠ R102), S156 (≠ G188), R281 (= R314), H285 (= H318), S286 (= S319), Y294 (= Y327)
- binding potassium ion: S155 (= S187), S156 (≠ G188), P157 (≠ N189), T160 (= T192), Q161 (= Q193)
- binding magnesium ion: E187 (= E219), N216 (= N248), Y218 (≠ W250)
- binding thiamine diphosphate: Q106 (≠ S138), Y107 (= Y139), R108 (= R140), L158 (= L190), G186 (= G218), E187 (= E219), G188 (= G220), A189 (≠ S221), R214 (≠ V246), N216 (= N248), Y218 (≠ W250), A219 (= A251), I220 (= I252), H285 (= H318)
1v1mA Crosstalk between cofactor binding and the phosphorylation loop conformation in the bckd machine (see paper)
36% identity, 83% coverage: 60:414/429 of query aligns to 28:354/372 of 1v1mA
- active site: E71 (≠ R102), S157 (≠ G188), R282 (= R314)
- binding manganese (ii) ion: E188 (= E219), N217 (= N248), Y219 (≠ W250)
- binding thiamine diphosphate: R109 (= R140), L159 (= L190), G187 (= G218), E188 (= E219), G189 (= G220), A190 (≠ S221), R215 (≠ V246), N217 (= N248), Y219 (≠ W250), A220 (= A251), I221 (= I252)
1oluA Roles of his291-alpha and his146-beta' in the reductive acylation reaction catalyzed by human branched-chain alpha-ketoacid dehydrogenase (see paper)
36% identity, 83% coverage: 60:414/429 of query aligns to 24:348/366 of 1oluA
- active site: E67 (≠ R102), S153 (≠ G188), R278 (= R314)
- binding magnesium ion: E184 (= E219), N213 (= N248), Y215 (≠ W250)
- binding thiamine diphosphate: R105 (= R140), L155 (= L190), G183 (= G218), E184 (= E219), G185 (= G220), A186 (≠ S221), N213 (= N248), A216 (= A251), I217 (= I252)
2bfcA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
36% identity, 83% coverage: 60:414/429 of query aligns to 28:353/371 of 2bfcA
- active site: E71 (≠ R102), S157 (≠ G188), R282 (= R314)
- binding manganese (ii) ion: E188 (= E219), N217 (= N248), Y219 (≠ W250)
- binding 2-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-2-oxo-2,3-dihydro-1,3-thiazol-5-yl}ethyl trihydrogendiphosphate: R109 (= R140), L159 (= L190), G187 (= G218), E188 (= E219), G189 (= G220), A190 (≠ S221), R215 (≠ V246), N217 (= N248), Y219 (≠ W250), A220 (= A251), I221 (= I252)
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)
35% identity, 83% coverage: 61:417/429 of query aligns to 16:366/367 of Q5SLR4
- F66 (= F111) binding substrate
- YYR 94:96 (≠ SYR 138:140) binding thiamine diphosphate
- Y95 (= Y139) binding substrate
- MPEH 128:131 (≠ LPIM 172:175) binding substrate
- S144 (≠ G188) binding substrate
- SPI 144:146 (≠ GNL 188:190) binding thiamine diphosphate
- 174:180 (vs. 218:224, 57% identical) binding thiamine diphosphate
- D175 (≠ E219) binding Mg(2+)
- N204 (= N248) binding Mg(2+)
- NFYAI 204:208 (≠ NQWAI 248:252) binding thiamine diphosphate
- Y206 (≠ W250) binding Mg(2+)
- H273 (= H318) 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)
35% identity, 83% coverage: 61:417/429 of query aligns to 11:361/362 of 1umdA
- active site: I52 (≠ R102), S139 (≠ G188), R264 (= R314), H268 (= H318), S269 (= S319), Y277 (= Y327)
- binding 2-oxo-4-methylpentanoic acid: F61 (= F111), Y90 (= Y139), S139 (≠ G188)
- binding magnesium ion: D170 (≠ E219), N199 (= N248), Y201 (≠ W250)
- binding thiamine diphosphate: Y89 (≠ S138), Y90 (= Y139), R91 (= R140), P140 (≠ N189), I141 (≠ L190), G169 (= G218), D170 (≠ E219), G171 (= G220), N199 (= N248), Y201 (≠ W250), A202 (= A251), I203 (= I252), H268 (= H318)
1umcA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methylpentanoate (see paper)
35% identity, 83% coverage: 61:417/429 of query aligns to 11:361/362 of 1umcA
- active site: I52 (≠ R102), S139 (≠ G188), R264 (= R314), H268 (= H318), S269 (= S319), Y277 (= Y327)
- binding 4-methyl valeric acid: Y90 (= Y139), H126 (≠ M175)
- binding magnesium ion: D170 (≠ E219), N199 (= N248), Y201 (≠ W250)
- binding thiamine diphosphate: Y89 (≠ S138), Y90 (= Y139), R91 (= R140), I141 (≠ L190), G169 (= G218), D170 (≠ E219), G171 (= G220), N199 (= N248), Y201 (≠ W250), I203 (= I252), H268 (= H318)
1umbA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 in holo-form (see paper)
35% identity, 83% coverage: 61:417/429 of query aligns to 11:361/362 of 1umbA
- active site: I52 (≠ R102), S139 (≠ G188), R264 (= R314), H268 (= H318), S269 (= S319), Y277 (= Y327)
- binding magnesium ion: D170 (≠ E219), N199 (= N248), Y201 (≠ W250)
- binding thiamine diphosphate: Y89 (≠ S138), Y90 (= Y139), R91 (= R140), P140 (≠ N189), I141 (≠ L190), G169 (= G218), D170 (≠ E219), G171 (= G220), N199 (= N248), Y201 (≠ W250), A202 (= A251), I203 (= I252), H268 (= H318)
3dufA Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
35% identity, 80% coverage: 76:418/429 of query aligns to 36:363/365 of 3dufA
- active site: S62 (≠ R102), I139 (≠ L190), R264 (= R314), H268 (= H318), T269 (≠ S319), Y278 (= Y327)
- binding magnesium ion: D170 (≠ E219), N199 (= N248), F201 (≠ W250)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1r)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: Y99 (= Y139), R100 (= R140), I141 (≠ T192), G169 (= G218), D170 (≠ E219), G171 (= G220), N199 (= N248), F201 (≠ W250), A202 (= A251), H268 (= H318)
1w85A The crystal structure of pyruvate dehydrogenase e1 bound to the peripheral subunit binding domain of e2 (see paper)
33% identity, 80% coverage: 76:418/429 of query aligns to 36:357/358 of 1w85A
- active site: S62 (≠ R102), I139 (≠ L190), R264 (= R314), H268 (= H318), T269 (≠ S319)
- binding magnesium ion: D170 (≠ E219), N199 (= N248), F201 (≠ W250)
- binding thiamine diphosphate: Y99 (= Y139), R100 (= R140), I139 (≠ L190), I141 (≠ T192), G169 (= G218), D170 (≠ E219), G171 (= G220), G172 (≠ S221), N199 (= N248), A202 (= A251), I203 (= I252), H268 (= H318)
3dv0A Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
33% identity, 80% coverage: 76:418/429 of query aligns to 36:348/349 of 3dv0A
- active site: S62 (≠ R102), I139 (≠ L190), R264 (= R314), H268 (= H318)
- binding magnesium ion: D170 (≠ E219), N199 (= N248), F201 (≠ W250)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: Y99 (= Y139), R100 (= R140), I141 (≠ T192), G169 (= G218), D170 (≠ E219), G171 (= G220), N199 (= N248), F201 (≠ W250), A202 (= A251), I203 (= I252), R264 (= R314)
3dv0E Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
33% identity, 80% coverage: 76:418/429 of query aligns to 36:343/344 of 3dv0E
- active site: S62 (≠ R102), I139 (≠ L190), R264 (= R314)
- binding magnesium ion: G169 (= G218), D170 (≠ E219), Q197 (≠ V246), N199 (= N248)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: Y99 (= Y139), R100 (= R140), I139 (≠ L190), I141 (≠ T192), G169 (= G218), D170 (≠ E219), G171 (= G220), N199 (= N248), F201 (≠ W250), A202 (= A251), I203 (= I252)
Query Sequence
>Ga0059261_2273 FitnessBrowser__Korea:Ga0059261_2273
MTVDAKRANLPPLSLHVPEPKFRPGDAVDFTEVAVPPAGAQSRPDTAADPSSFHELAYTL
VRVLDDNGQAVGPWNPKLDPDTLRKMLHDMALVRAFDERMFRAQRQGKTSFYMKCTGEEA
VAIAAAHALASDDMCFPSYRQQGLLIARGYSLVQMMNQIYSNKGDDLAGKQLPIMYSSKE
KGFFSISGNLTTQYPQAVGWAMASAAKGDTRIAATWCGEGSTAEGDFHSALTFATVYKAP
VILNVVNNQWAISSFSGFAGAEATTFAARALGYGIAGLRVDGNDALAVYAATLWAAERAR
TNQGPTLIEHFTYRTEGHSTSDDPTQYRSAGEPTAWPLGDPIARLKAHLIAIGEWDEERH
VEMDRELAEQVKVAQKEAEKNGILGHGLHQPLDSLFDGVFEEMPWHLREQRQMMLDEEEA
SGRPWARKQ
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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