SitesBLAST
Comparing Pf6N2E2_481 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_481 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)
87% identity, 99% coverage: 5:409/411 of query aligns to 3:407/407 of 1qs0A
- active site: V95 (= V97), G181 (= G183), R307 (= R309), H311 (= H313), S312 (= S314), Y320 (= Y322)
- binding magnesium ion: D212 (= D214), N241 (= N243), W243 (= W245)
- binding thiamine diphosphate: Y132 (= Y134), R133 (= R135), L183 (= L185), G211 (= G213), D212 (= D214), G213 (= G215), A214 (= A216), N241 (= N243), W243 (= W245), A244 (= A246), I245 (= I247), H311 (= H313)
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)
37% identity, 96% coverage: 17:409/411 of query aligns to 21:423/441 of P11960
- S333 (= S314) modified: Phosphoserine; by BCKDK
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)
38% identity, 86% coverage: 55:409/411 of query aligns to 78:427/445 of P12694
- Y158 (= Y134) binding thiamine diphosphate
- R159 (= R135) binding thiamine diphosphate; to W: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs769688327
- Q190 (= Q166) to K: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- S206 (= S182) binding K(+)
- S207 (≠ G183) binding thiamine diphosphate
- P208 (≠ N184) binding K(+)
- T211 (= T187) binding K(+); to M: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123503
- Q212 (= Q188) binding K(+)
- E238 (≠ D214) binding Mg(2+)
- G239 (= G215) binding thiamine diphosphate
- A240 (= A216) binding thiamine diphosphate
- G249 (≠ A225) 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 (= A229) to T: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs199599175
- A254 (≠ H230) to D: in MSUD1A; uncertain significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity
- R265 (≠ V241) 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 (= N243) 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
- Y269 (≠ W245) binding Mg(2+)
- A285 (= A262) 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 (= G267) 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 (= R274) to H: in MSUD1A; uncertain significance; decreased affinity for the cofactor thiamine diphosphate; decreased 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs200137189
- T310 (≠ S287) to R: in MSUD1A; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852875
- I326 (= I303) to T: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- H336 (= H313) binding thiamine diphosphate
- S337 (= S314) modified: Phosphoserine; by BCKDK; mutation to A: Substantially decreases the stability of the BCKD complex.
- S347 (≠ P324) mutation to A: Does not affect the stability of the BCKD complex.
- F409 (= F391) 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 (= Y395) 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
2bffA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
38% identity, 86% coverage: 55:409/411 of query aligns to 28:374/392 of 2bffA
- active site: E71 (≠ V97), S157 (≠ G183), R282 (= R309), H286 (= H313), S287 (= S314), Y295 (= Y322)
- binding manganese (ii) ion: E188 (≠ D214), N217 (= N243), Y219 (≠ W245)
- 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 (≠ T133), Y108 (= Y134), R109 (= R135), L159 (= L185), G187 (= G213), E188 (≠ D214), G189 (= G215), A190 (= A216), R215 (≠ V241), N217 (= N243), Y219 (≠ W245), A220 (= A246), I221 (= I247), H286 (= H313)
1wciA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
38% identity, 86% coverage: 55:409/411 of query aligns to 28:370/388 of 1wciA
- active site: E71 (≠ V97), S157 (≠ G183), R282 (= R309), H286 (= H313), S287 (= S314), Y295 (= Y322)
- binding manganese (ii) ion: E188 (≠ D214), N217 (= N243), Y219 (≠ W245), A220 (= A246)
- binding c2-1-hydroxy-3-methyl-butyl-thiamin: Q107 (≠ T133), Y108 (= Y134), R109 (= R135), L159 (= L185), G187 (= G213), E188 (≠ D214), G189 (= G215), A190 (= A216), R215 (≠ V241), N217 (= N243), Y219 (≠ W245), A220 (= A246), I221 (= I247), H286 (= H313)
2bewA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
38% identity, 86% coverage: 55:409/411 of query aligns to 28:372/390 of 2bewA
- active site: E71 (≠ V97), S157 (≠ G183), R282 (= R309), H286 (= H313), S287 (= S314), Y295 (= Y322)
- binding manganese (ii) ion: E188 (≠ D214), N217 (= N243), Y219 (≠ W245), A220 (= A246)
- binding c2-1-hydroxyphenyl-thiamin diphosphate: M82 (= M108), Q107 (≠ T133), Y108 (= Y134), R109 (= R135), L159 (= L185), G187 (= G213), E188 (≠ D214), G189 (= G215), A190 (= A216), R215 (≠ V241), N217 (= N243), Y219 (≠ W245), A220 (= A246), I221 (= I247), H286 (= H313)
2bevA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
38% identity, 86% coverage: 55:409/411 of query aligns to 28:372/390 of 2bevA
- active site: E71 (≠ V97), S157 (≠ G183), R282 (= R309), H286 (= H313), S287 (= S314), Y295 (= Y322)
- binding manganese (ii) ion: E188 (≠ D214), N217 (= N243), Y219 (≠ W245), A220 (= A246)
- binding c2-1-hydroxy-2-methyl-butyl-thiamin diphosphate: F80 (= F106), Q107 (≠ T133), Y108 (= Y134), R109 (= R135), S157 (≠ G183), L159 (= L185), G187 (= G213), E188 (≠ D214), G189 (= G215), A190 (= A216), R215 (≠ V241), N217 (= N243), Y219 (≠ W245), A220 (= A246), I221 (= I247), H286 (= H313)
2beuA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
38% identity, 86% coverage: 55:409/411 of query aligns to 28:372/390 of 2beuA
- active site: E71 (≠ V97), S157 (≠ G183), R282 (= R309), H286 (= H313), S287 (= S314), Y295 (= Y322)
- binding manganese (ii) ion: E188 (≠ D214), N217 (= N243), Y219 (≠ W245), A220 (= A246)
- binding c2-1-hydroxy-3-methyl-propyl-thiamin diphosphate: Q107 (≠ T133), Y108 (= Y134), R109 (= R135), S157 (≠ G183), L159 (= L185), G187 (= G213), E188 (≠ D214), G189 (= G215), A190 (= A216), R215 (≠ V241), N217 (= N243), Y219 (≠ W245), A220 (= A246), I221 (= I247), H286 (= H313)
1dtwA Human branched-chain alpha-keto acid dehydrogenase (see paper)
38% identity, 86% coverage: 55:409/411 of query aligns to 27:364/382 of 1dtwA
- active site: E70 (≠ V97), S156 (≠ G183), R281 (= R309), H285 (= H313), S286 (= S314), Y294 (= Y322)
- binding potassium ion: S155 (= S182), S156 (≠ G183), P157 (≠ N184), T160 (= T187), Q161 (= Q188)
- binding magnesium ion: E187 (≠ D214), N216 (= N243), Y218 (≠ W245)
- binding thiamine diphosphate: Q106 (≠ T133), Y107 (= Y134), R108 (= R135), L158 (= L185), G186 (= G213), E187 (≠ D214), G188 (= G215), A189 (= A216), R214 (≠ V241), N216 (= N243), Y218 (≠ W245), A219 (= A246), I220 (= I247), H285 (= H313)
1v1mA Crosstalk between cofactor binding and the phosphorylation loop conformation in the bckd machine (see paper)
35% identity, 86% coverage: 55:409/411 of query aligns to 28:354/372 of 1v1mA
- active site: E71 (≠ V97), S157 (≠ G183), R282 (= R309)
- binding manganese (ii) ion: E188 (≠ D214), N217 (= N243), Y219 (≠ W245)
- binding thiamine diphosphate: R109 (= R135), L159 (= L185), G187 (= G213), E188 (≠ D214), G189 (= G215), A190 (= A216), R215 (≠ V241), N217 (= N243), Y219 (≠ W245), A220 (= A246), I221 (= I247)
1umdA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methyl-2-oxopentanoate as an intermediate (see paper)
36% identity, 86% coverage: 56:409/411 of query aligns to 11:358/362 of 1umdA
- active site: I52 (≠ V97), S139 (≠ G183), R264 (= R309), H268 (= H313), S269 (= S314), Y277 (= Y322)
- binding 2-oxo-4-methylpentanoic acid: F61 (= F106), Y90 (= Y134), S139 (≠ G183)
- binding magnesium ion: D170 (= D214), N199 (= N243), Y201 (≠ W245)
- binding thiamine diphosphate: Y89 (≠ T133), Y90 (= Y134), R91 (= R135), P140 (≠ N184), I141 (≠ L185), G169 (= G213), D170 (= D214), G171 (= G215), N199 (= N243), Y201 (≠ W245), A202 (= A246), I203 (= I247), H268 (= H313)
1umcA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methylpentanoate (see paper)
36% identity, 86% coverage: 56:409/411 of query aligns to 11:358/362 of 1umcA
- active site: I52 (≠ V97), S139 (≠ G183), R264 (= R309), H268 (= H313), S269 (= S314), Y277 (= Y322)
- binding 4-methyl valeric acid: Y90 (= Y134), H126 (≠ M170)
- binding magnesium ion: D170 (= D214), N199 (= N243), Y201 (≠ W245)
- binding thiamine diphosphate: Y89 (≠ T133), Y90 (= Y134), R91 (= R135), I141 (≠ L185), G169 (= G213), D170 (= D214), G171 (= G215), N199 (= N243), Y201 (≠ W245), I203 (= I247), H268 (= H313)
1umbA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 in holo-form (see paper)
36% identity, 86% coverage: 56:409/411 of query aligns to 11:358/362 of 1umbA
- active site: I52 (≠ V97), S139 (≠ G183), R264 (= R309), H268 (= H313), S269 (= S314), Y277 (= Y322)
- binding magnesium ion: D170 (= D214), N199 (= N243), Y201 (≠ W245)
- binding thiamine diphosphate: Y89 (≠ T133), Y90 (= Y134), R91 (= R135), P140 (≠ N184), I141 (≠ L185), G169 (= G213), D170 (= D214), G171 (= G215), N199 (= N243), Y201 (≠ W245), A202 (= A246), I203 (= I247), H268 (= H313)
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)
36% identity, 86% coverage: 56:409/411 of query aligns to 16:363/367 of Q5SLR4
- F66 (= F106) binding substrate
- YYR 94:96 (≠ TYR 133:135) binding thiamine diphosphate
- Y95 (= Y134) binding substrate
- MPEH 128:131 (≠ LPIM 167:170) binding substrate
- S144 (≠ G183) binding substrate
- SPI 144:146 (≠ GNL 183:185) binding thiamine diphosphate
- 174:180 (vs. 213:219, 86% identical) binding thiamine diphosphate
- D175 (= D214) binding Mg(2+)
- N204 (= N243) binding Mg(2+)
- NFYAI 204:208 (≠ NQWAI 243:247) binding thiamine diphosphate
- Y206 (≠ W245) binding Mg(2+)
- H273 (= H313) binding thiamine diphosphate
1oluA Roles of his291-alpha and his146-beta' in the reductive acylation reaction catalyzed by human branched-chain alpha-ketoacid dehydrogenase (see paper)
35% identity, 86% coverage: 55:409/411 of query aligns to 24:348/366 of 1oluA
- active site: E67 (≠ V97), S153 (≠ G183), R278 (= R309)
- binding magnesium ion: E184 (≠ D214), N213 (= N243), Y215 (≠ W245)
- binding thiamine diphosphate: R105 (= R135), L155 (= L185), G183 (= G213), E184 (≠ D214), G185 (= G215), A186 (= A216), N213 (= N243), A216 (= A246), I217 (= I247)
2bfcA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
34% identity, 86% coverage: 55:409/411 of query aligns to 28:353/371 of 2bfcA
- active site: E71 (≠ V97), S157 (≠ G183), R282 (= R309)
- binding manganese (ii) ion: E188 (≠ D214), N217 (= N243), Y219 (≠ W245)
- 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 (= R135), L159 (= L185), G187 (= G213), E188 (≠ D214), G189 (= G215), A190 (= A216), R215 (≠ V241), N217 (= N243), Y219 (≠ W245), A220 (= A246), I221 (= I247)
3dufA Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
34% identity, 80% coverage: 78:405/411 of query aligns to 43:355/365 of 3dufA
- active site: S62 (≠ V97), I139 (≠ F178), R264 (= R309), H268 (= H313), T269 (≠ S314), Y278 (= Y322)
- binding magnesium ion: D170 (= D214), N199 (= N243), F201 (≠ W245)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1r)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: Y99 (= Y134), R100 (= R135), I141 (≠ L185), G169 (= G213), D170 (= D214), G171 (= G215), N199 (= N243), F201 (≠ W245), A202 (= A246), H268 (= H313)
1w85A The crystal structure of pyruvate dehydrogenase e1 bound to the peripheral subunit binding domain of e2 (see paper)
32% identity, 80% coverage: 78:405/411 of query aligns to 43:349/358 of 1w85A
- active site: S62 (≠ V97), I139 (≠ F178), R264 (= R309), H268 (= H313), T269 (≠ S314)
- binding magnesium ion: D170 (= D214), N199 (= N243), F201 (≠ W245)
- binding thiamine diphosphate: Y99 (= Y134), R100 (= R135), I139 (≠ F178), I141 (≠ L185), G169 (= G213), D170 (= D214), G171 (= G215), G172 (≠ A216), N199 (= N243), A202 (= A246), I203 (= I247), H268 (= H313)
3dv0A Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
32% identity, 80% coverage: 78:405/411 of query aligns to 43:340/349 of 3dv0A
- active site: S62 (≠ V97), I139 (≠ F178), R264 (= R309), H268 (= H313)
- binding magnesium ion: D170 (= D214), N199 (= N243), F201 (≠ W245)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: Y99 (= Y134), R100 (= R135), I141 (≠ L185), G169 (= G213), D170 (= D214), G171 (= G215), N199 (= N243), F201 (≠ W245), A202 (= A246), I203 (= I247), R264 (= R309)
3dv0E Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
31% identity, 80% coverage: 78:405/411 of query aligns to 43:335/344 of 3dv0E
- active site: S62 (≠ V97), I139 (≠ F178), R264 (= R309)
- binding magnesium ion: G169 (= G213), D170 (= D214), Q197 (≠ V241), N199 (= N243)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: Y99 (= Y134), R100 (= R135), I139 (≠ F178), I141 (≠ L185), G169 (= G213), D170 (= D214), G171 (= G215), N199 (= N243), F201 (≠ W245), A202 (= A246), I203 (= I247)
Query Sequence
>Pf6N2E2_481 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_481
MNPAYEPLRLHVPEPSGRPGCKTDFSYLHLSDAGTVRKPSIDVEPADTADLARSLIRVLD
DQGNAHGPWAEDVPLDILRKGMRAMLKTRIYDNRMVVAQRQKKMSFYMQSLGEEAIGSGQ
ALALNIDDMCFPTYRQQSILMAREVPLVGMICQLLSNERDPLKGRQLPIMYSVKDAGFFT
ISGNLATQFIQGVGWGMASAIKGDTKIASAWIGDGATAESDFHTALTFAHVYRAPVILNV
VNNQWAISTFQAIAGGEATTFAGRGVGCGIASLRVDGNDFMAVYAASRWAAERARRNLGP
ALIEWVTYRAGPHSTSDDPSKYRPADDWSHFPLGDPIARLKQHMVKIGQWSEEEHAAVTA
ELEAEVIAAQKEAEQYGTLAGGQIPSAATMFEDVYKEMPEHLKRQRQQLGI
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