SitesBLAST
Comparing GFF1675 FitnessBrowser__Marino:GFF1675 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)
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)
49% identity, 97% coverage: 2:372/382 of query aligns to 61:439/445 of P12694
- Y158 (= Y92) binding
- R159 (= R93) binding ; to W: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs769688327
- Q190 (= Q124) to K: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- S206 (= S140) binding
- S207 (= S141) binding
- P208 (= P142) binding
- T211 (= T145) binding ; to M: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123503
- Q212 (= Q146) binding
- E238 (= E172) binding
- G239 (= G173) binding
- A240 (= A174) binding
- G249 (≠ A183) 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 (= A187) to T: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs199599175
- A254 (= A188) to D: in MSUD1A; uncertain significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity
- R265 (= R199) 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 (= N201) 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 (= Y203) binding
- A285 (= A219) 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 (= G224) 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 (= R231) to H: in MSUD1A; uncertain significance; decreased affinity for the cofactor thiamine diphosphate; decreased 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs200137189
- T310 (= T244) 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
- S337 (= S271) modified: Phosphoserine; by BCKDK; mutation to A: Substantially decreases the stability of the BCKD complex.
- S347 (= S281) mutation to A: Does not affect the stability of the BCKD complex.
- F409 (≠ V342) 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 (= Y346) 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 (= Y371) 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
2bffA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
49% identity, 97% coverage: 2:372/382 of query aligns to 11:386/392 of 2bffA
- active site: E71 (≠ A55), S157 (= S141), R282 (= R266), H286 (= H270), S287 (= S271), Y295 (= Y279)
- binding manganese (ii) ion: E188 (= E172), N217 (= N201), Y219 (= Y203)
- 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 (= Q91), Y108 (= Y92), R109 (= R93), L159 (= L143), G187 (= G171), E188 (= E172), G189 (= G173), A190 (= A174), R215 (= R199), N217 (= N201), Y219 (= Y203), A220 (= A204), I221 (= I205), H286 (= H270)
2bewA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
49% identity, 97% coverage: 2:372/382 of query aligns to 11:384/390 of 2bewA
- active site: E71 (≠ A55), S157 (= S141), R282 (= R266), H286 (= H270), S287 (= S271), Y295 (= Y279)
- binding manganese (ii) ion: E188 (= E172), N217 (= N201), Y219 (= Y203), A220 (= A204)
- binding c2-1-hydroxyphenyl-thiamin diphosphate: M82 (= M66), Q107 (= Q91), Y108 (= Y92), R109 (= R93), L159 (= L143), G187 (= G171), E188 (= E172), G189 (= G173), A190 (= A174), R215 (= R199), N217 (= N201), Y219 (= Y203), A220 (= A204), I221 (= I205), H286 (= H270)
2bevA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
49% identity, 97% coverage: 2:372/382 of query aligns to 11:384/390 of 2bevA
- active site: E71 (≠ A55), S157 (= S141), R282 (= R266), H286 (= H270), S287 (= S271), Y295 (= Y279)
- binding manganese (ii) ion: E188 (= E172), N217 (= N201), Y219 (= Y203), A220 (= A204)
- binding c2-1-hydroxy-2-methyl-butyl-thiamin diphosphate: F80 (= F64), Q107 (= Q91), Y108 (= Y92), R109 (= R93), S157 (= S141), L159 (= L143), G187 (= G171), E188 (= E172), G189 (= G173), A190 (= A174), R215 (= R199), N217 (= N201), Y219 (= Y203), A220 (= A204), I221 (= I205), H286 (= H270)
2beuA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
49% identity, 97% coverage: 2:372/382 of query aligns to 11:384/390 of 2beuA
- active site: E71 (≠ A55), S157 (= S141), R282 (= R266), H286 (= H270), S287 (= S271), Y295 (= Y279)
- binding manganese (ii) ion: E188 (= E172), N217 (= N201), Y219 (= Y203), A220 (= A204)
- binding c2-1-hydroxy-3-methyl-propyl-thiamin diphosphate: Q107 (= Q91), Y108 (= Y92), R109 (= R93), S157 (= S141), L159 (= L143), G187 (= G171), E188 (= E172), G189 (= G173), A190 (= A174), R215 (= R199), N217 (= N201), Y219 (= Y203), A220 (= A204), I221 (= I205), H286 (= H270)
1wciA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
49% identity, 97% coverage: 2:372/382 of query aligns to 11:382/388 of 1wciA
- active site: E71 (≠ A55), S157 (= S141), R282 (= R266), H286 (= H270), S287 (= S271), Y295 (= Y279)
- binding manganese (ii) ion: E188 (= E172), N217 (= N201), Y219 (= Y203), A220 (= A204)
- binding c2-1-hydroxy-3-methyl-butyl-thiamin: Q107 (= Q91), Y108 (= Y92), R109 (= R93), L159 (= L143), G187 (= G171), E188 (= E172), G189 (= G173), A190 (= A174), R215 (= R199), N217 (= N201), Y219 (= Y203), A220 (= A204), I221 (= I205), H286 (= H270)
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)
48% identity, 97% coverage: 2:372/382 of query aligns to 57:435/441 of P11960
- S333 (= S271) modified: Phosphoserine; by BCKDK
1dtwA Human branched-chain alpha-keto acid dehydrogenase (see paper)
48% identity, 97% coverage: 2:372/382 of query aligns to 10:376/382 of 1dtwA
- active site: E70 (≠ A55), S156 (= S141), R281 (= R266), H285 (= H270), S286 (= S271), Y294 (= Y279)
- binding potassium ion: S155 (= S140), S156 (= S141), P157 (= P142), T160 (= T145), Q161 (= Q146)
- binding magnesium ion: E187 (= E172), N216 (= N201), Y218 (= Y203)
- binding thiamine diphosphate: Q106 (= Q91), Y107 (= Y92), R108 (= R93), L158 (= L143), G186 (= G171), E187 (= E172), G188 (= G173), A189 (= A174), R214 (= R199), N216 (= N201), Y218 (= Y203), A219 (= A204), I220 (= I205), H285 (= H270)
1v1mA Crosstalk between cofactor binding and the phosphorylation loop conformation in the bckd machine (see paper)
46% identity, 97% coverage: 2:372/382 of query aligns to 11:366/372 of 1v1mA
- active site: E71 (≠ A55), S157 (= S141), R282 (= R266)
- binding manganese (ii) ion: E188 (= E172), N217 (= N201), Y219 (= Y203)
- binding thiamine diphosphate: R109 (= R93), L159 (= L143), G187 (= G171), E188 (= E172), G189 (= G173), A190 (= A174), R215 (= R199), N217 (= N201), Y219 (= Y203), A220 (= A204), I221 (= I205)
1oluA Roles of his291-alpha and his146-beta' in the reductive acylation reaction catalyzed by human branched-chain alpha-ketoacid dehydrogenase (see paper)
46% identity, 97% coverage: 2:372/382 of query aligns to 10:360/366 of 1oluA
- active site: E67 (≠ A55), S153 (= S141), R278 (= R266)
- binding magnesium ion: E184 (= E172), N213 (= N201), Y215 (= Y203)
- binding thiamine diphosphate: R105 (= R93), L155 (= L143), G183 (= G171), E184 (= E172), G185 (= G173), A186 (= A174), N213 (= N201), A216 (= A204), I217 (= I205)
2bfcA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
46% identity, 97% coverage: 2:372/382 of query aligns to 11:365/371 of 2bfcA
- active site: E71 (≠ A55), S157 (= S141), R282 (= R266)
- binding manganese (ii) ion: E188 (= E172), N217 (= N201), Y219 (= Y203)
- 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 (= R93), L159 (= L143), G187 (= G171), E188 (= E172), G189 (= G173), A190 (= A174), R215 (= R199), N217 (= N201), Y219 (= Y203), A220 (= A204), I221 (= I205)
3dufA Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
37% identity, 92% coverage: 9:361/382 of query aligns to 16:360/365 of 3dufA
- active site: S62 (≠ A55), I139 (≠ S141), R264 (= R266), H268 (= H270), T269 (≠ S271), Y278 (= Y279)
- binding magnesium ion: D170 (≠ E172), N199 (= N201), F201 (≠ Y203)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1r)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: Y99 (= Y92), R100 (= R93), I141 (≠ L143), G169 (= G171), D170 (≠ E172), G171 (= G173), N199 (= N201), F201 (≠ Y203), A202 (= A204), H268 (= 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)
40% identity, 88% coverage: 30:364/382 of query aligns to 32:367/367 of Q5SLR4
1umdA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methyl-2-oxopentanoate as an intermediate (see paper)
40% identity, 87% coverage: 30:361/382 of query aligns to 27:359/362 of 1umdA
- active site: I52 (≠ A55), S139 (= S141), R264 (= R266), H268 (= H270), S269 (= S271), Y277 (= Y279)
- binding 2-oxo-4-methylpentanoic acid: F61 (= F64), Y90 (= Y92), S139 (= S141)
- binding magnesium ion: D170 (≠ E172), N199 (= N201), Y201 (= Y203)
- binding thiamine diphosphate: Y89 (≠ Q91), Y90 (= Y92), R91 (= R93), P140 (= P142), I141 (≠ L143), G169 (= G171), D170 (≠ E172), G171 (= G173), N199 (= N201), Y201 (= Y203), A202 (= A204), I203 (= I205), H268 (= H270)
1umcA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methylpentanoate (see paper)
40% identity, 87% coverage: 30:361/382 of query aligns to 27:359/362 of 1umcA
- active site: I52 (≠ A55), S139 (= S141), R264 (= R266), H268 (= H270), S269 (= S271), Y277 (= Y279)
- binding 4-methyl valeric acid: Y90 (= Y92), H126 (= H128)
- binding magnesium ion: D170 (≠ E172), N199 (= N201), Y201 (= Y203)
- binding thiamine diphosphate: Y89 (≠ Q91), Y90 (= Y92), R91 (= R93), I141 (≠ L143), G169 (= G171), D170 (≠ E172), G171 (= G173), N199 (= N201), Y201 (= Y203), I203 (= I205), H268 (= H270)
1umbA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 in holo-form (see paper)
40% identity, 87% coverage: 30:361/382 of query aligns to 27:359/362 of 1umbA
- active site: I52 (≠ A55), S139 (= S141), R264 (= R266), H268 (= H270), S269 (= S271), Y277 (= Y279)
- binding magnesium ion: D170 (≠ E172), N199 (= N201), Y201 (= Y203)
- binding thiamine diphosphate: Y89 (≠ Q91), Y90 (= Y92), R91 (= R93), P140 (= P142), I141 (≠ L143), G169 (= G171), D170 (≠ E172), G171 (= G173), N199 (= N201), Y201 (= Y203), A202 (= A204), I203 (= I205), H268 (= H270)
1w85A The crystal structure of pyruvate dehydrogenase e1 bound to the peripheral subunit binding domain of e2 (see paper)
36% identity, 92% coverage: 9:361/382 of query aligns to 16:354/358 of 1w85A
- active site: S62 (≠ A55), I139 (≠ S141), R264 (= R266), H268 (= H270), T269 (≠ S271)
- binding magnesium ion: D170 (≠ E172), N199 (= N201), F201 (≠ Y203)
- binding thiamine diphosphate: Y99 (= Y92), R100 (= R93), I139 (≠ S141), I141 (≠ L143), G169 (= G171), D170 (≠ E172), G171 (= G173), G172 (≠ A174), N199 (= N201), A202 (= A204), I203 (= I205), H268 (= H270)
1qs0A Crystal structure of pseudomonas putida 2-oxoisovalerate dehydrogenase (branched-chain alpha-keto acid dehydrogenase, e1b) (see paper)
38% identity, 93% coverage: 4:360/382 of query aligns to 45:407/407 of 1qs0A
- active site: V95 (≠ A55), G181 (≠ S141), R307 (= R266), H311 (= H270), S312 (= S271), Y320 (= Y279)
- binding magnesium ion: D212 (≠ E172), N241 (= N201), W243 (≠ Y203)
- binding thiamine diphosphate: Y132 (= Y92), R133 (= R93), L183 (= L143), G211 (= G171), D212 (≠ E172), G213 (= G173), A214 (= A174), N241 (= N201), W243 (≠ Y203), A244 (= A204), I245 (= I205), H311 (= H270)
3dv0A Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
35% identity, 92% coverage: 9:361/382 of query aligns to 16:345/349 of 3dv0A
- active site: S62 (≠ A55), I139 (≠ S141), R264 (= R266), H268 (= H270)
- binding magnesium ion: D170 (≠ E172), N199 (= N201), F201 (≠ Y203)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: Y99 (= Y92), R100 (= R93), I141 (≠ L143), G169 (= G171), D170 (≠ E172), G171 (= G173), N199 (= N201), F201 (≠ Y203), A202 (= A204), I203 (= I205), R264 (= R266)
3dv0E Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
34% identity, 92% coverage: 9:361/382 of query aligns to 16:340/344 of 3dv0E
- active site: S62 (≠ A55), I139 (≠ S141), R264 (= R266)
- binding magnesium ion: G169 (= G171), D170 (≠ E172), Q197 (≠ R199), N199 (= N201)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: Y99 (= Y92), R100 (= R93), I139 (≠ S141), I141 (≠ L143), G169 (= G171), D170 (≠ E172), G171 (= G173), N199 (= N201), F201 (≠ Y203), A202 (= A204), I203 (= I205)
Query Sequence
>GFF1675 FitnessBrowser__Marino:GFF1675
MFTDGAEFRIPTFKLLKQDGKLYKSAKAPDLDKDKALRIYRAMVTTRILDERMLAAQRQG
RLSFYMQCTGEEAAVIGSAAALDDGDMIMAQYREQGALAYRGFTIDEFMNQLFGNEMDYG
KGRQMPVHYGSKKLNYMTISSPLATQIPQAAGYAYGQKLRGEGLCTITYFGEGAASEGDF
HAALNMAAVHRVPVIFLCRNNGYAISTPAAEQFAADGVAPRAYGYKMDVIRVDGNDILAM
YQATQEARKLAVEHNRPVLIEAMSYRLAAHSSSDDPSGYRSKDEEAVWREKDPILRMRLW
LESKKWWSEDDEKQLQENMRREVLETMKRAQKRPPPPLESLVSDVYDEVPPALAEQFEKL
KAHIGRHPDEYPKSAEHAKGGA
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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