SitesBLAST
Comparing WP_004511701.1 NCBI__GCF_000012925.1:WP_004511701.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
P29803 Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial; PDHE1-A type II; EC 1.2.4.1 from Homo sapiens (Human) (see 4 papers)
44% identity, 98% coverage: 7:325/325 of query aligns to 52:368/388 of P29803
- M227 (≠ I184) to V: in SPGF70; uncertain significance; dbSNP:rs200969445
- S230 (= S187) mutation to A: Slightly reduces enzyme activity.
- S291 (= S250) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4; mutation to A: Strongly reduces enzyme activity. Increases enzyme activity in stem cells.; mutation S->E,D: Abolishes enzyme activity. Increases neuronal cell death in response to glutamate excitotoxicity.
- S293 (= S252) modified: Phosphoserine; mutation to A: Increases enzyme activity in stem cells.; mutation to D: Abolishes enzyme activity. Increases neuronal cell death in response to glutamate excitotoxicity.
- S298 (≠ K256) modified: Phosphoserine; by PDK3; mutation to A: Slightly reduces enzyme activity.
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)
44% identity, 96% coverage: 12:324/325 of query aligns to 79:391/420 of P16387
- S313 (= S250) modified: Phosphoserine; by PDK1 and PDK2
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
Q10489 Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial; PDHE1-A; EC 1.2.4.1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
44% identity, 96% coverage: 12:324/325 of query aligns to 76:388/409 of Q10489
- Y306 (≠ F246) modified: Phosphotyrosine
- S310 (= S250) modified: Phosphoserine
- S312 (= S252) modified: Phosphoserine
Sites not aligning to the query:
- 6 modified: Phosphothreonine
P26267 Pyruvate dehydrogenase E1 component subunit alpha type I, mitochondrial; PDHA1; PDHE1-A; EC 1.2.4.1 from Ascaris suum (Pig roundworm) (Ascaris lumbricoides) (see paper)
44% identity, 96% coverage: 13:324/325 of query aligns to 56:365/396 of P26267
- S289 (= S250) modified: Phosphoserine
- S296 (≠ K256) modified: Phosphoserine
P35486 Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial; PDHE1-A type I; EC 1.2.4.1 from Mus musculus (Mouse) (see 2 papers)
43% identity, 96% coverage: 15:325/325 of query aligns to 62:370/390 of P35486
- S232 (= S187) modified: Phosphoserine; by PDK1
- S293 (= S250) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- S300 (≠ K256) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- K336 (≠ E291) modified: N6-acetyllysine; mutation K->Q,R: Decreases phosphorylation at S-232 and S-300 but does not affect activity or substrate metabolism.
P26284 Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial; PDHE1-A type I; EC 1.2.4.1 from Rattus norvegicus (Rat) (see paper)
43% identity, 96% coverage: 15:325/325 of query aligns to 62:370/390 of P26284
- S232 (= S187) modified: Phosphoserine; by PDK1
- S293 (= S250) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- S300 (≠ K256) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
Q8H1Y0 Pyruvate dehydrogenase E1 component subunit alpha-2, mitochondrial; PDHE1-A; Protein IAA-CONJUGATE-RESISTANT 4; EC 1.2.4.1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
42% identity, 96% coverage: 13:324/325 of query aligns to 62:372/393 of Q8H1Y0
- R121 (= R72) mutation to C: In iar4-1; reduced sensitivity to several IAA-amino acid conjugates.
P08559 Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial; PDHE1-A type I; EC 1.2.4.1 from Homo sapiens (Human) (see 13 papers)
42% identity, 96% coverage: 15:325/325 of query aligns to 62:370/390 of P08559
- A136 (= A89) to T: found in a patient with moderate developmental delay, mild dysmorphism and mildly elevated serum lactate; uncertain significance; dbSNP:rs138727886
- S232 (= S187) modified: Phosphoserine; by PDK1; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-293 and A-300.
- M282 (≠ I239) to L: in dbSNP:rs2229137
- S293 (= S250) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4; mutation to A: Reduces enzyme activity. Abolishes inactivation by phosphorylation; when associated with A-232 and A-300.; mutation to E: Interferes with substrate binding.
- S300 (≠ K256) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-232 and A-293.
- R302 (= R258) to C: in PDHAD; loss of activity; common mutation; dbSNP:rs137853252
Sites not aligning to the query:
- 1:29 modified: transit peptide, Mitochondrion
- 10 R → P: in PDHAD; affects mitochondrial import of precursor protein; dbSNP:rs137853257
3exeA Crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex (see paper)
42% identity, 96% coverage: 15:325/325 of query aligns to 35:343/363 of 3exeA
- active site: Q53 (≠ E33), G138 (≠ A120), R261 (= R245), H265 (= H249), S266 (= S250), Y274 (= Y257)
- binding manganese (ii) ion: D169 (= D151), N198 (= N180), Y200 (= Y182)
- binding thiamine diphosphate: Y91 (= Y71), R92 (= R72), V140 (= V122), G168 (= G150), D169 (= D151), G170 (= G152), A171 (= A153), N198 (= N180), Y200 (= Y182), G201 (= G183), H265 (= H249)
6cfoA Human pyruvate dehydrogenase e1 component complex with covalent tdp adduct acetyl phosphinate (see paper)
42% identity, 96% coverage: 15:325/325 of query aligns to 34:342/362 of 6cfoA
- active site: Q52 (≠ E33), G137 (≠ A120), R260 (= R245), H264 (= H249), S265 (= S250), Y273 (= Y257)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-{(1S)-1-hydroxy-1-[(R)-hydroxy(oxo)-lambda~5~-phosphanyl]ethyl}-5-(2-{[(S)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: F62 (= F43), Y90 (= Y71), R91 (= R72), G137 (≠ A120), V139 (= V122), G167 (= G150), D168 (= D151), G169 (= G152), N197 (= N180), Y199 (= Y182), G200 (= G183), H264 (= H249)
- binding magnesium ion: D168 (= D151), N197 (= N180), Y199 (= Y182)
1ni4A Human pyruvate dehydrogenase (see paper)
42% identity, 96% coverage: 15:325/325 of query aligns to 34:342/362 of 1ni4A
- active site: Q52 (≠ E33), G137 (≠ A120), R260 (= R245), H264 (= H249), S265 (= S250), Y273 (= Y257)
- binding magnesium ion: D168 (= D151), N197 (= N180), Y199 (= Y182)
- binding thiamine diphosphate: Y90 (= Y71), R91 (= R72), V139 (= V122), G167 (= G150), D168 (= D151), G169 (= G152), A170 (= A153), N197 (= N180), G200 (= G183), H264 (= H249)
6cerA Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
37% identity, 96% coverage: 15:325/325 of query aligns to 35:322/342 of 6cerA
6cerE Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
37% identity, 96% coverage: 15:325/325 of query aligns to 34:320/340 of 6cerE
3exhE Crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex (see paper)
37% identity, 96% coverage: 15:325/325 of query aligns to 34:311/331 of 3exhE
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)
35% identity, 97% coverage: 9:324/325 of query aligns to 97:413/445 of P12694
- Y158 (= Y71) binding thiamine diphosphate
- R159 (= R72) binding thiamine diphosphate; to W: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs769688327
- Q190 (≠ G103) to K: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- S206 (≠ Y119) binding K(+)
- S207 (≠ A120) binding thiamine diphosphate
- P208 (≠ I121) binding K(+)
- T211 (≠ G124) binding K(+); to M: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123503
- Q212 (= Q125) binding K(+)
- E238 (≠ D151) binding Mg(2+)
- G239 (= G152) binding thiamine diphosphate
- A240 (= A153) binding thiamine diphosphate
- G249 (≠ S162) 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 (= A166) to T: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs199599175
- A254 (≠ R167) to D: in MSUD1A; uncertain significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs373713279
- R265 (≠ E178) 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 (= N180) 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 (= Y182) binding Mg(2+)
- A285 (≠ H198) 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 (= G203) 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 (= R210) to H: in MSUD1A; uncertain significance; decreased affinity for the cofactor thiamine diphosphate; decreased 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs200137189
- T310 (≠ V223) to R: in MSUD1A; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852875
- I326 (= I239) to T: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- H336 (= H249) binding thiamine diphosphate
- S337 (= S250) modified: Phosphoserine; by BCKDK; mutation to A: Substantially decreases the stability of the BCKD complex.
- S347 (= S259) mutation to A: Does not affect the stability of the BCKD complex.
- F409 (≠ W320) 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 (= Y324) 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)
35% identity, 97% coverage: 9:324/325 of query aligns to 93:409/441 of P11960
- S333 (= S250) modified: Phosphoserine; by BCKDK
2bffA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
34% identity, 97% coverage: 9:324/325 of query aligns to 47:360/392 of 2bffA
- active site: E71 (= E33), S157 (≠ A120), R282 (= R245), H286 (= H249), S287 (= S250), Y295 (= Y257)
- binding manganese (ii) ion: E188 (≠ D151), N217 (= N180), Y219 (= Y182)
- 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 (≠ A70), Y108 (= Y71), R109 (= R72), L159 (≠ V122), G187 (= G150), E188 (≠ D151), G189 (= G152), A190 (= A153), R215 (≠ E178), N217 (= N180), Y219 (= Y182), A220 (≠ G183), I221 (= I184), H286 (= H249)
2bewA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
34% identity, 97% coverage: 9:324/325 of query aligns to 47:358/390 of 2bewA
- active site: E71 (= E33), S157 (≠ A120), R282 (= R245), H286 (= H249), S287 (= S250), Y295 (≠ E262)
- binding manganese (ii) ion: E188 (≠ D151), N217 (= N180), Y219 (= Y182), A220 (≠ G183)
- binding c2-1-hydroxyphenyl-thiamin diphosphate: M82 (≠ L44), Q107 (≠ A70), Y108 (= Y71), R109 (= R72), L159 (≠ V122), G187 (= G150), E188 (≠ D151), G189 (= G152), A190 (= A153), R215 (≠ E178), N217 (= N180), Y219 (= Y182), A220 (≠ G183), I221 (= I184), H286 (= H249)
2bevA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
34% identity, 97% coverage: 9:324/325 of query aligns to 47:358/390 of 2bevA
- active site: E71 (= E33), S157 (≠ A120), R282 (= R245), H286 (= H249), S287 (= S250), Y295 (≠ E262)
- binding manganese (ii) ion: E188 (≠ D151), N217 (= N180), Y219 (= Y182), A220 (≠ G183)
- binding c2-1-hydroxy-2-methyl-butyl-thiamin diphosphate: F80 (≠ G42), Q107 (≠ A70), Y108 (= Y71), R109 (= R72), S157 (≠ A120), L159 (≠ V122), G187 (= G150), E188 (≠ D151), G189 (= G152), A190 (= A153), R215 (≠ E178), N217 (= N180), Y219 (= Y182), A220 (≠ G183), I221 (= I184), H286 (= H249)
2beuA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
34% identity, 97% coverage: 9:324/325 of query aligns to 47:358/390 of 2beuA
- active site: E71 (= E33), S157 (≠ A120), R282 (= R245), H286 (= H249), S287 (= S250), Y295 (≠ E262)
- binding manganese (ii) ion: E188 (≠ D151), N217 (= N180), Y219 (= Y182), A220 (≠ G183)
- binding c2-1-hydroxy-3-methyl-propyl-thiamin diphosphate: Q107 (≠ A70), Y108 (= Y71), R109 (= R72), S157 (≠ A120), L159 (≠ V122), G187 (= G150), E188 (≠ D151), G189 (= G152), A190 (= A153), R215 (≠ E178), N217 (= N180), Y219 (= Y182), A220 (≠ G183), I221 (= I184), H286 (= H249)
Query Sequence
>WP_004511701.1 NCBI__GCF_000012925.1:WP_004511701.1
MESKLRALLPDAELIRMYEQMVLSREFEESCAEQYTKGHITGFLHLYSGQEAVAVGATAG
LHRDDYILSAYREHAQAIVRGAEPRRVMAELFGKRTGICKGKGGSMHLFDPNLSFMGGYA
IVGGQFPIAVGLAFAAKFRKEGRIVACFFGDGAANQGTFHESLNWARLWELPVLFICENN
SYGIGTSVERASALPDIHRRTCGYDIPSERVHGMDVIAVYEAVKWAAEWVREQNRPFLIE
AITYRFRGHSMSDPGKYRSLAEVELWKSRDPIPAFANRLVEEEIATEAQLEGIKQQALVT
VADAVKFAEDSPWPEDSEVWEDVYA
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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