SitesBLAST
Comparing Ga0059261_0016 FitnessBrowser__Korea:Ga0059261_0016 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)
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)
51% identity, 89% coverage: 30:340/349 of query aligns to 57:364/390 of P35486
- S232 (= S208) modified: Phosphoserine; by PDK1
- S293 (= S271) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- S300 (≠ K277) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- K336 (= K312) modified: N6-acetyllysine; mutation K->Q,R: Decreases phosphorylation at S-232 and S-300 but does not affect activity or substrate metabolism.
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)
50% identity, 93% coverage: 24:346/349 of query aligns to 70:392/420 of P16387
- S313 (= S271) modified: Phosphoserine; by PDK1 and PDK2
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
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)
51% identity, 89% coverage: 30:340/349 of query aligns to 57:364/390 of P26284
- S232 (= S208) modified: Phosphoserine; by PDK1
- S293 (= S271) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- S300 (≠ K277) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
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)
51% identity, 93% coverage: 24:348/349 of query aligns to 46:368/396 of P26267
- S289 (= S271) modified: Phosphoserine
- S296 (≠ K277) modified: Phosphoserine
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)
50% identity, 96% coverage: 11:346/349 of query aligns to 38:373/393 of Q8H1Y0
- R121 (= R93) mutation to C: In iar4-1; reduced sensitivity to several IAA-amino acid conjugates.
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)
50% identity, 89% coverage: 30:340/349 of query aligns to 55:362/388 of P29803
- M227 (= M205) to V: in SPGF70; uncertain significance; dbSNP:rs200969445
- S230 (= S208) mutation to A: Slightly reduces enzyme activity.
- S291 (= S271) 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 (= S273) 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 (≠ K277) modified: Phosphoserine; by PDK3; mutation to A: Slightly reduces enzyme activity.
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)
51% identity, 91% coverage: 28:346/349 of query aligns to 72:389/409 of Q10489
- Y306 (= Y267) modified: Phosphotyrosine
- S310 (= S271) modified: Phosphoserine
- S312 (= S273) modified: Phosphoserine
Sites not aligning to the query:
- 6 modified: Phosphothreonine
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)
51% identity, 89% coverage: 30:340/349 of query aligns to 57:364/390 of P08559
- A136 (= A110) to T: found in a patient with moderate developmental delay, mild dysmorphism and mildly elevated serum lactate; uncertain significance; dbSNP:rs138727886
- S232 (= S208) modified: Phosphoserine; by PDK1; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-293 and A-300.
- M282 (≠ L260) to L: in dbSNP:rs2229137
- S293 (= S271) 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 (≠ K277) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-232 and A-293.
- R302 (= R279) 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)
51% identity, 89% coverage: 30:340/349 of query aligns to 30:337/363 of 3exeA
- active site: Q53 (= Q53), G138 (= G141), R261 (= R266), H265 (= H270), S266 (= S271), Y274 (= Y278)
- binding manganese (ii) ion: D169 (= D172), N198 (= N201), Y200 (= Y203)
- binding thiamine diphosphate: Y91 (= Y92), R92 (= R93), V140 (= V143), G168 (= G171), D169 (= D172), G170 (= G173), A171 (= A174), N198 (= N201), Y200 (= Y203), G201 (≠ A204), H265 (= H270)
6cfoA Human pyruvate dehydrogenase e1 component complex with covalent tdp adduct acetyl phosphinate (see paper)
51% identity, 89% coverage: 30:340/349 of query aligns to 29:336/362 of 6cfoA
- active site: Q52 (= Q53), G137 (= G141), R260 (= R266), H264 (= H270), S265 (= S271), Y273 (= Y278)
- 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 (= F63), Y90 (= Y92), R91 (= R93), G137 (= G141), V139 (= V143), G167 (= G171), D168 (= D172), G169 (= G173), N197 (= N201), Y199 (= Y203), G200 (≠ A204), H264 (= H270)
- binding magnesium ion: D168 (= D172), N197 (= N201), Y199 (= Y203)
1ni4A Human pyruvate dehydrogenase (see paper)
51% identity, 89% coverage: 30:340/349 of query aligns to 29:336/362 of 1ni4A
- active site: Q52 (= Q53), G137 (= G141), R260 (= R266), H264 (= H270), S265 (= S271), Y273 (= Y278)
- binding magnesium ion: D168 (= D172), N197 (= N201), Y199 (= Y203)
- binding thiamine diphosphate: Y90 (= Y92), R91 (= R93), V139 (= V143), G167 (= G171), D168 (= D172), G169 (= G173), A170 (= A174), N197 (= N201), G200 (≠ A204), H264 (= H270)
6cerA Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
46% identity, 89% coverage: 30:340/349 of query aligns to 30:316/342 of 6cerA
6cerE Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
46% identity, 89% coverage: 30:340/349 of query aligns to 29:314/340 of 6cerE
3exhE Crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex (see paper)
44% identity, 89% coverage: 30:340/349 of query aligns to 29:305/331 of 3exhE
1umdA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methyl-2-oxopentanoate as an intermediate (see paper)
33% identity, 90% coverage: 32:345/349 of query aligns to 31:344/362 of 1umdA
- active site: I52 (≠ Q53), S139 (≠ G141), R264 (= R266), H268 (= H270), S269 (= S271), Y277 (= Y278)
- binding 2-oxo-4-methylpentanoic acid: F61 (= F63), Y90 (= Y92), S139 (≠ G141)
- binding magnesium ion: D170 (= D172), N199 (= N201), Y201 (= Y203)
- binding thiamine diphosphate: Y89 (≠ G91), Y90 (= Y92), R91 (= R93), P140 (≠ I142), I141 (≠ V143), G169 (= G171), D170 (= D172), G171 (= G173), N199 (= N201), Y201 (= Y203), A202 (= A204), I203 (≠ M205), H268 (= H270)
1umcA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methylpentanoate (see paper)
33% identity, 90% coverage: 32:345/349 of query aligns to 31:344/362 of 1umcA
- active site: I52 (≠ Q53), S139 (≠ G141), R264 (= R266), H268 (= H270), S269 (= S271), Y277 (= Y278)
- binding 4-methyl valeric acid: Y90 (= Y92), H126 (= H128)
- binding magnesium ion: D170 (= D172), N199 (= N201), Y201 (= Y203)
- binding thiamine diphosphate: Y89 (≠ G91), Y90 (= Y92), R91 (= R93), I141 (≠ V143), G169 (= G171), D170 (= D172), G171 (= G173), N199 (= N201), Y201 (= Y203), I203 (≠ M205), H268 (= H270)
1umbA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 in holo-form (see paper)
33% identity, 90% coverage: 32:345/349 of query aligns to 31:344/362 of 1umbA
- active site: I52 (≠ Q53), S139 (≠ G141), R264 (= R266), H268 (= H270), S269 (= S271), Y277 (= Y278)
- binding magnesium ion: D170 (= D172), N199 (= N201), Y201 (= Y203)
- binding thiamine diphosphate: Y89 (≠ G91), Y90 (= Y92), R91 (= R93), P140 (≠ I142), I141 (≠ V143), G169 (= G171), D170 (= D172), G171 (= G173), N199 (= N201), Y201 (= Y203), A202 (= A204), I203 (≠ M205), 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)
33% identity, 90% coverage: 32:345/349 of query aligns to 36:349/367 of Q5SLR4
3dufA Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
32% identity, 90% coverage: 30:342/349 of query aligns to 39:342/365 of 3dufA
- active site: S62 (≠ Q53), I139 (≠ G141), R264 (= R266), H268 (= H270), T269 (≠ S271), Y278 (= Y278)
- binding magnesium ion: D170 (= D172), 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 (≠ V143), G169 (= G171), D170 (= D172), G171 (= G173), N199 (= N201), F201 (≠ Y203), A202 (= A204), H268 (= H270)
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)
32% identity, 90% coverage: 31:344/349 of query aligns to 99:412/445 of P12694
- Y158 (= Y92) binding
- R159 (= R93) binding ; to W: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs769688327
- Q190 (≠ G124) to K: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- S206 (≠ H140) binding
- S207 (≠ G141) binding
- P208 (≠ I142) binding
- T211 (≠ A145) binding ; to M: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123503
- Q212 (= Q146) binding
- E238 (≠ D172) binding
- G239 (= G173) binding
- A240 (= A174) binding
- G249 (≠ S183) 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 (≠ E188) to D: in MSUD1A; uncertain significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity
- R265 (≠ E199) 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 (≠ Y219) 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 (≠ S224) 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 (≠ Q231) to H: in MSUD1A; uncertain significance; decreased affinity for the cofactor thiamine diphosphate; decreased 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs200137189
- T310 (≠ A244) to R: in MSUD1A; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852875
- I326 (≠ L260) 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 (= S280) mutation to A: Does not affect the stability of the BCKD complex.
- F409 (≠ Y341) to C: in MSUD1A; decreased solubility; loss of mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852872
Sites not aligning to the query:
- 1:45 modified: transit peptide, Mitochondrion
- 413 Y → C: in MSUD1A; uncertain significance; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123508
- 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
Query Sequence
>Ga0059261_0016 FitnessBrowser__Korea:Ga0059261_0016
VAKAPAKSRKIEPAVTNRERPNEPDRYKASKEELLEFYRQMLLIRRFEEKAGQLYGLGFI
GGFCHLYIGQEAVAVGLQSALDGEKDSVITGYRDHGHMLAYGIDPKEIMAELTGRAAGIS
RGKGGSMHMFSTEKKFYGGHGIVGAQVSLGTGLAFTHKYNEDGGVAMAYFGDGASNQGQV
YESFNMAELWKLPIIYVIENNQYAMGTSVNRSSSEDQLYRRGESFRIPGIQVDGMDVLAC
RGAAEEALAWVRAGKGPIILEMKTYRYRGHSMSDPAKYRSRDEVQSVRDNSDPIEGVKKE
LEAAGVKEDELKAIEAEIRKAVNESADFAEQTPEPDPAELYTDVLVGTY
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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