SitesBLAST
Comparing SMc01030 SMc01030 pyruvate dehydrogenase alpha2 subunit protein 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)
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)
56% identity, 90% coverage: 31:342/348 of query aligns to 56:364/390 of P35486
- S232 (= S209) modified: Phosphoserine; by PDK1
- S293 (= S272) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- S300 (≠ K278) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- K336 (= K314) 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)
56% identity, 90% coverage: 31:342/348 of query aligns to 56:364/390 of P26284
- S232 (= S209) modified: Phosphoserine; by PDK1
- S293 (= S272) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- S300 (≠ K278) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
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)
56% identity, 90% coverage: 31:342/348 of query aligns to 54:362/388 of P29803
- M227 (= M206) to V: in SPGF70; unknown pathological significance; dbSNP:rs200969445
- S230 (= S209) mutation to A: Slightly reduces enzyme activity.
- S291 (= S272) 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 (= S274) 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 (≠ K278) modified: Phosphoserine; by PDK3; mutation to A: Slightly reduces enzyme activity.
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)
56% identity, 90% coverage: 31:342/348 of query aligns to 56:364/390 of P08559
- A136 (= A111) to T: probable disease-associated variant found in a patient with moderate developmental delay, mild dysmorphism and mildly elevated serum lactate; dbSNP:rs138727886
- S232 (= S209) modified: Phosphoserine; by PDK1; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-293 and A-300.
- M282 (≠ L261) to L: in dbSNP:rs2229137
- S293 (= S272) 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 (≠ K278) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-232 and A-293.
- R302 (= R280) 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)
56% identity, 90% coverage: 31:342/348 of query aligns to 29:337/363 of 3exeA
- active site: Q53 (= Q55), G138 (= G142), R261 (= R267), H265 (= H271), S266 (= S272), Y274 (= Y279)
- binding manganese (ii) ion: D169 (= D173), N198 (= N202), Y200 (= Y204), G201 (≠ A205)
- binding thiamine diphosphate: Y91 (= Y93), R92 (= R94), G138 (= G142), I139 (= I143), V140 (= V144), G168 (= G172), D169 (= D173), G170 (= G174), A171 (= A175), N198 (= N202), Y200 (= Y204), G201 (≠ A205), M202 (= M206), H265 (= H271)
6cfoA Human pyruvate dehydrogenase e1 component complex with covalent tdp adduct acetyl phosphinate (see paper)
56% identity, 90% coverage: 31:342/348 of query aligns to 28:336/362 of 6cfoA
- active site: Q52 (= Q55), G137 (= G142), R260 (= R267), H264 (= H271), S265 (= S272), Y273 (= Y279)
- 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 (= F65), H64 (= H67), Y90 (= Y93), R91 (= R94), G137 (= G142), I138 (= I143), V139 (= V144), G167 (= G172), D168 (= D173), G169 (= G174), A170 (= A175), N197 (= N202), Y199 (= Y204), G200 (≠ A205), M201 (= M206), H264 (= H271)
- binding magnesium ion: D168 (= D173), N197 (= N202), Y199 (= Y204), G200 (≠ A205)
1ni4A Human pyruvate dehydrogenase (see paper)
56% identity, 90% coverage: 31:342/348 of query aligns to 28:336/362 of 1ni4A
- active site: Q52 (= Q55), G137 (= G142), R260 (= R267), H264 (= H271), S265 (= S272), Y273 (= Y279)
- binding magnesium ion: D168 (= D173), N197 (= N202), Y199 (= Y204)
- binding thiamine diphosphate: Y90 (= Y93), R91 (= R94), G137 (= G142), I138 (= I143), V139 (= V144), G167 (= G172), D168 (= D173), G169 (= G174), A170 (= A175), N197 (= N202), Y199 (= Y204), G200 (≠ A205), M201 (= M206), H264 (= H271)
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)
51% identity, 92% coverage: 30:348/348 of query aligns to 75:392/420 of P16387
- S313 (= S272) modified: Phosphoserine; by PDK1 and PDK2
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
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)
52% identity, 91% coverage: 32:346/348 of query aligns to 53:364/396 of P26267
- S289 (= S272) modified: Phosphoserine
- S296 (≠ K278) 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, 91% coverage: 30:346/348 of query aligns to 57:371/393 of Q8H1Y0
- R121 (= R94) mutation to C: In iar4-1; reduced sensitivity to several IAA-amino acid conjugates.
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)
48% identity, 93% coverage: 27:348/348 of query aligns to 69:389/409 of Q10489
- Y306 (= Y268) modified: Phosphotyrosine
- S310 (= S272) modified: Phosphoserine
- S312 (= S274) modified: Phosphoserine
Sites not aligning to the query:
- 6 modified: Phosphothreonine
6cerE Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
51% identity, 90% coverage: 31:342/348 of query aligns to 28:314/340 of 6cerE
6cerA Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
51% identity, 90% coverage: 31:342/348 of query aligns to 29:316/342 of 6cerA
3exhE Crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex (see paper)
50% identity, 90% coverage: 31:342/348 of query aligns to 28:305/331 of 3exhE
- active site: Q52 (= Q55), G137 (= G142)
- binding manganese (ii) ion: D168 (= D173), N197 (= N202)
- binding thiamine diphosphate: Y90 (= Y93), R91 (= R94), G137 (= G142), I138 (= I143), V139 (= V144), G167 (= G172), D168 (= D173), G169 (= G174), A170 (= A175), N197 (= N202)
3dufA Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
31% identity, 91% coverage: 28:344/348 of query aligns to 35:342/365 of 3dufA