SitesBLAST
Comparing WP_012403064.1 NCBI__GCF_000020045.1:WP_012403064.1 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)
39% identity, 99% coverage: 3:325/327 of query aligns to 50:369/388 of P29803
- M227 (≠ E182) to V: in SPGF70; uncertain significance; dbSNP:rs200969445
- S230 (= S185) mutation to A: Slightly reduces enzyme activity.
- S291 (≠ F248) 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 (≠ G250) 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 (≠ T254) modified: Phosphoserine; by PDK3; mutation to A: Slightly reduces enzyme activity.
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)
39% identity, 99% coverage: 3:327/327 of query aligns to 52:373/390 of P35486
- S232 (= S185) modified: Phosphoserine; by PDK1
- S293 (≠ F248) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- S300 (≠ T254) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- K336 (≠ R290) 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)
39% identity, 99% coverage: 3:327/327 of query aligns to 52:373/390 of P26284
- S232 (= S185) modified: Phosphoserine; by PDK1
- S293 (≠ F248) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- S300 (≠ T254) 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)
38% identity, 99% coverage: 3:327/327 of query aligns to 48:369/396 of P26267
- S289 (≠ F248) modified: Phosphoserine
- S296 (vs. gap) 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)
37% identity, 99% coverage: 2:324/327 of query aligns to 53:373/393 of Q8H1Y0
- R121 (= R70) 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 16 papers)
39% identity, 99% coverage: 3:327/327 of query aligns to 52:373/390 of P08559
- Y118 (≠ H69) binding thiamine diphosphate
- R119 (= R70) binding thiamine diphosphate
- A136 (= A87) to T: found in a patient with moderate developmental delay, mild dysmorphism and mildly elevated serum lactate; uncertain significance; dbSNP:rs138727886
- G165 (= G118) binding thiamine diphosphate
- V167 (= V120) binding thiamine diphosphate; to M: in PDHAD; disrupts magnesium binding and results in deficient activity of the pyruvate dehydrogenase complex; dbSNP:rs2063174067
- D196 (= D149) binding Mg(2+); binding thiamine diphosphate
- G197 (= G150) binding thiamine diphosphate
- A198 (= A151) binding thiamine diphosphate
- N225 (= N178) binding Mg(2+); binding thiamine diphosphate
- Y227 (= Y180) binding Mg(2+)
- S232 (= S185) modified: Phosphoserine; by PDK1; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-293 and A-300.
- M282 (≠ V237) to L: in dbSNP:rs2229137
- H292 (= H247) binding thiamine diphosphate
- S293 (≠ F248) 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 (≠ T254) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-232 and A-293.
- R302 (= R256) 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
6cfoA Human pyruvate dehydrogenase e1 component complex with covalent tdp adduct acetyl phosphinate (see paper)
39% identity, 99% coverage: 3:327/327 of query aligns to 24:345/362 of 6cfoA
- active site: Q52 (≠ V31), G137 (= G118), R260 (= R243), H264 (= H247), S265 (≠ F248), Y273 (= Y255)
- 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 (= F41), Y90 (≠ H69), R91 (= R70), G137 (= G118), V139 (= V120), G167 (= G148), D168 (= D149), G169 (= G150), N197 (= N178), Y199 (= Y180), G200 (≠ A181), H264 (= H247)
- binding magnesium ion: D168 (= D149), N197 (= N178), Y199 (= Y180)
1ni4A Human pyruvate dehydrogenase (see paper)
39% identity, 99% coverage: 3:327/327 of query aligns to 24:345/362 of 1ni4A
- active site: Q52 (≠ V31), G137 (= G118), R260 (= R243), H264 (= H247), S265 (≠ F248), Y273 (= Y255)
- binding magnesium ion: D168 (= D149), N197 (= N178), Y199 (= Y180)
- binding thiamine diphosphate: Y90 (≠ H69), R91 (= R70), V139 (= V120), G167 (= G148), D168 (= D149), G169 (= G150), A170 (= A151), N197 (= N178), G200 (≠ A181), H264 (= H247)
3exeA Crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex (see paper)
39% identity, 99% coverage: 3:327/327 of query aligns to 25:346/363 of 3exeA
- active site: Q53 (≠ V31), G138 (= G118), R261 (= R243), H265 (= H247), S266 (≠ F248), Y274 (= Y255)
- binding manganese (ii) ion: D169 (= D149), N198 (= N178), Y200 (= Y180)
- binding thiamine diphosphate: Y91 (≠ H69), R92 (= R70), V140 (= V120), G168 (= G148), D169 (= D149), G170 (= G150), A171 (= A151), N198 (= N178), Y200 (= Y180), G201 (≠ A181), H265 (= H247)
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)
36% identity, 99% coverage: 2:325/327 of query aligns to 68:390/409 of Q10489
- Y306 (= Y244) modified: Phosphotyrosine
- S310 (≠ F248) modified: Phosphoserine
- S312 (≠ G250) modified: Phosphoserine
Sites not aligning to the query:
- 6 modified: Phosphothreonine
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)
37% identity, 98% coverage: 3:324/327 of query aligns to 72:392/420 of P16387
- S313 (≠ F248) modified: Phosphoserine; by PDK1 and PDK2
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
6cerE Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
37% identity, 99% coverage: 3:327/327 of query aligns to 24:323/340 of 6cerE
6cerA Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
37% identity, 99% coverage: 3:327/327 of query aligns to 25:325/342 of 6cerA
3exhE Crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex (see paper)
36% identity, 99% coverage: 3:327/327 of query aligns to 24:314/331 of 3exhE