SitesBLAST
Comparing WP_009546784.1 NCBI__GCF_000017845.1:WP_009546784.1 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)
39% identity, 98% coverage: 7:343/343 of query aligns to 46:372/390 of P35486
- S232 (≠ A203) modified: Phosphoserine; by PDK1
- S293 (= S266) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- S300 (≠ E272) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- K336 (≠ D307) 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, 98% coverage: 7:343/343 of query aligns to 46:372/390 of P26284
- S232 (≠ A203) modified: Phosphoserine; by PDK1
- S293 (= S266) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- S300 (≠ E272) 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)
38% identity, 98% coverage: 7:343/343 of query aligns to 44:370/388 of P29803
- M227 (≠ I200) to V: in SPGF70; uncertain significance; dbSNP:rs200969445
- S230 (≠ A203) mutation to A: Slightly reduces enzyme activity.
- S291 (= S266) 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 (≠ A268) 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 (≠ E272) modified: Phosphoserine; by PDK3; mutation to A: Slightly reduces enzyme activity.
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, 98% coverage: 7:343/343 of query aligns to 48:375/393 of Q8H1Y0
- R121 (= R81) 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)
40% identity, 94% coverage: 12:334/343 of query aligns to 68:380/409 of Q10489
- Y306 (≠ F262) modified: Phosphotyrosine
- S310 (= S266) modified: Phosphoserine
- S312 (≠ A268) 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 16 papers)
39% identity, 98% coverage: 7:343/343 of query aligns to 46:372/390 of P08559
- Y118 (= Y80) binding thiamine diphosphate
- R119 (= R81) binding thiamine diphosphate
- A136 (= A98) to T: found in a patient with moderate developmental delay, mild dysmorphism and mildly elevated serum lactate; uncertain significance; dbSNP:rs138727886
- G165 (≠ A129) binding thiamine diphosphate
- V167 (= V131) binding thiamine diphosphate; to M: in PDHAD; disrupts magnesium binding and results in deficient activity of the pyruvate dehydrogenase complex; dbSNP:rs2063174067
- D196 (= D167) binding Mg(2+); binding thiamine diphosphate
- G197 (= G168) binding thiamine diphosphate
- A198 (= A169) binding thiamine diphosphate
- N225 (= N196) binding Mg(2+); binding thiamine diphosphate
- Y227 (≠ W198) binding Mg(2+)
- S232 (≠ A203) modified: Phosphoserine; by PDK1; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-293 and A-300.
- M282 (≠ I255) to L: in dbSNP:rs2229137
- H292 (= H265) binding thiamine diphosphate
- S293 (= S266) 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 (≠ E272) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-232 and A-293.
- R302 (= R274) 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, 98% coverage: 7:343/343 of query aligns to 18:344/362 of 6cfoA
- active site: Q52 (≠ E41), G137 (≠ A129), R260 (= R261), H264 (= H265), S265 (= S266), Y273 (≠ L273)
- 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 (= F51), Y90 (= Y80), R91 (= R81), G137 (≠ A129), V139 (= V131), G167 (= G166), D168 (= D167), G169 (= G168), N197 (= N196), Y199 (≠ W198), G200 (≠ A199), H264 (= H265)
- binding magnesium ion: D168 (= D167), N197 (= N196), Y199 (≠ W198)
1ni4A Human pyruvate dehydrogenase (see paper)
39% identity, 98% coverage: 7:343/343 of query aligns to 18:344/362 of 1ni4A
- active site: Q52 (≠ E41), G137 (≠ A129), R260 (= R261), H264 (= H265), S265 (= S266), Y273 (≠ L273)
- binding magnesium ion: D168 (= D167), N197 (= N196), Y199 (≠ W198)
- binding thiamine diphosphate: Y90 (= Y80), R91 (= R81), V139 (= V131), G167 (= G166), D168 (= D167), G169 (= G168), A170 (= A169), N197 (= N196), G200 (≠ A199), H264 (= H265)
3exeA Crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex (see paper)
39% identity, 98% coverage: 7:343/343 of query aligns to 19:345/363 of 3exeA
- active site: Q53 (≠ E41), G138 (≠ A129), R261 (= R261), H265 (= H265), S266 (= S266), Y274 (≠ L273)
- binding manganese (ii) ion: D169 (= D167), N198 (= N196), Y200 (≠ W198)
- binding thiamine diphosphate: Y91 (= Y80), R92 (= R81), V140 (= V131), G168 (= G166), D169 (= D167), G170 (= G168), A171 (= A169), N198 (= N196), Y200 (≠ W198), G201 (≠ A199), H265 (= H265)
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)
36% identity, 93% coverage: 14:333/343 of query aligns to 73:382/420 of P16387
- S313 (= S266) 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)
38% identity, 96% coverage: 8:335/343 of query aligns to 46:359/396 of P26267
- S289 (= S266) modified: Phosphoserine
- S296 (≠ E272) modified: Phosphoserine
6cerA Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
37% identity, 98% coverage: 7:343/343 of query aligns to 19:324/342 of 6cerA
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)
35% identity, 96% coverage: 15:342/343 of query aligns to 31:351/367 of Q5SLR4
- F66 (= F51) binding substrate
- YYR 94:96 (≠ TYR 79:81) binding thiamine diphosphate
- Y95 (= Y80) binding substrate
- MPEH 128:131 (≠ GSMH 113:116) binding substrate
- S144 (≠ A129) binding substrate
- SPI 144:146 (≠ AFV 129:131) binding thiamine diphosphate
- 174:180 (vs. 166:172, 57% identical) binding thiamine diphosphate
- D175 (= D167) binding Mg(2+)
- N204 (= N196) binding Mg(2+)
- NFYAI 204:208 (≠ NKWAI 196:200) binding thiamine diphosphate
- Y206 (≠ W198) binding Mg(2+)
- H273 (= H265) binding thiamine diphosphate
1umdA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methyl-2-oxopentanoate as an intermediate (see paper)
35% identity, 96% coverage: 15:342/343 of query aligns to 26:346/362 of 1umdA