SitesBLAST
Comparing YP_004140672.1 NCBI__GCF_000185905.1:YP_004140672.1 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)
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, 93% coverage: 24:342/342 of query aligns to 57:371/388 of P29803
- M227 (= M197) to V: in SPGF70; uncertain significance; dbSNP:rs200969445
- S230 (= S200) mutation to A: Slightly reduces enzyme activity.
- S291 (= S263) 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 (= S265) 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 (≠ R269) 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)
40% identity, 89% coverage: 34:339/342 of query aligns to 68:370/390 of P35486
- S232 (= S200) modified: Phosphoserine; by PDK1
- S293 (= S263) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- S300 (≠ R269) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- K336 (≠ E305) 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)
40% identity, 89% coverage: 34:339/342 of query aligns to 68:370/390 of P26284
- S232 (= S200) modified: Phosphoserine; by PDK1
- S293 (= S263) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- S300 (≠ R269) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
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, 92% coverage: 16:329/342 of query aligns to 70:380/420 of P16387
- S313 (= S263) modified: Phosphoserine; by PDK1 and PDK2
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
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)
40% identity, 89% coverage: 34:339/342 of query aligns to 68:370/390 of P08559
- A136 (= A102) to T: found in a patient with moderate developmental delay, mild dysmorphism and mildly elevated serum lactate; uncertain significance; dbSNP:rs138727886
- S232 (= S200) modified: Phosphoserine; by PDK1; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-293 and A-300.
- M282 (≠ I252) to L: in dbSNP:rs2229137
- S293 (= S263) 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 (≠ R269) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-232 and A-293.
- R302 (= R271) 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)
40% identity, 89% coverage: 34:339/342 of query aligns to 40:342/362 of 6cfoA
- active site: Q52 (≠ E46), G137 (= G133), R260 (= R258), H264 (= H262), S265 (= S263), Y273 (= Y270)
- 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 (≠ T56), Y90 (≠ H84), R91 (= R85), G137 (= G133), V139 (= V135), G167 (= G163), D168 (= D164), G169 (= G165), N197 (= N193), Y199 (= Y195), G200 (= G196), H264 (= H262)
- binding magnesium ion: D168 (= D164), N197 (= N193), Y199 (= Y195)
1ni4A Human pyruvate dehydrogenase (see paper)
40% identity, 89% coverage: 34:339/342 of query aligns to 40:342/362 of 1ni4A
- active site: Q52 (≠ E46), G137 (= G133), R260 (= R258), H264 (= H262), S265 (= S263), Y273 (= Y270)
- binding magnesium ion: D168 (= D164), N197 (= N193), Y199 (= Y195)
- binding thiamine diphosphate: Y90 (≠ H84), R91 (= R85), V139 (= V135), G167 (= G163), D168 (= D164), G169 (= G165), A170 (= A166), N197 (= N193), G200 (= G196), H264 (= H262)
3exeA Crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex (see paper)
40% identity, 89% coverage: 34:339/342 of query aligns to 41:343/363 of 3exeA
- active site: Q53 (≠ E46), G138 (= G133), R261 (= R258), H265 (= H262), S266 (= S263), Y274 (= Y270)
- binding manganese (ii) ion: D169 (= D164), N198 (= N193), Y200 (= Y195)
- binding thiamine diphosphate: Y91 (≠ H84), R92 (= R85), V140 (= V135), G168 (= G163), D169 (= D164), G170 (= G165), A171 (= A166), N198 (= N193), Y200 (= Y195), G201 (= G196), H265 (= H262)
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)
37% identity, 94% coverage: 12:332/342 of query aligns to 63:380/409 of Q10489
- Y306 (≠ H259) modified: Phosphotyrosine
- S310 (= S263) modified: Phosphoserine
- S312 (= S265) 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)
39% identity, 86% coverage: 33:326/342 of query aligns to 63:356/396 of P26267
- S289 (= S263) modified: Phosphoserine
- S296 (≠ R269) 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)
36% identity, 94% coverage: 23:342/342 of query aligns to 59:376/393 of Q8H1Y0
- R121 (= R85) mutation to C: In iar4-1; reduced sensitivity to several IAA-amino acid conjugates.
6cerA Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
36% identity, 89% coverage: 34:339/342 of query aligns to 41:322/342 of 6cerA
6cerE Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
35% identity, 89% coverage: 34:339/342 of query aligns to 40:320/340 of 6cerE
3exhE Crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex (see paper)
34% identity, 89% coverage: 34:339/342 of query aligns to 40:311/331 of 3exhE
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)
32% identity, 89% coverage: 25:328/342 of query aligns to 36:340/367 of Q5SLR4
- F66 (≠ L59) binding substrate
- YYR 94:96 (≠ THR 83:85) binding thiamine diphosphate
- Y95 (≠ H84) binding substrate
- MPEH 128:131 (≠ GSMH 117:120) binding substrate
- S144 (≠ G133) binding substrate
- SPI 144:146 (≠ GIV 133:135) binding thiamine diphosphate
- 174:180 (vs. 163:169, 71% identical) binding thiamine diphosphate
- D175 (= D164) binding Mg(2+)
- N204 (= N193) binding Mg(2+)
- NFYAI 204:208 (≠ NGYGM 193:197) binding thiamine diphosphate
- Y206 (= Y195) binding Mg(2+)
- H273 (= H262) 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)
32% identity, 89% coverage: 25:328/342 of query aligns to 31:335/362 of 1umdA
- active site: I52 (≠ R50), S139 (≠ G133), R264 (= R258), H268 (= H262), S269 (= S263), Y277 (= Y270)
- binding 2-oxo-4-methylpentanoic acid: F61 (≠ L59), Y90 (≠ H84), S139 (≠ G133)
- binding magnesium ion: D170 (= D164), N199 (= N193), Y201 (= Y195)
- binding thiamine diphosphate: Y89 (≠ T83), Y90 (≠ H84), R91 (= R85), P140 (≠ I134), I141 (≠ V135), G169 (= G163), D170 (= D164), G171 (= G165), N199 (= N193), Y201 (= Y195), A202 (≠ G196), I203 (≠ M197), H268 (= H262)
1umcA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methylpentanoate (see paper)
32% identity, 89% coverage: 25:328/342 of query aligns to 31:335/362 of 1umcA
- active site: I52 (≠ R50), S139 (≠ G133), R264 (= R258), H268 (= H262), S269 (= S263), Y277 (= Y270)
- binding 4-methyl valeric acid: Y90 (≠ H84), H126 (= H120)
- binding magnesium ion: D170 (= D164), N199 (= N193), Y201 (= Y195)
- binding thiamine diphosphate: Y89 (≠ T83), Y90 (≠ H84), R91 (= R85), I141 (≠ V135), G169 (= G163), D170 (= D164), G171 (= G165), N199 (= N193), Y201 (= Y195), I203 (≠ M197), H268 (= H262)
1umbA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 in holo-form (see paper)
32% identity, 89% coverage: 25:328/342 of query aligns to 31:335/362 of 1umbA
- active site: I52 (≠ R50), S139 (≠ G133), R264 (= R258), H268 (= H262), S269 (= S263), Y277 (= Y270)
- binding magnesium ion: D170 (= D164), N199 (= N193), Y201 (= Y195)
- binding thiamine diphosphate: Y89 (≠ T83), Y90 (≠ H84), R91 (= R85), P140 (≠ I134), I141 (≠ V135), G169 (= G163), D170 (= D164), G171 (= G165), N199 (= N193), Y201 (= Y195), A202 (≠ G196), I203 (≠ M197), H268 (= H262)
3dufA Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
30% identity, 94% coverage: 21:340/342 of query aligns to 37:347/365 of 3dufA
- active site: S62 (≠ E46), I139 (≠ G133), R264 (= R258), H268 (= H262), T269 (≠ S263), Y278 (= Y270)
- binding magnesium ion: D170 (= D164), N199 (= N193), F201 (≠ Y195)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1r)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: Y99 (≠ H84), R100 (= R85), I141 (≠ V135), G169 (= G163), D170 (= D164), G171 (= G165), N199 (= N193), F201 (≠ Y195), A202 (≠ G196), H268 (= H262)
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)
30% identity, 92% coverage: 25:340/342 of query aligns to 100:415/445 of P12694
- Y158 (≠ H84) binding thiamine diphosphate
- R159 (= R85) binding thiamine diphosphate; to W: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs769688327
- Q190 (≠ G116) to K: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- S206 (≠ N132) binding K(+)
- S207 (≠ G133) binding thiamine diphosphate
- P208 (≠ I134) binding K(+)
- T211 (≠ G137) binding K(+); to M: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123503
- Q212 (≠ G138) binding K(+)
- E238 (≠ D164) binding Mg(2+)
- G239 (= G165) binding thiamine diphosphate
- A240 (= A166) binding thiamine diphosphate
- G249 (≠ A175) 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 (= A179) to T: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs199599175
- A254 (= A180) to D: in MSUD1A; uncertain significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs373713279
- R265 (≠ E191) 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 (= N193) 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 (= Y195) binding Mg(2+)
- A285 (= A211) 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 (≠ A216) 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 (≠ I223) to H: in MSUD1A; uncertain significance; decreased affinity for the cofactor thiamine diphosphate; decreased 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs200137189
- T310 (≠ S236) to R: in MSUD1A; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852875
- I326 (= I252) to T: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- H336 (= H262) binding thiamine diphosphate
- S337 (= S263) modified: Phosphoserine; by BCKDK; mutation to A: Substantially decreases the stability of the BCKD complex.
- S347 (≠ T272) mutation to A: Does not affect the stability of the BCKD complex.
- F409 (≠ G334) 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 (= Y338) 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
Query Sequence
>YP_004140672.1 NCBI__GCF_000185905.1:YP_004140672.1
MATASKAVTNSRANLPFVYRQYSAEQLKQVLHKMYLVRRFEEGAEECYTRGLIHGTMHLS
IGQEASAMGICMPLAEDDQITSTHRGHGHCIAKGAEVKRMFAEFFGKTTGYCKGRGGSMH
IADVGKGNLGANGIVGGGIPIAVGAALSSKMMKTGKVVVSFFGDGANNEGAFHEALNMAA
VWKLPVIFVCENNGYGMSTSTARSTAVKNIAERAAAYSMPGVIVNGNIFSEVAEASHQAV
ARARAGEGPTLIESKTYRHRGHSKSDRNRYRTKEEIEDWMSNRDPITLFESELREFGFID
DKGIEAIRDAVAQEIAEGIEFAKASPSPDISETGNYVYTEQA
Or try a new SitesBLAST search
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