SitesBLAST
Comparing Echvi_1221 Echvi_1221 pyruvate dehydrogenase E1 component, alpha subunit 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)
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)
50% identity, 90% coverage: 12:318/340 of query aligns to 49:356/396 of P26267
- S289 (= S256) modified: Phosphoserine
- S296 (≠ K262) modified: Phosphoserine
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)
47% identity, 93% coverage: 23:337/340 of query aligns to 64:375/390 of P35486
- S232 (= S193) modified: Phosphoserine; by PDK1
- S293 (= S256) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- S300 (≠ K262) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- K336 (= K297) 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)
47% identity, 93% coverage: 23:337/340 of query aligns to 64:375/390 of P26284
- S232 (= S193) modified: Phosphoserine; by PDK1
- S293 (= S256) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- S300 (≠ K262) 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)
46% identity, 91% coverage: 23:330/340 of query aligns to 62:367/388 of P29803
- M227 (= M190) to V: in SPGF70; uncertain significance; dbSNP:rs200969445
- S230 (= S193) mutation to A: Slightly reduces enzyme activity.
- S291 (= S256) 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 (= S258) 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 (≠ K262) 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)
44% identity, 94% coverage: 13:333/340 of query aligns to 56:375/393 of Q8H1Y0
- R121 (= R78) 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)
45% identity, 96% coverage: 11:336/340 of query aligns to 69:394/409 of Q10489
- Y306 (= Y252) modified: Phosphotyrosine
- S310 (= S256) modified: Phosphoserine
- S312 (= S258) 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)
47% identity, 93% coverage: 23:337/340 of query aligns to 64:375/390 of P08559
- A136 (= A95) to T: found in a patient with moderate developmental delay, mild dysmorphism and mildly elevated serum lactate; uncertain significance; dbSNP:rs138727886
- S232 (= S193) modified: Phosphoserine; by PDK1; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-293 and A-300.
- M282 (≠ L245) to L: in dbSNP:rs2229137
- S293 (= S256) 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 (≠ K262) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-232 and A-293.
- R302 (= R264) 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)
47% identity, 93% coverage: 23:337/340 of query aligns to 36:347/362 of 6cfoA
- active site: Q52 (= Q39), G137 (= G126), R260 (= R251), H264 (= H255), S265 (= S256), Y273 (= Y263)
- 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 (= F49), Y90 (= Y77), R91 (= R78), G137 (= G126), V139 (= V128), G167 (= G156), D168 (= D157), G169 (= G158), N197 (= N186), Y199 (= Y188), G200 (≠ A189), H264 (= H255)
- binding magnesium ion: D168 (= D157), N197 (= N186), Y199 (= Y188)
1ni4A Human pyruvate dehydrogenase (see paper)
47% identity, 93% coverage: 23:337/340 of query aligns to 36:347/362 of 1ni4A
- active site: Q52 (= Q39), G137 (= G126), R260 (= R251), H264 (= H255), S265 (= S256), Y273 (= Y263)
- binding magnesium ion: D168 (= D157), N197 (= N186), Y199 (= Y188)
- binding thiamine diphosphate: Y90 (= Y77), R91 (= R78), V139 (= V128), G167 (= G156), D168 (= D157), G169 (= G158), A170 (= A159), N197 (= N186), G200 (≠ A189), H264 (= H255)
3exeA Crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex (see paper)
47% identity, 93% coverage: 23:337/340 of query aligns to 37:348/363 of 3exeA
- active site: Q53 (= Q39), G138 (= G126), R261 (= R251), H265 (= H255), S266 (= S256), Y274 (= Y263)
- binding manganese (ii) ion: D169 (= D157), N198 (= N186), Y200 (= Y188)
- binding thiamine diphosphate: Y91 (= Y77), R92 (= R78), V140 (= V128), G168 (= G156), D169 (= D157), G170 (= G158), A171 (= A159), N198 (= N186), Y200 (= Y188), G201 (≠ A189), H265 (= H255)
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)
44% identity, 93% coverage: 16:332/340 of query aligns to 77:393/420 of P16387
- S313 (= S256) modified: Phosphoserine; by PDK1 and PDK2
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
6cerA Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
41% identity, 93% coverage: 23:337/340 of query aligns to 37:327/342 of 6cerA
6cerE Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
41% identity, 93% coverage: 23:337/340 of query aligns to 36:325/340 of 6cerE
3exhE Crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex (see paper)
40% identity, 93% coverage: 23:337/340 of query aligns to 36:316/331 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)
29% identity, 92% coverage: 24:335/340 of query aligns to 42:354/367 of Q5SLR4
- F66 (= F49) binding
- YYR 94:96 (≠ Y-R 77:78) binding
- Y95 (vs. gap) binding
- MPEH 128:131 (≠ GSMH 110:113) binding
- S144 (≠ G126) binding
- SPI 144:146 (≠ GIV 126:128) binding
- 174:180 (vs. 156:162, 57% identical) binding
- D175 (= D157) binding
- N204 (= N186) binding
- NFYAI 204:208 (≠ NGYAM 186:190) binding
- Y206 (= Y188) binding
- H273 (= H255) binding
1umdA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methyl-2-oxopentanoate as an intermediate (see paper)
29% identity, 92% coverage: 24:335/340 of query aligns to 37:349/362 of 1umdA
- active site: I52 (≠ Q39), S139 (≠ G126), R264 (= R251), H268 (= H255), S269 (= S256), Y277 (= Y263)
- binding 2-oxo-4-methylpentanoic acid: F61 (= F49), Y90 (vs. gap), S139 (≠ G126)
- binding magnesium ion: D170 (= D157), N199 (= N186), Y201 (= Y188)
- binding thiamine diphosphate: Y89 (= Y77), Y90 (vs. gap), R91 (= R78), P140 (≠ I127), I141 (≠ V128), G169 (= G156), D170 (= D157), G171 (= G158), N199 (= N186), Y201 (= Y188), A202 (= A189), I203 (≠ M190), H268 (= H255)
1umcA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methylpentanoate (see paper)
29% identity, 92% coverage: 24:335/340 of query aligns to 37:349/362 of 1umcA
- active site: I52 (≠ Q39), S139 (≠ G126), R264 (= R251), H268 (= H255), S269 (= S256), Y277 (= Y263)
- binding 4-methyl valeric acid: Y90 (vs. gap), H126 (= H113)
- binding magnesium ion: D170 (= D157), N199 (= N186), Y201 (= Y188)
- binding thiamine diphosphate: Y89 (= Y77), Y90 (vs. gap), R91 (= R78), I141 (≠ V128), G169 (= G156), D170 (= D157), G171 (= G158), N199 (= N186), Y201 (= Y188), I203 (≠ M190), H268 (= H255)
1umbA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 in holo-form (see paper)
29% identity, 92% coverage: 24:335/340 of query aligns to 37:349/362 of 1umbA
- active site: I52 (≠ Q39), S139 (≠ G126), R264 (= R251), H268 (= H255), S269 (= S256), Y277 (= Y263)
- binding magnesium ion: D170 (= D157), N199 (= N186), Y201 (= Y188)
- binding thiamine diphosphate: Y89 (= Y77), Y90 (vs. gap), R91 (= R78), P140 (≠ I127), I141 (≠ V128), G169 (= G156), D170 (= D157), G171 (= G158), N199 (= N186), Y201 (= Y188), A202 (= A189), I203 (≠ M190), H268 (= H255)
3dufA Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
32% identity, 91% coverage: 27:337/340 of query aligns to 50:350/365 of 3dufA
- active site: S62 (≠ Q39), I139 (≠ G126), R264 (= R251), H268 (= H255), T269 (≠ S256), Y278 (= Y263)
- binding magnesium ion: D170 (= D157), N199 (= N186), F201 (≠ Y188)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1r)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: Y99 (= Y77), R100 (= R78), I141 (≠ V128), G169 (= G156), D170 (= D157), G171 (= G158), N199 (= N186), F201 (≠ Y188), A202 (= A189), H268 (= H255)
P11960 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 Rattus norvegicus (Rat) (see paper)
31% identity, 91% coverage: 24:332/340 of query aligns to 102:411/441 of P11960
- S333 (= S256) modified: Phosphoserine; by BCKDK
Query Sequence
>Echvi_1221 Echvi_1221 pyruvate dehydrogenase E1 component, alpha subunit
MAKKSSTTTKSKVKYSKETYTFWYESMLLMRRFEEKAGQLYGQQKIRGFCHLYIGQEACA
AGAITALEKDDKWITAYRDHAHPLGLGTDPGAVMAELFGKATGTTKGKGGSMHIFDKERN
FMGGHGIVGAQVPMGLGIGFAEKYKGTKNLCICHMGDGAVRQGAVHESFNLAMLYKVPVI
FVIENNGYAMGTSVKRSSNVDDLSTLGESYDMPSFAVDGMNVEEVHEAVAEAAERARKGD
GPTLLEVRTYRYKGHSMSDPQKYRTREEVEEYKAKDPIEQVKKTILDNKILSEDDIKEID
AKVKKQVADAVKFAEESPWPDGQKAFEDVYMQEDYPFVME
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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