SitesBLAST
Comparing CCNA_01799 FitnessBrowser__Caulo:CCNA_01799 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)
50% identity, 93% coverage: 19:338/343 of query aligns to 52:369/390 of P35486
- S232 (≠ A201) modified: Phosphoserine; by PDK1
- S293 (= S264) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- S300 (≠ K270) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- K336 (= K305) modified: N6-acetyllysine; mutation K->Q,R: Decreases phosphorylation at S-232 and S-300 but does not affect activity or substrate metabolism.
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)
51% identity, 93% coverage: 19:338/343 of query aligns to 50:367/388 of P29803
- M227 (= M198) to V: in SPGF70; uncertain significance; dbSNP:rs200969445
- S230 (≠ A201) mutation to A: Slightly reduces enzyme activity.
- S291 (= S264) 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 (= S266) 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 (≠ K270) modified: Phosphoserine; by PDK3; mutation to A: Slightly reduces enzyme activity.
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)
50% identity, 93% coverage: 19:338/343 of query aligns to 52:369/390 of P26284
- S232 (≠ A201) modified: Phosphoserine; by PDK1
- S293 (= S264) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- S300 (≠ K270) 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)
50% identity, 93% coverage: 19:338/343 of query aligns to 48:365/396 of P26267
- S289 (= S264) modified: Phosphoserine
- S296 (≠ K270) 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, 92% coverage: 26:340/343 of query aligns to 61:374/393 of Q8H1Y0
- R121 (= R86) mutation to C: In iar4-1; reduced sensitivity to several IAA-amino acid conjugates.
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)
50% identity, 93% coverage: 25:343/343 of query aligns to 78:396/420 of P16387
- S313 (= S264) 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)
51% identity, 93% coverage: 19:338/343 of query aligns to 52:369/390 of P08559
- A136 (= A103) to T: found in a patient with moderate developmental delay, mild dysmorphism and mildly elevated serum lactate; uncertain significance; dbSNP:rs138727886
- S232 (≠ A201) modified: Phosphoserine; by PDK1; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-293 and A-300.
- M282 (≠ L253) to L: in dbSNP:rs2229137
- S293 (= S264) 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 (≠ K270) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-232 and A-293.
- R302 (= R272) 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)
51% identity, 93% coverage: 19:338/343 of query aligns to 24:341/362 of 6cfoA
- active site: Q52 (= Q47), G137 (= G134), R260 (= R259), H264 (= H263), S265 (= S264), Y273 (= Y271)
- 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 (= F57), Y90 (= Y85), R91 (= R86), G137 (= G134), V139 (= V136), G167 (= G164), D168 (= D165), G169 (= G166), N197 (= N194), Y199 (= Y196), G200 (≠ A197), H264 (= H263)
- binding magnesium ion: D168 (= D165), N197 (= N194), Y199 (= Y196)
1ni4A Human pyruvate dehydrogenase (see paper)
51% identity, 93% coverage: 19:338/343 of query aligns to 24:341/362 of 1ni4A
- active site: Q52 (= Q47), G137 (= G134), R260 (= R259), H264 (= H263), S265 (= S264), Y273 (= Y271)
- binding magnesium ion: D168 (= D165), N197 (= N194), Y199 (= Y196)
- binding thiamine diphosphate: Y90 (= Y85), R91 (= R86), V139 (= V136), G167 (= G164), D168 (= D165), G169 (= G166), A170 (= A167), N197 (= N194), G200 (≠ A197), H264 (= H263)
3exeA Crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex (see paper)
51% identity, 93% coverage: 19:338/343 of query aligns to 25:342/363 of 3exeA
- active site: Q53 (= Q47), G138 (= G134), R261 (= R259), H265 (= H263), S266 (= S264), Y274 (= Y271)
- binding manganese (ii) ion: D169 (= D165), N198 (= N194), Y200 (= Y196)
- binding thiamine diphosphate: Y91 (= Y85), R92 (= R86), V140 (= V136), G168 (= G164), D169 (= D165), G170 (= G166), A171 (= A167), N198 (= N194), Y200 (= Y196), G201 (≠ A197), H265 (= H263)
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)
47% identity, 94% coverage: 23:343/343 of query aligns to 73:393/409 of Q10489
- Y306 (= Y260) modified: Phosphotyrosine
- S310 (= S264) modified: Phosphoserine
- S312 (= S266) modified: Phosphoserine
Sites not aligning to the query:
- 6 modified: Phosphothreonine
6cerA Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
46% identity, 93% coverage: 19:338/343 of query aligns to 25:321/342 of 6cerA
6cerE Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
45% identity, 93% coverage: 19:338/343 of query aligns to 24:319/340 of 6cerE
3exhE Crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex (see paper)
44% identity, 93% coverage: 19:338/343 of query aligns to 24:310/331 of 3exhE
3dufA Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
31% identity, 92% coverage: 26:340/343 of query aligns to 40:347/365 of 3dufA
- active site: S62 (≠ Q47), I139 (= I125), R264 (= R259), H268 (= H263), T269 (≠ S264), Y278 (= Y271)
- binding magnesium ion: D170 (= D165), N199 (= N194), F201 (≠ Y196)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1r)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: Y99 (= Y85), R100 (= R86), I141 (≠ V136), G169 (= G164), D170 (= D165), G171 (= G166), N199 (= N194), F201 (≠ Y196), A202 (= A197), H268 (= H263)
1umdA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methyl-2-oxopentanoate as an intermediate (see paper)
31% identity, 92% coverage: 26:340/343 of query aligns to 31:346/362 of 1umdA
- active site: I52 (≠ Q47), S139 (≠ G134), R264 (= R259), H268 (= H263), S269 (= S264), Y277 (= Y271)
- binding 2-oxo-4-methylpentanoic acid: F61 (= F57), Y90 (= Y85), S139 (≠ G134)
- binding magnesium ion: D170 (= D165), N199 (= N194), Y201 (= Y196)
- binding thiamine diphosphate: Y89 (≠ G84), Y90 (= Y85), R91 (= R86), P140 (≠ I135), I141 (≠ V136), G169 (= G164), D170 (= D165), G171 (= G166), N199 (= N194), Y201 (= Y196), A202 (= A197), I203 (≠ M198), H268 (= H263)
1umcA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methylpentanoate (see paper)
31% identity, 92% coverage: 26:340/343 of query aligns to 31:346/362 of 1umcA
- active site: I52 (≠ Q47), S139 (≠ G134), R264 (= R259), H268 (= H263), S269 (= S264), Y277 (= Y271)
- binding 4-methyl valeric acid: Y90 (= Y85), H126 (= H121)
- binding magnesium ion: D170 (= D165), N199 (= N194), Y201 (= Y196)
- binding thiamine diphosphate: Y89 (≠ G84), Y90 (= Y85), R91 (= R86), I141 (≠ V136), G169 (= G164), D170 (= D165), G171 (= G166), N199 (= N194), Y201 (= Y196), I203 (≠ M198), H268 (= H263)
1umbA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 in holo-form (see paper)
31% identity, 92% coverage: 26:340/343 of query aligns to 31:346/362 of 1umbA
- active site: I52 (≠ Q47), S139 (≠ G134), R264 (= R259), H268 (= H263), S269 (= S264), Y277 (= Y271)
- binding magnesium ion: D170 (= D165), N199 (= N194), Y201 (= Y196)
- binding thiamine diphosphate: Y89 (≠ G84), Y90 (= Y85), R91 (= R86), P140 (≠ I135), I141 (≠ V136), G169 (= G164), D170 (= D165), G171 (= G166), N199 (= N194), Y201 (= Y196), A202 (= A197), I203 (≠ M198), H268 (= H263)
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)
31% identity, 92% coverage: 26:340/343 of query aligns to 36:351/367 of Q5SLR4
1w85A The crystal structure of pyruvate dehydrogenase e1 bound to the peripheral subunit binding domain of e2 (see paper)
30% identity, 92% coverage: 26:340/343 of query aligns to 40:341/358 of 1w85A
- active site: S62 (≠ Q47), I139 (= I125), R264 (= R259), H268 (= H263), T269 (≠ S264)
- binding magnesium ion: D170 (= D165), N199 (= N194), F201 (≠ Y196)
- binding thiamine diphosphate: Y99 (= Y85), R100 (= R86), I139 (= I125), I141 (≠ V136), G169 (= G164), D170 (= D165), G171 (= G166), G172 (≠ A167), N199 (= N194), A202 (= A197), I203 (≠ M198), H268 (= H263)
Query Sequence
>CCNA_01799 FitnessBrowser__Caulo:CCNA_01799
MARTRKAEASEGKAPETGVNAFVGKDELLKFYQDMLLIRRFEERAGQLYGMGLIGGFCHL
YIGQEAIAVGMQSISQKGDQIITGYRDHGHMLAAGMDPREVMAELTGRAGGSSKGKGGSM
HMFDIATGFYGGHGIVGAQVALGTGLALANSYRNNGNVSYAYMGDGAANQGQVYESFNMA
QLWKLPVVYVIENNQYAMGTAVERAASETAFHKRGVSFRIPGEEVDGMDVIAVREAGARA
TEHARSGQGPYILEMKTYRYRGHSMSDPAKYRTKEEVDEVKTTRDPIDHIKERLAKAGVT
EDDLKGVDAEVKRIVAEAAEFARTSPEPDPSELYTDVYLEAAE
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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