SitesBLAST
Comparing AZOBR_RS22245 FitnessBrowser__azobra:AZOBR_RS22245 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)
53% identity, 92% coverage: 21:330/338 of query aligns to 57:364/390 of P35486
- S232 (= S198) modified: Phosphoserine; by PDK1
- S293 (= S260) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- S300 (≠ K266) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- K336 (= K302) 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)
53% identity, 92% coverage: 21:330/338 of query aligns to 57:364/390 of P26284
- S232 (= S198) modified: Phosphoserine; by PDK1
- S293 (= S260) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- S300 (≠ K266) 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)
54% identity, 90% coverage: 26:330/338 of query aligns to 60:362/388 of P29803
- M227 (= M195) to V: in SPGF70; uncertain significance; dbSNP:rs200969445
- S230 (= S198) mutation to A: Slightly reduces enzyme activity.
- S291 (= S260) 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 (= S262) 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 (≠ K266) 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)
47% identity, 94% coverage: 21:337/338 of query aligns to 59:374/393 of Q8H1Y0
- R121 (= R83) 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 13 papers)
53% identity, 92% coverage: 21:330/338 of query aligns to 57:364/390 of P08559
- A136 (= A100) to T: found in a patient with moderate developmental delay, mild dysmorphism and mildly elevated serum lactate; uncertain significance; dbSNP:rs138727886
- S232 (= S198) modified: Phosphoserine; by PDK1; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-293 and A-300.
- M282 (≠ L249) to L: in dbSNP:rs2229137
- S293 (= S260) 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 (≠ K266) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-232 and A-293.
- R302 (= R268) 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)
53% identity, 92% coverage: 21:330/338 of query aligns to 29:336/362 of 6cfoA
- active site: Q52 (= Q44), G137 (= G131), R260 (= R255), H264 (= H259), S265 (= S260), Y273 (= Y267)
- 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 (= F54), Y90 (= Y82), R91 (= R83), G137 (= G131), V139 (= V133), G167 (= G161), D168 (= D162), G169 (= G163), N197 (= N191), Y199 (= Y193), G200 (≠ A194), H264 (= H259)
- binding magnesium ion: D168 (= D162), N197 (= N191), Y199 (= Y193)
1ni4A Human pyruvate dehydrogenase (see paper)
53% identity, 92% coverage: 21:330/338 of query aligns to 29:336/362 of 1ni4A
- active site: Q52 (= Q44), G137 (= G131), R260 (= R255), H264 (= H259), S265 (= S260), Y273 (= Y267)
- binding magnesium ion: D168 (= D162), N197 (= N191), Y199 (= Y193)
- binding thiamine diphosphate: Y90 (= Y82), R91 (= R83), V139 (= V133), G167 (= G161), D168 (= D162), G169 (= G163), A170 (= A164), N197 (= N191), G200 (≠ A194), H264 (= H259)
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, 94% coverage: 20:337/338 of query aligns to 76:393/420 of P16387
- S313 (= S260) modified: Phosphoserine; by PDK1 and PDK2
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
3exeA Crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex (see paper)
53% identity, 92% coverage: 21:330/338 of query aligns to 30:337/363 of 3exeA
- active site: Q53 (= Q44), G138 (= G131), R261 (= R255), H265 (= H259), S266 (= S260), Y274 (= Y267)
- binding manganese (ii) ion: D169 (= D162), N198 (= N191), Y200 (= Y193)
- binding thiamine diphosphate: Y91 (= Y82), R92 (= R83), V140 (= V133), G168 (= G161), D169 (= D162), G170 (= G163), A171 (= A164), N198 (= N191), Y200 (= Y193), G201 (≠ A194), H265 (= H259)
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)
49% identity, 93% coverage: 24:336/338 of query aligns to 77:389/409 of Q10489
- Y306 (= Y256) modified: Phosphotyrosine
- S310 (= S260) modified: Phosphoserine
- S312 (= S262) 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)
50% identity, 93% coverage: 21:334/338 of query aligns to 53:364/396 of P26267
- S289 (= S260) modified: Phosphoserine
- S296 (≠ K266) modified: Phosphoserine
6cerA Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
48% identity, 92% coverage: 21:330/338 of query aligns to 30:316/342 of 6cerA
6cerE Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
47% identity, 92% coverage: 21:330/338 of query aligns to 29:314/340 of 6cerE
3exhE Crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex (see paper)
47% identity, 92% coverage: 21:330/338 of query aligns to 29:305/331 of 3exhE
1umdA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methyl-2-oxopentanoate as an intermediate (see paper)
34% identity, 79% coverage: 23:290/338 of query aligns to 31:299/362 of 1umdA
- active site: I52 (≠ Q44), S139 (≠ G131), R264 (= R255), H268 (= H259), S269 (= S260), Y277 (= Y267)
- binding 2-oxo-4-methylpentanoic acid: F61 (= F54), Y90 (= Y82), S139 (≠ G131)
- binding magnesium ion: D170 (= D162), N199 (= N191), Y201 (= Y193)
- binding thiamine diphosphate: Y89 (≠ S81), Y90 (= Y82), R91 (= R83), P140 (≠ I132), I141 (≠ V133), G169 (= G161), D170 (= D162), G171 (= G163), N199 (= N191), Y201 (= Y193), A202 (= A194), I203 (≠ M195), H268 (= H259)
1umcA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methylpentanoate (see paper)
34% identity, 79% coverage: 23:290/338 of query aligns to 31:299/362 of 1umcA
- active site: I52 (≠ Q44), S139 (≠ G131), R264 (= R255), H268 (= H259), S269 (= S260), Y277 (= Y267)
- binding 4-methyl valeric acid: Y90 (= Y82), H126 (= H118)
- binding magnesium ion: D170 (= D162), N199 (= N191), Y201 (= Y193)
- binding thiamine diphosphate: Y89 (≠ S81), Y90 (= Y82), R91 (= R83), I141 (≠ V133), G169 (= G161), D170 (= D162), G171 (= G163), N199 (= N191), Y201 (= Y193), I203 (≠ M195), H268 (= H259)
1umbA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 in holo-form (see paper)
34% identity, 79% coverage: 23:290/338 of query aligns to 31:299/362 of 1umbA
- active site: I52 (≠ Q44), S139 (≠ G131), R264 (= R255), H268 (= H259), S269 (= S260), Y277 (= Y267)
- binding magnesium ion: D170 (= D162), N199 (= N191), Y201 (= Y193)
- binding thiamine diphosphate: Y89 (≠ S81), Y90 (= Y82), R91 (= R83), P140 (≠ I132), I141 (≠ V133), G169 (= G161), D170 (= D162), G171 (= G163), N199 (= N191), Y201 (= Y193), A202 (= A194), I203 (≠ M195), H268 (= H259)
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)
34% identity, 79% coverage: 23:290/338 of query aligns to 36:304/367 of Q5SLR4
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, 93% coverage: 23:337/338 of query aligns to 100:415/445 of P12694
- Y158 (= Y82) binding
- R159 (= R83) binding ; to W: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs769688327
- Q190 (≠ G114) to K: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- S206 (≠ H130) binding
- S207 (≠ G131) binding
- P208 (≠ I132) binding
- T211 (≠ A135) binding ; to M: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123503
- Q212 (= Q136) binding
- E238 (≠ D162) binding
- G239 (= G163) binding
- A240 (= A164) binding
- G249 (≠ S173) 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 (= A177) to T: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs199599175
- A254 (= A178) to D: in MSUD1A; uncertain significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity
- R265 (≠ E189) binding ; 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 (= N191) binding ; 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
- Y269 (= Y193) binding
- A285 (≠ H208) 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 (≠ A213) 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 (≠ Q220) to H: in MSUD1A; uncertain significance; decreased affinity for the cofactor thiamine diphosphate; decreased 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs200137189
- T310 (≠ A233) to R: in MSUD1A; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852875
- I326 (≠ L249) to T: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- H336 (= H259) binding
- S337 (= S260) modified: Phosphoserine; by BCKDK; mutation to A: Substantially decreases the stability of the BCKD complex.
- S347 (≠ T269) mutation to A: Does not affect the stability of the BCKD complex.
- F409 (≠ W331) 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 (≠ L335) 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
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)
30% identity, 93% coverage: 23:337/338 of query aligns to 96:411/441 of P11960
- S333 (= S260) modified: Phosphoserine; by BCKDK
Query Sequence
>AZOBR_RS22245 FitnessBrowser__azobra:AZOBR_RS22245
MAASRRRPKAQTDSASKQAASTEDLIKYYREMLLIRRFEEKAGQLYGMGLIGGFCHLYIG
QEAVVVGIQAALKDNDDVITSYRDHGHMLACGMDPKGVMAELTGRRGGYSKGKGGSMHMF
SREKNFYGGHGIVGAQVPLGTGLAFSHKYNKDDGLSAVYCGDGAINQGQVYESFNMAALW
KLPVLYVIENNKYAMGTSQERASAGELHQRGAAYGIPGHQVNGMDVLEVREAADKWVEYI
RAGNGPVILEMKTYRYRGHSMSDPAKYRTKEEVEKMRSESDPIDNLKRVLLEGAYVTEDQ
LKEIDREVKAVVTEAAEFAQQSPEPDPAELWTDVLVEA
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