SitesBLAST
Comparing AO353_19950 FitnessBrowser__pseudo3_N2E3:AO353_19950 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)
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)
43% identity, 97% coverage: 6:323/327 of query aligns to 52:369/396 of P26267
- S289 (= S247) modified: Phosphoserine
- S296 (≠ L253) 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)
38% identity, 98% coverage: 4:322/327 of query aligns to 54:370/390 of P35486
- S232 (≠ A184) modified: Phosphoserine; by PDK1
- S293 (= S247) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- S300 (vs. gap) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- K336 (≠ Q288) 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)
38% identity, 98% coverage: 4:322/327 of query aligns to 54:370/390 of P26284
- S232 (≠ A184) modified: Phosphoserine; by PDK1
- S293 (= S247) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- S300 (vs. gap) 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)
37% identity, 98% coverage: 6:326/327 of query aligns to 54:372/388 of P29803
- M227 (= M181) to V: in SPGF70; uncertain significance; dbSNP:rs200969445
- S230 (≠ A184) mutation to A: Slightly reduces enzyme activity.
- S291 (= S247) 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 (≠ F249) 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 (vs. gap) modified: Phosphoserine; by PDK3; mutation to A: Slightly reduces enzyme activity.
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)
39% identity, 98% coverage: 8:327/327 of query aligns to 78:397/420 of P16387
- S313 (= S247) modified: Phosphoserine; by PDK1 and PDK2
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
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)
38% identity, 96% coverage: 12:325/327 of query aligns to 79:392/409 of Q10489
- Y306 (≠ F243) modified: Phosphotyrosine
- S310 (= S247) modified: Phosphoserine
- S312 (≠ F249) 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)
38% identity, 97% coverage: 6:322/327 of query aligns to 56:370/390 of P08559
- A136 (= A86) to T: found in a patient with moderate developmental delay, mild dysmorphism and mildly elevated serum lactate; uncertain significance; dbSNP:rs138727886
- S232 (≠ A184) modified: Phosphoserine; by PDK1; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-293 and A-300.
- M282 (≠ L236) to L: in dbSNP:rs2229137
- S293 (= S247) 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 (vs. gap) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-232 and A-293.
- R302 (= R255) 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)
38% identity, 98% coverage: 4:322/327 of query aligns to 26:342/362 of 6cfoA
- active site: Q52 (≠ E30), G137 (≠ A117), R260 (= R242), H264 (= H246), S265 (= S247), Y273 (= Y254)
- 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 (= F40), Y90 (= Y68), R91 (= R69), G137 (≠ A117), V139 (= V119), G167 (= G147), D168 (≠ E148), G169 (= G149), N197 (= N177), Y199 (= Y179), G200 (≠ A180), H264 (= H246)
- binding magnesium ion: D168 (≠ E148), N197 (= N177), Y199 (= Y179)
1ni4A Human pyruvate dehydrogenase (see paper)
38% identity, 98% coverage: 4:322/327 of query aligns to 26:342/362 of 1ni4A
- active site: Q52 (≠ E30), G137 (≠ A117), R260 (= R242), H264 (= H246), S265 (= S247), Y273 (= Y254)
- binding magnesium ion: D168 (≠ E148), N197 (= N177), Y199 (= Y179)
- binding thiamine diphosphate: Y90 (= Y68), R91 (= R69), V139 (= V119), G167 (= G147), D168 (≠ E148), G169 (= G149), A170 (= A150), N197 (= N177), G200 (≠ A180), H264 (= H246)
3exeA Crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex (see paper)
38% identity, 98% coverage: 4:322/327 of query aligns to 27:343/363 of 3exeA
- active site: Q53 (≠ E30), G138 (≠ A117), R261 (= R242), H265 (= H246), S266 (= S247), Y274 (= Y254)
- binding manganese (ii) ion: D169 (≠ E148), N198 (= N177), Y200 (= Y179)
- binding thiamine diphosphate: Y91 (= Y68), R92 (= R69), V140 (= V119), G168 (= G147), D169 (≠ E148), G170 (= G149), A171 (= A150), N198 (= N177), Y200 (= Y179), G201 (≠ A180), H265 (= H246)
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)
38% identity, 96% coverage: 9:321/327 of query aligns to 61:372/393 of Q8H1Y0
- R121 (= R69) 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)
35% identity, 98% coverage: 4:322/327 of query aligns to 27:322/342 of 6cerA
6cerE Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
34% identity, 98% coverage: 4:322/327 of query aligns to 26:320/340 of 6cerE
3exhE Crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex (see paper)
34% identity, 98% coverage: 4:322/327 of query aligns to 26:311/331 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, 94% coverage: 14:321/327 of query aligns to 36:344/362 of 1umdA
- active site: I52 (≠ E30), S139 (≠ A117), R264 (= R242), H268 (= H246), S269 (= S247), Y277 (= Y254)
- binding 2-oxo-4-methylpentanoic acid: F61 (= F40), Y90 (= Y68), S139 (≠ A117)
- binding magnesium ion: D170 (≠ E148), N199 (= N177), Y201 (= Y179)
- binding thiamine diphosphate: Y89 (≠ T67), Y90 (= Y68), R91 (= R69), P140 (≠ I118), I141 (≠ V119), G169 (= G147), D170 (≠ E148), G171 (= G149), N199 (= N177), Y201 (= Y179), A202 (= A180), I203 (≠ M181), H268 (= H246)
1umcA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methylpentanoate (see paper)
34% identity, 94% coverage: 14:321/327 of query aligns to 36:344/362 of 1umcA
- active site: I52 (≠ E30), S139 (≠ A117), R264 (= R242), H268 (= H246), S269 (= S247), Y277 (= Y254)
- binding 4-methyl valeric acid: Y90 (= Y68), H126 (= H104)
- binding magnesium ion: D170 (≠ E148), N199 (= N177), Y201 (= Y179)
- binding thiamine diphosphate: Y89 (≠ T67), Y90 (= Y68), R91 (= R69), I141 (≠ V119), G169 (= G147), D170 (≠ E148), G171 (= G149), N199 (= N177), Y201 (= Y179), I203 (≠ M181), H268 (= H246)
1umbA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 in holo-form (see paper)
34% identity, 94% coverage: 14:321/327 of query aligns to 36:344/362 of 1umbA
- active site: I52 (≠ E30), S139 (≠ A117), R264 (= R242), H268 (= H246), S269 (= S247), Y277 (= Y254)
- binding magnesium ion: D170 (≠ E148), N199 (= N177), Y201 (= Y179)
- binding thiamine diphosphate: Y89 (≠ T67), Y90 (= Y68), R91 (= R69), P140 (≠ I118), I141 (≠ V119), G169 (= G147), D170 (≠ E148), G171 (= G149), N199 (= N177), Y201 (= Y179), A202 (= A180), I203 (≠ M181), H268 (= H246)
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, 94% coverage: 14:321/327 of query aligns to 41:349/367 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)
31% identity, 97% coverage: 6:321/327 of query aligns to 97:413/445 of P12694
- Y158 (= Y68) binding
- R159 (= R69) binding ; to W: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs769688327
- Q190 (≠ G100) to K: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- S206 (≠ N116) binding
- S207 (≠ A117) binding
- P208 (≠ I118) binding
- T211 (≠ G121) binding ; to M: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123503
- Q212 (≠ G122) binding
- E238 (= E148) binding
- G239 (= G149) binding
- A240 (= A150) binding
- G249 (≠ S159) 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 (= A163) to T: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs199599175
- A254 (= A164) to D: in MSUD1A; uncertain significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity
- R265 (≠ E175) 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 (= N177) 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 (= Y179) binding
- A285 (≠ C195) 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 (≠ A200) 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 (≠ S207) to H: in MSUD1A; uncertain significance; decreased affinity for the cofactor thiamine diphosphate; decreased 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs200137189
- T310 (= T220) to R: in MSUD1A; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852875
- I326 (≠ L236) to T: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- H336 (= H246) binding
- S337 (= S247) modified: Phosphoserine; by BCKDK; mutation to A: Substantially decreases the stability of the BCKD complex.
- S347 (≠ D256) mutation to A: Does not affect the stability of the BCKD complex.
- F409 (≠ S317) 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 (= Y321) 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)
32% identity, 97% coverage: 6:321/327 of query aligns to 93:409/441 of P11960
- S333 (= S247) modified: Phosphoserine; by BCKDK
Query Sequence
>AO353_19950 FitnessBrowser__pseudo3_N2E3:AO353_19950
MSLSSLPKELALGLLRDMLRIRRLEERAGELYGEGKIRGFLHLYIGEEAVAVGALHALAA
NDALVATYREHGHALIKGVPMKTIMAEMYGRQEGCSRGRGGSMHLFDVSTRFFGGNAIVA
GGLPLTVGLALAEHMQGGSRLSTCFFGEGAMAEGAFHESINLAALWQLPMLFCCENNLYA
MGTALARSQSQTDLCSKASAYKVEARSVDGMDVIAVYEATCLAVEHIRAGRGPYFLEFRT
YRFRAHSMFDPQLYRDKAEVEQWKTRGPIHTYSARLKAEGLLDEAGFQAILAEVDAEVEA
AVVFADSGSLEPVEDLSRDVYTPGTAS
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