SitesBLAST
Comparing AZOBR_RS25395 FitnessBrowser__azobra:AZOBR_RS25395 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)
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)
36% identity, 98% coverage: 1:309/316 of query aligns to 82:390/420 of P16387
- S313 (≠ T236) 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)
36% identity, 98% coverage: 1:309/316 of query aligns to 79:387/409 of Q10489
- Y306 (≠ F232) modified: Phosphotyrosine
- S310 (≠ T236) modified: Phosphoserine
- S312 (= S238) modified: Phosphoserine
Sites not aligning to the query:
- 6 modified: Phosphothreonine
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)
34% identity, 96% coverage: 1:302/316 of query aligns to 62:361/390 of P35486
- S232 (≠ R173) modified: Phosphoserine; by PDK1
- S293 (≠ T236) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- S300 (≠ T242) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- K336 (≠ E277) modified: N6-acetyllysine; mutation K->Q,R: Decreases phosphorylation at S-232 and S-300 but does not affect activity or substrate metabolism.
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)
35% identity, 97% coverage: 4:309/316 of query aligns to 61:364/396 of P26267
- S289 (≠ T236) modified: Phosphoserine
- S296 (vs. gap) modified: Phosphoserine
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)
34% identity, 96% coverage: 1:302/316 of query aligns to 62:361/390 of P26284
- S232 (≠ R173) modified: Phosphoserine; by PDK1
- S293 (≠ T236) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- S300 (≠ T242) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
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)
35% identity, 99% coverage: 1:313/316 of query aligns to 64:377/393 of Q8H1Y0
- R121 (= R58) mutation to C: In iar4-1; reduced sensitivity to several IAA-amino acid conjugates.
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)
34% identity, 96% coverage: 1:302/316 of query aligns to 60:359/388 of P29803
- M227 (≠ A170) to V: in SPGF70; uncertain significance; dbSNP:rs200969445
- S230 (≠ R173) mutation to A: Slightly reduces enzyme activity.
- S291 (≠ T236) 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 (= S238) 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 (≠ T242) modified: Phosphoserine; by PDK3; mutation to A: Slightly reduces enzyme activity.
6cfoA Human pyruvate dehydrogenase e1 component complex with covalent tdp adduct acetyl phosphinate (see paper)
34% identity, 96% coverage: 1:302/316 of query aligns to 34:333/362 of 6cfoA
- active site: Q52 (≠ E19), G137 (= G106), R260 (= R231), H264 (= H235), S265 (≠ T236), Y273 (= Y243)
- 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 (≠ Y29), Y90 (≠ H57), R91 (= R58), G137 (= G106), V139 (= V108), G167 (= G136), D168 (= D137), G169 (= G138), N197 (= N166), Y199 (= Y168), G200 (= G169), H264 (= H235)
- binding magnesium ion: D168 (= D137), N197 (= N166), Y199 (= Y168)
1ni4A Human pyruvate dehydrogenase (see paper)
34% identity, 96% coverage: 1:302/316 of query aligns to 34:333/362 of 1ni4A
- active site: Q52 (≠ E19), G137 (= G106), R260 (= R231), H264 (= H235), S265 (≠ T236), Y273 (= Y243)
- binding magnesium ion: D168 (= D137), N197 (= N166), Y199 (= Y168)
- binding thiamine diphosphate: Y90 (≠ H57), R91 (= R58), V139 (= V108), G167 (= G136), D168 (= D137), G169 (= G138), A170 (= A139), N197 (= N166), G200 (= G169), H264 (= H235)
3exeA Crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex (see paper)
34% identity, 96% coverage: 1:302/316 of query aligns to 35:334/363 of 3exeA
- active site: Q53 (≠ E19), G138 (= G106), R261 (= R231), H265 (= H235), S266 (≠ T236), Y274 (= Y243)
- binding manganese (ii) ion: D169 (= D137), N198 (= N166), Y200 (= Y168)
- binding thiamine diphosphate: Y91 (≠ H57), R92 (= R58), V140 (= V108), G168 (= G136), D169 (= D137), G170 (= G138), A171 (= A139), N198 (= N166), Y200 (= Y168), G201 (= G169), H265 (= H235)
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)
34% identity, 96% coverage: 1:302/316 of query aligns to 62:361/390 of P08559
- A136 (≠ R75) to T: found in a patient with moderate developmental delay, mild dysmorphism and mildly elevated serum lactate; uncertain significance; dbSNP:rs138727886
- S232 (≠ R173) modified: Phosphoserine; by PDK1; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-293 and A-300.
- M282 (≠ L225) to L: in dbSNP:rs2229137
- S293 (≠ T236) 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 (≠ T242) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-232 and A-293.
- R302 (= R244) 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
6cerE Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
33% identity, 82% coverage: 1:260/316 of query aligns to 34:286/340 of 6cerE
3exhE Crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex (see paper)
34% identity, 82% coverage: 1:260/316 of query aligns to 34:277/331 of 3exhE
6cerA Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
32% identity, 96% coverage: 1:302/316 of query aligns to 35:313/342 of 6cerA
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)
29% identity, 98% coverage: 1:309/316 of query aligns to 103:412/445 of P12694
- Y158 (≠ H57) binding
- R159 (= R58) binding ; to W: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs769688327
- Q190 (≠ G89) to K: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- S206 (≠ N105) binding
- S207 (≠ G106) binding
- P208 (≠ V107) binding
- T211 (≠ A110) binding ; to M: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123503
- Q212 (≠ G111) binding
- E238 (≠ D137) binding
- G239 (= G138) binding
- A240 (= A139) binding
- G249 (≠ A148) 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 (= A152) to T: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs199599175
- A254 (= A153) to D: in MSUD1A; uncertain significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity
- R265 (≠ E164) 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 (= N166) 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 (= Y168) binding
- A285 (≠ G184) 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 (≠ S189) 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 (≠ V196) to H: in MSUD1A; uncertain significance; decreased affinity for the cofactor thiamine diphosphate; decreased 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs200137189
- T310 (≠ A208) to R: in MSUD1A; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852875
- I326 (≠ L225) to T: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- H336 (= H235) binding
- S337 (≠ T236) modified: Phosphoserine; by BCKDK; mutation to A: Substantially decreases the stability of the BCKD complex.
- S347 (≠ D245) mutation to A: Does not affect the stability of the BCKD complex.
- F409 (= F306) to C: in MSUD1A; decreased solubility; loss of mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852872
Sites not aligning to the query:
- 1:45 modified: transit peptide, Mitochondrion
- 413 Y → C: in MSUD1A; uncertain significance; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123508
- 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)
28% identity, 98% coverage: 1:309/316 of query aligns to 99:408/441 of P11960
- S333 (≠ T236) modified: Phosphoserine; by BCKDK
2bffA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
28% identity, 98% coverage: 1:309/316 of query aligns to 53:359/392 of 2bffA
- active site: E71 (= E19), S157 (≠ G106), R282 (= R231), H286 (= H235), S287 (≠ T236), Y295 (= Y243)
- binding manganese (ii) ion: E188 (≠ D137), N217 (= N166), Y219 (= Y168)
- binding 2-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-2-oxo-2,3-dihydro-1,3-thiazol-5-yl}ethyl trihydrogendiphosphate: Q107 (≠ T56), Y108 (≠ H57), R109 (= R58), L159 (≠ V108), G187 (= G136), E188 (≠ D137), G189 (= G138), A190 (= A139), R215 (≠ E164), N217 (= N166), Y219 (= Y168), A220 (≠ G169), I221 (≠ A170), H286 (= H235)
2bewA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
28% identity, 98% coverage: 1:309/316 of query aligns to 53:357/390 of 2bewA
- active site: E71 (= E19), S157 (≠ G106), R282 (= R231), H286 (= H235), S287 (≠ T236), Y295 (= Y243)
- binding manganese (ii) ion: E188 (≠ D137), N217 (= N166), Y219 (= Y168), A220 (≠ G169)
- binding c2-1-hydroxyphenyl-thiamin diphosphate: M82 (≠ I30), Q107 (≠ T56), Y108 (≠ H57), R109 (= R58), L159 (≠ V108), G187 (= G136), E188 (≠ D137), G189 (= G138), A190 (= A139), R215 (≠ E164), N217 (= N166), Y219 (= Y168), A220 (≠ G169), I221 (≠ A170), H286 (= H235)
2bevA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
28% identity, 98% coverage: 1:309/316 of query aligns to 53:357/390 of 2bevA
- active site: E71 (= E19), S157 (≠ G106), R282 (= R231), H286 (= H235), S287 (≠ T236), Y295 (= Y243)
- binding manganese (ii) ion: E188 (≠ D137), N217 (= N166), Y219 (= Y168), A220 (≠ G169)
- binding c2-1-hydroxy-2-methyl-butyl-thiamin diphosphate: F80 (≠ G28), Q107 (≠ T56), Y108 (≠ H57), R109 (= R58), S157 (≠ G106), L159 (≠ V108), G187 (= G136), E188 (≠ D137), G189 (= G138), A190 (= A139), R215 (≠ E164), N217 (= N166), Y219 (= Y168), A220 (≠ G169), I221 (≠ A170), H286 (= H235)
2beuA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
28% identity, 98% coverage: 1:309/316 of query aligns to 53:357/390 of 2beuA
- active site: E71 (= E19), S157 (≠ G106), R282 (= R231), H286 (= H235), S287 (≠ T236), Y295 (= Y243)
- binding manganese (ii) ion: E188 (≠ D137), N217 (= N166), Y219 (= Y168), A220 (≠ G169)
- binding c2-1-hydroxy-3-methyl-propyl-thiamin diphosphate: Q107 (≠ T56), Y108 (≠ H57), R109 (= R58), S157 (≠ G106), L159 (≠ V108), G187 (= G136), E188 (≠ D137), G189 (= G138), A190 (= A139), R215 (≠ E164), N217 (= N166), Y219 (= Y168), A220 (≠ G169), I221 (≠ A170), H286 (= H235)
Query Sequence
>AZOBR_RS25395 FitnessBrowser__azobra:AZOBR_RS25395
LGLYATMQRIRVFETLADEAHKAGQVAGYIHLSIGQEAIAAAVGANLRADDVLTSTHRGH
GHTIAKGADPLAMFRELCGRAGGTCGGKGGSMHIADFSVGMLGANGVVAAGLPIAVGAAH
AIALKGEDRIAVCFFGDGATNRGPFLEALNWAAAFRLPVLFVCEDNGYGATTRTGSVSAG
GGPGVRAESLGIPVTVVDGNDLAAVDAAAAALVRAVRDGGGPQFLHARTYRFRGHTSSDP
ATYRDAAEVRAQLAGNDPLQRAAATLAELGVTPDALERVERHERETLAAALATALDSPWP
DLRTAFTDVQDIGAPQ
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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