SitesBLAST
Comparing WP_011765272.1 NCBI__GCF_000061505.1:WP_011765272.1 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)
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)
33% identity, 96% coverage: 13:319/320 of query aligns to 81:388/409 of Q10489
- Y306 (≠ L241) modified: Phosphotyrosine
- S310 (≠ F245) modified: Phosphoserine
- S312 (≠ P247) modified: Phosphoserine
Sites not aligning to the query:
- 6 modified: Phosphothreonine
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, 95% coverage: 17:320/320 of query aligns to 66:368/388 of P29803
- M227 (≠ F180) to V: in SPGF70; uncertain significance; dbSNP:rs200969445
- S230 (≠ R183) mutation to A: Slightly reduces enzyme activity.
- S291 (≠ F245) 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 (≠ P247) 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 (≠ A251) modified: Phosphoserine; by PDK3; mutation to A: Slightly reduces enzyme activity.
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)
33% identity, 95% coverage: 17:320/320 of query aligns to 68:370/390 of P35486
- S232 (≠ R183) modified: Phosphoserine; by PDK1
- S293 (≠ F245) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- S300 (≠ A251) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- K336 (≠ T286) 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)
33% identity, 95% coverage: 17:320/320 of query aligns to 68:370/390 of P26284
- S232 (≠ R183) modified: Phosphoserine; by PDK1
- S293 (≠ F245) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- S300 (≠ A251) 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)
32% identity, 96% coverage: 12:319/320 of query aligns to 65:372/393 of Q8H1Y0
- R121 (= R67) mutation to C: In iar4-1; reduced sensitivity to several IAA-amino acid conjugates.
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)
32% identity, 95% coverage: 17:319/320 of query aligns to 64:365/396 of P26267
- S289 (≠ F245) modified: Phosphoserine
- S296 (≠ A251) modified: Phosphoserine
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, 98% coverage: 5:319/320 of query aligns to 97:413/445 of P12694
- Y158 (≠ H66) binding thiamine diphosphate
- R159 (= R67) binding thiamine diphosphate; to W: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs769688327
- Q190 (≠ S98) to K: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- S206 (= S114) binding K(+)
- S207 (≠ T115) binding thiamine diphosphate
- P208 (≠ I116) binding K(+)
- T211 (≠ G119) binding K(+); to M: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123503
- Q212 (≠ E120) binding K(+)
- E238 (≠ D146) binding Mg(2+)
- G239 (= G147) binding thiamine diphosphate
- A240 (= A148) binding thiamine diphosphate
- G249 (≠ S157) 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 (= A161) to T: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs199599175
- A254 (= A162) to D: in MSUD1A; uncertain significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs373713279
- R265 (≠ E173) binding thiamine diphosphate; 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 (= N175) binding Mg(2+); 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; dbSNP:rs1568508047
- Y269 (≠ W177) binding Mg(2+)
- A285 (= A193) 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 (≠ N198) 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 (≠ T205) to H: in MSUD1A; uncertain significance; decreased affinity for the cofactor thiamine diphosphate; decreased 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs200137189
- T310 (≠ A218) to R: in MSUD1A; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852875
- I326 (≠ L234) to T: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- H336 (= H244) binding thiamine diphosphate
- S337 (≠ F245) modified: Phosphoserine; by BCKDK; mutation to A: Substantially decreases the stability of the BCKD complex.
- S347 (≠ D254) mutation to A: Does not affect the stability of the BCKD complex.
- F409 (≠ T315) 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 (= Y319) 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
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)
33% identity, 96% coverage: 13:319/320 of query aligns to 84:391/420 of P16387
- S313 (≠ F245) modified: Phosphoserine; by PDK1 and PDK2
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
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, 96% coverage: 13:319/320 of query aligns to 101:409/441 of P11960
- S333 (≠ F245) modified: Phosphoserine; by BCKDK
2bffA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
30% identity, 98% coverage: 5:319/320 of query aligns to 47:360/392 of 2bffA
- active site: E71 (≠ A29), S157 (≠ T115), R282 (= R240), H286 (= H244), S287 (≠ F245), Y295 (≠ T255)
- binding manganese (ii) ion: E188 (≠ D146), N217 (= N175), Y219 (≠ W177)
- 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 (≠ N65), Y108 (≠ H66), R109 (= R67), L159 (≠ V117), G187 (= G145), E188 (≠ D146), G189 (= G147), A190 (= A148), R215 (≠ E173), N217 (= N175), Y219 (≠ W177), A220 (≠ Q178), I221 (≠ A179), H286 (= H244)
2bewA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
30% identity, 98% coverage: 5:319/320 of query aligns to 47:358/390 of 2bewA
- active site: E71 (≠ A29), S157 (≠ T115), R282 (= R240), H286 (= H244), S287 (≠ F245), Y295 (= Y252)
- binding manganese (ii) ion: E188 (≠ D146), N217 (= N175), Y219 (≠ W177), A220 (≠ Q178)
- binding c2-1-hydroxyphenyl-thiamin diphosphate: M82 (≠ C40), Q107 (≠ N65), Y108 (≠ H66), R109 (= R67), L159 (≠ V117), G187 (= G145), E188 (≠ D146), G189 (= G147), A190 (= A148), R215 (≠ E173), N217 (= N175), Y219 (≠ W177), A220 (≠ Q178), I221 (≠ A179), H286 (= H244)
2bevA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
30% identity, 98% coverage: 5:319/320 of query aligns to 47:358/390 of 2bevA
- active site: E71 (≠ A29), S157 (≠ T115), R282 (= R240), H286 (= H244), S287 (≠ F245), Y295 (= Y252)
- binding manganese (ii) ion: E188 (≠ D146), N217 (= N175), Y219 (≠ W177), A220 (≠ Q178)
- binding c2-1-hydroxy-2-methyl-butyl-thiamin diphosphate: F80 (≠ G38), Q107 (≠ N65), Y108 (≠ H66), R109 (= R67), S157 (≠ T115), L159 (≠ V117), G187 (= G145), E188 (≠ D146), G189 (= G147), A190 (= A148), R215 (≠ E173), N217 (= N175), Y219 (≠ W177), A220 (≠ Q178), I221 (≠ A179), H286 (= H244)
2beuA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
30% identity, 98% coverage: 5:319/320 of query aligns to 47:358/390 of 2beuA
- active site: E71 (≠ A29), S157 (≠ T115), R282 (= R240), H286 (= H244), S287 (≠ F245), Y295 (= Y252)
- binding manganese (ii) ion: E188 (≠ D146), N217 (= N175), Y219 (≠ W177), A220 (≠ Q178)
- binding c2-1-hydroxy-3-methyl-propyl-thiamin diphosphate: Q107 (≠ N65), Y108 (≠ H66), R109 (= R67), S157 (≠ T115), L159 (≠ V117), G187 (= G145), E188 (≠ D146), G189 (= G147), A190 (= A148), R215 (≠ E173), N217 (= N175), Y219 (≠ W177), A220 (≠ Q178), I221 (≠ A179), H286 (= H244)
1wciA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
30% identity, 98% coverage: 5:319/320 of query aligns to 47:356/388 of 1wciA
- active site: E71 (≠ A29), S157 (≠ T115), R282 (= R240), H286 (= H244), S287 (≠ F245), Y295 (≠ A259)
- binding manganese (ii) ion: E188 (≠ D146), N217 (= N175), Y219 (≠ W177), A220 (≠ Q178)
- binding c2-1-hydroxy-3-methyl-butyl-thiamin: Q107 (≠ N65), Y108 (≠ H66), R109 (= R67), L159 (≠ V117), G187 (= G145), E188 (≠ D146), G189 (= G147), A190 (= A148), R215 (≠ E173), N217 (= N175), Y219 (≠ W177), A220 (≠ Q178), I221 (≠ A179), H286 (= H244)
1dtwA Human branched-chain alpha-keto acid dehydrogenase (see paper)
30% identity, 98% coverage: 5:319/320 of query aligns to 46:350/382 of 1dtwA
- active site: E70 (≠ A29), S156 (≠ T115), R281 (= R240), H285 (= H244), S286 (≠ F245), Y294 (≠ A263)
- binding potassium ion: S155 (= S114), S156 (≠ T115), P157 (≠ I116), T160 (≠ G119), Q161 (≠ E120)
- binding magnesium ion: E187 (≠ D146), N216 (= N175), Y218 (≠ W177)
- binding thiamine diphosphate: Q106 (≠ N65), Y107 (≠ H66), R108 (= R67), L158 (≠ V117), G186 (= G145), E187 (≠ D146), G188 (= G147), A189 (= A148), R214 (≠ E173), N216 (= N175), Y218 (≠ W177), A219 (≠ Q178), I220 (≠ A179), H285 (= H244)
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)
30% identity, 90% coverage: 8:296/320 of query aligns to 36:326/367 of Q5SLR4
- F66 (≠ G38) binding substrate
- YYR 94:96 (≠ NHR 65:67) binding thiamine diphosphate
- Y95 (≠ H66) binding substrate
- MPEH 128:131 (≠ GSLH 99:102) binding substrate
- S144 (≠ T115) binding substrate
- SPI 144:146 (≠ TIV 115:117) binding thiamine diphosphate
- 174:180 (vs. 145:151, 71% identical) binding thiamine diphosphate
- D175 (= D146) binding Mg(2+)
- N204 (= N175) binding Mg(2+)
- NFYAI 204:208 (≠ NEWQA 175:179) binding thiamine diphosphate
- Y206 (≠ W177) binding Mg(2+)
- H273 (= H244) binding thiamine diphosphate
3exeA Crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex (see paper)
33% identity, 95% coverage: 17:320/320 of query aligns to 41:343/363 of 3exeA
- active site: Q53 (≠ A29), G138 (≠ T115), R261 (= R240), H265 (= H244), S266 (≠ F245), Y274 (= Y252)
- binding manganese (ii) ion: D169 (= D146), N198 (= N175), Y200 (≠ W177)
- binding thiamine diphosphate: Y91 (≠ H66), R92 (= R67), V140 (= V117), G168 (= G145), D169 (= D146), G170 (= G147), A171 (= A148), N198 (= N175), Y200 (≠ W177), G201 (≠ A179), H265 (= H244)
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)
33% identity, 95% coverage: 17:320/320 of query aligns to 68:370/390 of P08559
- A136 (= A84) to T: found in a patient with moderate developmental delay, mild dysmorphism and mildly elevated serum lactate; uncertain significance; dbSNP:rs138727886
- S232 (≠ R183) modified: Phosphoserine; by PDK1; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-293 and A-300.
- M282 (≠ L234) to L: in dbSNP:rs2229137
- S293 (≠ F245) 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 (≠ A251) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-232 and A-293.
- R302 (≠ V253) 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)
33% identity, 95% coverage: 17:320/320 of query aligns to 40:342/362 of 6cfoA
- active site: Q52 (≠ A29), G137 (≠ T115), R260 (= R240), H264 (= H244), S265 (≠ F245), Y273 (= Y252)
- 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 (≠ T39), Y90 (≠ H66), R91 (= R67), G137 (≠ T115), V139 (= V117), G167 (= G145), D168 (= D146), G169 (= G147), N197 (= N175), Y199 (≠ W177), G200 (≠ A179), H264 (= H244)
- binding magnesium ion: D168 (= D146), N197 (= N175), Y199 (≠ W177)
1ni4A Human pyruvate dehydrogenase (see paper)
33% identity, 95% coverage: 17:320/320 of query aligns to 40:342/362 of 1ni4A
- active site: Q52 (≠ A29), G137 (≠ T115), R260 (= R240), H264 (= H244), S265 (≠ F245), Y273 (= Y252)
- binding magnesium ion: D168 (= D146), N197 (= N175), Y199 (≠ W177)
- binding thiamine diphosphate: Y90 (≠ H66), R91 (= R67), V139 (= V117), G167 (= G145), D168 (= D146), G169 (= G147), A170 (= A148), N197 (= N175), G200 (≠ A179), H264 (= H244)
Query Sequence
>WP_011765272.1 NCBI__GCF_000061505.1:WP_011765272.1
MGIRLYDERPEALLEAMLLIRAYEEKAAALQAESGTPGTCTAVGQEAAAVGVVAALGADE
LILTNHRSAGHLLARGADPGRLLAEVMGRRGGYCKGKSGSLHVSARELGVVLTSTIVGGE
LALATGVALAQKQLRRPGAVVCFFGDGAACEGRFHESLNLAALWGLPVLYVCENNEWQAF
VHRRETMLAEGIAGWAGNYGIDHATVDGNDVEQVRAVAAAALESVRGRGRPFLLEARTYR
LRGHFEPDDQAYVDTDELAAWRARDPLPRMEARLLASGRCDAGAITAMKAAVAAQVAAAH
AFAIDSPYPALEELTTDVYA
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