SitesBLAST
Comparing WP_042451488.1 NCBI__GCF_002893965.1:WP_042451488.1 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)
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)
37% identity, 99% coverage: 1:304/307 of query aligns to 64:365/396 of P26267
- S289 (≠ F230) modified: Phosphoserine
- S296 (≠ L236) modified: Phosphoserine
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)
35% identity, 100% coverage: 1:306/307 of query aligns to 66:369/388 of P29803
- M227 (≠ E164) to V: in SPGF70; uncertain significance; dbSNP:rs200969445
- S230 (≠ G167) mutation to A: Slightly reduces enzyme activity.
- S291 (≠ F230) 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 (≠ G232) 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.
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: 1:305/307 of query aligns to 70:373/393 of Q8H1Y0
- R121 (= R52) mutation to C: In iar4-1; reduced sensitivity to several IAA-amino acid conjugates.
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, 100% coverage: 1:306/307 of query aligns to 68:371/390 of P35486
- S232 (≠ G167) modified: Phosphoserine; by PDK1
- S293 (≠ F230) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- S300 (vs. gap) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- K336 (≠ D271) modified: N6-acetyllysine; mutation K->Q,R: Decreases phosphorylation at S-232 and S-300 but does not affect activity or substrate metabolism.
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, 93% coverage: 20:306/307 of query aligns to 107:393/420 of P16387
- S313 (≠ F230) modified: Phosphoserine; by PDK1 and PDK2
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
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, 100% coverage: 1:306/307 of query aligns to 68:371/390 of P26284
- S232 (≠ G167) modified: Phosphoserine; by PDK1
- S293 (≠ F230) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
- S300 (vs. gap) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
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, 100% coverage: 1:306/307 of query aligns to 85:390/409 of Q10489
- Y306 (≠ W226) modified: Phosphotyrosine
- S310 (≠ F230) modified: Phosphoserine
- S312 (≠ G232) modified: Phosphoserine
Sites not aligning to the query:
- 6 modified: Phosphothreonine
3exeA Crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex (see paper)
33% identity, 100% coverage: 1:306/307 of query aligns to 41:344/363 of 3exeA
- active site: Q53 (≠ R10), G138 (≠ A100), R261 (= R225), H265 (= H229), S266 (≠ F230), Y274 (= Y237)
- binding manganese (ii) ion: D169 (= D131), N198 (= N160), Y200 (≠ F162)
- binding thiamine diphosphate: Y91 (≠ H51), R92 (= R52), V140 (= V102), G168 (= G130), D169 (= D131), G170 (= G132), A171 (≠ G133), N198 (= N160), Y200 (≠ F162), G201 (= G163), H265 (= H229)
6cfoA Human pyruvate dehydrogenase e1 component complex with covalent tdp adduct acetyl phosphinate (see paper)
33% identity, 100% coverage: 1:306/307 of query aligns to 40:343/362 of 6cfoA
- active site: Q52 (≠ R10), G137 (≠ A100), R260 (= R225), H264 (= H229), S265 (≠ F230), Y273 (= Y237)
- 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 (= F23), Y90 (≠ H51), R91 (= R52), G137 (≠ A100), V139 (= V102), G167 (= G130), D168 (= D131), G169 (= G132), N197 (= N160), Y199 (≠ F162), G200 (= G163), H264 (= H229)
- binding magnesium ion: D168 (= D131), N197 (= N160), Y199 (≠ F162)
1ni4A Human pyruvate dehydrogenase (see paper)
33% identity, 100% coverage: 1:306/307 of query aligns to 40:343/362 of 1ni4A
- active site: Q52 (≠ R10), G137 (≠ A100), R260 (= R225), H264 (= H229), S265 (≠ F230), Y273 (= Y237)
- binding magnesium ion: D168 (= D131), N197 (= N160), Y199 (≠ F162)
- binding thiamine diphosphate: Y90 (≠ H51), R91 (= R52), V139 (= V102), G167 (= G130), D168 (= D131), G169 (= G132), A170 (≠ G133), N197 (= N160), G200 (= G163), H264 (= H229)
P08559 Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial; PDHE1-A type I; EC 1.2.4.1 from Homo sapiens (Human) (see 16 papers)
33% identity, 100% coverage: 1:306/307 of query aligns to 68:371/390 of P08559
- Y118 (≠ H51) binding thiamine diphosphate
- R119 (= R52) binding thiamine diphosphate
- A136 (= A69) to T: found in a patient with moderate developmental delay, mild dysmorphism and mildly elevated serum lactate; uncertain significance; dbSNP:rs138727886
- G165 (≠ A100) binding thiamine diphosphate
- V167 (= V102) binding thiamine diphosphate; to M: in PDHAD; disrupts magnesium binding and results in deficient activity of the pyruvate dehydrogenase complex; dbSNP:rs2063174067
- D196 (= D131) binding Mg(2+); binding thiamine diphosphate
- G197 (= G132) binding thiamine diphosphate
- A198 (≠ G133) binding thiamine diphosphate
- N225 (= N160) binding Mg(2+); binding thiamine diphosphate
- Y227 (≠ F162) binding Mg(2+)
- S232 (≠ G167) modified: Phosphoserine; by PDK1; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-293 and A-300.
- M282 (≠ I219) to L: in dbSNP:rs2229137
- H292 (= H229) binding thiamine diphosphate
- S293 (≠ F230) 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 (= R238) 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
6cerA Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
32% identity, 100% coverage: 1:306/307 of query aligns to 41:323/342 of 6cerA
6cerE Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
31% identity, 100% coverage: 1:306/307 of query aligns to 40:321/340 of 6cerE
1umdA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methyl-2-oxopentanoate as an intermediate (see paper)
29% identity, 92% coverage: 23:304/307 of query aligns to 61:344/362 of 1umdA
- active site: S139 (≠ A100), R264 (= R225), H268 (= H229), S269 (≠ F230), Y277 (= Y237)
- binding 2-oxo-4-methylpentanoic acid: F61 (= F23), Y90 (≠ H51), S139 (≠ A100)
- binding magnesium ion: D170 (= D131), N199 (= N160), Y201 (≠ F162)
- binding thiamine diphosphate: Y89 (≠ T50), Y90 (≠ H51), R91 (= R52), P140 (≠ I101), I141 (≠ V102), G169 (= G130), D170 (= D131), G171 (= G132), N199 (= N160), Y201 (≠ F162), A202 (≠ G163), I203 (≠ E164), H268 (= H229)
Sites not aligning to the query:
1umcA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methylpentanoate (see paper)
29% identity, 92% coverage: 23:304/307 of query aligns to 61:344/362 of 1umcA
- active site: S139 (≠ A100), R264 (= R225), H268 (= H229), S269 (≠ F230), Y277 (= Y237)
- binding 4-methyl valeric acid: Y90 (≠ H51), H126 (= H87)
- binding magnesium ion: D170 (= D131), N199 (= N160), Y201 (≠ F162)
- binding thiamine diphosphate: Y89 (≠ T50), Y90 (≠ H51), R91 (= R52), I141 (≠ V102), G169 (= G130), D170 (= D131), G171 (= G132), N199 (= N160), Y201 (≠ F162), I203 (≠ E164), H268 (= H229)
Sites not aligning to the query:
1umbA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 in holo-form (see paper)
29% identity, 92% coverage: 23:304/307 of query aligns to 61:344/362 of 1umbA
- active site: S139 (≠ A100), R264 (= R225), H268 (= H229), S269 (≠ F230), Y277 (= Y237)
- binding magnesium ion: D170 (= D131), N199 (= N160), Y201 (≠ F162)
- binding thiamine diphosphate: Y89 (≠ T50), Y90 (≠ H51), R91 (= R52), P140 (≠ I101), I141 (≠ V102), G169 (= G130), D170 (= D131), G171 (= G132), N199 (= N160), Y201 (≠ F162), A202 (≠ G163), I203 (≠ E164), H268 (= H229)
Sites not aligning to the query:
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)
29% identity, 92% coverage: 23:304/307 of query aligns to 66:349/367 of Q5SLR4
- F66 (= F23) binding substrate
- YYR 94:96 (≠ THR 50:52) binding thiamine diphosphate
- Y95 (≠ H51) binding substrate
- MPEH 128:131 (≠ GSMH 84:87) binding substrate
- S144 (≠ A100) binding substrate
- SPI 144:146 (≠ AIV 100:102) binding thiamine diphosphate
- 174:180 (vs. 130:136, 43% identical) binding thiamine diphosphate
- D175 (= D131) binding Mg(2+)
- N204 (= N160) binding Mg(2+)
- NFYAI 204:208 (≠ NGFGE 160:164) binding thiamine diphosphate
- Y206 (≠ F162) binding Mg(2+)
- H273 (= H229) binding thiamine diphosphate
3dufA Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
31% identity, 99% coverage: 1:304/307 of query aligns to 50:345/365 of 3dufA
- active site: S62 (≠ E13), I139 (≠ A100), R264 (= R225), H268 (= H229), T269 (vs. gap), Y278 (≠ R238)
- binding magnesium ion: D170 (= D131), N199 (= N160), F201 (= F162)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1r)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: Y99 (≠ H51), R100 (= R52), I141 (≠ V102), G169 (= G130), D170 (= D131), G171 (= G132), N199 (= N160), F201 (= F162), A202 (≠ G163), H268 (= H229)
3exhE Crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex (see paper)
31% identity, 100% coverage: 1:306/307 of query aligns to 40:312/331 of 3exhE
1w85A The crystal structure of pyruvate dehydrogenase e1 bound to the peripheral subunit binding domain of e2 (see paper)
31% identity, 99% coverage: 1:304/307 of query aligns to 50:339/358 of 1w85A
- active site: S62 (≠ E13), I139 (≠ A100), R264 (= R225), H268 (= H229), T269 (vs. gap)
- binding magnesium ion: D170 (= D131), N199 (= N160), F201 (= F162)
- binding thiamine diphosphate: Y99 (≠ H51), R100 (= R52), I139 (≠ A100), I141 (≠ V102), G169 (= G130), D170 (= D131), G171 (= G132), G172 (= G133), N199 (= N160), A202 (≠ G163), I203 (≠ E164), H268 (= H229)
Query Sequence
>WP_042451488.1 NCBI__GCF_002893965.1:WP_042451488.1
MSRIRAFEDRLHEENATGDIPGFIHLYSGQEAIAVGVCENLSDADYIGSTHRGHGHCIAK
GCDLNGMMAEIFGKDDGLCRGKGGSMHIADLSVGMLGANAIVGGAPSLAIGAALSGKTLR
NGVIAASFTGDGGSNQGTVFEAMNMAVVLDLPIVFVIENNGFGEATGTDYAVGAPDIAAR
AASFGMPAVKVDGTDFFAVYDAMAEASERARIGGGPTTIEAAAFRWHGHFEGDAQLYRTA
EQVAQLRETKDPLKNFRSSVDVKKVSTADLDAVDEQSRVLVDEAVAKARAAAYPPVENLL
TDVYVSY
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