SitesBLAST
Comparing WP_058931512.1 NCBI__GCF_001484605.1:WP_058931512.1 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)
3dufA Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
36% identity, 70% coverage: 68:351/405 of query aligns to 36:320/365 of 3dufA
- active site: S62 (≠ A94), I139 (vs. gap), R264 (= R296), H268 (= H300), T269 (= T301), Y278 (= Y309)
- binding magnesium ion: D170 (= D202), N199 (= N231), F201 (≠ Y233)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1r)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: Y99 (= Y131), R100 (= R132), I141 (≠ L173), G169 (= G201), D170 (= D202), G171 (= G203), N199 (= N231), F201 (≠ Y233), A202 (= A234), H268 (= H300)
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)
35% identity, 88% coverage: 37:394/405 of query aligns to 1:367/367 of Q5SLR4
- F66 (≠ V103) binding substrate
- YYR 94:96 (≠ TYR 130:132) binding thiamine diphosphate
- Y95 (= Y131) binding substrate
- MPEH 128:131 (≠ PARH 161:164) binding substrate
- S144 (≠ T171) binding substrate
- SPI 144:146 (≠ TPL 171:173) binding thiamine diphosphate
- 174:180 (vs. 201:207, 100% identical) binding thiamine diphosphate
- D175 (= D202) binding Mg(2+)
- N204 (= N231) binding Mg(2+)
- NFYAI 204:208 (≠ NKYAI 231:235) binding thiamine diphosphate
- Y206 (= Y233) binding Mg(2+)
- H273 (= H300) binding thiamine diphosphate
1umdA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methyl-2-oxopentanoate as an intermediate (see paper)
35% identity, 87% coverage: 42:394/405 of query aligns to 1:362/362 of 1umdA
- active site: I52 (≠ A94), S139 (≠ T171), R264 (= R296), H268 (= H300), S269 (≠ T301), Y277 (= Y309)
- binding 2-oxo-4-methylpentanoic acid: F61 (≠ V103), Y90 (= Y131), S139 (≠ T171)
- binding magnesium ion: D170 (= D202), N199 (= N231), Y201 (= Y233)
- binding thiamine diphosphate: Y89 (≠ T130), Y90 (= Y131), R91 (= R132), P140 (= P172), I141 (≠ L173), G169 (= G201), D170 (= D202), G171 (= G203), N199 (= N231), Y201 (= Y233), A202 (= A234), I203 (= I235), H268 (= H300)
1umcA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methylpentanoate (see paper)
35% identity, 87% coverage: 42:394/405 of query aligns to 1:362/362 of 1umcA
- active site: I52 (≠ A94), S139 (≠ T171), R264 (= R296), H268 (= H300), S269 (≠ T301), Y277 (= Y309)
- binding 4-methyl valeric acid: Y90 (= Y131), H126 (= H164)
- binding magnesium ion: D170 (= D202), N199 (= N231), Y201 (= Y233)
- binding thiamine diphosphate: Y89 (≠ T130), Y90 (= Y131), R91 (= R132), I141 (≠ L173), G169 (= G201), D170 (= D202), G171 (= G203), N199 (= N231), Y201 (= Y233), I203 (= I235), H268 (= H300)
1umbA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 in holo-form (see paper)
35% identity, 87% coverage: 42:394/405 of query aligns to 1:362/362 of 1umbA
- active site: I52 (≠ A94), S139 (≠ T171), R264 (= R296), H268 (= H300), S269 (≠ T301), Y277 (= Y309)
- binding magnesium ion: D170 (= D202), N199 (= N231), Y201 (= Y233)
- binding thiamine diphosphate: Y89 (≠ T130), Y90 (= Y131), R91 (= R132), P140 (= P172), I141 (≠ L173), G169 (= G201), D170 (= D202), G171 (= G203), N199 (= N231), Y201 (= Y233), A202 (= A234), I203 (= I235), H268 (= H300)
1w85A The crystal structure of pyruvate dehydrogenase e1 bound to the peripheral subunit binding domain of e2 (see paper)
34% identity, 70% coverage: 68:351/405 of query aligns to 36:314/358 of 1w85A
- active site: S62 (≠ A94), I139 (vs. gap), R264 (= R296), H268 (= H300), T269 (= T301)
- binding magnesium ion: D170 (= D202), N199 (= N231), F201 (≠ Y233)
- binding thiamine diphosphate: Y99 (= Y131), R100 (= R132), I139 (vs. gap), I141 (≠ L173), G169 (= G201), D170 (= D202), G171 (= G203), G172 (≠ A204), N199 (= N231), A202 (= A234), I203 (= I235), H268 (= H300)
3dv0A Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
34% identity, 70% coverage: 68:351/405 of query aligns to 36:305/349 of 3dv0A
- active site: S62 (≠ A94), I139 (vs. gap), R264 (= R296), H268 (= H300)
- binding magnesium ion: D170 (= D202), N199 (= N231), F201 (≠ Y233)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: Y99 (= Y131), R100 (= R132), I141 (≠ L173), G169 (= G201), D170 (= D202), G171 (= G203), N199 (= N231), F201 (≠ Y233), A202 (= A234), I203 (= I235), R264 (= R296)
3dv0E Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
33% identity, 70% coverage: 68:351/405 of query aligns to 36:300/344 of 3dv0E
- active site: S62 (≠ A94), I139 (vs. gap), R264 (= R296)
- binding magnesium ion: G169 (= G201), D170 (= D202), Q197 (= Q229), N199 (= N231)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: Y99 (= Y131), R100 (= R132), I139 (vs. gap), I141 (≠ L173), G169 (= G201), D170 (= D202), G171 (= G203), N199 (= N231), F201 (≠ Y233), A202 (= A234), I203 (= I235)
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: 7:394/405 of query aligns to 32:427/441 of P11960
- S333 (≠ T301) modified: Phosphoserine; by BCKDK
1w88A The crystal structure of pyruvate dehydrogenase e1(d180n,e183q) bound to the peripheral subunit binding domain of e2 (see paper)
32% identity, 70% coverage: 68:351/405 of query aligns to 35:296/340 of 1w88A
- active site: S61 (≠ A94), I138 (vs. gap), R263 (= R296)
- binding magnesium ion: D169 (= D202), N198 (= N231), F200 (≠ Y233)
- binding thiamine diphosphate: Y98 (= Y131), R99 (= R132), I140 (≠ L173), G168 (= G201), D169 (= D202), G170 (= G203), A201 (= A234), I202 (= I235)
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)
33% identity, 86% coverage: 45:394/405 of query aligns to 80:431/445 of P12694
- Y158 (= Y131) binding thiamine diphosphate
- R159 (= R132) binding thiamine diphosphate; to W: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs769688327
- Q190 (vs. gap) to K: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- S206 (≠ C170) binding K(+)
- S207 (≠ T171) binding thiamine diphosphate
- P208 (= P172) binding K(+)
- T211 (= T175) binding K(+); to M: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123503
- Q212 (= Q176) binding K(+)
- E238 (≠ D202) binding Mg(2+)
- G239 (= G203) binding thiamine diphosphate
- A240 (= A204) binding thiamine diphosphate
- G249 (≠ A213) 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 (= A217) to T: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs199599175
- A254 (= A218) to D: in MSUD1A; uncertain significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs373713279
- R265 (≠ Q229) 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 (= N231) 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 (= Y233) binding Mg(2+)
- A285 (= A249) 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 (= G254) 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 (= R261) to H: in MSUD1A; uncertain significance; decreased affinity for the cofactor thiamine diphosphate; decreased 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs200137189
- T310 (≠ L274) to R: in MSUD1A; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852875
- I326 (≠ V290) to T: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- H336 (= H300) binding thiamine diphosphate
- S337 (≠ T301) modified: Phosphoserine; by BCKDK; mutation to A: Substantially decreases the stability of the BCKD complex.
- S347 (≠ Q311) mutation to A: Does not affect the stability of the BCKD complex.
- F409 (= F372) 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 (≠ F376) 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
2bffA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
33% identity, 86% coverage: 45:394/405 of query aligns to 30:378/392 of 2bffA
- active site: E71 (≠ A94), S157 (≠ T171), R282 (= R296), H286 (= H300), S287 (≠ T301), Y295 (= Y309)
- binding manganese (ii) ion: E188 (≠ D202), N217 (= N231), Y219 (= Y233)
- 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 (≠ T130), Y108 (= Y131), R109 (= R132), L159 (= L173), G187 (= G201), E188 (≠ D202), G189 (= G203), A190 (= A204), R215 (≠ Q229), N217 (= N231), Y219 (= Y233), A220 (= A234), I221 (= I235), H286 (= H300)
1wciA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
33% identity, 86% coverage: 45:394/405 of query aligns to 30:374/388 of 1wciA
- active site: E71 (vs. gap), S157 (≠ T171), R282 (= R296), H286 (= H300), S287 (≠ T301), Y295 (= Y309)
- binding manganese (ii) ion: E188 (≠ D202), N217 (= N231), Y219 (= Y233), A220 (= A234)
- binding c2-1-hydroxy-3-methyl-butyl-thiamin: Q107 (≠ T130), Y108 (= Y131), R109 (= R132), L159 (= L173), G187 (= G201), E188 (≠ D202), G189 (= G203), A190 (= A204), R215 (≠ Q229), N217 (= N231), Y219 (= Y233), A220 (= A234), I221 (= I235), H286 (= H300)
2bewA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
33% identity, 86% coverage: 45:394/405 of query aligns to 30:376/390 of 2bewA
- active site: E71 (vs. gap), S157 (≠ T171), R282 (= R296), H286 (= H300), S287 (≠ T301), Y295 (= Y309)
- binding manganese (ii) ion: E188 (≠ D202), N217 (= N231), Y219 (= Y233), A220 (= A234)
- binding c2-1-hydroxyphenyl-thiamin diphosphate: M82 (≠ P105), Q107 (≠ T130), Y108 (= Y131), R109 (= R132), L159 (= L173), G187 (= G201), E188 (≠ D202), G189 (= G203), A190 (= A204), R215 (≠ Q229), N217 (= N231), Y219 (= Y233), A220 (= A234), I221 (= I235), H286 (= H300)
2bevA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
33% identity, 86% coverage: 45:394/405 of query aligns to 30:376/390 of 2bevA
- active site: E71 (vs. gap), S157 (≠ T171), R282 (= R296), H286 (= H300), S287 (≠ T301), Y295 (= Y309)
- binding manganese (ii) ion: E188 (≠ D202), N217 (= N231), Y219 (= Y233), A220 (= A234)
- binding c2-1-hydroxy-2-methyl-butyl-thiamin diphosphate: F80 (≠ V103), Q107 (≠ T130), Y108 (= Y131), R109 (= R132), S157 (≠ T171), L159 (= L173), G187 (= G201), E188 (≠ D202), G189 (= G203), A190 (= A204), R215 (≠ Q229), N217 (= N231), Y219 (= Y233), A220 (= A234), I221 (= I235), H286 (= H300)
2beuA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
33% identity, 86% coverage: 45:394/405 of query aligns to 30:376/390 of 2beuA
- active site: E71 (vs. gap), S157 (≠ T171), R282 (= R296), H286 (= H300), S287 (≠ T301), Y295 (= Y309)
- binding manganese (ii) ion: E188 (≠ D202), N217 (= N231), Y219 (= Y233), A220 (= A234)
- binding c2-1-hydroxy-3-methyl-propyl-thiamin diphosphate: Q107 (≠ T130), Y108 (= Y131), R109 (= R132), S157 (≠ T171), L159 (= L173), G187 (= G201), E188 (≠ D202), G189 (= G203), A190 (= A204), R215 (≠ Q229), N217 (= N231), Y219 (= Y233), A220 (= A234), I221 (= I235), H286 (= H300)
1dtwA Human branched-chain alpha-keto acid dehydrogenase (see paper)
32% identity, 86% coverage: 45:394/405 of query aligns to 29:368/382 of 1dtwA
- active site: E70 (vs. gap), S156 (≠ T171), R281 (= R296), H285 (= H300), S286 (≠ T301), Y294 (= Y309)
- binding potassium ion: S155 (≠ C170), S156 (≠ T171), P157 (= P172), T160 (= T175), Q161 (= Q176)
- binding magnesium ion: E187 (≠ D202), N216 (= N231), Y218 (= Y233)
- binding thiamine diphosphate: Q106 (≠ T130), Y107 (= Y131), R108 (= R132), L158 (= L173), G186 (= G201), E187 (≠ D202), G188 (= G203), A189 (= A204), R214 (≠ Q229), N216 (= N231), Y218 (= Y233), A219 (= A234), I220 (= I235), H285 (= H300)
1qs0A Crystal structure of pseudomonas putida 2-oxoisovalerate dehydrogenase (branched-chain alpha-keto acid dehydrogenase, e1b) (see paper)
36% identity, 65% coverage: 72:335/405 of query aligns to 72:346/407 of 1qs0A
- active site: V95 (≠ L95), G181 (vs. gap), R307 (= R296), H311 (= H300), S312 (≠ T301), Y320 (= Y309)
- binding magnesium ion: D212 (= D202), N241 (= N231), W243 (≠ Y233)
- binding thiamine diphosphate: Y132 (= Y131), R133 (= R132), L183 (= L173), G211 (= G201), D212 (= D202), G213 (= G203), A214 (= A204), N241 (= N231), W243 (≠ Y233), A244 (= A234), I245 (= I235), H311 (= H300)
1v1mA Crosstalk between cofactor binding and the phosphorylation loop conformation in the bckd machine (see paper)
31% identity, 86% coverage: 45:394/405 of query aligns to 30:358/372 of 1v1mA
- active site: E71 (vs. gap), S157 (≠ T171), R282 (= R296)
- binding manganese (ii) ion: E188 (≠ D202), N217 (= N231), Y219 (= Y233)
- binding thiamine diphosphate: R109 (= R132), L159 (= L173), G187 (= G201), E188 (≠ D202), G189 (= G203), A190 (= A204), R215 (≠ Q229), N217 (= N231), Y219 (= Y233), A220 (= A234), I221 (= I235)
2bfcA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
31% identity, 86% coverage: 45:394/405 of query aligns to 30:357/371 of 2bfcA
- active site: E71 (vs. gap), S157 (≠ T171), R282 (= R296)
- binding manganese (ii) ion: E188 (≠ D202), N217 (= N231), Y219 (= Y233)
- binding 2-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-2-oxo-2,3-dihydro-1,3-thiazol-5-yl}ethyl trihydrogendiphosphate: R109 (= R132), L159 (= L173), G187 (= G201), E188 (≠ D202), G189 (= G203), A190 (= A204), R215 (≠ Q229), N217 (= N231), Y219 (= Y233), A220 (= A234), I221 (= I235)
Query Sequence
>WP_058931512.1 NCBI__GCF_001484605.1:WP_058931512.1
MTISADHTAPDQAQRLPAEDAASEAVRKFGITVEDYMLPARHQIQMVDQDGQLKAEGEQG
TEPGHEYPLPADEELLAAYEQLVVGRRVNDQNSALVRQGRMAVYPSSHGQEACQVAAALC
LSDGDWLFPTYRDAVAVMARGVDPVETMTIFRGDWHSGYDPARHKVGIQCTPLTTQLLHG
VGVAHAAKLRGEDTVVLAMCGDGATSEGDFHEALNFAAVFHLPVVFFVQNNKYAISVPLA
HQSVAPSLAHKAVGYGMAGERVDGNDVVALLAVLDRAVKLAREGSGPLLVEAHTYRMQAH
TNADDATRYRQDSEVAEWLAKDPISRMKTYLTGRGLLDDDGAARIAAHAEDVATQLREGL
GEDVPVDPQELFRHVFSVPTPQLKEQSAMLADELAREASSEESPK
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