SitesBLAST
Comparing N515DRAFT_0356 FitnessBrowser__Dyella79:N515DRAFT_0356 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)
37% identity, 88% coverage: 34:352/361 of query aligns to 41:358/365 of 3dufA
- active site: S62 (≠ A55), I139 (≠ V134), R264 (= R259), H268 (= H263), T269 (= T264), Y278 (= Y272)
- binding magnesium ion: D170 (= D165), N199 (= N194), F201 (≠ W196)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1r)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: Y99 (= Y92), R100 (= R93), I141 (= I136), G169 (= G164), D170 (= D165), G171 (= G166), N199 (= N194), F201 (≠ W196), A202 (= A197), H268 (= H263)
1w85A The crystal structure of pyruvate dehydrogenase e1 bound to the peripheral subunit binding domain of e2 (see paper)
36% identity, 88% coverage: 34:352/361 of query aligns to 41:352/358 of 1w85A
- active site: S62 (≠ A55), I139 (≠ V134), R264 (= R259), H268 (= H263), T269 (= T264)
- binding magnesium ion: D170 (= D165), N199 (= N194), F201 (≠ W196)
- binding thiamine diphosphate: Y99 (= Y92), R100 (= R93), I139 (≠ V134), I141 (= I136), G169 (= G164), D170 (= D165), G171 (= G166), G172 (= G167), N199 (= N194), A202 (= A197), I203 (= I198), H268 (= H263)
3dv0A Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
35% identity, 88% coverage: 34:352/361 of query aligns to 41:343/349 of 3dv0A
- active site: S62 (≠ A55), I139 (≠ V134), R264 (= R259), H268 (= H263)
- binding magnesium ion: D170 (= D165), N199 (= N194), F201 (≠ W196)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: Y99 (= Y92), R100 (= R93), I141 (= I136), G169 (= G164), D170 (= D165), G171 (= G166), N199 (= N194), F201 (≠ W196), A202 (= A197), I203 (= I198), R264 (= R259)
3dv0E Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
34% identity, 88% coverage: 34:352/361 of query aligns to 41:338/344 of 3dv0E
- active site: S62 (≠ A55), I139 (≠ V134), R264 (= R259)
- binding magnesium ion: G169 (= G164), D170 (= D165), Q197 (≠ V192), N199 (= N194)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: Y99 (= Y92), R100 (= R93), I139 (≠ V134), I141 (= I136), G169 (= G164), D170 (= D165), G171 (= G166), N199 (= N194), F201 (≠ W196), A202 (= A197), I203 (= I198)
1w88A The crystal structure of pyruvate dehydrogenase e1(d180n,e183q) bound to the peripheral subunit binding domain of e2 (see paper)
34% identity, 88% coverage: 34:352/361 of query aligns to 40:334/340 of 1w88A
- active site: S61 (≠ A55), I138 (≠ V134), R263 (= R259)
- binding magnesium ion: D169 (= D165), N198 (= N194), F200 (≠ W196)
- binding thiamine diphosphate: Y98 (= Y92), R99 (= R93), I140 (= I136), G168 (= G164), D169 (= D165), G170 (= G166), A201 (= A197), I202 (= I198)
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, 96% coverage: 7:352/361 of query aligns to 11:362/367 of Q5SLR4
1umdA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methyl-2-oxopentanoate as an intermediate (see paper)
35% identity, 96% coverage: 7:352/361 of query aligns to 6:357/362 of 1umdA
- active site: I52 (≠ A55), S139 (≠ V134), R264 (= R259), H268 (= H263), S269 (≠ T264), Y277 (= Y272)
- binding 2-oxo-4-methylpentanoic acid: F61 (≠ T64), Y90 (= Y92), S139 (≠ V134)
- binding magnesium ion: D170 (= D165), N199 (= N194), Y201 (≠ W196)
- binding thiamine diphosphate: Y89 (≠ S91), Y90 (= Y92), R91 (= R93), P140 (= P135), I141 (= I136), G169 (= G164), D170 (= D165), G171 (= G166), N199 (= N194), Y201 (≠ W196), A202 (= A197), I203 (= I198), H268 (= H263)
1umcA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methylpentanoate (see paper)
35% identity, 96% coverage: 7:352/361 of query aligns to 6:357/362 of 1umcA
- active site: I52 (≠ A55), S139 (≠ V134), R264 (= R259), H268 (= H263), S269 (≠ T264), Y277 (= Y272)
- binding 4-methyl valeric acid: Y90 (= Y92), H126 (≠ E124)
- binding magnesium ion: D170 (= D165), N199 (= N194), Y201 (≠ W196)
- binding thiamine diphosphate: Y89 (≠ S91), Y90 (= Y92), R91 (= R93), I141 (= I136), G169 (= G164), D170 (= D165), G171 (= G166), N199 (= N194), Y201 (≠ W196), I203 (= I198), H268 (= H263)
1umbA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 in holo-form (see paper)
35% identity, 96% coverage: 7:352/361 of query aligns to 6:357/362 of 1umbA
- active site: I52 (≠ A55), S139 (≠ V134), R264 (= R259), H268 (= H263), S269 (≠ T264), Y277 (= Y272)
- binding magnesium ion: D170 (= D165), N199 (= N194), Y201 (≠ W196)
- binding thiamine diphosphate: Y89 (≠ S91), Y90 (= Y92), R91 (= R93), P140 (= P135), I141 (= I136), G169 (= G164), D170 (= D165), G171 (= G166), N199 (= N194), Y201 (≠ W196), A202 (= A197), I203 (= I198), H268 (= H263)
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, 88% coverage: 34:351/361 of query aligns to 100:425/445 of P12694
- Y158 (= Y92) binding
- R159 (= R93) binding ; to W: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs769688327
- Q190 (= Q122) to K: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- S206 (= S133) binding
- S207 (≠ V134) binding
- P208 (= P135) binding
- T211 (= T138) binding ; to M: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123503
- Q212 (= Q139) binding
- E238 (≠ D165) binding
- G239 (= G166) binding
- A240 (≠ G167) binding
- G249 (≠ A176) 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 (≠ T180) to T: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs199599175
- A254 (≠ G181) to D: in MSUD1A; uncertain significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity
- R265 (≠ V192) 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 (= N194) 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 (≠ W196) binding
- A285 (= A212) 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 (≠ A217) 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 (≠ Q224) to H: in MSUD1A; uncertain significance; decreased affinity for the cofactor thiamine diphosphate; decreased 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs200137189
- T310 (≠ M237) to R: in MSUD1A; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852875
- I326 (≠ L253) to T: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- H336 (= H263) binding
- S337 (≠ T264) modified: Phosphoserine; by BCKDK; mutation to A: Substantially decreases the stability of the BCKD complex.
- S347 (≠ G274) mutation to A: Does not affect the stability of the BCKD complex.
- F409 (= F335) 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 (≠ F339) 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
1qs0A Crystal structure of pseudomonas putida 2-oxoisovalerate dehydrogenase (branched-chain alpha-keto acid dehydrogenase, e1b) (see paper)
31% identity, 96% coverage: 5:350/361 of query aligns to 47:404/407 of 1qs0A
- active site: V95 (≠ A55), G181 (≠ V134), R307 (= R259), H311 (= H263), S312 (≠ T264), Y320 (= Y272)
- binding magnesium ion: D212 (= D165), N241 (= N194), W243 (= W196)
- binding thiamine diphosphate: Y132 (= Y92), R133 (= R93), L183 (≠ I136), G211 (= G164), D212 (= D165), G213 (= G166), A214 (≠ G167), N241 (= N194), W243 (= W196), A244 (= A197), I245 (= I198), H311 (= H263)
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, 88% coverage: 34:351/361 of query aligns to 96:421/441 of P11960
- S333 (≠ T264) modified: Phosphoserine; by BCKDK
2bewA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
32% identity, 88% coverage: 34:351/361 of query aligns to 50:370/390 of 2bewA
- active site: E71 (≠ A55), S157 (≠ V134), R282 (= R259), H286 (= H263), S287 (≠ T264), Y295 (= Y272)
- binding manganese (ii) ion: E188 (≠ D165), N217 (= N194), Y219 (≠ W196), A220 (= A197)
- binding c2-1-hydroxyphenyl-thiamin diphosphate: M82 (≠ A66), Q107 (≠ S91), Y108 (= Y92), R109 (= R93), L159 (≠ I136), G187 (= G164), E188 (≠ D165), G189 (= G166), A190 (≠ G167), R215 (≠ V192), N217 (= N194), Y219 (≠ W196), A220 (= A197), I221 (= I198), H286 (= H263)
2bevA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
32% identity, 88% coverage: 34:351/361 of query aligns to 50:370/390 of 2bevA
- active site: E71 (≠ A55), S157 (≠ V134), R282 (= R259), H286 (= H263), S287 (≠ T264), Y295 (= Y272)
- binding manganese (ii) ion: E188 (≠ D165), N217 (= N194), Y219 (≠ W196), A220 (= A197)
- binding c2-1-hydroxy-2-methyl-butyl-thiamin diphosphate: F80 (≠ T64), Q107 (≠ S91), Y108 (= Y92), R109 (= R93), S157 (≠ V134), L159 (≠ I136), G187 (= G164), E188 (≠ D165), G189 (= G166), A190 (≠ G167), R215 (≠ V192), N217 (= N194), Y219 (≠ W196), A220 (= A197), I221 (= I198), H286 (= H263)
2beuA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
32% identity, 88% coverage: 34:351/361 of query aligns to 50:370/390 of 2beuA
- active site: E71 (≠ A55), S157 (≠ V134), R282 (= R259), H286 (= H263), S287 (≠ T264), Y295 (= Y272)
- binding manganese (ii) ion: E188 (≠ D165), N217 (= N194), Y219 (≠ W196), A220 (= A197)
- binding c2-1-hydroxy-3-methyl-propyl-thiamin diphosphate: Q107 (≠ S91), Y108 (= Y92), R109 (= R93), S157 (≠ V134), L159 (≠ I136), G187 (= G164), E188 (≠ D165), G189 (= G166), A190 (≠ G167), R215 (≠ V192), N217 (= N194), Y219 (≠ W196), A220 (= A197), I221 (= I198), H286 (= H263)
1wciA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
33% identity, 88% coverage: 34:351/361 of query aligns to 50:368/388 of 1wciA
- active site: E71 (≠ A55), S157 (≠ V134), R282 (= R259), H286 (= H263), S287 (≠ T264), Y295 (= Y272)
- binding manganese (ii) ion: E188 (≠ D165), N217 (= N194), Y219 (≠ W196), A220 (= A197)
- binding c2-1-hydroxy-3-methyl-butyl-thiamin: Q107 (≠ S91), Y108 (= Y92), R109 (= R93), L159 (≠ I136), G187 (= G164), E188 (≠ D165), G189 (= G166), A190 (≠ G167), R215 (≠ V192), N217 (= N194), Y219 (≠ W196), A220 (= A197), I221 (= I198), H286 (= H263)
2bffA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
33% identity, 88% coverage: 34:351/361 of query aligns to 50:372/392 of 2bffA
- active site: E71 (≠ A55), S157 (≠ V134), R282 (= R259), H286 (= H263), S287 (≠ T264), Y295 (= Y272)
- binding manganese (ii) ion: E188 (≠ D165), N217 (= N194), Y219 (≠ W196)
- 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 (≠ S91), Y108 (= Y92), R109 (= R93), L159 (≠ I136), G187 (= G164), E188 (≠ D165), G189 (= G166), A190 (≠ G167), R215 (≠ V192), N217 (= N194), Y219 (≠ W196), A220 (= A197), I221 (= I198), H286 (= H263)
1dtwA Human branched-chain alpha-keto acid dehydrogenase (see paper)
32% identity, 88% coverage: 34:351/361 of query aligns to 49:362/382 of 1dtwA
- active site: E70 (≠ A55), S156 (≠ V134), R281 (= R259), H285 (= H263), S286 (≠ T264), Y294 (= Y272)
- binding potassium ion: S155 (= S133), S156 (≠ V134), P157 (= P135), T160 (= T138), Q161 (= Q139)
- binding magnesium ion: E187 (≠ D165), N216 (= N194), Y218 (≠ W196)
- binding thiamine diphosphate: Q106 (≠ S91), Y107 (= Y92), R108 (= R93), L158 (≠ I136), G186 (= G164), E187 (≠ D165), G188 (= G166), A189 (≠ G167), R214 (≠ V192), N216 (= N194), Y218 (≠ W196), A219 (= A197), I220 (= I198), H285 (= H263)
1v1mA Crosstalk between cofactor binding and the phosphorylation loop conformation in the bckd machine (see paper)
31% identity, 88% coverage: 34:351/361 of query aligns to 50:352/372 of 1v1mA
- active site: E71 (≠ A55), S157 (≠ V134), R282 (= R259)
- binding manganese (ii) ion: E188 (≠ D165), N217 (= N194), Y219 (≠ W196)
- binding thiamine diphosphate: R109 (= R93), L159 (≠ I136), G187 (= G164), E188 (≠ D165), G189 (= G166), A190 (≠ G167), R215 (≠ V192), N217 (= N194), Y219 (≠ W196), A220 (= A197), I221 (= I198)
1oluA Roles of his291-alpha and his146-beta' in the reductive acylation reaction catalyzed by human branched-chain alpha-ketoacid dehydrogenase (see paper)
31% identity, 88% coverage: 34:351/361 of query aligns to 46:346/366 of 1oluA
- active site: E67 (≠ A55), S153 (≠ V134), R278 (= R259)
- binding magnesium ion: E184 (≠ D165), N213 (= N194), Y215 (≠ W196)
- binding thiamine diphosphate: R105 (= R93), L155 (≠ I136), G183 (= G164), E184 (≠ D165), G185 (= G166), A186 (≠ G167), N213 (= N194), A216 (= A197), I217 (= I198)
Query Sequence
>N515DRAFT_0356 FitnessBrowser__Dyella79:N515DRAFT_0356
MSIAAKFEIEYLQYLDAEGNQVRDDLPAFAKDLDHMVELYKLMMSTRVFDAKSVALQRTG
KLGTYASCLGHEAAHVGIGSAMKPEDVFAPSYREYGAQLYRGVQPREVYMYWGGDERGND
YQKEPARHDFAWSVPIATQCLHAAGSALAFKIRNEKRVAVCTIGDGGSSKGDFYGAINIT
GAQNLPMVAVIVNNQWAISVPRKIQSGAPTLAQKGIAAGLFSIQVDGNDIIAVRKAMEDA
LDRARNGQGGSVLELVTYRLSDHTTADDARRYRGEQEVKDAWAKEPMKRLRAWLVAKNVW
DDAKEEAWKAECDEWMDNEVNAYLETKTQPVTAMFDYTFAEVPADLAKQRDLALSLDKKA
H
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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