SitesBLAST
Comparing Pf1N1B4_1020 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_1020 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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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)
40% identity, 98% coverage: 1:324/332 of query aligns to 43:365/365 of 3dufA
- active site: S62 (≠ A20), I139 (≠ V99), R264 (= R224), H268 (= H228), T269 (= T229), Y278 (= Y237)
- binding magnesium ion: D170 (= D130), N199 (= N159), F201 (≠ W161)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1r)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: Y99 (= Y57), R100 (= R58), I141 (= I101), G169 (= G129), D170 (= D130), G171 (= G131), N199 (= N159), F201 (≠ W161), A202 (= A162), H268 (= H228)
1w85A The crystal structure of pyruvate dehydrogenase e1 bound to the peripheral subunit binding domain of e2 (see paper)
39% identity, 97% coverage: 1:321/332 of query aligns to 43:356/358 of 1w85A
- active site: S62 (≠ A20), I139 (≠ V99), R264 (= R224), H268 (= H228), T269 (= T229)
- binding magnesium ion: D170 (= D130), N199 (= N159), F201 (≠ W161)
- binding thiamine diphosphate: Y99 (= Y57), R100 (= R58), I139 (≠ V99), I141 (= I101), G169 (= G129), D170 (= D130), G171 (= G131), G172 (= G132), N199 (= N159), A202 (= A162), I203 (= I163), H268 (= H228)
3dv0A Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
38% identity, 97% coverage: 1:321/332 of query aligns to 43:347/349 of 3dv0A
- active site: S62 (≠ A20), I139 (≠ V99), R264 (= R224), H268 (= H228)
- binding magnesium ion: D170 (= D130), N199 (= N159), F201 (≠ W161)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: Y99 (= Y57), R100 (= R58), I141 (= I101), G169 (= G129), D170 (= D130), G171 (= G131), N199 (= N159), F201 (≠ W161), A202 (= A162), I203 (= I163), R264 (= R224)
3dv0E Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
37% identity, 97% coverage: 1:321/332 of query aligns to 43:342/344 of 3dv0E
- active site: S62 (≠ A20), I139 (≠ V99), R264 (= R236)
- binding magnesium ion: G169 (= G129), D170 (= D130), Q197 (≠ N157), N199 (= N159)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: Y99 (= Y57), R100 (= R58), I139 (≠ V99), I141 (= I101), G169 (= G129), D170 (= D130), G171 (= G131), N199 (= N159), F201 (≠ W161), A202 (= A162), I203 (= I163)
1w88A The crystal structure of pyruvate dehydrogenase e1(d180n,e183q) bound to the peripheral subunit binding domain of e2 (see paper)
36% identity, 97% coverage: 1:321/332 of query aligns to 42:338/340 of 1w88A
- active site: S61 (≠ A20), I138 (≠ V99), R263 (= R224)
- binding magnesium ion: D169 (= D130), N198 (= N159), F200 (≠ W161)
- binding thiamine diphosphate: Y98 (= Y57), R99 (= R58), I140 (= I101), G168 (= G129), D169 (= D130), G170 (= G131), A201 (= A162), I202 (= I163)
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)
37% identity, 95% coverage: 1:314/332 of query aligns to 38:359/367 of Q5SLR4
- F66 (≠ T29) binding
- YYR 94:96 (= YYR 56:58) binding
- Y95 (= Y57) binding
- MPEH 128:131 (≠ FP-- 95:96) binding
- S144 (≠ V99) binding
- SPI 144:146 (≠ VPI 99:101) binding
- 174:180 (vs. 129:135, 71% identical) binding
- D175 (= D130) binding
- N204 (= N159) binding
- NFYAI 204:208 (≠ NQWAI 159:163) binding
- Y206 (≠ W161) binding
- H273 (= H228) binding
1umdA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methyl-2-oxopentanoate as an intermediate (see paper)
37% identity, 95% coverage: 1:314/332 of query aligns to 33:354/362 of 1umdA
- active site: I52 (≠ A20), S139 (≠ V99), R264 (= R224), H268 (= H228), S269 (≠ T229), Y277 (= Y237)
- binding 2-oxo-4-methylpentanoic acid: F61 (≠ T29), Y90 (= Y57), S139 (≠ V99)
- binding magnesium ion: D170 (= D130), N199 (= N159), Y201 (≠ W161)
- binding thiamine diphosphate: Y89 (= Y56), Y90 (= Y57), R91 (= R58), P140 (= P100), I141 (= I101), G169 (= G129), D170 (= D130), G171 (= G131), N199 (= N159), Y201 (≠ W161), A202 (= A162), I203 (= I163), H268 (= H228)
1umcA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methylpentanoate (see paper)
37% identity, 95% coverage: 1:314/332 of query aligns to 33:354/362 of 1umcA
- active site: I52 (≠ A20), S139 (≠ V99), R264 (= R224), H268 (= H228), S269 (≠ T229), Y277 (= Y237)
- binding 4-methyl valeric acid: Y90 (= Y57), H126 (vs. gap)
- binding magnesium ion: D170 (= D130), N199 (= N159), Y201 (≠ W161)
- binding thiamine diphosphate: Y89 (= Y56), Y90 (= Y57), R91 (= R58), I141 (= I101), G169 (= G129), D170 (= D130), G171 (= G131), N199 (= N159), Y201 (≠ W161), I203 (= I163), H268 (= H228)
1umbA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 in holo-form (see paper)
37% identity, 95% coverage: 1:314/332 of query aligns to 33:354/362 of 1umbA
- active site: I52 (≠ A20), S139 (≠ V99), R264 (= R224), H268 (= H228), S269 (≠ T229), Y277 (= Y237)
- binding magnesium ion: D170 (= D130), N199 (= N159), Y201 (≠ W161)
- binding thiamine diphosphate: Y89 (= Y56), Y90 (= Y57), R91 (= R58), P140 (= P100), I141 (= I101), G169 (= G129), D170 (= D130), G171 (= G131), N199 (= N159), Y201 (≠ W161), A202 (= A162), I203 (= I163), H268 (= H228)
1qs0A Crystal structure of pseudomonas putida 2-oxoisovalerate dehydrogenase (branched-chain alpha-keto acid dehydrogenase, e1b) (see paper)
34% identity, 94% coverage: 6:318/332 of query aligns to 81:407/407 of 1qs0A
- active site: V95 (≠ A20), G181 (vs. gap), R307 (= R224), H311 (= H228), S312 (≠ T229), Y320 (= Y237)
- binding magnesium ion: D212 (= D130), N241 (= N159), W243 (= W161)
- binding thiamine diphosphate: Y132 (= Y57), R133 (= R58), L183 (vs. gap), G211 (= G129), D212 (= D130), G213 (= G131), A214 (≠ G132), N241 (= N159), W243 (= W161), A244 (= A162), I245 (= I163), H311 (= H228)
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: 1:318/332 of query aligns to 98:423/441 of P11960
- S333 (≠ T229) modified: Phosphoserine; by BCKDK
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, 96% coverage: 1:318/332 of query aligns to 102:427/445 of P12694
- Y158 (= Y57) binding
- R159 (= R58) binding ; to W: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs769688327
- Q190 (≠ D94) to K: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- S206 (≠ C98) binding
- S207 (≠ V99) binding
- P208 (= P100) binding
- T211 (= T103) binding ; to M: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123503
- Q212 (= Q104) binding
- E238 (≠ D130) binding
- G239 (= G131) binding
- A240 (≠ G132) binding
- G249 (≠ A141) 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 (= A145) to T: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs199599175
- A254 (≠ G146) to D: in MSUD1A; uncertain significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity
- R265 (≠ N157) 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 (= N159) 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 (≠ W161) binding
- A285 (= A177) 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 (= G182) 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 (≠ Q189) to H: in MSUD1A; uncertain significance; decreased affinity for the cofactor thiamine diphosphate; decreased 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs200137189
- T310 (≠ V202) to R: in MSUD1A; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852875
- I326 (≠ L218) to T: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- H336 (= H228) binding
- S337 (≠ T229) modified: Phosphoserine; by BCKDK; mutation to A: Substantially decreases the stability of the BCKD complex.
- S347 (= S239) mutation to A: Does not affect the stability of the BCKD complex.
- F409 (≠ M300) 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 (= Y304) 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
2bewA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
29% identity, 96% coverage: 1:318/332 of query aligns to 52:372/390 of 2bewA
- active site: E71 (≠ A20), S157 (≠ V99), R282 (= R224), H286 (= H228), S287 (≠ T229), Y295 (= Y237)
- binding manganese (ii) ion: E188 (≠ D130), N217 (= N159), Y219 (≠ W161), A220 (= A162)
- binding c2-1-hydroxyphenyl-thiamin diphosphate: M82 (≠ A31), Q107 (≠ Y56), Y108 (= Y57), R109 (= R58), L159 (≠ I101), G187 (= G129), E188 (≠ D130), G189 (= G131), A190 (≠ G132), R215 (≠ N157), N217 (= N159), Y219 (≠ W161), A220 (= A162), I221 (= I163), H286 (= H228)
2bevA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
29% identity, 96% coverage: 1:318/332 of query aligns to 52:372/390 of 2bevA
- active site: E71 (≠ A20), S157 (≠ V99), R282 (= R224), H286 (= H228), S287 (≠ T229), Y295 (= Y237)
- binding manganese (ii) ion: E188 (≠ D130), N217 (= N159), Y219 (≠ W161), A220 (= A162)
- binding c2-1-hydroxy-2-methyl-butyl-thiamin diphosphate: F80 (≠ T29), Q107 (≠ Y56), Y108 (= Y57), R109 (= R58), S157 (≠ V99), L159 (≠ I101), G187 (= G129), E188 (≠ D130), G189 (= G131), A190 (≠ G132), R215 (≠ N157), N217 (= N159), Y219 (≠ W161), A220 (= A162), I221 (= I163), H286 (= H228)
2beuA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
29% identity, 96% coverage: 1:318/332 of query aligns to 52:372/390 of 2beuA
- active site: E71 (≠ A20), S157 (≠ V99), R282 (= R224), H286 (= H228), S287 (≠ T229), Y295 (= Y237)
- binding manganese (ii) ion: E188 (≠ D130), N217 (= N159), Y219 (≠ W161), A220 (= A162)
- binding c2-1-hydroxy-3-methyl-propyl-thiamin diphosphate: Q107 (≠ Y56), Y108 (= Y57), R109 (= R58), S157 (≠ V99), L159 (≠ I101), G187 (= G129), E188 (≠ D130), G189 (= G131), A190 (≠ G132), R215 (≠ N157), N217 (= N159), Y219 (≠ W161), A220 (= A162), I221 (= I163), H286 (= H228)
1wciA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
29% identity, 96% coverage: 1:318/332 of query aligns to 52:370/388 of 1wciA
- active site: E71 (≠ A20), S157 (≠ V99), R282 (= R224), H286 (= H228), S287 (≠ T229), Y295 (= Y237)
- binding manganese (ii) ion: E188 (≠ D130), N217 (= N159), Y219 (≠ W161), A220 (= A162)
- binding c2-1-hydroxy-3-methyl-butyl-thiamin: Q107 (≠ Y56), Y108 (= Y57), R109 (= R58), L159 (≠ I101), G187 (= G129), E188 (≠ D130), G189 (= G131), A190 (≠ G132), R215 (≠ N157), N217 (= N159), Y219 (≠ W161), A220 (= A162), I221 (= I163), H286 (= H228)
2bffA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
29% identity, 96% coverage: 1:318/332 of query aligns to 52:374/392 of 2bffA
- active site: E71 (≠ A20), S157 (≠ V99), R282 (= R224), H286 (= H228), S287 (≠ T229), Y295 (= Y237)
- binding manganese (ii) ion: E188 (≠ D130), N217 (= N159), Y219 (≠ W161)
- 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 (≠ Y56), Y108 (= Y57), R109 (= R58), L159 (≠ I101), G187 (= G129), E188 (≠ D130), G189 (= G131), A190 (≠ G132), R215 (≠ N157), N217 (= N159), Y219 (≠ W161), A220 (= A162), I221 (= I163), H286 (= H228)
1dtwA Human branched-chain alpha-keto acid dehydrogenase (see paper)
29% identity, 96% coverage: 1:318/332 of query aligns to 51:364/382 of 1dtwA
- active site: E70 (≠ A20), S156 (≠ V99), R281 (= R224), H285 (= H228), S286 (≠ T229), Y294 (= Y237)
- binding potassium ion: S155 (≠ C98), S156 (≠ V99), P157 (= P100), T160 (= T103), Q161 (= Q104)
- binding magnesium ion: E187 (≠ D130), N216 (= N159), Y218 (≠ W161)
- binding thiamine diphosphate: Q106 (≠ Y56), Y107 (= Y57), R108 (= R58), L158 (≠ I101), G186 (= G129), E187 (≠ D130), G188 (= G131), A189 (≠ G132), R214 (≠ N157), N216 (= N159), Y218 (≠ W161), A219 (= A162), I220 (= I163), H285 (= H228)
1v1mA Crosstalk between cofactor binding and the phosphorylation loop conformation in the bckd machine (see paper)
28% identity, 96% coverage: 1:318/332 of query aligns to 52:354/372 of 1v1mA
- active site: E71 (≠ A20), S157 (≠ V99), R282 (= R224)
- binding manganese (ii) ion: E188 (≠ D130), N217 (= N159), Y219 (≠ W161)
- binding thiamine diphosphate: R109 (= R58), L159 (≠ I101), G187 (= G129), E188 (≠ D130), G189 (= G131), A190 (≠ G132), R215 (≠ N157), N217 (= N159), Y219 (≠ W161), A220 (= A162), I221 (= I163)
1oluA Roles of his291-alpha and his146-beta' in the reductive acylation reaction catalyzed by human branched-chain alpha-ketoacid dehydrogenase (see paper)
28% identity, 96% coverage: 1:318/332 of query aligns to 48:348/366 of 1oluA
- active site: E67 (≠ A20), S153 (≠ V99), R278 (= R224)
- binding magnesium ion: E184 (≠ D130), N213 (= N159), Y215 (≠ W161)
- binding thiamine diphosphate: R105 (= R58), L155 (≠ I101), G183 (= G129), E184 (≠ D130), G185 (= G131), A186 (≠ G132), N213 (= N159), A216 (= A162), I217 (= I163)
Query Sequence
>Pf1N1B4_1020 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_1020
LTRLYRQMVLTRLFDQKAVALQRTGRIGTYAPTLGQEAIGVAVGSLMHAEDVLIPYYRDT
AVQLMRGVRMEEILLYWGGDERGSDFADPAVAQDFPICVPIATQALHACGVASAFKIRGE
HRVAVTTCGDGGTSKGDFLEALNVAGAWQLPVVFMVNNNQWAISVPRRIQCGAPTLAQKA
IGAGFHGEQVDGNDMLAVYDRVQAALERTRHGKGPVLLECLSYRLGDHTTADDATRYRSA
DEVKQAWLEEPIKRLQRFMAGQGVWDEGREQALISECQGLVQRAVDNFEAAGLQAPESVM
DHVYAQWPQALAEQREDFLERVARRTGGSSDE
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