SitesBLAST
Comparing CA265_RS18405 FitnessBrowser__Pedo557:CA265_RS18405 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)
P21953 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial; Branched-chain alpha-keto acid dehydrogenase E1 component beta chain; BCKDE1B; BCKDH E1-beta; EC 1.2.4.4 from Homo sapiens (Human) (see 2 papers)
38% identity, 53% coverage: 313:658/658 of query aligns to 42:392/392 of P21953
- Y152 (≠ F423) binding
- N176 (vs. gap) to Y: in MSUD1B; uncertain significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity
- G178 (≠ A446) binding
- L180 (≠ V448) binding
- T181 (≠ V449) binding
- H206 (≠ K474) to R: in MSUD1B; loss of 3-methyl-2-oxobutanoate dehydrogenase activity
- C228 (≠ A496) binding
- D231 (= D499) binding
- N233 (= N501) binding
2j9fD Human branched-chain alpha-ketoacid dehydrogenase-decarboxylase e1b (see paper)
40% identity, 48% coverage: 344:658/658 of query aligns to 11:329/329 of 2j9fD
1dtwB Human branched-chain alpha-keto acid dehydrogenase (see paper)
40% identity, 48% coverage: 344:658/658 of query aligns to 8:326/326 of 1dtwB
- active site: E60 (= E397), H130 (= H464)
- binding potassium ion: G112 (≠ A446), S113 (≠ D447), L114 (≠ V448), T115 (≠ V449), C162 (≠ A496), I163 (= I497), D165 (= D499), N167 (= N501), P168 (= P502), C169 (≠ V503)
1qs0B Crystal structure of pseudomonas putida 2-oxoisovalerate dehydrogenase (branched-chain alpha-keto acid dehydrogenase, e1b) (see paper)
39% identity, 49% coverage: 337:657/658 of query aligns to 1:337/338 of 1qs0B
3dv0D Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
40% identity, 45% coverage: 344:636/658 of query aligns to 6:302/324 of 3dv0D
3dv0B Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
40% identity, 45% coverage: 344:636/658 of query aligns to 6:302/324 of 3dv0B
3dufD Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
40% identity, 45% coverage: 344:636/658 of query aligns to 6:302/324 of 3dufD
1w85B The crystal structure of pyruvate dehydrogenase e1 bound to the peripheral subunit binding domain of e2 (see paper)
40% identity, 45% coverage: 344:636/658 of query aligns to 6:302/324 of 1w85B
1umdD Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methyl-2-oxopentanoate as an intermediate (see paper)
43% identity, 45% coverage: 344:636/658 of query aligns to 6:302/323 of 1umdD
1umcD Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methylpentanoate (see paper)
43% identity, 45% coverage: 344:636/658 of query aligns to 6:302/323 of 1umcD
1umbD Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 in holo-form (see paper)
43% identity, 45% coverage: 344:636/658 of query aligns to 6:302/323 of 1umbD
Q5SLR3 2-oxoisovalerate dehydrogenase subunit beta; Branched-chain alpha-keto acid dehydrogenase E1 component beta chain; BCKDH E1-beta; EC 1.2.4.4 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
43% identity, 45% coverage: 344:636/658 of query aligns to 7:303/324 of Q5SLR3
- E29 (≠ Q366) binding
- Q82 (= Q419) binding
6cfoB Human pyruvate dehydrogenase e1 component complex with covalent tdp adduct acetyl phosphinate (see paper)
33% identity, 46% coverage: 345:647/658 of query aligns to 8:318/330 of 6cfoB
6cerD Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
33% identity, 46% coverage: 345:647/658 of query aligns to 9:319/331 of 6cerD
P11177 Pyruvate dehydrogenase E1 component subunit beta, mitochondrial; PDHE1-B; EC 1.2.4.1 from Homo sapiens (Human) (see 6 papers)
33% identity, 46% coverage: 345:647/658 of query aligns to 37:347/359 of P11177
- E89 (= E397) binding
- E259 (≠ S562) mutation E->A,Q: Does not affect interaction with DLAT.
- E262 (vs. gap) mutation E->A,Q: Does not affect interaction with DLAT.
- E264 (≠ T565) mutation E->A,Q: Does not affect interaction with DLAT.
- D319 (= D619) Important for interaction with DLAT; mutation to A: Inhibits interaction with DLAT. Does not affect pyruvate decarboxylase activity. Loss of multienzyme pyruvate dehydrogenase complex activity.; mutation to N: Reduces interaction with DLAT. Reduces multienzyme pyruvate dehydrogenase complex activity. Does not affect pyruvate decarboxylase activity.
Sites not aligning to the query:
- 1:30 modified: transit peptide, Mitochondrion
- 31 natural variant: L -> V
- 359 I→A: Reduces pyruvate decarboxylase and multienzyme pyruvate dehydrogenase complex activity. Does not affect interaction with DLAT.; mutation Missing: Reduces pyruvate decarboxylase and multienzyme pyruvate dehydrogenase complex activity. Does not affect interaction with DLAT.
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)
32% identity, 49% coverage: 13:337/658 of query aligns to 102:426/445 of P12694
- Y158 (≠ H69) binding
- R159 (= R70) binding ; to W: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs769688327
- Q190 (≠ D101) to K: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- S206 (≠ I117) binding
- S207 (= S118) binding
- P208 (≠ H119) binding
- T211 (≠ P122) binding ; to M: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123503
- Q212 (= Q123) binding
- E238 (= E149) binding
- G239 (= G150) binding
- A240 (= A151) binding
- G249 (≠ A160) 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 (= A164) to T: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs199599175
- A254 (= A165) to D: in MSUD1A; uncertain significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity
- R265 (≠ E176) 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 (= N178) 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 (= Y180) binding
- A285 (≠ V196) 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 (= G201) 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 (≠ Q208) to H: in MSUD1A; uncertain significance; decreased affinity for the cofactor thiamine diphosphate; decreased 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs200137189
- T310 (≠ I221) to R: in MSUD1A; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852875
- I326 (≠ V237) to T: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- H336 (≠ E248) binding
- S337 (≠ E249) modified: Phosphoserine; by BCKDK; mutation to A: Substantially decreases the stability of the BCKD complex.
- S347 (≠ P257) mutation to A: Does not affect the stability of the BCKD complex.
- F409 (≠ E320) 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 (= Y324) 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)
32% identity, 49% coverage: 13:337/658 of query aligns to 52:373/392 of 2bffA
- active site: E71 (≠ K32), S157 (= S118), R282 (= R243), H286 (≠ E248), S287 (≠ E249), Y295 (≠ P257)
- binding manganese (ii) ion: E188 (= E149), N217 (= N178), Y219 (= Y180)
- 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 (≠ M68), Y108 (≠ H69), R109 (= R70), L159 (= L120), G187 (= G148), E188 (= E149), G189 (= G150), A190 (= A151), R215 (≠ E176), N217 (= N178), Y219 (= Y180), A220 (≠ G181), I221 (≠ L182), H286 (≠ E248)
2bewA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
32% identity, 49% coverage: 13:337/658 of query aligns to 52:371/390 of 2bewA
- active site: E71 (≠ K32), S157 (= S118), R282 (= R243), H286 (≠ E248), S287 (≠ E249), Y295 (≠ P257)
- binding manganese (ii) ion: E188 (= E149), N217 (= N178), Y219 (= Y180), A220 (≠ G181)
- binding c2-1-hydroxyphenyl-thiamin diphosphate: M82 (≠ F43), Q107 (≠ M68), Y108 (≠ H69), R109 (= R70), L159 (= L120), G187 (= G148), E188 (= E149), G189 (= G150), A190 (= A151), R215 (≠ E176), N217 (= N178), Y219 (= Y180), A220 (≠ G181), I221 (≠ L182), H286 (≠ E248)
2bevA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
32% identity, 49% coverage: 13:337/658 of query aligns to 52:371/390 of 2bevA
- active site: E71 (≠ K32), S157 (= S118), R282 (= R243), H286 (≠ E248), S287 (≠ E249), Y295 (≠ P257)
- binding manganese (ii) ion: E188 (= E149), N217 (= N178), Y219 (= Y180), A220 (≠ G181)
- binding c2-1-hydroxy-2-methyl-butyl-thiamin diphosphate: F80 (≠ K41), Q107 (≠ M68), Y108 (≠ H69), R109 (= R70), S157 (= S118), L159 (= L120), G187 (= G148), E188 (= E149), G189 (= G150), A190 (= A151), R215 (≠ E176), N217 (= N178), Y219 (= Y180), A220 (≠ G181), I221 (≠ L182), H286 (≠ E248)
2beuA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
32% identity, 49% coverage: 13:337/658 of query aligns to 52:371/390 of 2beuA
- active site: E71 (≠ K32), S157 (= S118), R282 (= R243), H286 (≠ E248), S287 (≠ E249), Y295 (≠ P257)
- binding manganese (ii) ion: E188 (= E149), N217 (= N178), Y219 (= Y180), A220 (≠ G181)
- binding c2-1-hydroxy-3-methyl-propyl-thiamin diphosphate: Q107 (≠ M68), Y108 (≠ H69), R109 (= R70), S157 (= S118), L159 (= L120), G187 (= G148), E188 (= E149), G189 (= G150), A190 (= A151), R215 (≠ E176), N217 (= N178), Y219 (= Y180), A220 (≠ G181), I221 (≠ L182), H286 (≠ E248)
Query Sequence
>CA265_RS18405 FitnessBrowser__Pedo557:CA265_RS18405
MQFKRGDKDDKFLLNLYRRLLYPRMVEDKMLKLLRQGRIGKWFSGIGQEAIAVGSTLAMQ
SDEYILPMHRNLGVFTSRDIPLKKLMAQWQGKITGFSKGRDRSFHFGTQEYKIIGMISHL
GPQMALADGIALADVLRNQPHATLVYTGEGATSEGDFHEAVNVAAVWNLPVIFLIENNGY
GLSTPKSEQFRCKNLVDKAIGYGVEGIQIDGNNILEVYDTINQLAMEIRKDPRPVLVECL
TFRMRGHEEASGTKYVPQELFDEWEKKDPLNNYEAYLIEQGVLTPDTVIDIKIQVKRDIE
LEIEEAFNEDEPIANADQEETDMYFPYRQQVIQPDESSTEKRYLDAITDGLDLAMQKYPN
LVLMGQDIADYGGAFKITDGFTAKYGRGRVRNTPICESAIVGAGLGLSINGYKAVVEMQF
ADFVTVGFNQIVNNLAKTHYRWGEKADVVVRMPTGAGTGAGPFHSQSNEAWFTKTPGLKI
VYPAFPEDAKGLLLAAIEDPNPVLYFEHKYLYRSLSAPVPDGYYTTEIGKAVRLAEGDKF
TIITYGLGVHWALDYMEQYPESGATLIDLRTLQPWDKETVSAAVKATGRVLILHEDTLTN
GFGAELSAWIGEHCFAYLDAPVMRCASLDTAIPMSKILEEDFLAKARLAETIDKLLKY
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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