SitesBLAST
Comparing Echvi_1750 Echvi_1750 Pyruvate/2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, eukaryotic type, beta subunit 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)
41% identity, 49% coverage: 336:661/661 of query aligns to 61:392/392 of P21953
- Y152 (≠ F427) binding
- N176 (≠ Q448) to Y: in MSUD1B; uncertain significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity
- G178 (≠ A450) binding
- L180 (≠ V452) binding
- T181 (≠ V453) binding
- H206 (= H478) to R: in MSUD1B; loss of 3-methyl-2-oxobutanoate dehydrogenase activity
- C228 (≠ A500) binding
- D231 (= D503) binding
- N233 (= N505) binding
1dtwB Human branched-chain alpha-keto acid dehydrogenase (see paper)
40% identity, 48% coverage: 342:661/661 of query aligns to 2:326/326 of 1dtwB
- active site: E60 (= E401), H130 (= H468)
- binding potassium ion: G112 (≠ A450), S113 (≠ D451), L114 (≠ V452), T115 (≠ V453), C162 (≠ A500), I163 (= I501), D165 (= D503), N167 (= N505), P168 (= P506), C169 (= C507)
2j9fD Human branched-chain alpha-ketoacid dehydrogenase-decarboxylase e1b (see paper)
40% identity, 48% coverage: 342:661/661 of query aligns to 5:329/329 of 2j9fD
1umdD Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methyl-2-oxopentanoate as an intermediate (see paper)
45% identity, 44% coverage: 347:640/661 of query aligns to 5:303/323 of 1umdD
1umcD Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methylpentanoate (see paper)
45% identity, 44% coverage: 347:640/661 of query aligns to 5:303/323 of 1umcD
1umbD Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 in holo-form (see paper)
45% identity, 44% coverage: 347:640/661 of query aligns to 5:303/323 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)
45% identity, 44% coverage: 347:640/661 of query aligns to 6:304/324 of Q5SLR3
- E29 (≠ Q370) binding
- Q82 (= Q423) binding
3dv0D Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
41% identity, 47% coverage: 347:655/661 of query aligns to 5:315/324 of 3dv0D
3dv0B Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
41% identity, 47% coverage: 347:655/661 of query aligns to 5:315/324 of 3dv0B
3dufD Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
41% identity, 47% coverage: 347:655/661 of query aligns to 5:315/324 of 3dufD
1w85B The crystal structure of pyruvate dehydrogenase e1 bound to the peripheral subunit binding domain of e2 (see paper)
41% identity, 47% coverage: 347:655/661 of query aligns to 5:315/324 of 1w85B
1qs0B Crystal structure of pseudomonas putida 2-oxoisovalerate dehydrogenase (branched-chain alpha-keto acid dehydrogenase, e1b) (see paper)
39% identity, 45% coverage: 341:638/661 of query aligns to 1:316/338 of 1qs0B
P11177 Pyruvate dehydrogenase E1 component subunit beta, mitochondrial; PDHE1-B; EC 1.2.4.1 from Homo sapiens (Human) (see 6 papers)
34% identity, 48% coverage: 339:658/661 of query aligns to 27:353/359 of P11177
- L31 (≠ T343) natural variant: L -> V
- E89 (= E401) binding
- E259 (≠ L563) mutation E->A,Q: Does not affect interaction with DLAT.
- E262 (≠ R566) mutation E->A,Q: Does not affect interaction with DLAT.
- E264 (≠ D568) mutation E->A,Q: Does not affect interaction with DLAT.
- D319 (= D622) 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
- 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.
6cfoB Human pyruvate dehydrogenase e1 component complex with covalent tdp adduct acetyl phosphinate (see paper)
35% identity, 47% coverage: 349:658/661 of query aligns to 8:324/330 of 6cfoB
6cerD Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
35% identity, 47% coverage: 349:658/661 of query aligns to 9:325/331 of 6cerD
2bewA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
31% identity, 44% coverage: 17:310/661 of query aligns to 52:342/390 of 2bewA
- active site: E71 (≠ L36), S157 (= S122), R282 (= R247), H286 (≠ E252), S287 (≠ E253), Y295 (≠ P261)
- binding manganese (ii) ion: E188 (≠ D153), N217 (= N182), Y219 (= Y184), A220 (≠ G185)
- binding c2-1-hydroxyphenyl-thiamin diphosphate: M82 (≠ F47), Q107 (≠ M72), Y108 (≠ H73), R109 (= R74), L159 (= L124), G187 (= G152), E188 (≠ D153), G189 (= G154), A190 (= A155), R215 (≠ E180), N217 (= N182), Y219 (= Y184), A220 (≠ G185), I221 (≠ L186), H286 (≠ E252)
2bevA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
31% identity, 44% coverage: 17:310/661 of query aligns to 52:342/390 of 2bevA
- active site: E71 (≠ L36), S157 (= S122), R282 (= R247), H286 (≠ E252), S287 (≠ E253), Y295 (≠ P261)
- binding manganese (ii) ion: E188 (≠ D153), N217 (= N182), Y219 (= Y184), A220 (≠ G185)
- binding c2-1-hydroxy-2-methyl-butyl-thiamin diphosphate: F80 (≠ K45), Q107 (≠ M72), Y108 (≠ H73), R109 (= R74), S157 (= S122), L159 (= L124), G187 (= G152), E188 (≠ D153), G189 (= G154), A190 (= A155), R215 (≠ E180), N217 (= N182), Y219 (= Y184), A220 (≠ G185), I221 (≠ L186), H286 (≠ E252)
2beuA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
31% identity, 44% coverage: 17:310/661 of query aligns to 52:342/390 of 2beuA
- active site: E71 (≠ L36), S157 (= S122), R282 (= R247), H286 (≠ E252), S287 (≠ E253), Y295 (≠ P261)
- binding manganese (ii) ion: E188 (≠ D153), N217 (= N182), Y219 (= Y184), A220 (≠ G185)
- binding c2-1-hydroxy-3-methyl-propyl-thiamin diphosphate: Q107 (≠ M72), Y108 (≠ H73), R109 (= R74), S157 (= S122), L159 (= L124), G187 (= G152), E188 (≠ D153), G189 (= G154), A190 (= A155), R215 (≠ E180), N217 (= N182), Y219 (= Y184), A220 (≠ G185), I221 (≠ L186), H286 (≠ E252)
2bffA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
32% identity, 44% coverage: 17:310/661 of query aligns to 52:344/392 of 2bffA
- active site: E71 (≠ L36), S157 (= S122), R282 (= R247), H286 (= H251), S287 (≠ E252), Y295 (= Y264)
- binding manganese (ii) ion: E188 (≠ D153), N217 (= N182), Y219 (= Y184)
- 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 (≠ M72), Y108 (≠ H73), R109 (= R74), L159 (= L124), G187 (= G152), E188 (≠ D153), G189 (= G154), A190 (= A155), R215 (≠ E180), N217 (= N182), Y219 (= Y184), A220 (≠ G185), I221 (≠ L186), H286 (= H251)
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, 43% coverage: 17:303/661 of query aligns to 102:390/445 of P12694
- Y158 (≠ H73) binding
- R159 (= R74) binding ; to W: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs769688327
- Q190 (≠ D105) to K: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- S206 (≠ I121) binding
- S207 (= S122) binding
- P208 (≠ H123) binding
- T211 (≠ P126) binding ; to M: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123503
- Q212 (= Q127) binding
- E238 (≠ D153) binding
- G239 (= G154) binding
- A240 (= A155) binding
- G249 (≠ A164) 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 (= A168) to T: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs199599175
- A254 (= A169) to D: in MSUD1A; uncertain significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity
- R265 (≠ E180) 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 (= N182) 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 (= Y184) binding
- A285 (≠ I200) 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 (= G205) 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 (≠ K212) to H: in MSUD1A; uncertain significance; decreased affinity for the cofactor thiamine diphosphate; decreased 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs200137189
- T310 (≠ L225) to R: in MSUD1A; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852875
- I326 (≠ V241) to T: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- H336 (= H251) binding
- S337 (vs. gap) modified: Phosphoserine; by BCKDK; mutation to A: Substantially decreases the stability of the BCKD complex.
- S347 (≠ Y259) mutation to A: Does not affect the stability of the BCKD complex.
Sites not aligning to the query:
- 1:45 modified: transit peptide, Mitochondrion
- 409 F → C: in MSUD1A; decreased solubility; loss of mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852872
- 413 Y → C: in MSUD1A; uncertain significance; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123508
- 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
Query Sequence
>Echvi_1750 Echvi_1750 Pyruvate/2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, eukaryotic type, beta subunit
MAPNMVFDRKDLSDGDLLHFYEMLLMPRKIEEKMLLLLRQGKISKWFSGWGQEAISIAAV
MAMREDEFLLPMHRNLGVFTGRGLPLGKLFAQFQGKYSGFTKGRDRSFHFGSVAHHVVGM
ISHLGPQLAVADGIALASKLGGERKATLVFTGDGATSEGDFHEALNVAAVWQLPVIFVVE
HNGYGLSTPSAEQFRFKQFIDKGPGYGMEAVKVDGNNVLELYHALSGIAEDIRHRPRPFL
VEAMTYRMRGHEESSGTKYVPKAYFEEGEKYDPVRNFEDYLQEIGVLDQSAKGVIEKRLS
EQIEAGLASAFSAEFPVAGEEELADVYCPSEGKPKEPHSSATTEKRLVDAISDGLRLSMR
QFSNLVLMGQDIGEYGGAFKVTAGFLSEFGAERVRNTPLCESAIIGAALGLSVKGFKSVV
EMQFADFVSCGFNQIVNNLAKVHYRWGQHADVVIRMPTGAGVGAGPFHSQSNEAWFFHTP
GLKILYPSSPQDAKGLLAAAIEDPNPCLFFEHKALYRSVIGQVPDEYYTVEIGKAHLVKE
GDQATVVTYGMGVHWAKRVMESLDVRVDLLDLRTLLPWDKEAVEKSVKKTNKVMILHEDC
LTGGIGAEIAAWISEHCFECLDAPVMREGSLDTPVPFAANLEENFLPENRFKDKLMALLA
Y
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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