SitesBLAST
Comparing N515DRAFT_0481 FitnessBrowser__Dyella79:N515DRAFT_0481 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)
3dv0D Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
31% identity, 44% coverage: 426:755/755 of query aligns to 9:322/324 of 3dv0D
3dv0B Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
31% identity, 44% coverage: 426:755/755 of query aligns to 9:322/324 of 3dv0B
3dufD Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
31% identity, 44% coverage: 426:755/755 of query aligns to 9:322/324 of 3dufD
1w85B The crystal structure of pyruvate dehydrogenase e1 bound to the peripheral subunit binding domain of e2 (see paper)
31% identity, 44% coverage: 426:755/755 of query aligns to 9:322/324 of 1w85B
1umdD Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methyl-2-oxopentanoate as an intermediate (see paper)
32% identity, 44% coverage: 426:755/755 of query aligns to 9:321/323 of 1umdD
1umcD Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methylpentanoate (see paper)
32% identity, 44% coverage: 426:755/755 of query aligns to 9:321/323 of 1umcD
1umbD Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 in holo-form (see paper)
32% identity, 44% coverage: 426:755/755 of query aligns to 9:321/323 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)
32% identity, 44% coverage: 426:755/755 of query aligns to 10:322/324 of Q5SLR3
- E29 (= E445) binding
- Q82 (= Q498) binding
1qs0B Crystal structure of pseudomonas putida 2-oxoisovalerate dehydrogenase (branched-chain alpha-keto acid dehydrogenase, e1b) (see paper)
30% identity, 42% coverage: 441:755/755 of query aligns to 26:336/338 of 1qs0B
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)
30% identity, 41% coverage: 421:732/755 of query aligns to 72:368/392 of P21953
- Y152 (= Y502) binding
- N176 (= N527) to Y: in MSUD1B; uncertain significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity
- G178 (≠ L529) binding
- L180 (≠ M531) binding
- T181 (≠ R532) binding
- H206 (≠ D557) to R: in MSUD1B; loss of 3-methyl-2-oxobutanoate dehydrogenase activity
- C228 (≠ L579) binding
- D231 (= D586) binding
- N233 (≠ R588) binding
1dtwB Human branched-chain alpha-keto acid dehydrogenase (see paper)
30% identity, 41% coverage: 421:732/755 of query aligns to 6:302/326 of 1dtwB
- active site: E60 (= E476), H130 (= H547)
- binding potassium ion: G112 (≠ L529), S113 (≠ V530), L114 (≠ M531), T115 (≠ R532), C162 (≠ L579), I163 (≠ M580), D165 (= D586), N167 (≠ R588), P168 (≠ V589), C169 (= C590)
2j9fD Human branched-chain alpha-ketoacid dehydrogenase-decarboxylase e1b (see paper)
30% identity, 41% coverage: 421:732/755 of query aligns to 9:305/329 of 2j9fD
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)
25% identity, 47% coverage: 16:369/755 of query aligns to 59:396/441 of P11960
- S333 (≠ A307) modified: Phosphoserine; by BCKDK
P11177 Pyruvate dehydrogenase E1 component subunit beta, mitochondrial; PDHE1-B; EC 1.2.4.1 from Homo sapiens (Human) (see 6 papers)
25% identity, 41% coverage: 426:734/755 of query aligns to 39:335/359 of P11177
- E89 (= E476) binding
- E259 (≠ H661) mutation E->A,Q: Does not affect interaction with DLAT.
- E262 (≠ R664) mutation E->A,Q: Does not affect interaction with DLAT.
- E264 (≠ R666) mutation E->A,Q: Does not affect interaction with DLAT.
- D319 (vs. gap) 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.
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)
28% identity, 42% coverage: 52:367/755 of query aligns to 33:334/367 of Q5SLR4
1umdA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methyl-2-oxopentanoate as an intermediate (see paper)
28% identity, 42% coverage: 52:367/755 of query aligns to 28:329/362 of 1umdA
- active site: I52 (≠ V76), S139 (= S166), R264 (= R302), H268 (= H306), S269 (≠ A307), Y277 (≠ W315)
- binding 2-oxo-4-methylpentanoic acid: F61 (≠ Y85), Y90 (= Y112), S139 (= S166)
- binding magnesium ion: D170 (= D206), N199 (= N240), Y201 (≠ I242)
- binding thiamine diphosphate: Y89 (≠ H111), Y90 (= Y112), R91 (= R113), P140 (≠ T167), I141 (= I168), G169 (= G205), D170 (= D206), G171 (≠ A207), N199 (= N240), Y201 (≠ I242), A202 (≠ G243), I203 (= I244), H268 (= H306)
1umcA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methylpentanoate (see paper)
28% identity, 42% coverage: 52:367/755 of query aligns to 28:329/362 of 1umcA
- active site: I52 (≠ V76), S139 (= S166), R264 (= R302), H268 (= H306), S269 (≠ A307), Y277 (≠ W315)
- binding 4-methyl valeric acid: Y90 (= Y112), H126 (≠ W154)
- binding magnesium ion: D170 (= D206), N199 (= N240), Y201 (≠ I242)
- binding thiamine diphosphate: Y89 (≠ H111), Y90 (= Y112), R91 (= R113), I141 (= I168), G169 (= G205), D170 (= D206), G171 (≠ A207), N199 (= N240), Y201 (≠ I242), I203 (= I244), H268 (= H306)
1umbA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 in holo-form (see paper)
28% identity, 42% coverage: 52:367/755 of query aligns to 28:329/362 of 1umbA
- active site: I52 (≠ V76), S139 (= S166), R264 (= R302), H268 (= H306), S269 (≠ A307), Y277 (≠ W315)
- binding magnesium ion: D170 (= D206), N199 (= N240), Y201 (≠ I242)
- binding thiamine diphosphate: Y89 (≠ H111), Y90 (= Y112), R91 (= R113), P140 (≠ T167), I141 (= I168), G169 (= G205), D170 (= D206), G171 (≠ A207), N199 (= N240), Y201 (≠ I242), A202 (≠ G243), I203 (= I244), H268 (= H306)
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)
24% identity, 47% coverage: 15:371/755 of query aligns to 62:402/445 of P12694
- Y158 (= Y112) binding
- R159 (= R113) binding ; to W: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs769688327
- Q190 (≠ R150) to K: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- S206 (≠ T165) binding
- S207 (= S166) binding
- P208 (≠ T167) binding
- T211 (≠ S170) binding ; to M: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123503
- Q212 (≠ H171) binding
- E238 (≠ D206) binding
- G239 (≠ A207) binding
- A240 (≠ S208) binding
- G249 (≠ A217) 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 (= A221) to T: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs199599175
- A254 (= A222) to D: in MSUD1A; uncertain significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity
- R265 (≠ E238) 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 (= N240) 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 (≠ I242) binding
- A285 (≠ R258) 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 (vs. gap) 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 (≠ H267) to H: in MSUD1A; uncertain significance; decreased affinity for the cofactor thiamine diphosphate; decreased 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs200137189
- T310 (≠ V280) to R: in MSUD1A; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852875
- I326 (≠ L296) to T: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- H336 (= H306) binding
- S337 (≠ A307) modified: Phosphoserine; by BCKDK; mutation to A: Substantially decreases the stability of the BCKD complex.
- S347 (= S317) 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
6cfoB Human pyruvate dehydrogenase e1 component complex with covalent tdp adduct acetyl phosphinate (see paper)
25% identity, 41% coverage: 426:734/755 of query aligns to 10:306/330 of 6cfoB
Query Sequence
>N515DRAFT_0481 FitnessBrowser__Dyella79:N515DRAFT_0481
MTALPFSLSARHKGFNRAEIVDQNFIEFVQLWQGHARAAPRDGEAVLPGSALDAQGFRDL
LESQLISRHLDLMARVLRVQNKVFYTIGSSGHEGNAMVARLTRHTDPAFLHYRSGGFMAE
RFRKLPGMDPVMDSALSFAASMEDPASGGRHKVWGSKPLWVLPQTSTIASHLPKAFGTAV
AIEQARRIGHPLPVPQDSIAICSFGDASSNHATAQTAFNAAAWTAYQKLPAPVLFVCEDN
GIGISVKTPSGWIANNFRQRPDLDYFHADGLDLAEGYGQVREAVEHCRRTRRPTFLHLRT
TRVMGHAGTDFEIEWRSVDELFALEATDPLLRSAEIALASGLYTRESLLALYEATRKQCF
AAAEEADRRPRLGTLAEVMKPLAPYTPAAVKAEAERADYAARRAEVFGGEDKLPEKQAPR
HLAIQIGQALHEVMAKYPESLLFGEDVALKGGVYTVTKGLFKTFKGNRVFNTLLDETVIL
GLAQGYANMGMLPMPEIQYLAYFHNACDQIRGEACSLQFFSNDQYRNPLVMRVAALGYQK
GFGGHFHNDNSIAALRDIPGLVVGCPSRGDDAAAMLRTLMALAKVDGRVCAFLEPIALYM
TKDLYEAGDGQWQFAYPAPGEALPLGEGRVYEQDADDLVVFTFGNGVPMALRAAREIEKK
HGWRTRVVDLRWLAPLNDKFIAGQARNARRILVLDEGRRSAGVGEGIITAIVEGGCGATP
LQRVVGADTYTPLAGAALLVLPGEAEIVAAAERML
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