SitesBLAST
Comparing CA265_RS11665 FitnessBrowser__Pedo557:CA265_RS11665 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)
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)
37% identity, 33% coverage: 476:738/806 of query aligns to 8:268/324 of Q5SLR3
- E29 (= E497) binding
- Q82 (= Q550) binding
1umdD Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methyl-2-oxopentanoate as an intermediate (see paper)
38% identity, 33% coverage: 476:738/806 of query aligns to 7:267/323 of 1umdD
1umcD Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methylpentanoate (see paper)
38% identity, 33% coverage: 476:738/806 of query aligns to 7:267/323 of 1umcD
1umbD Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 in holo-form (see paper)
38% identity, 33% coverage: 476:738/806 of query aligns to 7:267/323 of 1umbD
3dv0D Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
32% identity, 38% coverage: 489:795/806 of query aligns to 20:323/324 of 3dv0D
3dv0B Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
32% identity, 38% coverage: 489:795/806 of query aligns to 20:323/324 of 3dv0B
3dufD Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
32% identity, 38% coverage: 489:795/806 of query aligns to 20:323/324 of 3dufD
1w85B The crystal structure of pyruvate dehydrogenase e1 bound to the peripheral subunit binding domain of e2 (see paper)
32% identity, 38% coverage: 489:795/806 of query aligns to 20:323/324 of 1w85B
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)
32% identity, 35% coverage: 465:748/806 of query aligns to 65:348/392 of P21953
- Y152 (= Y554) binding
- N176 (≠ Q577) to Y: in MSUD1B; uncertain significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity
- G178 (≠ A579) binding
- L180 (≠ V581) binding
- T181 (≠ I582) binding
- H206 (≠ A606) to R: in MSUD1B; loss of 3-methyl-2-oxobutanoate dehydrogenase activity
- C228 (≠ L628) binding
- D231 (≠ A631) binding
- N233 (≠ E633) binding
2j9fD Human branched-chain alpha-ketoacid dehydrogenase-decarboxylase e1b (see paper)
32% identity, 35% coverage: 465:748/806 of query aligns to 2:285/329 of 2j9fD
1dtwB Human branched-chain alpha-keto acid dehydrogenase (see paper)
31% identity, 35% coverage: 468:748/806 of query aligns to 1:282/326 of 1dtwB
- active site: E60 (= E528), H130 (= H595)
- binding potassium ion: G112 (≠ A579), S113 (≠ P580), L114 (≠ V581), T115 (≠ I582), C162 (≠ L628), I163 (≠ F629), D165 (≠ A631), N167 (≠ E633), P168 (= P634), C169 (≠ A635)
1qs0B Crystal structure of pseudomonas putida 2-oxoisovalerate dehydrogenase (branched-chain alpha-keto acid dehydrogenase, e1b) (see paper)
30% identity, 38% coverage: 476:782/806 of query aligns to 9:326/338 of 1qs0B
6cerD Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
29% identity, 41% coverage: 469:795/806 of query aligns to 2:330/331 of 6cerD
6cfoB Human pyruvate dehydrogenase e1 component complex with covalent tdp adduct acetyl phosphinate (see paper)
29% identity, 41% coverage: 469:795/806 of query aligns to 1:329/330 of 6cfoB
P11177 Pyruvate dehydrogenase E1 component subunit beta, mitochondrial; PDHE1-B; EC 1.2.4.1 from Homo sapiens (Human) (see 6 papers)
29% identity, 40% coverage: 475:795/806 of query aligns to 36:358/359 of P11177
- E89 (= E528) binding
- E259 (≠ L695) mutation E->A,Q: Does not affect interaction with DLAT.
- E262 (≠ S698) mutation E->A,Q: Does not affect interaction with DLAT.
- E264 (= E700) mutation E->A,Q: Does not affect interaction with DLAT.
- D319 (≠ G757) 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)
29% identity, 35% coverage: 46:330/806 of query aligns to 59:304/367 of Q5SLR4
1umdA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methyl-2-oxopentanoate as an intermediate (see paper)
29% identity, 35% coverage: 46:330/806 of query aligns to 54:299/362 of 1umdA
- active site: S139 (≠ K141), R264 (≠ Q295), H268 (= H299), S269 (= S300), Y277 (= Y308)
- binding 2-oxo-4-methylpentanoic acid: F61 (= F53), Y90 (= Y81), S139 (≠ K141)
- binding magnesium ion: D170 (≠ N193), N199 (≠ D222), Y201 (= Y224)
- binding thiamine diphosphate: Y89 (= Y80), Y90 (= Y81), R91 (= R82), P140 (≠ N142), I141 (≠ C143), G169 (= G192), D170 (≠ N193), G171 (≠ A194), N199 (≠ D222), Y201 (= Y224), A202 (≠ G225), I203 (= I226), H268 (= H299)
Sites not aligning to the query:
1umcA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methylpentanoate (see paper)
29% identity, 35% coverage: 46:330/806 of query aligns to 54:299/362 of 1umcA
- active site: S139 (≠ K141), R264 (≠ Q295), H268 (= H299), S269 (= S300), Y277 (= Y308)
- binding 4-methyl valeric acid: Y90 (= Y81), H126 (= H122)
- binding magnesium ion: D170 (≠ N193), N199 (≠ D222), Y201 (= Y224)
- binding thiamine diphosphate: Y89 (= Y80), Y90 (= Y81), R91 (= R82), I141 (≠ C143), G169 (= G192), D170 (≠ N193), G171 (≠ A194), N199 (≠ D222), Y201 (= Y224), I203 (= I226), H268 (= H299)
Sites not aligning to the query:
1umbA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 in holo-form (see paper)
29% identity, 35% coverage: 46:330/806 of query aligns to 54:299/362 of 1umbA
- active site: S139 (≠ K141), R264 (≠ Q295), H268 (= H299), S269 (= S300), Y277 (= Y308)
- binding magnesium ion: D170 (≠ N193), N199 (≠ D222), Y201 (= Y224)
- binding thiamine diphosphate: Y89 (= Y80), Y90 (= Y81), R91 (= R82), P140 (≠ N142), I141 (≠ C143), G169 (= G192), D170 (≠ N193), G171 (≠ A194), N199 (≠ D222), Y201 (= Y224), A202 (≠ G225), I203 (= I226), H268 (= H299)
Sites not aligning to the query:
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)
26% identity, 39% coverage: 49:359/806 of query aligns to 126:397/445 of P12694
- Y158 (= Y81) binding
- R159 (= R82) binding ; to W: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs769688327
- Q190 (= Q118) to K: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- S206 (≠ I147) binding
- S207 (= S148) binding
- P208 (= P149) binding
- T211 (≠ G152) binding ; to M: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123503
- Q212 (= Q153) binding
- E238 (≠ N193) binding
- G239 (≠ A194) binding
- A240 (≠ S195) binding
- G249 (≠ A204) 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 (= A208) to T: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs199599175
- A254 (≠ G209) to D: in MSUD1A; uncertain significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity
- R265 (≠ W220) 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 (≠ D222) 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 (= Y224) binding
- A285 (≠ S240) 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 (= G254) 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 (≠ K259) to H: in MSUD1A; uncertain significance; decreased affinity for the cofactor thiamine diphosphate; decreased 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs200137189
- T310 (≠ Y272) to R: in MSUD1A; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852875
- I326 (= I288) to T: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
- H336 (= H299) binding
- S337 (= S300) modified: Phosphoserine; by BCKDK; mutation to A: Substantially decreases the stability of the BCKD complex.
- S347 (= S310) 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
>CA265_RS11665 FitnessBrowser__Pedo557:CA265_RS11665
MPNEKLMTNTIDASELSFNDFKSIVINDYKIAFESRQASVLGRREVLTGKAKFGIFGDGK
EVPQVAMAKAFKNGDWRSGYYRDQTFAFATGISTIKEFFAQLYANPTEGADPFSGGRQMN
CHFATKSVNEDGSWNDLTQIKNCSSDISPTGGQMARLVGLAYASKLFRQNKELDYLKNFS
VNGNEVAFGTIGNASTSEGVFFEAINAAGVLQIPMAISIWDDAYGISVPAKYQTTKEDIS
EVLKGFQRDADQPGYEIYKVKGWDYPALCEVYEKAIHVCRDEHVPVLIHVTELTQPQGHS
TSGSHERYKSKDRLSWETEHDCILKMRAWMLDSAVATEEEIAEIEKEAKVFVRNAQKEAW
NEFLDSIKPEQKQVIDLISGVAKHQPELAKIAASLASTADAQRREVFTAARKAIRLSASF
NSPERNELLAWYKQQAKFNYDRYNSKLHTNGKESPDMIAVVNAAYDEQSKMVDGREVLNA
CFNENFARDPRLVAFGEDLGNIGDVNQGFAGLQAKYGELRITDTGIREMTIMGQGIGLAM
RGLKPIAEIQYLDYLIFALNVLSDDLASLSYRTKGIQKAPVIVRTRGHRLEGIWHSGSPI
SMILGALRGMHLCVPRNMTQAAGMYNTLFRADEPAVVIECLNGYRLKEKLPVNVGEFTVP
LGKAEVLEEGTDITVISYGSSLRIVQEAAEELSLLGISVEIIDPQTLLPFDTTQVCVNSL
AKTNKLLVVDEDVPGGASAYILQKVLEEQKGYFHLDGQPKTLSAKAHRPPFGSDGDYFSK
PSVDDVIETIYQMMHDANPVKYPSFF
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