SitesBLAST
Comparing Ac3H11_2921 FitnessBrowser__acidovorax_3H11:Ac3H11_2921 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)
4n0wA X-ray crystal structure of a serine hydroxymethyltransferase from burkholderia cenocepacia with covalently attached pyridoxal phosphate
78% identity, 100% coverage: 1:414/414 of query aligns to 2:416/416 of 4n0wA
- active site: Y57 (= Y55), E59 (= E57), D202 (= D200), T228 (= T226), K231 (= K229), R237 (= R235)
- binding pyridoxal-5'-phosphate: S99 (≠ C97), G100 (= G98), S101 (≠ A99), H128 (= H126), D202 (= D200), A204 (= A202), H205 (= H203), K231 (= K229)
4ot8A X-ray crystal structure of serine hydroxymethyl transferase from burkholderia cenocepacia bound to plp and serine
78% identity, 100% coverage: 2:414/414 of query aligns to 1:414/414 of 4ot8A
- active site: Y55 (= Y55), E57 (= E57), D200 (= D200), T226 (= T226), K229 (= K229), R235 (= R235)
- binding pyridoxal-5'-phosphate: S97 (≠ C97), G98 (= G98), S99 (≠ A99), H126 (= H126), D200 (= D200), A202 (= A202), H203 (= H203), K229 (= K229)
- binding serine: S35 (= S35), E57 (= E57), Y65 (= Y65), H126 (= H126), H203 (= H203), R360 (= R360)
4otlA X-ray crystal structure of serine hydroxymethyl transferase from burkholderia cenocepacia bound to plp and glycine
78% identity, 98% coverage: 8:414/414 of query aligns to 3:409/409 of 4otlA
- active site: Y50 (= Y55), E52 (= E57), D195 (= D200), T221 (= T226), K224 (= K229), R230 (= R235)
- binding glycine: S30 (= S35), Y50 (= Y55), Y60 (= Y65), H121 (= H126), K224 (= K229), R355 (= R360)
- binding pyridoxal-5'-phosphate: S92 (≠ C97), G93 (= G98), S94 (≠ A99), H121 (= H126), S170 (= S175), D195 (= D200), A197 (= A202), H198 (= H203), K224 (= K229)
1dfoB Crystal structure at 2.4 angstrom resolution of e. Coli serine hydroxymethyltransferase in complex with glycine and 5-formyl tetrahydrofolate (see paper)
63% identity, 100% coverage: 1:413/414 of query aligns to 1:416/417 of 1dfoB
- active site: Y55 (= Y55), E57 (= E57), D200 (= D200), T226 (= T226), K229 (= K229), R235 (= R235)
- binding N-[4-({[(6S)-2-amino-5-formyl-4-oxo-3,4,5,6,7,8-hexahydropteridin-6-yl]methyl}amino)benzoyl]-L-glutamic acid: E57 (= E57), Y64 (= Y64), Y65 (= Y65), L121 (= L121), G125 (= G125), H126 (= H126), L127 (= L127), S175 (= S175), S245 (≠ H245), E247 (vs. gap), N347 (= N344), S355 (≠ K352), P356 (= P353), F357 (≠ M354)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S35 (= S35), Y55 (= Y55), Y65 (= Y65), S97 (≠ C97), G98 (= G98), S99 (≠ A99), H126 (= H126), F174 (≠ A174), S175 (= S175), D200 (= D200), A202 (= A202), H203 (= H203), K229 (= K229), G262 (= G259), R363 (= R360)
P0A825 Serine hydroxymethyltransferase; SHMT; Serine methylase; EC 2.1.2.1 from Escherichia coli (strain K12) (see 8 papers)
63% identity, 100% coverage: 1:413/414 of query aligns to 1:416/417 of P0A825
- K54 (= K54) modified: N6-acetyllysine
- Y55 (= Y55) mutation to F: 50 and 15-fold increase in the affinity for serine and tetrahydrofolate, respectively, and 4-fold decrease in the catalytic efficiency.
- K62 (= K62) modified: N6-succinyllysine
- Y65 (= Y65) mutation to F: Decrease in catalytic activity.
- L85 (≠ I85) mutation to A: Alteration of the dimer-monomer equilibrium accompanied by minor changes in the catalytic properties and whitout any significant change of tertiary structure. In the monomeric state; when associated with A-276.
- P214 (= P214) mutation to A: No significant difference in catalytic efficiency and affinity compared to the wild-type.; mutation to G: No significant difference in catalytic efficiency and affinity compared to the wild-type.
- P216 (= P216) mutation to A: No significant difference in catalytic efficiency and affinity compared to the wild-type. Alteration in the folding rate.; mutation to G: Important decrease in affinity and catalytic efficiency. Severely compromised in folding into a catalytically competent enzyme.
- P218 (= P218) mutation to A: No significant difference in catalytic efficiency and affinity compared to the wild-type.; mutation to G: No significant difference in catalytic efficiency and affinity compared to the wild-type.
- H228 (= H228) Plays an important role in substrate specificity; binding ; mutation H->D,N: Utilize substrates and substrate analogs more effectively for a variety of alternate non-physiological reactions.
- K229 (= K229) modified: N6-(pyridoxal phosphate)lysine
- R235 (= R235) binding ; mutation to K: 1500- and 20-fold increase in the affinity for serine and tetrahydrofolate, respectively, and 15-fold decrease in the catalytic efficiency.; mutation to L: 450- and 11-fold increase in the affinity for serine and tetrahydrofolate, respectively, and 60-fold decrease in the catalytic efficiency.; mutation to Q: 900- and 17-fold increase in the affinity for serine and tetrahydrofolate, respectively, and 30-fold decrease in the catalytic efficiency.
- K242 (= K242) modified: N6-succinyllysine
- K250 (= K247) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- P258 (= P255) mutation to A: Important decrease in affinity and catalytic efficiency. Reduced thermal stability.; mutation to G: Important decrease in affinity and catalytic efficiency.
- P264 (= P261) mutation to A: Important decrease in affinity and catalytic efficiency.; mutation to G: Important decrease in affinity and catalytic efficiency.
- L276 (≠ F273) mutation to A: Alteration of the dimer-monomer equilibrium accompanied by minor changes in the catalytic properties and whitout any significant change of tertiary structure. In the monomeric state; when associated with A-85.
- K277 (= K274) modified: N6-succinyllysine
- K285 (= K282) modified: N6-acetyllysine
- K293 (= K290) modified: N6-succinyllysine
- K331 (= K328) modified: N6-succinyllysine
- K346 (= K343) modified: N6-succinyllysine
- K354 (≠ E351) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- R363 (= R360) mutation to A: It does not bind serine and glycine and shows no activity with serine as the substrate.; mutation to K: Exhibits only 0.03% of the catalytic activity of the wild-type and a 15-fold reduction in affinity for glycine and serine.
- R372 (= R369) mutation to A: No significant difference compared to the wild-type.; mutation to K: No significant difference compared to the wild-type.
- K375 (= K372) modified: N6-acetyllysine
1eqbA X-ray crystal structure at 2.7 angstroms resolution of ternary complex between the y65f mutant of e-coli serine hydroxymethyltransferase, glycine and 5-formyl tetrahydrofolate (see paper)
62% identity, 99% coverage: 4:413/414 of query aligns to 3:415/416 of 1eqbA
- active site: Y54 (= Y55), E56 (= E57), D199 (= D200), T225 (= T226), K228 (= K229), R234 (= R235)
- binding N-[4-({[(6S)-2-amino-5-formyl-4-oxo-3,4,5,6,7,8-hexahydropteridin-6-yl]methyl}amino)benzoyl]-L-glutamic acid: E56 (= E57), Y63 (= Y64), L120 (= L121), G123 (= G124), G124 (= G125), H125 (= H126), L126 (= L127), S174 (= S175), N346 (= N344), S354 (≠ K352), P355 (= P353), F356 (≠ M354)
- binding glycine: S34 (= S35), Y54 (= Y55), F64 (≠ Y65), H202 (= H203), K228 (= K229), R362 (= R360)
- binding pyridoxal-5'-phosphate: S96 (≠ C97), G97 (= G98), S98 (≠ A99), H125 (= H126), F173 (≠ A174), S174 (= S175), D199 (= D200), H202 (= H203), H227 (= H228), K228 (= K229)
6ymfA Crystal structure of serine hydroxymethyltransferase from aphanothece halophytica in the plp-serine external aldimine state (see paper)
59% identity, 98% coverage: 10:413/414 of query aligns to 9:414/418 of 6ymfA
- active site: Y54 (= Y55), E56 (= E57), D200 (= D200), T226 (= T226), K229 (= K229), R235 (= R235)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: S34 (= S35), S96 (≠ C97), G97 (= G98), A98 (= A99), H125 (= H126), S175 (= S175), D200 (= D200), A202 (= A202), H203 (= H203), T226 (= T226), K229 (= K229), R361 (= R360)
6ymdA Crystal structure of serine hydroxymethyltransferase from aphanothece halophytica in the covalent complex with malonate (see paper)
59% identity, 98% coverage: 10:413/414 of query aligns to 9:414/420 of 6ymdA
- active site: Y54 (= Y55), E56 (= E57), D200 (= D200), T226 (= T226), K229 (= K229), R235 (= R235)
- binding malonate ion: S34 (= S35), Y54 (= Y55), E56 (= E57), Y64 (= Y65), H125 (= H126), H203 (= H203), K229 (= K229), R361 (= R360)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: Y54 (= Y55), S96 (≠ C97), G97 (= G98), A98 (= A99), H125 (= H126), Y174 (≠ A174), S175 (= S175), D200 (= D200), A202 (= A202), T226 (= T226), K229 (= K229), G261 (= G260)
7x5oB Crystal structure of e. Faecium shmt in complex with me-thf and plp- gly (see paper)
59% identity, 97% coverage: 12:414/414 of query aligns to 7:412/412 of 7x5oB
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S30 (= S35), Y50 (= Y55), Y60 (= Y65), S92 (≠ C97), G93 (= G98), S94 (≠ A99), H121 (= H126), S171 (= S175), D196 (= D200), A198 (= A202), H199 (= H203), K225 (= K229), R358 (= R360)
- binding n-[4-({[(6s)-2-amino-4-hydroxy-5-methyl-5,6,7,8-tetrahydropteridin-6-yl]methyl}amino)benzoyl]-l-glutamic acid: E52 (= E57), Y59 (= Y64), L116 (= L121), G119 (= G124), G120 (= G125), H121 (= H126), S171 (= S175), P252 (= P255), N342 (= N344), P351 (= P353)
7x5nA Crystal structure of e. Faecium shmt in complex with (+)-shin-1 and plp-ser (see paper)
59% identity, 97% coverage: 12:412/414 of query aligns to 6:409/409 of 7x5nA
- binding (4R)-6-azanyl-4-[3-(hydroxymethyl)-5-phenyl-phenyl]-3-methyl-4-propan-2-yl-1H-pyrano[2,3-c]pyrazole-5-carbonitrile: E51 (= E57), Y58 (= Y64), Y59 (= Y65), L115 (= L121), G119 (= G125), H120 (= H126), L121 (= L127), K340 (= K343), N341 (= N344), S342 (≠ A345), P350 (= P353), F351 (≠ M354), R357 (= R360)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: S29 (= S35), Y49 (= Y55), E51 (= E57), Y59 (= Y65), S91 (≠ C97), G92 (= G98), S93 (≠ A99), H120 (= H126), S170 (= S175), D195 (= D200), A197 (= A202), H198 (= H203), K224 (= K229), R357 (= R360)
7v3dA Complex structure of serine hydroxymethyltransferase from enterococcus faecium and its inhibitor (see paper)
59% identity, 97% coverage: 12:412/414 of query aligns to 6:409/409 of 7v3dA
- binding (4R)-6-azanyl-4-[3-(hydroxymethyl)-5-phenyl-phenyl]-3-methyl-4-propan-2-yl-1H-pyrano[2,3-c]pyrazole-5-carbonitrile: E51 (= E57), Y58 (= Y64), L115 (= L121), G119 (= G125), H120 (= H126), L121 (= L127), K340 (= K343), S342 (≠ A345), P350 (= P353), F351 (≠ M354), R357 (= R360)
- binding pyridoxal-5'-phosphate: Y49 (= Y55), S91 (≠ C97), G92 (= G98), S93 (≠ A99), H120 (= H126), S170 (= S175), D195 (= D200), A197 (= A202), K224 (= K229), G255 (= G259)
1kl2A Crystal structure of serine hydroxymethyltransferase complexed with glycine and 5-formyl tetrahydrofolate (see paper)
60% identity, 96% coverage: 10:407/414 of query aligns to 6:404/405 of 1kl2A
- active site: Y51 (= Y55), E53 (= E57), D197 (= D200), T223 (= T226), K226 (= K229), R232 (= R235)
- binding N-{[4-({[(6R)-2-amino-5-formyl-4-oxo-1,4,5,6,7,8-hexahydropteridin-6-yl]methyl}amino)phenyl]carbonyl}-L-glutamic acid: E53 (= E57), Y60 (= Y64), G121 (= G125), H122 (= H126), S172 (= S175), F251 (= F254), N341 (= N344)
- binding glycine: S31 (= S35), Y51 (= Y55), Y61 (= Y65), H200 (= H203), R357 (= R360)
- binding pyridoxal-5'-phosphate: S93 (≠ C97), G94 (= G98), A95 (= A99), H122 (= H126), S172 (= S175), D197 (= D200), A199 (= A202), H200 (= H203), T223 (= T226), H225 (= H228), K226 (= K229)
1kl1A Crystal structure of serine hydroxymethyltransferase complexed with glycine (see paper)
60% identity, 96% coverage: 10:407/414 of query aligns to 6:404/405 of 1kl1A
- active site: Y51 (= Y55), E53 (= E57), D197 (= D200), T223 (= T226), K226 (= K229), R232 (= R235)
- binding glycine: S31 (= S35), H122 (= H126), R357 (= R360)
- binding pyridoxal-5'-phosphate: S93 (≠ C97), G94 (= G98), A95 (= A99), H122 (= H126), A171 (= A174), S172 (= S175), D197 (= D200), A199 (= A202), H200 (= H203), T223 (= T226), H225 (= H228), K226 (= K229)
1kkpA Crystal structure of serine hydroxymethyltransferase complexed with serine (see paper)
60% identity, 96% coverage: 10:407/414 of query aligns to 6:404/405 of 1kkpA
- active site: Y51 (= Y55), E53 (= E57), D197 (= D200), T223 (= T226), K226 (= K229), R232 (= R235)
- binding pyridoxal-5'-phosphate: S93 (≠ C97), G94 (= G98), A95 (= A99), H122 (= H126), S172 (= S175), D197 (= D200), A199 (= A202), H200 (= H203), K226 (= K229)
- binding serine: S31 (= S35), H122 (= H126), R357 (= R360)
1kkjA Crystal structure of serine hydroxymethyltransferase from b.Stearothermophilus (see paper)
60% identity, 96% coverage: 10:407/414 of query aligns to 6:404/405 of 1kkjA
- active site: Y51 (= Y55), E53 (= E57), D197 (= D200), T223 (= T226), K226 (= K229), R232 (= R235)
- binding pyridoxal-5'-phosphate: S93 (≠ C97), G94 (= G98), A95 (= A99), H122 (= H126), S172 (= S175), D197 (= D200), A199 (= A202), H200 (= H203), T223 (= T226), H225 (= H228), K226 (= K229)
2vmyA Crystal structure of f351gbsshmt in complex with gly and fthf (see paper)
60% identity, 96% coverage: 10:407/414 of query aligns to 6:404/405 of 2vmyA
- active site: Y51 (= Y55), E53 (= E57), D197 (= D200), T223 (= T226), K226 (= K229), R232 (= R235)
- binding N-[4-({[(6S)-2-amino-5-formyl-4-oxo-3,4,5,6,7,8-hexahydropteridin-6-yl]methyl}amino)benzoyl]-L-glutamic acid: E53 (= E57), Y60 (= Y64), Y61 (= Y65), L117 (= L121), G121 (= G125), H122 (= H126), L123 (= L127), S172 (= S175), K248 (≠ S251), F251 (= F254), N341 (= N344), S349 (≠ K352), P350 (= P353), G351 (≠ M354), R357 (= R360)
- binding glycine: S31 (= S35), Y51 (= Y55), Y61 (= Y65), H200 (= H203), K226 (= K229), R357 (= R360)
- binding pyridoxal-5'-phosphate: Y51 (= Y55), S93 (≠ C97), G94 (= G98), A95 (= A99), H122 (= H126), S172 (= S175), D197 (= D200), A199 (= A202), H200 (= H203), T223 (= T226), K226 (= K229), G257 (= G260)
2vmxA Crystal structure of f351gbsshmt in complex with l-allo-thr (see paper)
60% identity, 96% coverage: 10:407/414 of query aligns to 6:404/405 of 2vmxA
- active site: Y51 (= Y55), E53 (= E57), D197 (= D200), T223 (= T226), K226 (= K229), R232 (= R235)
- binding allo-threonine: S31 (= S35), H122 (= H126), H200 (= H203), R357 (= R360)
- binding pyridoxal-5'-phosphate: S93 (≠ C97), G94 (= G98), A95 (= A99), H122 (= H126), S172 (= S175), D197 (= D200), A199 (= A202), H200 (= H203), T223 (= T226), K226 (= K229)
3pgyB Serine hydroxymethyltransferase from staphylococcus aureus, s95p mutant.
58% identity, 98% coverage: 8:413/414 of query aligns to 4:404/404 of 3pgyB
8suiB Joint x-ray/neutron structure of thermus thermophilus serine hydroxymethyltransferase (tthshmt) in internal aldimine state with l- ser bound in a pre-michalis complex (see paper)
58% identity, 97% coverage: 10:412/414 of query aligns to 1:401/402 of 8suiB
8ssyA Room-temperature x-ray structure of thermus thermophilus serine hydroxymethyltransferase (shmt) bound with d-ser in a pseudo- michaelis complex (see paper)
58% identity, 97% coverage: 10:412/414 of query aligns to 1:401/402 of 8ssyA
Query Sequence
>Ac3H11_2921 FitnessBrowser__acidovorax_3H11:Ac3H11_2921
MYDRNILVEQTDPEVFAAIQAENARQEHHIELIASENYASPAVMWAQGTQLTNKYAEGYP
GKRYYGGCEHVDVAEQLAIDRVKKIFGADAANVQPHCGASANEAVFLAFLKPGDTIMGMS
LAEGGHLTHGMPLNMSGKWFNVVSYGLDKNEAIDYDAMEAKAREHKPKLIVAGASAYSLH
IDFERFAKIAKEIGAIFMVDMAHYAGLIAAGVYPNPVPHADVVTSTTHKSLRGPRGGIIL
MKAEHEKAINSAIFPGLQGGPLMHVIAAKAVAFKEAMQPEFKAYQEQVAKNAKVVAETLT
ARGLRIVSGGTQSHVMLVDLRAKGITGKEAEAVLGAAHMTINKNAIPNDPEKPMVTSGVR
IGTPAMTTRGFKEEEARITANLIADVLDNPRDEANIAAVRAKVNALTARFPVYR
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