SitesBLAST
Comparing WP_011512688.1 NCBI__GCF_000013905.1:WP_011512688.1 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)
1dfoB Crystal structure at 2.4 angstrom resolution of e. Coli serine hydroxymethyltransferase in complex with glycine and 5-formyl tetrahydrofolate (see paper)
71% identity, 99% coverage: 3:415/418 of query aligns to 4:417/417 of 1dfoB
- active site: Y55 (= Y54), E57 (= E56), 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 (= E56), Y64 (= Y63), Y65 (= Y64), L121 (= L120), G125 (= G124), H126 (= H125), L127 (= L126), S175 (= S175), S245 (≠ D243), E247 (≠ V245), N347 (= N345), S355 (= S353), P356 (= P354), F357 (= F355)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S35 (= S34), Y55 (= Y54), Y65 (= Y64), S97 (= S96), G98 (= G97), S99 (= S98), H126 (= H125), F174 (= F174), S175 (= S175), D200 (= D200), A202 (= A202), H203 (= H203), K229 (= K229), G262 (= G260), R363 (= R361)
P0A825 Serine hydroxymethyltransferase; SHMT; Serine methylase; EC 2.1.2.1 from Escherichia coli (strain K12) (see 8 papers)
71% identity, 99% coverage: 3:415/418 of query aligns to 4:417/417 of P0A825
- K54 (= K53) modified: N6-acetyllysine
- Y55 (= Y54) 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 (= K61) modified: N6-succinyllysine
- Y65 (= Y64) mutation to F: Decrease in catalytic activity.
- L85 (= L84) 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 pyridoxal 5'-phosphate; 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 pyridoxal 5'-phosphate; 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 (≠ R242) modified: N6-succinyllysine
- K250 (= K248) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- P258 (= P256) mutation to A: Important decrease in affinity and catalytic efficiency. Reduced thermal stability.; mutation to G: Important decrease in affinity and catalytic efficiency.
- P264 (= P262) mutation to A: Important decrease in affinity and catalytic efficiency.; mutation to G: Important decrease in affinity and catalytic efficiency.
- L276 (≠ F274) 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 (= K275) modified: N6-succinyllysine
- K285 (= K283) modified: N6-acetyllysine
- K293 (= K291) modified: N6-succinyllysine
- K331 (= K329) modified: N6-succinyllysine
- K346 (= K344) modified: N6-succinyllysine
- K354 (= K352) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- R363 (= R361) 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 (= R370) mutation to A: No significant difference compared to the wild-type.; mutation to K: No significant difference compared to the wild-type.
- K375 (≠ N373) 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)
71% identity, 99% coverage: 3:415/418 of query aligns to 3:416/416 of 1eqbA
- active site: Y54 (= Y54), E56 (= E56), 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 (= E56), Y63 (= Y63), L120 (= L120), G123 (= G123), G124 (= G124), H125 (= H125), L126 (= L126), S174 (= S175), N346 (= N345), S354 (= S353), P355 (= P354), F356 (= F355)
- binding glycine: S34 (= S34), Y54 (= Y54), F64 (≠ Y64), H202 (= H203), K228 (= K229), R362 (= R361)
- binding pyridoxal-5'-phosphate: S96 (= S96), G97 (= G97), S98 (= S98), H125 (= H125), F173 (= F174), S174 (= S175), D199 (= D200), H202 (= H203), H227 (= H228), K228 (= K229)
4otlA X-ray crystal structure of serine hydroxymethyl transferase from burkholderia cenocepacia bound to plp and glycine
62% identity, 98% coverage: 6:414/418 of query aligns to 2:408/409 of 4otlA
- active site: Y50 (= Y54), E52 (= E56), D195 (= D200), T221 (= T226), K224 (= K229), R230 (= R235)
- binding glycine: S30 (= S34), Y50 (= Y54), Y60 (= Y64), H121 (= H125), K224 (= K229), R355 (= R361)
- binding pyridoxal-5'-phosphate: S92 (= S96), G93 (= G97), S94 (= S98), H121 (= H125), S170 (= S175), D195 (= D200), A197 (= A202), H198 (= H203), K224 (= K229)
4ot8A X-ray crystal structure of serine hydroxymethyl transferase from burkholderia cenocepacia bound to plp and serine
62% identity, 98% coverage: 6:414/418 of query aligns to 7:413/414 of 4ot8A
- active site: Y55 (= Y54), E57 (= E56), D200 (= D200), T226 (= T226), K229 (= K229), R235 (= R235)
- binding pyridoxal-5'-phosphate: S97 (= S96), G98 (= G97), S99 (= S98), H126 (= H125), D200 (= D200), A202 (= A202), H203 (= H203), K229 (= K229)
- binding serine: S35 (= S34), E57 (= E56), Y65 (= Y64), H126 (= H125), H203 (= H203), R360 (= R361)
4n0wA X-ray crystal structure of a serine hydroxymethyltransferase from burkholderia cenocepacia with covalently attached pyridoxal phosphate
62% identity, 98% coverage: 6:414/418 of query aligns to 9:415/416 of 4n0wA
- active site: Y57 (= Y54), E59 (= E56), D202 (= D200), T228 (= T226), K231 (= K229), R237 (= R235)
- binding pyridoxal-5'-phosphate: S99 (= S96), G100 (= G97), S101 (= S98), H128 (= H125), D202 (= D200), A204 (= A202), H205 (= H203), K231 (= K229)
7x5oB Crystal structure of e. Faecium shmt in complex with me-thf and plp- gly (see paper)
61% identity, 98% coverage: 5:414/418 of query aligns to 1:411/412 of 7x5oB
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S30 (= S34), Y50 (= Y54), Y60 (= Y64), S92 (= S96), G93 (= G97), S94 (= S98), H121 (= H125), S171 (= S175), D196 (= D200), A198 (= A202), H199 (= H203), K225 (= K229), R358 (= R361)
- binding n-[4-({[(6s)-2-amino-4-hydroxy-5-methyl-5,6,7,8-tetrahydropteridin-6-yl]methyl}amino)benzoyl]-l-glutamic acid: E52 (= E56), Y59 (= Y63), L116 (= L120), G119 (= G123), G120 (= G124), H121 (= H125), S171 (= S175), P252 (= P256), N342 (= N345), P351 (= P354)
7x5nA Crystal structure of e. Faecium shmt in complex with (+)-shin-1 and plp-ser (see paper)
62% identity, 97% coverage: 8:413/418 of query aligns to 3:409/409 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 (= E56), Y58 (= Y63), Y59 (= Y64), L115 (= L120), G119 (= G124), H120 (= H125), L121 (= L126), K340 (= K344), N341 (= N345), S342 (≠ A346), P350 (= P354), F351 (= F355), R357 (= R361)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: S29 (= S34), Y49 (= Y54), E51 (= E56), Y59 (= Y64), S91 (= S96), G92 (= G97), S93 (= S98), H120 (= H125), S170 (= S175), D195 (= D200), A197 (= A202), H198 (= H203), K224 (= K229), R357 (= R361)
7v3dA Complex structure of serine hydroxymethyltransferase from enterococcus faecium and its inhibitor (see paper)
62% identity, 97% coverage: 8:413/418 of query aligns to 3:409/409 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 (= E56), Y58 (= Y63), L115 (= L120), G119 (= G124), H120 (= H125), L121 (= L126), K340 (= K344), S342 (≠ A346), P350 (= P354), F351 (= F355), R357 (= R361)
- binding pyridoxal-5'-phosphate: Y49 (= Y54), S91 (= S96), G92 (= G97), S93 (= S98), H120 (= H125), S170 (= S175), D195 (= D200), A197 (= A202), K224 (= K229), G255 (= G260)
1kl2A Crystal structure of serine hydroxymethyltransferase complexed with glycine and 5-formyl tetrahydrofolate (see paper)
60% identity, 95% coverage: 11:408/418 of query aligns to 8:404/405 of 1kl2A
- active site: Y51 (= Y54), E53 (= E56), 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 (= E56), Y60 (= Y63), G121 (= G124), H122 (= H125), S172 (= S175), F251 (= F255), N341 (= N345)
- binding glycine: S31 (= S34), Y51 (= Y54), Y61 (= Y64), H200 (= H203), R357 (= R361)
- binding pyridoxal-5'-phosphate: S93 (= S96), G94 (= G97), A95 (≠ S98), H122 (= H125), 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, 95% coverage: 11:408/418 of query aligns to 8:404/405 of 1kl1A