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Comparing 7023874 FitnessBrowser__ANA3:7023874 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)
84% identity, 100% coverage: 1:416/417 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 (≠ D245), E247 (= E247), N347 (= N347), S355 (= S355), P356 (= P356), F357 (= F357)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S35 (= S35), Y55 (= Y55), Y65 (= Y65), S97 (= S97), G98 (= G98), S99 (= S99), H126 (= H126), F174 (= F174), S175 (= S175), D200 (= D200), A202 (= A202), H203 (= H203), K229 (= K229), G262 (= G262), R363 (= R363)
P0A825 Serine hydroxymethyltransferase; SHMT; Serine methylase; EC 2.1.2.1 from Escherichia coli (strain K12) (see 8 papers)
84% identity, 100% coverage: 1:416/417 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 (= L85) 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 (≠ A242) modified: N6-succinyllysine
- K250 (= K250) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- P258 (= P258) mutation to A: Important decrease in affinity and catalytic efficiency. Reduced thermal stability.; mutation to G: Important decrease in affinity and catalytic efficiency.
- P264 (= P264) mutation to A: Important decrease in affinity and catalytic efficiency.; mutation to G: Important decrease in affinity and catalytic efficiency.
- L276 (≠ F276) 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 (= K277) modified: N6-succinyllysine
- K285 (= K285) modified: N6-acetyllysine
- K293 (= K293) modified: N6-succinyllysine
- K331 (= K331) modified: N6-succinyllysine
- K346 (= K346) modified: N6-succinyllysine
- K354 (≠ R354) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- R363 (= R363) 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 (= R372) mutation to A: No significant difference compared to the wild-type.; mutation to K: No significant difference compared to the wild-type.
- K375 (= K375) 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)
83% identity, 100% coverage: 2:416/417 of query aligns to 1:415/416 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 (= N347), S354 (= S355), P355 (= P356), F356 (= F357)
- binding glycine: S34 (= S35), Y54 (= Y55), F64 (≠ Y65), H202 (= H203), K228 (= K229), R362 (= R363)
- binding pyridoxal-5'-phosphate: S96 (= S97), G97 (= G98), S98 (= S99), H125 (= H126), F173 (= F174), S174 (= S175), D199 (= D200), H202 (= H203), H227 (= H228), K228 (= K229)
4n0wA X-ray crystal structure of a serine hydroxymethyltransferase from burkholderia cenocepacia with covalently attached pyridoxal phosphate
66% identity, 98% coverage: 8:416/417 of query aligns to 10:415/416 of 4n0wA
- active site: Y57 (= Y55), E59 (= E57), D202 (= D200), T228 (= T226), K231 (= K229), R237 (= R235)
- binding pyridoxal-5'-phosphate: S99 (= S97), G100 (= G98), S101 (= S99), H128 (= H126), D202 (= D200), A204 (= A202), H205 (= H203), K231 (= K229)
4otlA X-ray crystal structure of serine hydroxymethyl transferase from burkholderia cenocepacia bound to plp and glycine
66% identity, 98% coverage: 8:416/417 of query aligns to 3:408/409 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 (= R363)
- binding pyridoxal-5'-phosphate: S92 (= S97), G93 (= G98), S94 (= S99), H121 (= H126), 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
66% identity, 98% coverage: 8:416/417 of query aligns to 8:413/414 of 4ot8A
- active site: Y55 (= Y55), E57 (= E57), D200 (= D200), T226 (= T226), K229 (= K229), R235 (= R235)
- binding pyridoxal-5'-phosphate: S97 (= S97), G98 (= G98), S99 (= S99), H126 (= H126), D200 (= D200), A202 (= A202), H203 (= H203), K229 (= K229)
- binding serine: S35 (= S35), E57 (= E57), Y65 (= Y65), H126 (= H126), H203 (= H203), R360 (= R363)
7x5oB Crystal structure of e. Faecium shmt in complex with me-thf and plp- gly (see paper)
61% identity, 97% coverage: 11:416/417 of query aligns to 6:411/412 of 7x5oB
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S30 (= S35), Y50 (= Y55), Y60 (= Y65), S92 (= S97), G93 (= G98), S94 (= S99), H121 (= H126), S171 (= S175), D196 (= D200), A198 (= A202), H199 (= H203), K225 (= K229), R358 (= R363)
- 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 (= P258), N342 (= N347), P351 (= P356)
7x5nA Crystal structure of e. Faecium shmt in complex with (+)-shin-1 and plp-ser (see paper)
61% identity, 97% coverage: 11:415/417 of query aligns to 5:409/409 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 (= K346), N341 (= N347), S342 (= S348), P350 (= P356), F351 (= F357), R357 (= R363)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: S29 (= S35), Y49 (= Y55), E51 (= E57), Y59 (= Y65), S91 (= S97), G92 (= G98), S93 (= S99), H120 (= H126), S170 (= S175), D195 (= D200), A197 (= A202), H198 (= H203), K224 (= K229), R357 (= R363)
7v3dA Complex structure of serine hydroxymethyltransferase from enterococcus faecium and its inhibitor (see paper)
61% identity, 97% coverage: 11:415/417 of query aligns to 5:409/409 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 (= K346), S342 (= S348), P350 (= P356), F351 (= F357), R357 (= R363)
- binding pyridoxal-5'-phosphate: Y49 (= Y55), S91 (= S97), G92 (= G98), S93 (= S99), H120 (= H126), S170 (= S175), D195 (= D200), A197 (= A202), K224 (= K229), G255 (= G262)
4wxgA Crystal structure of l-serine hydroxymethyltransferase in complex with a mixture of l-threonine and glycine (see paper)
61% identity, 97% coverage: 11:416/417 of query aligns to 5:410/410 of 4wxgA
- active site: T43 (≠ S49), L45 (= L51), G189 (= G194), A215 (= A220), T218 (≠ V223), R230 (= R235)
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-threonine: S29 (= S35), Y49 (= Y55), E51 (= E57), Y59 (= Y65), S91 (= S97), G92 (= G98), S93 (= S99), H120 (= H126), S170 (= S175), D195 (= D200), A197 (= A202), H198 (= H203), T221 (= T226), K224 (= K229), G255 (= G262), R357 (= R363)
4wxfA Crystal structure of l-serine hydroxymethyltransferase in complex with glycine (see paper)
61% identity, 97% coverage: 11:416/417 of query aligns to 5:410/410 of 4wxfA
- active site: T43 (≠ S49), L45 (= L51), G189 (= G194), A215 (= A220), T218 (≠ V223), R230 (= R235)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S29 (= S35), Y49 (= Y55), Y59 (= Y65), S91 (= S97), G92 (= G98), S93 (= S99), H120 (= H126), S170 (= S175), D195 (= D200), A197 (= A202), H198 (= H203), H223 (= H228), K224 (= K229), G255 (= G262), R357 (= R363)
6ymdA Crystal structure of serine hydroxymethyltransferase from aphanothece halophytica in the covalent complex with malonate (see paper)
59% identity, 97% coverage: 12:416/417 of query aligns to 11:414/420 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 (= R363)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: Y54 (= Y55), S96 (= S97), G97 (= G98), A98 (≠ S99), H125 (= H126), Y174 (≠ F174), S175 (= S175), D200 (= D200), A202 (= A202), T226 (= T226), K229 (= K229), G261 (= G263)
6ymfA Crystal structure of serine hydroxymethyltransferase from aphanothece halophytica in the plp-serine external aldimine state (see paper)
59% identity, 97% coverage: 12:416/417 of query aligns to 11:414/418 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 (= S97), G97 (= G98), A98 (≠ S99), H125 (= H126), S175 (= S175), D200 (= D200), A202 (= A202), H203 (= H203), T226 (= T226), K229 (= K229), R361 (= R363)
6ti4A Shmt from streptococcus thermophilus tyr55ser variant in complex with plp/d-serine/lys230 gem diamine complex
61% identity, 97% coverage: 11:416/417 of query aligns to 5:410/410 of 6ti4A
- active site: S49 (≠ Y55), E51 (= E57), D195 (= D200), T221 (= T226), K224 (= K229), R230 (= R235)
- binding magnesium ion: A50 (= A56), E51 (= E57), Y58 (= Y64), Y59 (= Y65)
- binding (2~{R})-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]-3-oxidanyl-propanoic acid: E51 (= E57), Y59 (= Y65), S91 (= S97), G92 (= G98), S93 (= S99), H120 (= H126), S170 (= S175), D195 (= D200), A197 (= A202), H198 (= H203), K224 (= K229), G255 (= G262), R357 (= R363)
6ti3A Apo-shmt from streptococcus thermophilus tyr55ser variant in complex with d-threonine
61% identity, 97% coverage: 11:416/417 of query aligns to 5:410/410 of 6ti3A
- active site: S49 (≠ Y55), E51 (= E57), D195 (= D200), T221 (= T226), K224 (= K229), R230 (= R235)
- binding d-threonine: S91 (= S97), G92 (= G98), S93 (= S99), H223 (= H228), G255 (= G262), G256 (= G263)
6tghC Shmt from streptococcus thermophilus tyr55thr variant in complex with d-serine both as external aldimine and as non-covalent complex
61% identity, 97% coverage: 11:416/417 of query aligns to 5:410/410 of 6tghC
- active site: T49 (≠ Y55), E51 (= E57), D195 (= D200), T221 (= T226), K224 (= K229), R230 (= R235)
- binding d-serine: S29 (= S35), H198 (= H203), R357 (= R363)
- binding L-Serine, N-[[3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]-4-pyridinyl]methylene]: E51 (= E57), G255 (= G262)
- binding pyridoxal-5'-phosphate: S91 (= S97), G92 (= G98), S93 (= S99), H120 (= H126), D195 (= D200), A197 (= A202), H198 (= H203), T221 (= T226), K224 (= K229)
6tghA Shmt from streptococcus thermophilus tyr55thr variant in complex with d-serine both as external aldimine and as non-covalent complex
61% identity, 97% coverage: 11:416/417 of query aligns to 5:410/410 of 6tghA
- active site: T49 (≠ Y55), E51 (= E57), D195 (= D200), T221 (= T226), K224 (= K229), R230 (= R235)
- binding d-serine: E51 (= E57), Y59 (= Y65)
- binding L-Serine, N-[[3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]-4-pyridinyl]methylene]: S29 (= S35), S91 (= S97), G92 (= G98), S93 (= S99), H120 (= H126), S170 (= S175), D195 (= D200), A197 (= A202), H198 (= H203), K224 (= K229), R357 (= R363)
1kl2A Crystal structure of serine hydroxymethyltransferase complexed with glycine and 5-formyl tetrahydrofolate (see paper)
61% identity, 96% coverage: 12:410/417 of query aligns to 8:404/405 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 (= F257), N341 (= N347)
- binding glycine: S31 (= S35), Y51 (= Y55), Y61 (= Y65), H200 (= H203), R357 (= R363)
- binding pyridoxal-5'-phosphate: S93 (= S97), G94 (= G98), A95 (≠ S99), 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)
61% identity, 96% coverage: 12:410/417 of query aligns to 8:404/405 of 1kl1A
- active site: Y51 (= Y55), E53 (= E57), D197 (= D200), T223 (= T226), K226 (= K229), R232 (= R235)
- binding glycine: S31 (= S35), H122 (= H126), R357 (= R363)
- binding pyridoxal-5'-phosphate: S93 (= S97), G94 (= G98), A95 (≠ S99), H122 (= H126), A171 (≠ F174), 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)
61% identity, 96% coverage: 12:410/417 of query aligns to 8:404/405 of 1kkpA
- active site: Y51 (= Y55), E53 (= E57), D197 (= D200), T223 (= T226), K226 (= K229), R232 (= R235)
- binding pyridoxal-5'-phosphate: S93 (= S97), G94 (= G98), A95 (≠ S99), H122 (= H126), S172 (= S175), D197 (= D200), A199 (= A202), H200 (= H203), K226 (= K229)
- binding serine: S31 (= S35), H122 (= H126), R357 (= R363)
Query Sequence
>7023874 FitnessBrowser__ANA3:7023874
MLKKDMNIADYDPELFNAIQNETLRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYP
GKRYYGGCEYVDVVETLAIERAKQLFGATYANVQPHSGSQANSAVYMALLKPGDTVLGMN
LAHGGHLTHGSPVNFSGRLYNIIPYGIDESGKIDYDEMERLAVEHKPKMMIGGFSAYSGI
VDWARMREIADKIGAYLFVDMAHVAGLIAAGVYPNPVPHAHVVTSTTHKTLAGPRGGIIL
SAADDEELYKKLNSAVFPGGQGGPLMHVIAGKAVAFKEALEPEFKAYQQQVVKNAKAMVE
VFLERGYKIVSGGTDNHLMLVDLIGRDLTGKEADAALGSANITVNKNSVPNDPRSPFVTS
GVRIGTPAITRRGFKEAEAKELTGWICDILDDAHNPAVIERVKGQVLALCARFPVYG
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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