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Comparing AO356_16850 FitnessBrowser__pseudo5_N2C3_1:AO356_16850 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)
4otlA X-ray crystal structure of serine hydroxymethyl transferase from burkholderia cenocepacia bound to plp and glycine
65% identity, 99% coverage: 2:409/412 of query aligns to 2:408/409 of 4otlA
- active site: Y50 (= Y50), E52 (= E52), D195 (= D196), T221 (= T222), K224 (= K225), R230 (= R231)
- binding glycine: S30 (= S30), Y50 (= Y50), Y60 (= Y60), H121 (= H121), K224 (= K225), R355 (= R356)
- binding pyridoxal-5'-phosphate: S92 (= S92), G93 (= G93), S94 (= S94), H121 (= H121), S170 (= S171), D195 (= D196), A197 (= A198), H198 (= H199), K224 (= K225)
4n0wA X-ray crystal structure of a serine hydroxymethyltransferase from burkholderia cenocepacia with covalently attached pyridoxal phosphate
65% identity, 99% coverage: 2:409/412 of query aligns to 9:415/416 of 4n0wA
- active site: Y57 (= Y50), E59 (= E52), D202 (= D196), T228 (= T222), K231 (= K225), R237 (= R231)
- binding pyridoxal-5'-phosphate: S99 (= S92), G100 (= G93), S101 (= S94), H128 (= H121), D202 (= D196), A204 (= A198), H205 (= H199), K231 (= K225)
4ot8A X-ray crystal structure of serine hydroxymethyl transferase from burkholderia cenocepacia bound to plp and serine
65% identity, 99% coverage: 2:409/412 of query aligns to 7:413/414 of 4ot8A
- active site: Y55 (= Y50), E57 (= E52), D200 (= D196), T226 (= T222), K229 (= K225), R235 (= R231)
- binding pyridoxal-5'-phosphate: S97 (= S92), G98 (= G93), S99 (= S94), H126 (= H121), D200 (= D196), A202 (= A198), H203 (= H199), K229 (= K225)
- binding serine: S35 (= S30), E57 (= E52), Y65 (= Y60), H126 (= H121), H203 (= H199), R360 (= R356)
2vmyA Crystal structure of f351gbsshmt in complex with gly and fthf (see paper)
61% identity, 97% coverage: 7:404/412 of query aligns to 8:405/405 of 2vmyA
- active site: Y51 (= Y50), E53 (= E52), D197 (= D196), T223 (= T222), K226 (= K225), R232 (= R231)
- 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 (= E52), Y60 (= Y59), Y61 (= Y60), L117 (= L116), G121 (= G120), H122 (= H121), L123 (= L122), S172 (= S171), K248 (= K247), F251 (= F250), N341 (= N340), S349 (≠ K348), P350 (= P349), G351 (≠ A350), R357 (= R356)
- binding glycine: S31 (= S30), Y51 (= Y50), Y61 (= Y60), H200 (= H199), K226 (= K225), R357 (= R356)
- binding pyridoxal-5'-phosphate: Y51 (= Y50), S93 (= S92), G94 (= G93), A95 (≠ S94), H122 (= H121), S172 (= S171), D197 (= D196), A199 (= A198), H200 (= H199), T223 (= T222), K226 (= K225), G257 (= G256)
2vmxA Crystal structure of f351gbsshmt in complex with l-allo-thr (see paper)
61% identity, 97% coverage: 7:404/412 of query aligns to 8:405/405 of 2vmxA
- active site: Y51 (= Y50), E53 (= E52), D197 (= D196), T223 (= T222), K226 (= K225), R232 (= R231)
- binding allo-threonine: S31 (= S30), H122 (= H121), H200 (= H199), R357 (= R356)
- binding pyridoxal-5'-phosphate: S93 (= S92), G94 (= G93), A95 (≠ S94), H122 (= H121), S172 (= S171), D197 (= D196), A199 (= A198), H200 (= H199), T223 (= T222), K226 (= K225)
1kl2A Crystal structure of serine hydroxymethyltransferase complexed with glycine and 5-formyl tetrahydrofolate (see paper)
61% identity, 97% coverage: 7:404/412 of query aligns to 8:405/405 of 1kl2A
- active site: Y51 (= Y50), E53 (= E52), D197 (= D196), T223 (= T222), K226 (= K225), R232 (= R231)
- 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 (= E52), Y60 (= Y59), G121 (= G120), H122 (= H121), S172 (= S171), F251 (= F250), N341 (= N340)
- binding glycine: S31 (= S30), Y51 (= Y50), Y61 (= Y60), H200 (= H199), R357 (= R356)
- binding pyridoxal-5'-phosphate: S93 (= S92), G94 (= G93), A95 (≠ S94), H122 (= H121), S172 (= S171), D197 (= D196), A199 (= A198), H200 (= H199), T223 (= T222), H225 (= H224), K226 (= K225)
1kl1A Crystal structure of serine hydroxymethyltransferase complexed with glycine (see paper)
61% identity, 97% coverage: 7:404/412 of query aligns to 8:405/405 of 1kl1A
- active site: Y51 (= Y50), E53 (= E52), D197 (= D196), T223 (= T222), K226 (= K225), R232 (= R231)
- binding glycine: S31 (= S30), H122 (= H121), R357 (= R356)
- binding pyridoxal-5'-phosphate: S93 (= S92), G94 (= G93), A95 (≠ S94), H122 (= H121), A171 (= A170), S172 (= S171), D197 (= D196), A199 (= A198), H200 (= H199), T223 (= T222), H225 (= H224), K226 (= K225)
1kkpA Crystal structure of serine hydroxymethyltransferase complexed with serine (see paper)
61% identity, 97% coverage: 7:404/412 of query aligns to 8:405/405 of 1kkpA
- active site: Y51 (= Y50), E53 (= E52), D197 (= D196), T223 (= T222), K226 (= K225), R232 (= R231)
- binding pyridoxal-5'-phosphate: S93 (= S92), G94 (= G93), A95 (≠ S94), H122 (= H121), S172 (= S171), D197 (= D196), A199 (= A198), H200 (= H199), K226 (= K225)
- binding serine: S31 (= S30), H122 (= H121), R357 (= R356)
1kkjA Crystal structure of serine hydroxymethyltransferase from b.Stearothermophilus (see paper)
61% identity, 97% coverage: 7:404/412 of query aligns to 8:405/405 of 1kkjA
- active site: Y51 (= Y50), E53 (= E52), D197 (= D196), T223 (= T222), K226 (= K225), R232 (= R231)
- binding pyridoxal-5'-phosphate: S93 (= S92), G94 (= G93), A95 (≠ S94), H122 (= H121), S172 (= S171), D197 (= D196), A199 (= A198), H200 (= H199), T223 (= T222), H225 (= H224), K226 (= K225)
3pgyB Serine hydroxymethyltransferase from staphylococcus aureus, s95p mutant.
59% identity, 98% coverage: 7:409/412 of query aligns to 8:404/404 of 3pgyB
1dfoB Crystal structure at 2.4 angstrom resolution of e. Coli serine hydroxymethyltransferase in complex with glycine and 5-formyl tetrahydrofolate (see paper)
59% identity, 99% coverage: 1:409/412 of query aligns to 6:416/417 of 1dfoB
- active site: Y55 (= Y50), E57 (= E52), D200 (= D196), T226 (= T222), K229 (= K225), R235 (= R231)
- 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 (= E52), Y64 (= Y59), Y65 (= Y60), L121 (= L116), G125 (= G120), H126 (= H121), L127 (= L122), S175 (= S171), S245 (≠ Y241), E247 (≠ A243), N347 (= N340), S355 (≠ K348), P356 (= P349), F357 (≠ A350)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S35 (= S30), Y55 (= Y50), Y65 (= Y60), S97 (= S92), G98 (= G93), S99 (= S94), H126 (= H121), F174 (≠ A170), S175 (= S171), D200 (= D196), A202 (= A198), H203 (= H199), K229 (= K225), G262 (= G255), R363 (= R356)
P0A825 Serine hydroxymethyltransferase; SHMT; Serine methylase; EC 2.1.2.1 from Escherichia coli (strain K12) (see 8 papers)
59% identity, 99% coverage: 1:409/412 of query aligns to 6:416/417 of P0A825
- K54 (= K49) modified: N6-acetyllysine
- Y55 (= Y50) 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 (= K57) modified: N6-succinyllysine
- Y65 (= Y60) mutation to F: Decrease in catalytic activity.
- L85 (= L80) 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 (= P210) 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 (= P212) 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 (≠ G214) 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 (= H224) 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 (= K225) modified: N6-(pyridoxal phosphate)lysine
- R235 (= R231) 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 (= K238) modified: N6-succinyllysine
- K250 (vs. gap) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- P258 (= P251) mutation to A: Important decrease in affinity and catalytic efficiency. Reduced thermal stability.; mutation to G: Important decrease in affinity and catalytic efficiency.
- P264 (= P257) mutation to A: Important decrease in affinity and catalytic efficiency.; mutation to G: Important decrease in affinity and catalytic efficiency.
- L276 (≠ F269) 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 (≠ N270) modified: N6-succinyllysine
- K285 (= K278) modified: N6-acetyllysine
- K293 (≠ D286) modified: N6-succinyllysine
- K331 (= K324) modified: N6-succinyllysine
- K346 (= K339) modified: N6-succinyllysine
- K354 (≠ Q347) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- R363 (= R356) 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 (= R365) mutation to A: No significant difference compared to the wild-type.; mutation to K: No significant difference compared to the wild-type.
- K375 (≠ G368) modified: N6-acetyllysine
Q5SI56 Serine hydroxymethyltransferase; SHMT; Serine methylase; EC 2.1.2.1 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
62% identity, 96% coverage: 7:401/412 of query aligns to 8:404/407 of Q5SI56
- Y51 (= Y50) binding
- GS 94:95 (= GS 93:94) binding
- S172 (= S171) binding
- H200 (= H199) binding
- H225 (= H224) binding
- K226 (= K225) modified: N6-(pyridoxal phosphate)lysine
- G258 (= G256) binding
7x5oB Crystal structure of e. Faecium shmt in complex with me-thf and plp- gly (see paper)
58% identity, 99% coverage: 4:409/412 of query aligns to 4:411/412 of 7x5oB
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S30 (= S30), Y50 (= Y50), Y60 (= Y60), S92 (= S92), G93 (= G93), S94 (= S94), H121 (= H121), S171 (= S171), D196 (= D196), A198 (= A198), H199 (= H199), K225 (= K225), R358 (= R356)
- binding n-[4-({[(6s)-2-amino-4-hydroxy-5-methyl-5,6,7,8-tetrahydropteridin-6-yl]methyl}amino)benzoyl]-l-glutamic acid: E52 (= E52), Y59 (= Y59), L116 (= L116), G119 (= G119), G120 (= G120), H121 (= H121), S171 (= S171), P252 (= P251), N342 (= N340), P351 (= P349)
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)
62% identity, 96% coverage: 7:401/412 of query aligns to 3:399/402 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)
62% identity, 96% coverage: 7:401/412 of query aligns to 3:399/402 of 8ssyA
2dkjA Crystal structure of t.Th.Hb8 serine hydroxymethyltransferase
62% identity, 96% coverage: 7:401/412 of query aligns to 3:399/402 of 2dkjA
- active site: Y46 (= Y50), E48 (= E52), D192 (= D196), T218 (= T222), K221 (= K225), R227 (= R231)
- binding pyridoxal-5'-phosphate: S88 (= S92), G89 (= G93), S90 (= S94), H117 (= H121), S167 (= S171), D192 (= D196), A194 (= A198), H220 (= H224), K221 (= K225)
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)
59% identity, 99% coverage: 1:409/412 of query aligns to 5:415/416 of 1eqbA
- active site: Y54 (= Y50), E56 (= E52), D199 (= D196), T225 (= T222), K228 (= K225), R234 (= R231)
- 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 (= E52), Y63 (= Y59), L120 (= L116), G123 (= G119), G124 (= G120), H125 (= H121), L126 (= L122), S174 (= S171), N346 (= N340), S354 (≠ K348), P355 (= P349), F356 (≠ A350)
- binding glycine: S34 (= S30), Y54 (= Y50), F64 (≠ Y60), H202 (= H199), K228 (= K225), R362 (= R356)
- binding pyridoxal-5'-phosphate: S96 (= S92), G97 (= G93), S98 (= S94), H125 (= H121), F173 (≠ A170), S174 (= S171), D199 (= D196), H202 (= H199), H227 (= H224), K228 (= K225)
7x5nA Crystal structure of e. Faecium shmt in complex with (+)-shin-1 and plp-ser (see paper)
58% identity, 98% coverage: 4:408/412 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 (= E52), Y58 (= Y59), Y59 (= Y60), L115 (= L116), G119 (= G120), H120 (= H121), L121 (= L122), K340 (= K339), N341 (= N340), S342 (≠ A341), P350 (= P349), F351 (≠ A350), R357 (= R356)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: S29 (= S30), Y49 (= Y50), E51 (= E52), Y59 (= Y60), S91 (= S92), G92 (= G93), S93 (= S94), H120 (= H121), S170 (= S171), D195 (= D196), A197 (= A198), H198 (= H199), K224 (= K225), R357 (= R356)
7v3dA Complex structure of serine hydroxymethyltransferase from enterococcus faecium and its inhibitor (see paper)
58% identity, 98% coverage: 4:408/412 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 (= E52), Y58 (= Y59), L115 (= L116), G119 (= G120), H120 (= H121), L121 (= L122), K340 (= K339), S342 (≠ A341), P350 (= P349), F351 (≠ A350), R357 (= R356)
- binding pyridoxal-5'-phosphate: Y49 (= Y50), S91 (= S92), G92 (= G93), S93 (= S94), H120 (= H121), S170 (= S171), D195 (= D196), A197 (= A198), K224 (= K225), G255 (= G255)
Query Sequence
>AO356_16850 FitnessBrowser__pseudo5_N2C3_1:AO356_16850
MSLQNFDPAIARLIDRERNRQETHLELIASENYVSEEVLQAQGSVLTNKYAEGYPGKRYY
GGCKVVDEIENLAIERARKLFNCEYVNVQPHSGSQANQAVFLAVLEPGDTILGMSLAHGG
HLTHGASVNFSGKLYRAFSYGLDTETETLDYEEMEALAREHRPKMIIAGASAYSRTLDFQ
RFRKICDEVGAYLMVDMAHYAGLIAAGVYPSPVGIADFITSTTHKTLRGPRGGLILAKAQ
YAALLDKTIFPVYQGGPLMHVIAAKAVAFNEALGDGFKHYQQRVIDNARVMADVLTRRGL
RVVSGGTDCHMFLLDLRSMNITGKDAEALLESAHITLNKNAIPNDPQKPAVTSGIRIGTP
ALTTRGFGEAECAEVANLIADLLEQPDNAARLDNTRRRVMHLCECFPVYLLR
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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