SitesBLAST
Comparing WP_013537969.1 NCBI__GCF_000185805.1:WP_013537969.1 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)
1kl2A Crystal structure of serine hydroxymethyltransferase complexed with glycine and 5-formyl tetrahydrofolate (see paper)
66% identity, 96% coverage: 1:400/418 of query aligns to 1:400/405 of 1kl2A
- active site: Y51 (= Y51), E53 (= E53), D197 (= D197), T223 (= T223), K226 (= K226), R232 (= R232)
- 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 (= E53), Y60 (= Y60), G121 (= G121), H122 (= H122), S172 (= S172), F251 (= F251), N341 (= N341)
- binding glycine: S31 (= S31), Y51 (= Y51), Y61 (= Y61), H200 (= H200), R357 (= R357)
- binding pyridoxal-5'-phosphate: S93 (= S93), G94 (= G94), A95 (≠ S95), H122 (= H122), S172 (= S172), D197 (= D197), A199 (= A199), H200 (= H200), T223 (= T223), H225 (= H225), K226 (= K226)
1kl1A Crystal structure of serine hydroxymethyltransferase complexed with glycine (see paper)
66% identity, 96% coverage: 1:400/418 of query aligns to 1:400/405 of 1kl1A
- active site: Y51 (= Y51), E53 (= E53), D197 (= D197), T223 (= T223), K226 (= K226), R232 (= R232)
- binding glycine: S31 (= S31), H122 (= H122), R357 (= R357)
- binding pyridoxal-5'-phosphate: S93 (= S93), G94 (= G94), A95 (≠ S95), H122 (= H122), A171 (= A171), S172 (= S172), D197 (= D197), A199 (= A199), H200 (= H200), T223 (= T223), H225 (= H225), K226 (= K226)
1kkpA Crystal structure of serine hydroxymethyltransferase complexed with serine (see paper)
66% identity, 96% coverage: 1:400/418 of query aligns to 1:400/405 of 1kkpA
- active site: Y51 (= Y51), E53 (= E53), D197 (= D197), T223 (= T223), K226 (= K226), R232 (= R232)
- binding pyridoxal-5'-phosphate: S93 (= S93), G94 (= G94), A95 (≠ S95), H122 (= H122), S172 (= S172), D197 (= D197), A199 (= A199), H200 (= H200), K226 (= K226)
- binding serine: S31 (= S31), H122 (= H122), R357 (= R357)
1kkjA Crystal structure of serine hydroxymethyltransferase from b.Stearothermophilus (see paper)
66% identity, 96% coverage: 1:400/418 of query aligns to 1:400/405 of 1kkjA
- active site: Y51 (= Y51), E53 (= E53), D197 (= D197), T223 (= T223), K226 (= K226), R232 (= R232)
- binding pyridoxal-5'-phosphate: S93 (= S93), G94 (= G94), A95 (≠ S95), H122 (= H122), S172 (= S172), D197 (= D197), A199 (= A199), H200 (= H200), T223 (= T223), H225 (= H225), K226 (= K226)
2vmyA Crystal structure of f351gbsshmt in complex with gly and fthf (see paper)
65% identity, 96% coverage: 1:400/418 of query aligns to 1:400/405 of 2vmyA
- active site: Y51 (= Y51), E53 (= E53), D197 (= D197), T223 (= T223), K226 (= K226), R232 (= R232)
- 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 (= E53), Y60 (= Y60), Y61 (= Y61), L117 (= L117), G121 (= G121), H122 (= H122), L123 (= L123), S172 (= S172), K248 (= K248), F251 (= F251), N341 (= N341), S349 (= S349), P350 (= P350), G351 (≠ F351), R357 (= R357)
- binding glycine: S31 (= S31), Y51 (= Y51), Y61 (= Y61), H200 (= H200), K226 (= K226), R357 (= R357)
- binding pyridoxal-5'-phosphate: Y51 (= Y51), S93 (= S93), G94 (= G94), A95 (≠ S95), H122 (= H122), S172 (= S172), D197 (= D197), A199 (= A199), H200 (= H200), T223 (= T223), K226 (= K226), G257 (= G257)
2vmxA Crystal structure of f351gbsshmt in complex with l-allo-thr (see paper)
65% identity, 96% coverage: 1:400/418 of query aligns to 1:400/405 of 2vmxA
- active site: Y51 (= Y51), E53 (= E53), D197 (= D197), T223 (= T223), K226 (= K226), R232 (= R232)
- binding allo-threonine: S31 (= S31), H122 (= H122), H200 (= H200), R357 (= R357)
- binding pyridoxal-5'-phosphate: S93 (= S93), G94 (= G94), A95 (≠ S95), H122 (= H122), S172 (= S172), D197 (= D197), A199 (= A199), H200 (= H200), T223 (= T223), K226 (= K226)
4ot8A X-ray crystal structure of serine hydroxymethyl transferase from burkholderia cenocepacia bound to plp and serine
64% identity, 97% coverage: 7:410/418 of query aligns to 11:413/414 of 4ot8A
- active site: Y55 (= Y51), E57 (= E53), D200 (= D197), T226 (= T223), K229 (= K226), R235 (= R232)
- binding pyridoxal-5'-phosphate: S97 (= S93), G98 (= G94), S99 (= S95), H126 (= H122), D200 (= D197), A202 (= A199), H203 (= H200), K229 (= K226)
- binding serine: S35 (= S31), E57 (= E53), Y65 (= Y61), H126 (= H122), H203 (= H200), R360 (= R357)
4otlA X-ray crystal structure of serine hydroxymethyl transferase from burkholderia cenocepacia bound to plp and glycine
64% identity, 97% coverage: 7:410/418 of query aligns to 6:408/409 of 4otlA
- active site: Y50 (= Y51), E52 (= E53), D195 (= D197), T221 (= T223), K224 (= K226), R230 (= R232)
- binding glycine: S30 (= S31), Y50 (= Y51), Y60 (= Y61), H121 (= H122), K224 (= K226), R355 (= R357)
- binding pyridoxal-5'-phosphate: S92 (= S93), G93 (= G94), S94 (= S95), H121 (= H122), S170 (= S172), D195 (= D197), A197 (= A199), H198 (= H200), K224 (= K226)
4n0wA X-ray crystal structure of a serine hydroxymethyltransferase from burkholderia cenocepacia with covalently attached pyridoxal phosphate
64% identity, 97% coverage: 7:410/418 of query aligns to 13:415/416 of 4n0wA
- active site: Y57 (= Y51), E59 (= E53), D202 (= D197), T228 (= T223), K231 (= K226), R237 (= R232)
- binding pyridoxal-5'-phosphate: S99 (= S93), G100 (= G94), S101 (= S95), H128 (= H122), D202 (= D197), A204 (= A199), H205 (= H200), K231 (= K226)
3pgyB Serine hydroxymethyltransferase from staphylococcus aureus, s95p mutant.
63% identity, 98% coverage: 1:410/418 of query aligns to 1:404/404 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)
65% identity, 96% coverage: 8:410/418 of query aligns to 12:416/417 of 1dfoB
- active site: Y55 (= Y51), E57 (= E53), D200 (= D197), T226 (= T223), K229 (= K226), R235 (= R232)
- 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 (= E53), Y64 (= Y60), Y65 (= Y61), L121 (= L117), G125 (= G121), H126 (= H122), L127 (= L123), S175 (= S172), S245 (vs. gap), E247 (= E241), N347 (= N341), S355 (= S349), P356 (= P350), F357 (= F351)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S35 (= S31), Y55 (= Y51), Y65 (= Y61), S97 (= S93), G98 (= G94), S99 (= S95), H126 (= H122), F174 (≠ A171), S175 (= S172), D200 (= D197), A202 (= A199), H203 (= H200), K229 (= K226), G262 (= G256), R363 (= R357)
P0A825 Serine hydroxymethyltransferase; SHMT; Serine methylase; EC 2.1.2.1 from Escherichia coli (strain K12) (see 8 papers)
65% identity, 96% coverage: 8:410/418 of query aligns to 12:416/417 of P0A825
- K54 (= K50) modified: N6-acetyllysine
- Y55 (= Y51) 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 (= K58) modified: N6-succinyllysine
- Y65 (= Y61) mutation to F: Decrease in catalytic activity.
- L85 (= L81) 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 (= P211) 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 (= P213) 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 (≠ E215) 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 (= H225) 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 (= K226) modified: N6-(pyridoxal phosphate)lysine
- R235 (= R232) 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 (= K239) modified: N6-succinyllysine
- K250 (= K244) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- P258 (= P252) mutation to A: Important decrease in affinity and catalytic efficiency. Reduced thermal stability.; mutation to G: Important decrease in affinity and catalytic efficiency.
- P264 (= P258) mutation to A: Important decrease in affinity and catalytic efficiency.; mutation to G: Important decrease in affinity and catalytic efficiency.
- L276 (≠ F270) 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 (= K271) modified: N6-succinyllysine
- K285 (= K279) modified: N6-acetyllysine
- K293 (= K287) modified: N6-succinyllysine
- K331 (= K325) modified: N6-succinyllysine
- K346 (= K340) modified: N6-succinyllysine
- K354 (≠ R348) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- R363 (= R357) 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 (= R366) mutation to A: No significant difference compared to the wild-type.; mutation to K: No significant difference compared to the wild-type.
- K375 (≠ R369) 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)
65% identity, 96% coverage: 8:410/418 of query aligns to 11:415/416 of 1eqbA
- active site: Y54 (= Y51), E56 (= E53), D199 (= D197), T225 (= T223), K228 (= K226), R234 (= R232)
- 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 (= E53), Y63 (= Y60), L120 (= L117), G123 (= G120), G124 (= G121), H125 (= H122), L126 (= L123), S174 (= S172), N346 (= N341), S354 (= S349), P355 (= P350), F356 (= F351)
- binding glycine: S34 (= S31), Y54 (= Y51), F64 (≠ Y61), H202 (= H200), K228 (= K226), R362 (= R357)
- binding pyridoxal-5'-phosphate: S96 (= S93), G97 (= G94), S98 (= S95), H125 (= H122), F173 (≠ A171), S174 (= S172), D199 (= D197), H202 (= H200), H227 (= H225), K228 (= K226)
6ymfA Crystal structure of serine hydroxymethyltransferase from aphanothece halophytica in the plp-serine external aldimine state (see paper)
60% identity, 99% coverage: 1:414/418 of query aligns to 4:418/418 of 6ymfA
- active site: Y54 (= Y51), E56 (= E53), D200 (= D197), T226 (= T223), K229 (= K226), R235 (= R232)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: S34 (= S31), S96 (= S93), G97 (= G94), A98 (≠ S95), H125 (= H122), S175 (= S172), D200 (= D197), A202 (= A199), H203 (= H200), T226 (= T223), K229 (= K226), R361 (= R357)
6ymdA Crystal structure of serine hydroxymethyltransferase from aphanothece halophytica in the covalent complex with malonate (see paper)
60% identity, 99% coverage: 1:414/418 of query aligns to 4:418/420 of 6ymdA
- active site: Y54 (= Y51), E56 (= E53), D200 (= D197), T226 (= T223), K229 (= K226), R235 (= R232)
- binding malonate ion: S34 (= S31), Y54 (= Y51), E56 (= E53), Y64 (= Y61), H125 (= H122), H203 (= H200), K229 (= K226), R361 (= R357)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: Y54 (= Y51), S96 (= S93), G97 (= G94), A98 (≠ S95), H125 (= H122), Y174 (≠ A171), S175 (= S172), D200 (= D197), A202 (= A199), T226 (= T223), K229 (= K226), G261 (= G257)
7x5oB Crystal structure of e. Faecium shmt in complex with me-thf and plp- gly (see paper)
63% identity, 97% coverage: 5:410/418 of query aligns to 4:411/412 of 7x5oB
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S30 (= S31), Y50 (= Y51), Y60 (= Y61), S92 (= S93), G93 (= G94), S94 (= S95), H121 (= H122), S171 (= S172), D196 (= D197), A198 (= A199), H199 (= H200), K225 (= K226), R358 (= R357)
- binding n-[4-({[(6s)-2-amino-4-hydroxy-5-methyl-5,6,7,8-tetrahydropteridin-6-yl]methyl}amino)benzoyl]-l-glutamic acid: E52 (= E53), Y59 (= Y60), L116 (= L117), G119 (= G120), G120 (= G121), H121 (= H122), S171 (= S172), P252 (= P252), N342 (= N341), P351 (= P350)
7x5nA Crystal structure of e. Faecium shmt in complex with (+)-shin-1 and plp-ser (see paper)
63% identity, 97% coverage: 5:409/418 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 (= E53), Y58 (= Y60), Y59 (= Y61), L115 (= L117), G119 (= G121), H120 (= H122), L121 (= L123), K340 (= K340), N341 (= N341), S342 (≠ T342), P350 (= P350), F351 (= F351), R357 (= R357)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: S29 (= S31), Y49 (= Y51), E51 (= E53), Y59 (= Y61), S91 (= S93), G92 (= G94), S93 (= S95), H120 (= H122), S170 (= S172), D195 (= D197), A197 (= A199), H198 (= H200), K224 (= K226), R357 (= R357)
7v3dA Complex structure of serine hydroxymethyltransferase from enterococcus faecium and its inhibitor (see paper)
63% identity, 97% coverage: 5:409/418 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 (= E53), Y58 (= Y60), L115 (= L117), G119 (= G121), H120 (= H122), L121 (= L123), K340 (= K340), S342 (≠ T342), P350 (= P350), F351 (= F351), R357 (= R357)
- binding pyridoxal-5'-phosphate: Y49 (= Y51), S91 (= S93), G92 (= G94), S93 (= S95), H120 (= H122), S170 (= S172), D195 (= D197), A197 (= A199), K224 (= K226), G255 (= G256)
Q5SI56 Serine hydroxymethyltransferase; SHMT; Serine methylase; EC 2.1.2.1 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
62% identity, 96% coverage: 8:409/418 of query aligns to 8:406/407 of Q5SI56
- Y51 (= Y51) binding pyridoxal 5'-phosphate
- GS 94:95 (= GS 94:95) binding pyridoxal 5'-phosphate
- S172 (= S172) binding pyridoxal 5'-phosphate
- H200 (= H200) binding pyridoxal 5'-phosphate
- H225 (= H225) binding pyridoxal 5'-phosphate
- K226 (= K226) modified: N6-(pyridoxal phosphate)lysine
- G258 (= G257) binding pyridoxal 5'-phosphate
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: 8:409/418 of query aligns to 3:401/402 of 8suiB
Query Sequence
>WP_013537969.1 NCBI__GCF_000185805.1:WP_013537969.1
MKHLKAVDPEIFDALKCEFKRQNEHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRY
YGGCECVDIAEELAIKRCKELFGAEHVNVQPHSGSQANQAVYLATLKPGDTILSMNLSHG
GHLSHGSPVNMTGKYFNVVQYGVRKDTETIDFDQVYRLAKEHKPKMIICGASAYPRVIDF
DKFREIADEVGAYLLADIAHIAGLVVAGLHPSPIEACHFVTTTTHKTLRGPRGGVVMCKA
EFAKEIDKAVFPGLQGGPLMHVIAAKAVAFKEAQSEEFKKYQEQIVKNAKAMAEELQRQG
FRLVSGGTDNHLMLVDLTDKGITGKEAEAALGRANITVNKNTIPFDTRSPFVTSGIRIGT
PAITSRGIREDEARRIAQLIAEVLKNINDEGVIERVKAEVLEICGKHPLYPDLKELYS
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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