SitesBLAST
Comparing WP_011384736.1 NCBI__GCF_000009985.1:WP_011384736.1 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)
4n0wA X-ray crystal structure of a serine hydroxymethyltransferase from burkholderia cenocepacia with covalently attached pyridoxal phosphate
66% identity, 98% coverage: 11:427/427 of query aligns to 7:416/416 of 4n0wA
- active site: Y57 (= Y61), E59 (= E63), D202 (= D207), T228 (= T233), K231 (= K236), R237 (= R242)
- binding pyridoxal-5'-phosphate: S99 (= S103), G100 (= G104), S101 (= S105), H128 (= H132), D202 (= D207), A204 (= A209), H205 (= H210), K231 (= K236)
4ot8A X-ray crystal structure of serine hydroxymethyl transferase from burkholderia cenocepacia bound to plp and serine
66% identity, 98% coverage: 11:427/427 of query aligns to 5:414/414 of 4ot8A
- active site: Y55 (= Y61), E57 (= E63), D200 (= D207), T226 (= T233), K229 (= K236), R235 (= R242)
- binding pyridoxal-5'-phosphate: S97 (= S103), G98 (= G104), S99 (= S105), H126 (= H132), D200 (= D207), A202 (= A209), H203 (= H210), K229 (= K236)
- binding serine: S35 (= S41), E57 (= E63), Y65 (= Y71), H126 (= H132), H203 (= H210), R360 (= R368)
4otlA X-ray crystal structure of serine hydroxymethyl transferase from burkholderia cenocepacia bound to plp and glycine
67% identity, 97% coverage: 14:427/427 of query aligns to 3:409/409 of 4otlA
- active site: Y50 (= Y61), E52 (= E63), D195 (= D207), T221 (= T233), K224 (= K236), R230 (= R242)
- binding glycine: S30 (= S41), Y50 (= Y61), Y60 (= Y71), H121 (= H132), K224 (= K236), R355 (= R368)
- binding pyridoxal-5'-phosphate: S92 (= S103), G93 (= G104), S94 (= S105), H121 (= H132), S170 (= S182), D195 (= D207), A197 (= A209), H198 (= H210), K224 (= K236)
1kl2A Crystal structure of serine hydroxymethyltransferase complexed with glycine and 5-formyl tetrahydrofolate (see paper)
64% identity, 94% coverage: 14:413/427 of query aligns to 4:399/405 of 1kl2A
- active site: Y51 (= Y61), E53 (= E63), D197 (= D207), T223 (= T233), K226 (= K236), R232 (= R242)
- 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 (= E63), Y60 (= Y70), G121 (= G131), H122 (= H132), S172 (= S182), F251 (= F262), N341 (= N352)
- binding glycine: S31 (= S41), Y51 (= Y61), Y61 (= Y71), H200 (= H210), R357 (= R368)
- binding pyridoxal-5'-phosphate: S93 (= S103), G94 (= G104), A95 (≠ S105), H122 (= H132), S172 (= S182), D197 (= D207), A199 (= A209), H200 (= H210), T223 (= T233), H225 (= H235), K226 (= K236)
1kl1A Crystal structure of serine hydroxymethyltransferase complexed with glycine (see paper)
64% identity, 94% coverage: 14:413/427 of query aligns to 4:399/405 of 1kl1A
- active site: Y51 (= Y61), E53 (= E63), D197 (= D207), T223 (= T233), K226 (= K236), R232 (= R242)
- binding glycine: S31 (= S41), H122 (= H132), R357 (= R368)
- binding pyridoxal-5'-phosphate: S93 (= S103), G94 (= G104), A95 (≠ S105), H122 (= H132), A171 (≠ G181), S172 (= S182), D197 (= D207), A199 (= A209), H200 (= H210), T223 (= T233), H225 (= H235), K226 (= K236)
1kkpA Crystal structure of serine hydroxymethyltransferase complexed with serine (see paper)
64% identity, 94% coverage: 14:413/427 of query aligns to 4:399/405 of 1kkpA
- active site: Y51 (= Y61), E53 (= E63), D197 (= D207), T223 (= T233), K226 (= K236), R232 (= R242)
- binding pyridoxal-5'-phosphate: S93 (= S103), G94 (= G104), A95 (≠ S105), H122 (= H132), S172 (= S182), D197 (= D207), A199 (= A209), H200 (= H210), K226 (= K236)
- binding serine: S31 (= S41), H122 (= H132), R357 (= R368)
1kkjA Crystal structure of serine hydroxymethyltransferase from b.Stearothermophilus (see paper)
64% identity, 94% coverage: 14:413/427 of query aligns to 4:399/405 of 1kkjA
- active site: Y51 (= Y61), E53 (= E63), D197 (= D207), T223 (= T233), K226 (= K236), R232 (= R242)
- binding pyridoxal-5'-phosphate: S93 (= S103), G94 (= G104), A95 (≠ S105), H122 (= H132), S172 (= S182), D197 (= D207), A199 (= A209), H200 (= H210), T223 (= T233), H225 (= H235), K226 (= K236)
2vmyA Crystal structure of f351gbsshmt in complex with gly and fthf (see paper)
64% identity, 94% coverage: 14:413/427 of query aligns to 4:399/405 of 2vmyA
- active site: Y51 (= Y61), E53 (= E63), D197 (= D207), T223 (= T233), K226 (= K236), R232 (= R242)
- 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 (= E63), Y60 (= Y70), Y61 (= Y71), L117 (= L127), G121 (= G131), H122 (= H132), L123 (= L133), S172 (= S182), K248 (≠ S259), F251 (= F262), N341 (= N352), S349 (≠ K360), P350 (= P361), G351 (≠ T362), R357 (= R368)
- binding glycine: S31 (= S41), Y51 (= Y61), Y61 (= Y71), H200 (= H210), K226 (= K236), R357 (= R368)
- binding pyridoxal-5'-phosphate: Y51 (= Y61), S93 (= S103), G94 (= G104), A95 (≠ S105), H122 (= H132), S172 (= S182), D197 (= D207), A199 (= A209), H200 (= H210), T223 (= T233), K226 (= K236), G257 (= G268)
2vmxA Crystal structure of f351gbsshmt in complex with l-allo-thr (see paper)
64% identity, 94% coverage: 14:413/427 of query aligns to 4:399/405 of 2vmxA
- active site: Y51 (= Y61), E53 (= E63), D197 (= D207), T223 (= T233), K226 (= K236), R232 (= R242)
- binding allo-threonine: S31 (= S41), H122 (= H132), H200 (= H210), R357 (= R368)
- binding pyridoxal-5'-phosphate: S93 (= S103), G94 (= G104), A95 (≠ S105), H122 (= H132), S172 (= S182), D197 (= D207), A199 (= A209), H200 (= H210), T223 (= T233), K226 (= K236)
6ymdA Crystal structure of serine hydroxymethyltransferase from aphanothece halophytica in the covalent complex with malonate (see paper)
61% identity, 97% coverage: 14:426/427 of query aligns to 7:414/420 of 6ymdA
- active site: Y54 (= Y61), E56 (= E63), D200 (= D207), T226 (= T233), K229 (= K236), R235 (= R242)
- binding malonate ion: S34 (= S41), Y54 (= Y61), E56 (= E63), Y64 (= Y71), H125 (= H132), H203 (= H210), K229 (= K236), R361 (= R368)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: Y54 (= Y61), S96 (= S103), G97 (= G104), A98 (≠ S105), H125 (= H132), Y174 (≠ G181), S175 (= S182), D200 (= D207), A202 (= A209), T226 (= T233), K229 (= K236), G261 (= G268)
Q5SI56 Serine hydroxymethyltransferase; SHMT; Serine methylase; EC 2.1.2.1 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
67% identity, 89% coverage: 16:395/427 of query aligns to 6:385/407 of Q5SI56
- Y51 (= Y61) binding
- GS 94:95 (= GS 104:105) binding
- S172 (= S182) binding
- H200 (= H210) binding
- H225 (= H235) binding
- K226 (= K236) modified: N6-(pyridoxal phosphate)lysine
- G258 (= G268) binding
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)
67% identity, 89% coverage: 16:395/427 of query aligns to 1:380/402 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)
67% identity, 89% coverage: 16:395/427 of query aligns to 1:380/402 of 8ssyA
2dkjA Crystal structure of t.Th.Hb8 serine hydroxymethyltransferase
67% identity, 89% coverage: 16:395/427 of query aligns to 1:380/402 of 2dkjA
- active site: Y46 (= Y61), E48 (= E63), D192 (= D207), T218 (= T233), K221 (= K236), R227 (= R242)
- binding pyridoxal-5'-phosphate: S88 (= S103), G89 (= G104), S90 (= S105), H117 (= H132), S167 (= S182), D192 (= D207), A194 (= A209), H220 (= H235), K221 (= K236)
6ymfA Crystal structure of serine hydroxymethyltransferase from aphanothece halophytica in the plp-serine external aldimine state (see paper)
61% identity, 97% coverage: 14:426/427 of query aligns to 7:414/418 of 6ymfA
- active site: Y54 (= Y61), E56 (= E63), D200 (= D207), T226 (= T233), K229 (= K236), R235 (= R242)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: S34 (= S41), S96 (= S103), G97 (= G104), A98 (≠ S105), H125 (= H132), S175 (= S182), D200 (= D207), A202 (= A209), H203 (= H210), T226 (= T233), K229 (= K236), R361 (= R368)
7x5oB Crystal structure of e. Faecium shmt in complex with me-thf and plp- gly (see paper)
59% identity, 96% coverage: 18:427/427 of query aligns to 7:412/412 of 7x5oB
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S30 (= S41), Y50 (= Y61), Y60 (= Y71), S92 (= S103), G93 (= G104), S94 (= S105), H121 (= H132), S171 (= S182), D196 (= D207), A198 (= A209), H199 (= H210), K225 (= K236), R358 (= R368)
- binding n-[4-({[(6s)-2-amino-4-hydroxy-5-methyl-5,6,7,8-tetrahydropteridin-6-yl]methyl}amino)benzoyl]-l-glutamic acid: E52 (= E63), Y59 (= Y70), L116 (= L127), G119 (= G130), G120 (= G131), H121 (= H132), S171 (= S182), P252 (= P263), N342 (= N352), P351 (= P361)
7x5nA Crystal structure of e. Faecium shmt in complex with (+)-shin-1 and plp-ser (see paper)
59% identity, 96% coverage: 18:425/427 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 (= E63), Y58 (= Y70), Y59 (= Y71), L115 (= L127), G119 (= G131), H120 (= H132), L121 (= L133), K340 (= K351), N341 (= N352), S342 (≠ G353), P350 (= P361), F351 (≠ T362), R357 (= R368)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: S29 (= S41), Y49 (= Y61), E51 (= E63), Y59 (= Y71), S91 (= S103), G92 (= G104), S93 (= S105), H120 (= H132), S170 (= S182), D195 (= D207), A197 (= A209), H198 (= H210), K224 (= K236), R357 (= R368)
7v3dA Complex structure of serine hydroxymethyltransferase from enterococcus faecium and its inhibitor (see paper)
59% identity, 96% coverage: 18:425/427 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 (= E63), Y58 (= Y70), L115 (= L127), G119 (= G131), H120 (= H132), L121 (= L133), K340 (= K351), S342 (≠ G353), P350 (= P361), F351 (≠ T362), R357 (= R368)
- binding pyridoxal-5'-phosphate: Y49 (= Y61), S91 (= S103), G92 (= G104), S93 (= S105), H120 (= H132), S170 (= S182), D195 (= D207), A197 (= A209), K224 (= K236), G255 (= G267)
1dfoB Crystal structure at 2.4 angstrom resolution of e. Coli serine hydroxymethyltransferase in complex with glycine and 5-formyl tetrahydrofolate (see paper)
57% identity, 97% coverage: 14:426/427 of query aligns to 8:416/417 of 1dfoB
- active site: Y55 (= Y61), E57 (= E63), D200 (= D207), T226 (= T233), K229 (= K236), R235 (= R242)
- 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 (= E63), Y64 (= Y70), Y65 (= Y71), L121 (= L127), G125 (= G131), H126 (= H132), L127 (= L133), S175 (= S182), S245 (≠ D250), E247 (≠ D252), N347 (= N352), S355 (≠ K360), P356 (= P361), F357 (≠ T362)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S35 (= S41), Y55 (= Y61), Y65 (= Y71), S97 (= S103), G98 (= G104), S99 (= S105), H126 (= H132), F174 (≠ G181), S175 (= S182), D200 (= D207), A202 (= A209), H203 (= H210), K229 (= K236), G262 (= G267), R363 (= R368)
P0A825 Serine hydroxymethyltransferase; SHMT; Serine methylase; EC 2.1.2.1 from Escherichia coli (strain K12) (see 8 papers)
57% identity, 97% coverage: 14:426/427 of query aligns to 8:416/417 of P0A825
- K54 (= K60) modified: N6-acetyllysine
- Y55 (= Y61) 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 (= K68) modified: N6-succinyllysine
- Y65 (= Y71) mutation to F: Decrease in catalytic activity.
- L85 (≠ I91) 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 (= P221) 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 (= P223) 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 (= P225) 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 (= H235) 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 (= K236) modified: N6-(pyridoxal phosphate)lysine
- R235 (= R242) 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 (≠ N249) modified: N6-succinyllysine
- K250 (= K255) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- P258 (= P263) mutation to A: Important decrease in affinity and catalytic efficiency. Reduced thermal stability.; mutation to G: Important decrease in affinity and catalytic efficiency.
- P264 (= P269) mutation to A: Important decrease in affinity and catalytic efficiency.; mutation to G: Important decrease in affinity and catalytic efficiency.
- L276 (≠ F281) 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 (≠ G282) modified: N6-succinyllysine
- K285 (= K290) modified: N6-acetyllysine
- K293 (≠ D298) modified: N6-succinyllysine
- K331 (= K336) modified: N6-succinyllysine
- K346 (= K351) modified: N6-succinyllysine
- K354 (≠ E359) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- R363 (= R368) 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 (= R377) mutation to A: No significant difference compared to the wild-type.; mutation to K: No significant difference compared to the wild-type.
- K375 (≠ G380) modified: N6-acetyllysine
Query Sequence
>WP_011384736.1 NCBI__GCF_000009985.1:WP_011384736.1
MSSAPTDAFFRTPLSERDPEVFAAITQELKRQQDQIELIASENIVSRAVLEAQGSVMTNK
YAEGYPGKRYYGGCEFVDIAESLAISRACQIFGCSYANVQPSSGSQANQGVFMALLQPGD
TIMGMSLAAGGHLTHGAAPNQSGKWFKAVQYGVRQQDSQIDFAEVEELARTHRPKLIIAG
GSAYPRTIDFARFRKIADEVGAFFMVDMAHFAGLVAGGVYPNPLPHAHVVTTTTHKTLRG
PRGGMILSNDADIGKKINSAIFPGIQGGPLMHVIAGKAVAFGEALKPEFKLYAKQVVDNA
RALADTLVRRGLDIVSGGTDSHLMLVDLRPKKLTGKAAEASLEHAGMTCNKNGIPFDPEK
PTITSGVRLGTPAATTRGFGVEEFKKVGELIGDVLDGLAANPEDNSAAEARARAEVAELC
RRFPIYQ
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