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Comparing WP_028310448.1 NCBI__GCF_000482785.1:WP_028310448.1 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
81% identity, 99% coverage: 1:414/417 of query aligns to 2:415/416 of 4n0wA
- active site: Y57 (= Y56), E59 (= E58), D202 (= D201), T228 (= T227), K231 (= K230), R237 (= R236)
- binding pyridoxal-5'-phosphate: S99 (= S98), G100 (= G99), S101 (= S100), H128 (= H127), D202 (= D201), A204 (= A203), H205 (= H204), K231 (= K230)
4ot8A X-ray crystal structure of serine hydroxymethyl transferase from burkholderia cenocepacia bound to plp and serine
81% identity, 99% coverage: 2:414/417 of query aligns to 1:413/414 of 4ot8A
- active site: Y55 (= Y56), E57 (= E58), D200 (= D201), T226 (= T227), K229 (= K230), R235 (= R236)
- binding pyridoxal-5'-phosphate: S97 (= S98), G98 (= G99), S99 (= S100), H126 (= H127), D200 (= D201), A202 (= A203), H203 (= H204), K229 (= K230)
- binding serine: S35 (= S36), E57 (= E58), Y65 (= Y66), H126 (= H127), H203 (= H204), R360 (= R361)
4otlA X-ray crystal structure of serine hydroxymethyl transferase from burkholderia cenocepacia bound to plp and glycine
82% identity, 98% coverage: 8:414/417 of query aligns to 2:408/409 of 4otlA
- active site: Y50 (= Y56), E52 (= E58), D195 (= D201), T221 (= T227), K224 (= K230), R230 (= R236)
- binding glycine: S30 (= S36), Y50 (= Y56), Y60 (= Y66), H121 (= H127), K224 (= K230), R355 (= R361)
- binding pyridoxal-5'-phosphate: S92 (= S98), G93 (= G99), S94 (= S100), H121 (= H127), S170 (= S176), D195 (= D201), A197 (= A203), H198 (= H204), K224 (= K230)
1dfoB Crystal structure at 2.4 angstrom resolution of e. Coli serine hydroxymethyltransferase in complex with glycine and 5-formyl tetrahydrofolate (see paper)
63% identity, 98% coverage: 8:414/417 of query aligns to 7:416/417 of 1dfoB
- active site: Y55 (= Y56), E57 (= E58), D200 (= D201), T226 (= T227), K229 (= K230), R235 (= R236)
- 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 (= E58), Y64 (= Y65), Y65 (= Y66), L121 (= L122), G125 (= G126), H126 (= H127), L127 (= L128), S175 (= S176), S245 (≠ H246), E247 (vs. gap), N347 (= N345), S355 (≠ K353), P356 (= P354), F357 (= F355)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S35 (= S36), Y55 (= Y56), Y65 (= Y66), S97 (= S98), G98 (= G99), S99 (= S100), H126 (= H127), F174 (≠ A175), S175 (= S176), D200 (= D201), A202 (= A203), H203 (= H204), K229 (= K230), G262 (= G260), R363 (= R361)
P0A825 Serine hydroxymethyltransferase; SHMT; Serine methylase; EC 2.1.2.1 from Escherichia coli (strain K12) (see 8 papers)
63% identity, 98% coverage: 8:414/417 of query aligns to 7:416/417 of P0A825
- K54 (= K55) modified: N6-acetyllysine
- Y55 (= Y56) 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 (= K63) modified: N6-succinyllysine
- Y65 (= Y66) mutation to F: Decrease in catalytic activity.
- L85 (= L86) 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 (= P215) 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 (= P217) 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 (= P219) 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 (= H229) 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 (= K230) modified: N6-(pyridoxal phosphate)lysine
- R235 (= R236) 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 (= K243) 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 (≠ Q275) modified: N6-succinyllysine
- K285 (= K283) modified: N6-acetyllysine
- K293 (≠ R291) modified: N6-succinyllysine
- K331 (= K329) modified: N6-succinyllysine
- K346 (= K344) modified: N6-succinyllysine
- K354 (≠ E352) 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 (= K373) 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)
63% identity, 98% coverage: 8:414/417 of query aligns to 6:415/416 of 1eqbA
- active site: Y54 (= Y56), E56 (= E58), D199 (= D201), T225 (= T227), K228 (= K230), R234 (= R236)
- 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 (= E58), Y63 (= Y65), L120 (= L122), G123 (= G125), G124 (= G126), H125 (= H127), L126 (= L128), S174 (= S176), N346 (= N345), S354 (≠ K353), P355 (= P354), F356 (= F355)
- binding glycine: S34 (= S36), Y54 (= Y56), F64 (≠ Y66), H202 (= H204), K228 (= K230), R362 (= R361)
- binding pyridoxal-5'-phosphate: S96 (= S98), G97 (= G99), S98 (= S100), H125 (= H127), F173 (≠ A175), S174 (= S176), D199 (= D201), H202 (= H204), H227 (= H229), K228 (= K230)
7x5oB Crystal structure of e. Faecium shmt in complex with me-thf and plp- gly (see paper)
61% identity, 97% coverage: 11:414/417 of query aligns to 5:411/412 of 7x5oB
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S30 (= S36), Y50 (= Y56), Y60 (= Y66), S92 (= S98), G93 (= G99), S94 (= S100), H121 (= H127), S171 (= S176), D196 (= D201), A198 (= A203), H199 (= H204), K225 (= K230), 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 (= E58), Y59 (= Y65), L116 (= L122), G119 (= G125), G120 (= G126), H121 (= H127), S171 (= S176), P252 (= P256), N342 (= N345), P351 (= P354)
7x5nA Crystal structure of e. Faecium shmt in complex with (+)-shin-1 and plp-ser (see paper)
61% identity, 97% coverage: 11:413/417 of query aligns to 4:409/409 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 (= E58), Y58 (= Y65), Y59 (= Y66), L115 (= L122), G119 (= G126), H120 (= H127), L121 (= L128), K340 (= K344), N341 (= N345), S342 (≠ G346), P350 (= P354), F351 (= F355), R357 (= R361)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: S29 (= S36), Y49 (= Y56), E51 (= E58), Y59 (= Y66), S91 (= S98), G92 (= G99), S93 (= S100), H120 (= H127), S170 (= S176), D195 (= D201), A197 (= A203), H198 (= H204), K224 (= K230), R357 (= R361)
7v3dA Complex structure of serine hydroxymethyltransferase from enterococcus faecium and its inhibitor (see paper)
61% identity, 97% coverage: 11:413/417 of query aligns to 4:409/409 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 (= E58), Y58 (= Y65), L115 (= L122), G119 (= G126), H120 (= H127), L121 (= L128), K340 (= K344), S342 (≠ G346), P350 (= P354), F351 (= F355), R357 (= R361)
- binding pyridoxal-5'-phosphate: Y49 (= Y56), S91 (= S98), G92 (= G99), S93 (= S100), H120 (= H127), S170 (= S176), D195 (= D201), A197 (= A203), K224 (= K230), G255 (= G260)
6ymfA Crystal structure of serine hydroxymethyltransferase from aphanothece halophytica in the plp-serine external aldimine state (see paper)
58% identity, 97% coverage: 9:414/417 of query aligns to 7:414/418 of 6ymfA
- active site: Y54 (= Y56), E56 (= E58), D200 (= D201), T226 (= T227), K229 (= K230), R235 (= R236)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: S34 (= S36), S96 (= S98), G97 (= G99), A98 (≠ S100), H125 (= H127), S175 (= S176), D200 (= D201), A202 (= A203), H203 (= H204), T226 (= T227), K229 (= K230), R361 (= R361)
6ymdA Crystal structure of serine hydroxymethyltransferase from aphanothece halophytica in the covalent complex with malonate (see paper)
58% identity, 97% coverage: 9:414/417 of query aligns to 7:414/420 of 6ymdA
- active site: Y54 (= Y56), E56 (= E58), D200 (= D201), T226 (= T227), K229 (= K230), R235 (= R236)
- binding malonate ion: S34 (= S36), Y54 (= Y56), E56 (= E58), Y64 (= Y66), H125 (= H127), H203 (= H204), K229 (= K230), R361 (= R361)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: Y54 (= Y56), S96 (= S98), G97 (= G99), A98 (≠ S100), H125 (= H127), Y174 (≠ A175), S175 (= S176), D200 (= D201), A202 (= A203), T226 (= T227), K229 (= K230), G261 (= G261)
1kl2A Crystal structure of serine hydroxymethyltransferase complexed with glycine and 5-formyl tetrahydrofolate (see paper)
61% identity, 95% coverage: 13:409/417 of query aligns to 8:405/405 of 1kl2A
- active site: Y51 (= Y56), E53 (= E58), D197 (= D201), T223 (= T227), K226 (= K230), R232 (= R236)
- 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 (= E58), Y60 (= Y65), G121 (= G126), H122 (= H127), S172 (= S176), F251 (= F255), N341 (= N345)
- binding glycine: S31 (= S36), Y51 (= Y56), Y61 (= Y66), H200 (= H204), R357 (= R361)
- binding pyridoxal-5'-phosphate: S93 (= S98), G94 (= G99), A95 (≠ S100), H122 (= H127), S172 (= S176), D197 (= D201), A199 (= A203), H200 (= H204), T223 (= T227), H225 (= H229), K226 (= K230)
1kl1A Crystal structure of serine hydroxymethyltransferase complexed with glycine (see paper)
61% identity, 95% coverage: 13:409/417 of query aligns to 8:405/405 of 1kl1A
- active site: Y51 (= Y56), E53 (= E58), D197 (= D201), T223 (= T227), K226 (= K230), R232 (= R236)
- binding glycine: S31 (= S36), H122 (= H127), R357 (= R361)
- binding pyridoxal-5'-phosphate: S93 (= S98), G94 (= G99), A95 (≠ S100), H122 (= H127), A171 (= A175), S172 (= S176), D197 (= D201), A199 (= A203), H200 (= H204), T223 (= T227), H225 (= H229), K226 (= K230)
1kkpA Crystal structure of serine hydroxymethyltransferase complexed with serine (see paper)
61% identity, 95% coverage: 13:409/417 of query aligns to 8:405/405 of 1kkpA
- active site: Y51 (= Y56), E53 (= E58), D197 (= D201), T223 (= T227), K226 (= K230), R232 (= R236)
- binding pyridoxal-5'-phosphate: S93 (= S98), G94 (= G99), A95 (≠ S100), H122 (= H127), S172 (= S176), D197 (= D201), A199 (= A203), H200 (= H204), K226 (= K230)
- binding serine: S31 (= S36), H122 (= H127), R357 (= R361)
1kkjA Crystal structure of serine hydroxymethyltransferase from b.Stearothermophilus (see paper)
61% identity, 95% coverage: 13:409/417 of query aligns to 8:405/405 of 1kkjA
- active site: Y51 (= Y56), E53 (= E58), D197 (= D201), T223 (= T227), K226 (= K230), R232 (= R236)
- binding pyridoxal-5'-phosphate: S93 (= S98), G94 (= G99), A95 (≠ S100), H122 (= H127), S172 (= S176), D197 (= D201), A199 (= A203), H200 (= H204), T223 (= T227), H225 (= H229), K226 (= K230)
2vmyA Crystal structure of f351gbsshmt in complex with gly and fthf (see paper)
61% identity, 95% coverage: 13:409/417 of query aligns to 8:405/405 of 2vmyA
- active site: Y51 (= Y56), E53 (= E58), D197 (= D201), T223 (= T227), K226 (= K230), R232 (= R236)
- 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 (= E58), Y60 (= Y65), Y61 (= Y66), L117 (= L122), G121 (= G126), H122 (= H127), L123 (= L128), S172 (= S176), K248 (≠ S252), F251 (= F255), N341 (= N345), S349 (≠ K353), P350 (= P354), G351 (≠ F355), R357 (= R361)
- binding glycine: S31 (= S36), Y51 (= Y56), Y61 (= Y66), H200 (= H204), K226 (= K230), R357 (= R361)
- binding pyridoxal-5'-phosphate: Y51 (= Y56), S93 (= S98), G94 (= G99), A95 (≠ S100), H122 (= H127), S172 (= S176), D197 (= D201), A199 (= A203), H200 (= H204), T223 (= T227), K226 (= K230), G257 (= G261)
2vmxA Crystal structure of f351gbsshmt in complex with l-allo-thr (see paper)
61% identity, 95% coverage: 13:409/417 of query aligns to 8:405/405 of 2vmxA
- active site: Y51 (= Y56), E53 (= E58), D197 (= D201), T223 (= T227), K226 (= K230), R232 (= R236)
- binding allo-threonine: S31 (= S36), H122 (= H127), H200 (= H204), R357 (= R361)
- binding pyridoxal-5'-phosphate: S93 (= S98), G94 (= G99), A95 (≠ S100), H122 (= H127), S172 (= S176), D197 (= D201), A199 (= A203), H200 (= H204), T223 (= T227), K226 (= K230)
3pgyB Serine hydroxymethyltransferase from staphylococcus aureus, s95p mutant.
58% identity, 97% coverage: 9:414/417 of query aligns to 4:404/404 of 3pgyB
4wxgA Crystal structure of l-serine hydroxymethyltransferase in complex with a mixture of l-threonine and glycine (see paper)
58% identity, 96% coverage: 13:414/417 of query aligns to 6:410/410 of 4wxgA
- active site: T43 (≠ S50), L45 (= L52), G189 (= G195), A215 (= A221), T218 (≠ V224), R230 (= R236)
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-threonine: S29 (= S36), Y49 (= Y56), E51 (= E58), Y59 (= Y66), S91 (= S98), G92 (= G99), S93 (= S100), H120 (= H127), S170 (= S176), D195 (= D201), A197 (= A203), H198 (= H204), T221 (= T227), K224 (= K230), G255 (= G260), R357 (= R361)
4wxfA Crystal structure of l-serine hydroxymethyltransferase in complex with glycine (see paper)
58% identity, 96% coverage: 13:414/417 of query aligns to 6:410/410 of 4wxfA
- active site: T43 (≠ S50), L45 (= L52), G189 (= G195), A215 (= A221), T218 (≠ V224), R230 (= R236)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S29 (= S36), Y49 (= Y56), Y59 (= Y66), S91 (= S98), G92 (= G99), S93 (= S100), H120 (= H127), S170 (= S176), D195 (= D201), A197 (= A203), H198 (= H204), H223 (= H229), K224 (= K230), G255 (= G260), R357 (= R361)
Query Sequence
>WP_028310448.1 NCBI__GCF_000482785.1:WP_028310448.1
MFNRATHTIASVDPELWSAIQAENGRQQDHIELIASENYTSPAVMEAQGSQLTNKYAEGY
PGKRYYGGCEYVDVVEQLAIDRLKKLFGAEAANVQPNSGSQANQAVFMAFLKPGDTIMGM
SLAEGGHLTHGMALNQSGKWFNVVSYGLNEAEDIDYDRMEALAREHKPKLIIAGASAFAL
RIDFERFGKIAKEVGAIFMVDMAHYAGLIAAGVYPNPVPFADVVTSTTHKSLRGPRGGII
LMKAEHEKAINSAIFPGIQGGPLMHVIAGKAVAFQEALQPEFKAYQEQVARNAKVMAETL
TKRGLRIVSGRTESHVMLVDLRALKITGKEAEKLLGEAHLTVNKNGIPNDPEKPFVTSGI
RIGTPALTTRGFKEAEAEKTANLIADVLAAPGDAAVLERVRAEVKKLTDAFPVYGGK
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