SitesBLAST
Comparing 350266 FitnessBrowser__Btheta:350266 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)
Q5SI56 Serine hydroxymethyltransferase; SHMT; Serine methylase; EC 2.1.2.1 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
56% identity, 96% coverage: 1:411/426 of query aligns to 5:398/407 of Q5SI56
- Y51 (= Y47) binding
- GS 94:95 (≠ GA 90:91) binding
- S172 (= S168) binding
- H200 (= H196) binding
- H225 (= H221) binding
- K226 (= K222) modified: N6-(pyridoxal phosphate)lysine
- G258 (= G269) binding
1kl2A Crystal structure of serine hydroxymethyltransferase complexed with glycine and 5-formyl tetrahydrofolate (see paper)
58% identity, 97% coverage: 2:414/426 of query aligns to 6:400/405 of 1kl2A
- active site: Y51 (= Y47), E53 (= E49), D197 (= D193), T223 (= T219), K226 (= K222), R232 (= R228)
- 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 (= E49), Y60 (= Y56), G121 (= G117), H122 (= H118), S172 (= S168), F251 (= F263), N341 (= N355)
- binding glycine: S31 (= S27), Y51 (= Y47), Y61 (= Y57), H200 (= H196), R357 (= R371)
- binding pyridoxal-5'-phosphate: S93 (= S89), G94 (= G90), A95 (= A91), H122 (= H118), S172 (= S168), D197 (= D193), A199 (= A195), H200 (= H196), T223 (= T219), H225 (= H221), K226 (= K222)
1kl1A Crystal structure of serine hydroxymethyltransferase complexed with glycine (see paper)
58% identity, 97% coverage: 2:414/426 of query aligns to 6:400/405 of 1kl1A
- active site: Y51 (= Y47), E53 (= E49), D197 (= D193), T223 (= T219), K226 (= K222), R232 (= R228)
- binding glycine: S31 (= S27), H122 (= H118), R357 (= R371)
- binding pyridoxal-5'-phosphate: S93 (= S89), G94 (= G90), A95 (= A91), H122 (= H118), A171 (≠ G167), S172 (= S168), D197 (= D193), A199 (= A195), H200 (= H196), T223 (= T219), H225 (= H221), K226 (= K222)
1kkpA Crystal structure of serine hydroxymethyltransferase complexed with serine (see paper)
58% identity, 97% coverage: 2:414/426 of query aligns to 6:400/405 of 1kkpA
- active site: Y51 (= Y47), E53 (= E49), D197 (= D193), T223 (= T219), K226 (= K222), R232 (= R228)
- binding pyridoxal-5'-phosphate: S93 (= S89), G94 (= G90), A95 (= A91), H122 (= H118), S172 (= S168), D197 (= D193), A199 (= A195), H200 (= H196), K226 (= K222)
- binding serine: S31 (= S27), H122 (= H118), R357 (= R371)
1kkjA Crystal structure of serine hydroxymethyltransferase from b.Stearothermophilus (see paper)
58% identity, 97% coverage: 2:414/426 of query aligns to 6:400/405 of 1kkjA
- active site: Y51 (= Y47), E53 (= E49), D197 (= D193), T223 (= T219), K226 (= K222), R232 (= R228)
- binding pyridoxal-5'-phosphate: S93 (= S89), G94 (= G90), A95 (= A91), H122 (= H118), S172 (= S168), D197 (= D193), A199 (= A195), H200 (= H196), T223 (= T219), H225 (= H221), K226 (= K222)
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)
56% identity, 96% coverage: 2:411/426 of query aligns to 1:393/402 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)
56% identity, 96% coverage: 2:411/426 of query aligns to 1:393/402 of 8ssyA
2dkjA Crystal structure of t.Th.Hb8 serine hydroxymethyltransferase
56% identity, 96% coverage: 2:411/426 of query aligns to 1:393/402 of 2dkjA
- active site: Y46 (= Y47), E48 (= E49), D192 (= D193), T218 (= T219), K221 (= K222), R227 (= R228)
- binding pyridoxal-5'-phosphate: S88 (= S89), G89 (= G90), S90 (≠ A91), H117 (= H118), S167 (= S168), D192 (= D193), A194 (= A195), H220 (= H221), K221 (= K222)
2vmyA Crystal structure of f351gbsshmt in complex with gly and fthf (see paper)
57% identity, 97% coverage: 2:414/426 of query aligns to 6:400/405 of 2vmyA
- active site: Y51 (= Y47), E53 (= E49), D197 (= D193), T223 (= T219), K226 (= K222), R232 (= R228)
- 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 (= E49), Y60 (= Y56), Y61 (= Y57), L117 (= L113), G121 (= G117), H122 (= H118), L123 (= L119), S172 (= S168), K248 (≠ S260), F251 (= F263), N341 (= N355), S349 (= S363), P350 (≠ A364), G351 (≠ F365), R357 (= R371)
- binding glycine: S31 (= S27), Y51 (= Y47), Y61 (= Y57), H200 (= H196), K226 (= K222), R357 (= R371)
- binding pyridoxal-5'-phosphate: Y51 (= Y47), S93 (= S89), G94 (= G90), A95 (= A91), H122 (= H118), S172 (= S168), D197 (= D193), A199 (= A195), H200 (= H196), T223 (= T219), K226 (= K222), G257 (= G269)
2vmxA Crystal structure of f351gbsshmt in complex with l-allo-thr (see paper)
57% identity, 97% coverage: 2:414/426 of query aligns to 6:400/405 of 2vmxA
- active site: Y51 (= Y47), E53 (= E49), D197 (= D193), T223 (= T219), K226 (= K222), R232 (= R228)
- binding allo-threonine: S31 (= S27), H122 (= H118), H200 (= H196), R357 (= R371)
- binding pyridoxal-5'-phosphate: S93 (= S89), G94 (= G90), A95 (= A91), H122 (= H118), S172 (= S168), D197 (= D193), A199 (= A195), H200 (= H196), T223 (= T219), K226 (= K222)
3pgyB Serine hydroxymethyltransferase from staphylococcus aureus, s95p mutant.
55% identity, 99% coverage: 2:424/426 of query aligns to 6:404/404 of 3pgyB
6ymfA Crystal structure of serine hydroxymethyltransferase from aphanothece halophytica in the plp-serine external aldimine state (see paper)
55% identity, 100% coverage: 1:424/426 of query aligns to 8:414/418 of 6ymfA
- active site: Y54 (= Y47), E56 (= E49), D200 (= D193), T226 (= T219), K229 (= K222), R235 (= R228)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: S34 (= S27), S96 (= S89), G97 (= G90), A98 (= A91), H125 (= H118), S175 (= S168), D200 (= D193), A202 (= A195), H203 (= H196), T226 (= T219), K229 (= K222), R361 (= R371)
6ymdA Crystal structure of serine hydroxymethyltransferase from aphanothece halophytica in the covalent complex with malonate (see paper)
55% identity, 100% coverage: 1:424/426 of query aligns to 8:414/420 of 6ymdA
- active site: Y54 (= Y47), E56 (= E49), D200 (= D193), T226 (= T219), K229 (= K222), R235 (= R228)
- binding malonate ion: S34 (= S27), Y54 (= Y47), E56 (= E49), Y64 (= Y57), H125 (= H118), H203 (= H196), K229 (= K222), R361 (= R371)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: Y54 (= Y47), S96 (= S89), G97 (= G90), A98 (= A91), H125 (= H118), Y174 (≠ G167), S175 (= S168), D200 (= D193), A202 (= A195), T226 (= T219), K229 (= K222), G261 (= G269)
4n0wA X-ray crystal structure of a serine hydroxymethyltransferase from burkholderia cenocepacia with covalently attached pyridoxal phosphate
56% identity, 99% coverage: 4:424/426 of query aligns to 14:415/416 of 4n0wA
- active site: Y57 (= Y47), E59 (= E49), D202 (= D193), T228 (= T219), K231 (= K222), R237 (= R228)
- binding pyridoxal-5'-phosphate: S99 (= S89), G100 (= G90), S101 (≠ A91), H128 (= H118), D202 (= D193), A204 (= A195), H205 (= H196), K231 (= K222)
4otlA X-ray crystal structure of serine hydroxymethyl transferase from burkholderia cenocepacia bound to plp and glycine
56% identity, 99% coverage: 4:424/426 of query aligns to 7:408/409 of 4otlA
- active site: Y50 (= Y47), E52 (= E49), D195 (= D193), T221 (= T219), K224 (= K222), R230 (= R228)
- binding glycine: S30 (= S27), Y50 (= Y47), Y60 (= Y57), H121 (= H118), K224 (= K222), R355 (= R371)
- binding pyridoxal-5'-phosphate: S92 (= S89), G93 (= G90), S94 (≠ A91), H121 (= H118), S170 (= S168), D195 (= D193), A197 (= A195), H198 (= H196), K224 (= K222)
4ot8A X-ray crystal structure of serine hydroxymethyl transferase from burkholderia cenocepacia bound to plp and serine
56% identity, 99% coverage: 4:424/426 of query aligns to 12:413/414 of 4ot8A
- active site: Y55 (= Y47), E57 (= E49), D200 (= D193), T226 (= T219), K229 (= K222), R235 (= R228)
- binding pyridoxal-5'-phosphate: S97 (= S89), G98 (= G90), S99 (≠ A91), H126 (= H118), D200 (= D193), A202 (= A195), H203 (= H196), K229 (= K222)
- binding serine: S35 (= S27), E57 (= E49), Y65 (= Y57), H126 (= H118), H203 (= H196), R360 (= R371)
1dfoB Crystal structure at 2.4 angstrom resolution of e. Coli serine hydroxymethyltransferase in complex with glycine and 5-formyl tetrahydrofolate (see paper)
56% identity, 99% coverage: 4:425/426 of query aligns to 12:417/417 of 1dfoB
- active site: Y55 (= Y47), E57 (= E49), D200 (= D193), T226 (= T219), K229 (= K222), R235 (= R228)
- 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 (= E49), Y64 (= Y56), Y65 (= Y57), L121 (= L113), G125 (= G117), H126 (= H118), L127 (= L119), S175 (= S168), S245 (≠ I251), E247 (≠ M253), N347 (= N355), S355 (= S363), P356 (≠ A364), F357 (= F365)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S35 (= S27), Y55 (= Y47), Y65 (= Y57), S97 (= S89), G98 (= G90), S99 (≠ A91), H126 (= H118), F174 (≠ G167), S175 (= S168), D200 (= D193), A202 (= A195), H203 (= H196), K229 (= K222), G262 (= G268), R363 (= R371)
P0A825 Serine hydroxymethyltransferase; SHMT; Serine methylase; EC 2.1.2.1 from Escherichia coli (strain K12) (see 8 papers)
56% identity, 99% coverage: 4:425/426 of query aligns to 12:417/417 of P0A825
- K54 (= K46) modified: N6-acetyllysine
- Y55 (= Y47) 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 (= K54) modified: N6-succinyllysine
- Y65 (= Y57) mutation to F: Decrease in catalytic activity.
- L85 (≠ I77) 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 (≠ E207) 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 (= P209) 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 (≠ K211) 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 (= H221) 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 (= K222) modified: N6-(pyridoxal phosphate)lysine
- R235 (= R228) 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 (= K248) modified: N6-succinyllysine
- K250 (≠ Q256) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- P258 (= P264) mutation to A: Important decrease in affinity and catalytic efficiency. Reduced thermal stability.; mutation to G: Important decrease in affinity and catalytic efficiency.
- P264 (= P270) mutation to A: Important decrease in affinity and catalytic efficiency.; mutation to G: Important decrease in affinity and catalytic efficiency.
- L276 (≠ F282) 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 (≠ G283) modified: N6-succinyllysine
- K285 (= K291) modified: N6-acetyllysine
- K293 (= K299) modified: N6-succinyllysine
- K331 (= K339) modified: N6-succinyllysine
- K346 (= K354) modified: N6-succinyllysine
- K354 (≠ R362) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- R363 (= R371) 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 (= R380) mutation to A: No significant difference compared to the wild-type.; mutation to K: No significant difference compared to the wild-type.
- K375 (= K383) 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)
56% identity, 99% coverage: 4:425/426 of query aligns to 11:416/416 of 1eqbA
- active site: Y54 (= Y47), E56 (= E49), D199 (= D193), T225 (= T219), K228 (= K222), R234 (= R228)
- 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 (= E49), Y63 (= Y56), L120 (= L113), G123 (= G116), G124 (= G117), H125 (= H118), L126 (= L119), S174 (= S168), N346 (= N355), S354 (= S363), P355 (≠ A364), F356 (= F365)
- binding glycine: S34 (= S27), Y54 (= Y47), F64 (≠ Y57), H202 (= H196), K228 (= K222), R362 (= R371)
- binding pyridoxal-5'-phosphate: S96 (= S89), G97 (= G90), S98 (≠ A91), H125 (= H118), F173 (≠ G167), S174 (= S168), D199 (= D193), H202 (= H196), H227 (= H221), K228 (= K222)
7x5nA Crystal structure of e. Faecium shmt in complex with (+)-shin-1 and plp-ser (see paper)
52% identity, 99% coverage: 4:423/426 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 (= E49), Y58 (= Y56), Y59 (= Y57), L115 (= L113), G119 (= G117), H120 (= H118), L121 (= L119), K340 (= K354), N341 (= N355), S342 (≠ M356), P350 (≠ A364), F351 (= F365), R357 (= R371)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: S29 (= S27), Y49 (= Y47), E51 (= E49), Y59 (= Y57), S91 (= S89), G92 (= G90), S93 (≠ A91), H120 (= H118), S170 (= S168), D195 (= D193), A197 (= A195), H198 (= H196), K224 (= K222), R357 (= R371)
Query Sequence
>350266 FitnessBrowser__Btheta:350266
MKRDDLIFDIIEKEHQRQLKGIELIASENFVSDQVMQAMGSCLTNKYAEGYPGKRYYGGC
EVVDQSEQIAIDRLKEIFGAEWANVQPHSGAQANAAVFLAVLNPGDKFMGLNLAHGGHLS
HGSLVNTSGIIYTPCEYNLNQETGRVDYDQMEEVALREKPKMIIGGGSAYSREWDYKRMR
EIADKVGAILMIDMAHPAGLIAAGLLENPVKYAHIVTSTTHKTLRGPRGGVIMMGKDFPN
PWGKKTPKGEIKMMSQLLDSAVFPGVQGGPLEHVIAAKAVAFGEILQPEYKEYAKQVQKN
AAILAQALIDRGFTIVSGGTDNHSMLVDLRSKYPDLTGKVAEKALVSADITVNKNMVPFD
SRSAFQTSGIRLGTPAITTRGAKEDLMIEIAEMIETVLSNVENEEVIAQVRARVNETMKK
YPLFAD
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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