SitesBLAST
Comparing WP_012384224.1 NCBI__GCF_000019845.1:WP_012384224.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
6ymdA Crystal structure of serine hydroxymethyltransferase from aphanothece halophytica in the covalent complex with malonate (see paper)
59% identity, 96% coverage: 20:433/433 of query aligns to 7:414/420 of 6ymdA
- active site: Y54 (= Y67), E56 (= E69), D200 (= D213), T226 (= T239), K229 (= K242), R235 (= R248)
- binding malonate ion: S34 (= S47), Y54 (= Y67), E56 (= E69), Y64 (= Y77), H125 (= H138), H203 (= H216), K229 (= K242), R361 (= R374)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: Y54 (= Y67), S96 (= S109), G97 (= G110), A98 (≠ S111), H125 (= H138), Y174 (≠ G187), S175 (= S188), D200 (= D213), A202 (= A215), T226 (= T239), K229 (= K242), G261 (= G274)
6ymfA Crystal structure of serine hydroxymethyltransferase from aphanothece halophytica in the plp-serine external aldimine state (see paper)
59% identity, 96% coverage: 20:433/433 of query aligns to 7:414/418 of 6ymfA
- active site: Y54 (= Y67), E56 (= E69), D200 (= D213), T226 (= T239), K229 (= K242), R235 (= R248)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: S34 (= S47), S96 (= S109), G97 (= G110), A98 (≠ S111), H125 (= H138), S175 (= S188), D200 (= D213), A202 (= A215), H203 (= H216), T226 (= T239), K229 (= K242), R361 (= R374)
4n0wA X-ray crystal structure of a serine hydroxymethyltransferase from burkholderia cenocepacia with covalently attached pyridoxal phosphate
63% identity, 96% coverage: 18:433/433 of query aligns to 8:415/416 of 4n0wA
- active site: Y57 (= Y67), E59 (= E69), D202 (= D213), T228 (= T239), K231 (= K242), R237 (= R248)
- binding pyridoxal-5'-phosphate: S99 (= S109), G100 (= G110), S101 (= S111), H128 (= H138), D202 (= D213), A204 (= A215), H205 (= H216), K231 (= K242)
4otlA X-ray crystal structure of serine hydroxymethyl transferase from burkholderia cenocepacia bound to plp and glycine
63% identity, 96% coverage: 18:433/433 of query aligns to 1:408/409 of 4otlA
- active site: Y50 (= Y67), E52 (= E69), D195 (= D213), T221 (= T239), K224 (= K242), R230 (= R248)
- binding glycine: S30 (= S47), Y50 (= Y67), Y60 (= Y77), H121 (= H138), K224 (= K242), R355 (= R374)
- binding pyridoxal-5'-phosphate: S92 (= S109), G93 (= G110), S94 (= S111), H121 (= H138), S170 (= S188), D195 (= D213), A197 (= A215), H198 (= H216), K224 (= K242)
4ot8A X-ray crystal structure of serine hydroxymethyl transferase from burkholderia cenocepacia bound to plp and serine
63% identity, 96% coverage: 18:433/433 of query aligns to 6:413/414 of 4ot8A
- active site: Y55 (= Y67), E57 (= E69), D200 (= D213), T226 (= T239), K229 (= K242), R235 (= R248)
- binding pyridoxal-5'-phosphate: S97 (= S109), G98 (= G110), S99 (= S111), H126 (= H138), D200 (= D213), A202 (= A215), H203 (= H216), K229 (= K242)
- binding serine: S35 (= S47), E57 (= E69), Y65 (= Y77), H126 (= H138), H203 (= H216), R360 (= R374)
Q5SI56 Serine hydroxymethyltransferase; SHMT; Serine methylase; EC 2.1.2.1 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
64% identity, 87% coverage: 24:401/433 of query aligns to 8:385/407 of Q5SI56
- Y51 (= Y67) binding pyridoxal 5'-phosphate
- GS 94:95 (= GS 110:111) binding pyridoxal 5'-phosphate
- S172 (= S188) binding pyridoxal 5'-phosphate
- H200 (= H216) binding pyridoxal 5'-phosphate
- H225 (= H241) binding pyridoxal 5'-phosphate
- K226 (= K242) modified: N6-(pyridoxal phosphate)lysine
- G258 (= G274) 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)
64% identity, 87% coverage: 24:401/433 of query aligns to 3:380/402 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)
64% identity, 87% coverage: 24:401/433 of query aligns to 3:380/402 of 8ssyA
2dkjA Crystal structure of t.Th.Hb8 serine hydroxymethyltransferase
64% identity, 87% coverage: 24:401/433 of query aligns to 3:380/402 of 2dkjA
- active site: Y46 (= Y67), E48 (= E69), D192 (= D213), T218 (= T239), K221 (= K242), R227 (= R248)
- binding pyridoxal-5'-phosphate: S88 (= S109), G89 (= G110), S90 (= S111), H117 (= H138), S167 (= S188), D192 (= D213), A194 (= A215), H220 (= H241), K221 (= K242)
1kl2A Crystal structure of serine hydroxymethyltransferase complexed with glycine and 5-formyl tetrahydrofolate (see paper)
60% identity, 94% coverage: 20:427/433 of query aligns to 4:404/405 of 1kl2A
- active site: Y51 (= Y67), E53 (= E69), D197 (= D213), T223 (= T239), K226 (= K242), R232 (= R248)
- 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 (= E69), Y60 (= Y76), G121 (= G137), H122 (= H138), S172 (= S188), F251 (= F268), N341 (= N358)
- binding glycine: S31 (= S47), Y51 (= Y67), Y61 (= Y77), H200 (= H216), R357 (= R374)
- binding pyridoxal-5'-phosphate: S93 (= S109), G94 (= G110), A95 (≠ S111), H122 (= H138), S172 (= S188), D197 (= D213), A199 (= A215), H200 (= H216), T223 (= T239), H225 (= H241), K226 (= K242)
1kl1A Crystal structure of serine hydroxymethyltransferase complexed with glycine (see paper)
60% identity, 94% coverage: 20:427/433 of query aligns to 4:404/405 of 1kl1A
- active site: Y51 (= Y67), E53 (= E69), D197 (= D213), T223 (= T239), K226 (= K242), R232 (= R248)
- binding glycine: S31 (= S47), H122 (= H138), R357 (= R374)
- binding pyridoxal-5'-phosphate: S93 (= S109), G94 (= G110), A95 (≠ S111), H122 (= H138), A171 (≠ G187), S172 (= S188), D197 (= D213), A199 (= A215), H200 (= H216), T223 (= T239), H225 (= H241), K226 (= K242)
1kkpA Crystal structure of serine hydroxymethyltransferase complexed with serine (see paper)
60% identity, 94% coverage: 20:427/433 of query aligns to 4:404/405 of 1kkpA
- active site: Y51 (= Y67), E53 (= E69), D197 (= D213), T223 (= T239), K226 (= K242), R232 (= R248)
- binding pyridoxal-5'-phosphate: S93 (= S109), G94 (= G110), A95 (≠ S111), H122 (= H138), S172 (= S188), D197 (= D213), A199 (= A215), H200 (= H216), K226 (= K242)
- binding serine: S31 (= S47), H122 (= H138), R357 (= R374)
1kkjA Crystal structure of serine hydroxymethyltransferase from b.Stearothermophilus (see paper)
60% identity, 94% coverage: 20:427/433 of query aligns to 4:404/405 of 1kkjA
- active site: Y51 (= Y67), E53 (= E69), D197 (= D213), T223 (= T239), K226 (= K242), R232 (= R248)
- binding pyridoxal-5'-phosphate: S93 (= S109), G94 (= G110), A95 (≠ S111), H122 (= H138), S172 (= S188), D197 (= D213), A199 (= A215), H200 (= H216), T223 (= T239), H225 (= H241), K226 (= K242)
2vmyA Crystal structure of f351gbsshmt in complex with gly and fthf (see paper)
60% identity, 94% coverage: 20:427/433 of query aligns to 4:404/405 of 2vmyA
- active site: Y51 (= Y67), E53 (= E69), D197 (= D213), T223 (= T239), K226 (= K242), R232 (= R248)
- 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 (= E69), Y60 (= Y76), Y61 (= Y77), L117 (= L133), G121 (= G137), H122 (= H138), L123 (= L139), S172 (= S188), K248 (≠ S265), F251 (= F268), N341 (= N358), S349 (= S366), P350 (= P367), G351 (≠ F368), R357 (= R374)
- binding glycine: S31 (= S47), Y51 (= Y67), Y61 (= Y77), H200 (= H216), K226 (= K242), R357 (= R374)
- binding pyridoxal-5'-phosphate: Y51 (= Y67), S93 (= S109), G94 (= G110), A95 (≠ S111), H122 (= H138), S172 (= S188), D197 (= D213), A199 (= A215), H200 (= H216), T223 (= T239), K226 (= K242), G257 (= G274)
2vmxA Crystal structure of f351gbsshmt in complex with l-allo-thr (see paper)
60% identity, 94% coverage: 20:427/433 of query aligns to 4:404/405 of 2vmxA
- active site: Y51 (= Y67), E53 (= E69), D197 (= D213), T223 (= T239), K226 (= K242), R232 (= R248)
- binding allo-threonine: S31 (= S47), H122 (= H138), H200 (= H216), R357 (= R374)
- binding pyridoxal-5'-phosphate: S93 (= S109), G94 (= G110), A95 (≠ S111), H122 (= H138), S172 (= S188), D197 (= D213), A199 (= A215), H200 (= H216), T223 (= T239), K226 (= K242)
7x5oB Crystal structure of e. Faecium shmt in complex with me-thf and plp- gly (see paper)
58% identity, 95% coverage: 24:433/433 of query aligns to 7:411/412 of 7x5oB
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S30 (= S47), Y50 (= Y67), Y60 (= Y77), S92 (= S109), G93 (= G110), S94 (= S111), H121 (= H138), S171 (= S188), D196 (= D213), A198 (= A215), H199 (= H216), K225 (= K242), R358 (= R374)
- binding n-[4-({[(6s)-2-amino-4-hydroxy-5-methyl-5,6,7,8-tetrahydropteridin-6-yl]methyl}amino)benzoyl]-l-glutamic acid: E52 (= E69), Y59 (= Y76), L116 (= L133), G119 (= G136), G120 (= G137), H121 (= H138), S171 (= S188), P252 (= P269), N342 (= N358), P351 (= P367)
7x5nA Crystal structure of e. Faecium shmt in complex with (+)-shin-1 and plp-ser (see paper)
59% identity, 94% coverage: 24:432/433 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 (= E69), Y58 (= Y76), Y59 (= Y77), L115 (= L133), G119 (= G137), H120 (= H138), L121 (= L139), K340 (= K357), N341 (= N358), S342 (≠ G359), P350 (= P367), F351 (= F368), R357 (= R374)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: S29 (= S47), Y49 (= Y67), E51 (= E69), Y59 (= Y77), S91 (= S109), G92 (= G110), S93 (= S111), H120 (= H138), S170 (= S188), D195 (= D213), A197 (= A215), H198 (= H216), K224 (= K242), R357 (= R374)
7v3dA Complex structure of serine hydroxymethyltransferase from enterococcus faecium and its inhibitor (see paper)
59% identity, 94% coverage: 24:432/433 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 (= E69), Y58 (= Y76), L115 (= L133), G119 (= G137), H120 (= H138), L121 (= L139), K340 (= K357), S342 (≠ G359), P350 (= P367), F351 (= F368), R357 (= R374)
- binding pyridoxal-5'-phosphate: Y49 (= Y67), S91 (= S109), G92 (= G110), S93 (= S111), H120 (= H138), S170 (= S188), D195 (= D213), A197 (= A215), K224 (= K242), G255 (= G273)
4wxgA Crystal structure of l-serine hydroxymethyltransferase in complex with a mixture of l-threonine and glycine (see paper)
59% identity, 95% coverage: 24:433/433 of query aligns to 6:410/410 of 4wxgA
- active site: T43 (≠ S61), L45 (≠ M63), G189 (= G207), A215 (= A233), T218 (≠ V236), R230 (= R248)
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-threonine: S29 (= S47), Y49 (= Y67), E51 (= E69), Y59 (= Y77), S91 (= S109), G92 (= G110), S93 (= S111), H120 (= H138), S170 (= S188), D195 (= D213), A197 (= A215), H198 (= H216), T221 (= T239), K224 (= K242), G255 (= G273), R357 (= R374)
4wxfA Crystal structure of l-serine hydroxymethyltransferase in complex with glycine (see paper)
59% identity, 95% coverage: 24:433/433 of query aligns to 6:410/410 of 4wxfA
- active site: T43 (≠ S61), L45 (≠ M63), G189 (= G207), A215 (= A233), T218 (≠ V236), R230 (= R248)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S29 (= S47), Y49 (= Y67), Y59 (= Y77), S91 (= S109), G92 (= G110), S93 (= S111), H120 (= H138), S170 (= S188), D195 (= D213), A197 (= A215), H198 (= H216), H223 (= H241), K224 (= K242), G255 (= G273), R357 (= R374)
Query Sequence
>WP_012384224.1 NCBI__GCF_000019845.1:WP_012384224.1
MNAKVEVGQPAANSFFAANLADADPEIAKAIELELGRQRHEIELIASENIVSKAVLEAQG
SIMTNKYAEGYPGKRYYGGCQFVDIAENLAIERVRKLFDCQFANVQPNSGSQANQAVFLA
LLQPGDVFMGLDLAAGGHLTHGSPVNLSGKWFKAVSYGVRQSDHLIDMDAVEALAKEHKP
KLIIAGGSAYPRHWDFARFRAIADSVGAYFFVDMAHFAGLVAGGAHPSPFPHAHVVTSTT
HKTLRGPRGGLVLTNDADIAKKINSAVFPGLQGGPLMHVIAAKAVAFGEALRPDFRLYAQ
QVVVNAGTLASRLVEKGFAISSGGTDNHLMLVDLRPKQLTGKAAEAALGRASITCNKNGV
PFDTASPFVTSGIRLGSPAATSRGFGTKEFQDVADLIAETLDGLAKNGEEGNAAVEASVK
ERAIALTQRFPIY
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