SitesBLAST
Comparing WP_011973756.1 NCBI__GCF_000017185.1:WP_011973756.1 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)
4uqvG Methanococcus jannaschii serine hydroxymethyl-transferase in complex with plp (see paper)
80% identity, 100% coverage: 1:429/429 of query aligns to 1:429/429 of 4uqvG
- active site: Y50 (= Y50), E52 (= E52), D196 (= D196), S223 (= S223), K226 (= K226), Q232 (= Q232)
- binding pyridoxal-5'-phosphate: G93 (= G93), V94 (= V94), H121 (= H121), A198 (= A198), H199 (= H199), S223 (= S223), H225 (= H225), K226 (= K226)
4bhdB Methanococcus jannaschii serine hydroxymethyl-transferase, apo form (see paper)
74% identity, 99% coverage: 4:429/429 of query aligns to 3:395/395 of 4bhdB
2vmyA Crystal structure of f351gbsshmt in complex with gly and fthf (see paper)
37% identity, 84% coverage: 25:386/429 of query aligns to 26:380/405 of 2vmyA
- active site: Y51 (= Y50), E53 (= E52), D197 (= D196), T223 (≠ S223), K226 (= K226), R232 (≠ Q232)
- 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 (= E52), Y60 (≠ L59), Y61 (= Y60), L117 (≠ V116), G121 (= G120), H122 (= H121), L123 (≠ I122), S172 (= S171), K248 (≠ D248), F251 (= F251), N341 (= N346), S349 (= S354), P350 (≠ N355), G351 (≠ S356), R357 (= R363)
- binding glycine: S31 (= S30), Y51 (= Y50), Y61 (= Y60), H200 (= H199), K226 (= K226), R357 (= R363)
- binding pyridoxal-5'-phosphate: Y51 (= Y50), S93 (= S92), G94 (= G93), A95 (≠ V94), H122 (= H121), S172 (= S171), D197 (= D196), A199 (= A198), H200 (= H199), T223 (≠ S223), K226 (= K226), G257 (≠ N257)
2vmxA Crystal structure of f351gbsshmt in complex with l-allo-thr (see paper)
37% identity, 84% coverage: 25:386/429 of query aligns to 26:380/405 of 2vmxA
- active site: Y51 (= Y50), E53 (= E52), D197 (= D196), T223 (≠ S223), K226 (= K226), R232 (≠ Q232)
- binding allo-threonine: S31 (= S30), H122 (= H121), H200 (= H199), R357 (= R363)
- binding pyridoxal-5'-phosphate: S93 (= S92), G94 (= G93), A95 (≠ V94), H122 (= H121), S172 (= S171), D197 (= D196), A199 (= A198), H200 (= H199), T223 (≠ S223), K226 (= K226)
6ymfA Crystal structure of serine hydroxymethyltransferase from aphanothece halophytica in the plp-serine external aldimine state (see paper)
35% identity, 93% coverage: 16:412/429 of query aligns to 20:409/418 of 6ymfA
- active site: Y54 (= Y50), E56 (= E52), D200 (= D196), T226 (≠ S223), K229 (= K226), R235 (≠ Q232)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: S34 (= S30), S96 (= S92), G97 (= G93), A98 (≠ V94), H125 (= H121), S175 (= S171), D200 (= D196), A202 (= A198), H203 (= H199), T226 (≠ S223), K229 (= K226), R361 (= R363)
6ymdA Crystal structure of serine hydroxymethyltransferase from aphanothece halophytica in the covalent complex with malonate (see paper)
35% identity, 93% coverage: 16:412/429 of query aligns to 20:409/420 of 6ymdA
- active site: Y54 (= Y50), E56 (= E52), D200 (= D196), T226 (≠ S223), K229 (= K226), R235 (≠ Q232)
- binding malonate ion: S34 (= S30), Y54 (= Y50), E56 (= E52), Y64 (= Y60), H125 (= H121), H203 (= H199), K229 (= K226), R361 (= R363)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: Y54 (= Y50), S96 (= S92), G97 (= G93), A98 (≠ V94), H125 (= H121), Y174 (≠ G170), S175 (= S171), D200 (= D196), A202 (= A198), T226 (≠ S223), K229 (= K226), G261 (≠ N257)
4n0wA X-ray crystal structure of a serine hydroxymethyltransferase from burkholderia cenocepacia with covalently attached pyridoxal phosphate
35% identity, 93% coverage: 14:410/429 of query aligns to 20:412/416 of 4n0wA
- active site: Y57 (= Y50), E59 (= E52), D202 (= D196), T228 (≠ S223), K231 (= K226), R237 (≠ Q232)
- binding pyridoxal-5'-phosphate: S99 (= S92), G100 (= G93), S101 (≠ V94), H128 (= H121), D202 (= D196), A204 (= A198), H205 (= H199), K231 (= K226)
4otlA X-ray crystal structure of serine hydroxymethyl transferase from burkholderia cenocepacia bound to plp and glycine
35% identity, 93% coverage: 14:410/429 of query aligns to 13:405/409 of 4otlA
- active site: Y50 (= Y50), E52 (= E52), D195 (= D196), T221 (≠ S223), K224 (= K226), R230 (≠ Q232)
- binding glycine: S30 (= S30), Y50 (= Y50), Y60 (= Y60), H121 (= H121), K224 (= K226), R355 (= R363)
- binding pyridoxal-5'-phosphate: S92 (= S92), G93 (= G93), S94 (≠ V94), H121 (= H121), S170 (= S171), D195 (= D196), A197 (= A198), H198 (= H199), K224 (= K226)
4ot8A X-ray crystal structure of serine hydroxymethyl transferase from burkholderia cenocepacia bound to plp and serine
35% identity, 93% coverage: 14:410/429 of query aligns to 18:410/414 of 4ot8A
- active site: Y55 (= Y50), E57 (= E52), D200 (= D196), T226 (≠ S223), K229 (= K226), R235 (≠ Q232)
- binding pyridoxal-5'-phosphate: S97 (= S92), G98 (= G93), S99 (≠ V94), H126 (= H121), D200 (= D196), A202 (= A198), H203 (= H199), K229 (= K226)
- binding serine: S35 (= S30), E57 (= E52), Y65 (= Y60), H126 (= H121), H203 (= H199), R360 (= R363)
1kl2A Crystal structure of serine hydroxymethyltransferase complexed with glycine and 5-formyl tetrahydrofolate (see paper)
37% identity, 84% coverage: 25:386/429 of query aligns to 26:380/405 of 1kl2A
- active site: Y51 (= Y50), E53 (= E52), D197 (= D196), T223 (≠ S223), K226 (= K226), R232 (≠ Q232)
- 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 (= E52), Y60 (≠ L59), G121 (= G120), H122 (= H121), S172 (= S171), F251 (= F251), N341 (= N346)
- binding glycine: S31 (= S30), Y51 (= Y50), Y61 (= Y60), H200 (= H199), R357 (= R363)
- binding pyridoxal-5'-phosphate: S93 (= S92), G94 (= G93), A95 (≠ V94), H122 (= H121), S172 (= S171), D197 (= D196), A199 (= A198), H200 (= H199), T223 (≠ S223), H225 (= H225), K226 (= K226)
1kl1A Crystal structure of serine hydroxymethyltransferase complexed with glycine (see paper)
37% identity, 84% coverage: 25:386/429 of query aligns to 26:380/405 of 1kl1A
- active site: Y51 (= Y50), E53 (= E52), D197 (= D196), T223 (≠ S223), K226 (= K226), R232 (≠ Q232)
- binding glycine: S31 (= S30), H122 (= H121), R357 (= R363)
- binding pyridoxal-5'-phosphate: S93 (= S92), G94 (= G93), A95 (≠ V94), H122 (= H121), A171 (≠ G170), S172 (= S171), D197 (= D196), A199 (= A198), H200 (= H199), T223 (≠ S223), H225 (= H225), K226 (= K226)
1kkpA Crystal structure of serine hydroxymethyltransferase complexed with serine (see paper)
37% identity, 84% coverage: 25:386/429 of query aligns to 26:380/405 of 1kkpA
- active site: Y51 (= Y50), E53 (= E52), D197 (= D196), T223 (≠ S223), K226 (= K226), R232 (≠ Q232)
- binding pyridoxal-5'-phosphate: S93 (= S92), G94 (= G93), A95 (≠ V94), H122 (= H121), S172 (= S171), D197 (= D196), A199 (= A198), H200 (= H199), K226 (= K226)
- binding serine: S31 (= S30), H122 (= H121), R357 (= R363)
1kkjA Crystal structure of serine hydroxymethyltransferase from b.Stearothermophilus (see paper)
37% identity, 84% coverage: 25:386/429 of query aligns to 26:380/405 of 1kkjA
- active site: Y51 (= Y50), E53 (= E52), D197 (= D196), T223 (≠ S223), K226 (= K226), R232 (≠ Q232)
- binding pyridoxal-5'-phosphate: S93 (= S92), G94 (= G93), A95 (≠ V94), H122 (= H121), S172 (= S171), D197 (= D196), A199 (= A198), H200 (= H199), T223 (≠ S223), H225 (= H225), K226 (= K226)
Q5SI56 Serine hydroxymethyltransferase; SHMT; Serine methylase; EC 2.1.2.1 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
36% identity, 91% coverage: 22:410/429 of query aligns to 23:404/407 of Q5SI56
- Y51 (= Y50) binding
- GS 94:95 (≠ GV 93:94) binding
- S172 (= S171) binding
- H200 (= H199) binding
- H225 (= H225) binding
- K226 (= K226) modified: N6-(pyridoxal phosphate)lysine
- G258 (≠ N257) 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)
36% identity, 91% coverage: 22:410/429 of query aligns to 18:399/402 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)
36% identity, 91% coverage: 22:410/429 of query aligns to 18:399/402 of 8ssyA
2dkjA Crystal structure of t.Th.Hb8 serine hydroxymethyltransferase
36% identity, 91% coverage: 22:410/429 of query aligns to 18:399/402 of 2dkjA
- active site: Y46 (= Y50), E48 (= E52), D192 (= D196), T218 (≠ S223), K221 (= K226), R227 (≠ Q232)
- binding pyridoxal-5'-phosphate: S88 (= S92), G89 (= G93), S90 (≠ V94), H117 (= H121), S167 (= S171), D192 (= D196), A194 (= A198), H220 (= H225), K221 (= K226)
3pgyB Serine hydroxymethyltransferase from staphylococcus aureus, s95p mutant.
33% identity, 94% coverage: 8:410/429 of query aligns to 9:401/404 of 3pgyB
Sites not aligning to the query:
8dskA Structure of the n358y variant of serine hydroxymethyltransferase 8 in complex with plp, glycine, and formyl tetrahydrofolate (see paper)
34% identity, 88% coverage: 22:398/429 of query aligns to 30:425/472 of 8dskA
- 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: E62 (= E52), Y69 (≠ L59), Y70 (= Y60), L130 (≠ V116), G133 (= G119), G134 (= G120), H135 (= H121), L136 (≠ I122), Y140 (≠ K126), S191 (= S171), F282 (≠ D248), N375 (= N346), A383 (≠ S356)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S40 (= S30), Y60 (= Y50), Y70 (= Y60), S106 (= S92), G107 (= G93), S108 (≠ V94), H135 (= H121), G190 (= G170), S191 (= S171), D216 (= D196), A218 (= A198), H219 (= H199), K245 (= K226), G290 (≠ S256), R390 (= R363)
Q2F5L3 Serine hydroxymethyltransferase; SHMT; Glycine hydroxymethyltransferase; Serine methylase; bmSHMT; EC 2.1.2.1 from Bombyx mori (Silk moth) (see paper)
34% identity, 93% coverage: 15:412/429 of query aligns to 22:435/465 of Q2F5L3
- H119 (≠ G108) mutation to A: The kcat/Km for tetrahydrofolate is 1.1-fold lower than that of the wild-type. The kcat/Km for L-serine decreases to 30% compared to the wild-type.
- H132 (= H121) mutation to A: The kcat/Km for tetrahydrofolate is 7.4-fold lower than that of the wild-type.
- H135 (= H124) mutation to A: The kcat/Km for tetrahydrofolate is 1.7-fold lower than that of the wild-type. The kcat/Km for L-serine decreases to 32% compared to the wild-type.
Query Sequence
>WP_011973756.1 NCBI__GCF_000017185.1:WP_011973756.1
MNPSEVQQFVRETALKQHNWMRECIKLIASENITSIPVREACATDFMHRYAEGLPNNRLY
QGCEYIDDIENLCIELSEDIFKAEHANVQPTSGVVANLAVFFAEAKPGDKLMAMDVPNGG
HISHWKVSAAGIRGLRASAHPFDAEEMNIDVDKMVKQILEEKPRLVLFGGSLFPFPHPVK
DAVDAANEVGATIAYDGAHVLGLIAGGQFQDPLREGAEYMMGSTHKTLFGTQGGVVLTEK
KNAKKIDDKIFPGVVSNHHLHHKAGLAIALAETKEFGEAYAKQVVKNAKALGQALYERGC
NVLCEHKGFTESHQVILDIEKSECIEFSARELATMFEEANIILNKNLLPWDDVSNSDNPS
GIRLGSQECTRLGMKESEMDEIAEFMKRIAIDGEDIKKVKEDIVEFAKSYSEIHYAFEGG
DAFKYLKFY
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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