SitesBLAST
Comparing WP_011781806.1 NCBI__GCF_000015305.1:WP_011781806.1 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)
A0R2V7 Serine hydroxymethyltransferase; SHMT; Serine methylase; EC 2.1.2.1 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
88% identity, 100% coverage: 2:487/487 of query aligns to 9:490/490 of A0R2V7
- K362 (= K355) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
1kl2A Crystal structure of serine hydroxymethyltransferase complexed with glycine and 5-formyl tetrahydrofolate (see paper)
47% identity, 86% coverage: 25:444/487 of query aligns to 1:387/405 of 1kl2A
- active site: Y51 (= Y75), E53 (= E77), D197 (= D252), T223 (= T281), K226 (= K284), R232 (= R290)
- 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 (= E77), Y60 (≠ F84), G121 (= G176), H122 (= H177), S172 (= S227), F251 (vs. gap), N341 (= N398)
- binding glycine: S31 (= S55), Y51 (= Y75), Y61 (= Y85), H200 (= H255), R357 (= R414)
- binding pyridoxal-5'-phosphate: S93 (= S117), G94 (= G118), A95 (≠ I119), H122 (= H177), S172 (= S227), D197 (= D252), A199 (= A254), H200 (= H255), T223 (= T281), H225 (= H283), K226 (= K284)
1kl1A Crystal structure of serine hydroxymethyltransferase complexed with glycine (see paper)
47% identity, 86% coverage: 25:444/487 of query aligns to 1:387/405 of 1kl1A
- active site: Y51 (= Y75), E53 (= E77), D197 (= D252), T223 (= T281), K226 (= K284), R232 (= R290)
- binding glycine: S31 (= S55), H122 (= H177), R357 (= R414)
- binding pyridoxal-5'-phosphate: S93 (= S117), G94 (= G118), A95 (≠ I119), H122 (= H177), A171 (≠ Y226), S172 (= S227), D197 (= D252), A199 (= A254), H200 (= H255), T223 (= T281), H225 (= H283), K226 (= K284)
1kkpA Crystal structure of serine hydroxymethyltransferase complexed with serine (see paper)
47% identity, 86% coverage: 25:444/487 of query aligns to 1:387/405 of 1kkpA
- active site: Y51 (= Y75), E53 (= E77), D197 (= D252), T223 (= T281), K226 (= K284), R232 (= R290)
- binding pyridoxal-5'-phosphate: S93 (= S117), G94 (= G118), A95 (≠ I119), H122 (= H177), S172 (= S227), D197 (= D252), A199 (= A254), H200 (= H255), K226 (= K284)
- binding serine: S31 (= S55), H122 (= H177), R357 (= R414)
1kkjA Crystal structure of serine hydroxymethyltransferase from b.Stearothermophilus (see paper)
47% identity, 86% coverage: 25:444/487 of query aligns to 1:387/405 of 1kkjA
- active site: Y51 (= Y75), E53 (= E77), D197 (= D252), T223 (= T281), K226 (= K284), R232 (= R290)
- binding pyridoxal-5'-phosphate: S93 (= S117), G94 (= G118), A95 (≠ I119), H122 (= H177), S172 (= S227), D197 (= D252), A199 (= A254), H200 (= H255), T223 (= T281), H225 (= H283), K226 (= K284)
2vmyA Crystal structure of f351gbsshmt in complex with gly and fthf (see paper)
47% identity, 86% coverage: 25:444/487 of query aligns to 1:387/405 of 2vmyA
- active site: Y51 (= Y75), E53 (= E77), D197 (= D252), T223 (= T281), K226 (= K284), R232 (= R290)
- 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 (= E77), Y60 (≠ F84), Y61 (= Y85), L117 (= L172), G121 (= G176), H122 (= H177), L123 (= L178), S172 (= S227), K248 (= K306), F251 (vs. gap), N341 (= N398), S349 (≠ G406), P350 (≠ A407), G351 (≠ W408), R357 (= R414)
- binding glycine: S31 (= S55), Y51 (= Y75), Y61 (= Y85), H200 (= H255), K226 (= K284), R357 (= R414)
- binding pyridoxal-5'-phosphate: Y51 (= Y75), S93 (= S117), G94 (= G118), A95 (≠ I119), H122 (= H177), S172 (= S227), D197 (= D252), A199 (= A254), H200 (= H255), T223 (= T281), K226 (= K284), G257 (= G314)
2vmxA Crystal structure of f351gbsshmt in complex with l-allo-thr (see paper)
47% identity, 86% coverage: 25:444/487 of query aligns to 1:387/405 of 2vmxA
- active site: Y51 (= Y75), E53 (= E77), D197 (= D252), T223 (= T281), K226 (= K284), R232 (= R290)
- binding allo-threonine: S31 (= S55), H122 (= H177), H200 (= H255), R357 (= R414)
- binding pyridoxal-5'-phosphate: S93 (= S117), G94 (= G118), A95 (≠ I119), H122 (= H177), S172 (= S227), D197 (= D252), A199 (= A254), H200 (= H255), T223 (= T281), K226 (= K284)
6ymfA Crystal structure of serine hydroxymethyltransferase from aphanothece halophytica in the plp-serine external aldimine state (see paper)
43% identity, 95% coverage: 25:486/487 of query aligns to 4:418/418 of 6ymfA
- active site: Y54 (= Y75), E56 (= E77), D200 (= D252), T226 (= T281), K229 (= K284), R235 (= R290)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: S34 (= S55), S96 (= S117), G97 (= G118), A98 (≠ I119), H125 (= H177), S175 (= S227), D200 (= D252), A202 (= A254), H203 (= H255), T226 (= T281), K229 (= K284), R361 (= R414)
6ymdA Crystal structure of serine hydroxymethyltransferase from aphanothece halophytica in the covalent complex with malonate (see paper)
42% identity, 95% coverage: 25:486/487 of query aligns to 4:418/420 of 6ymdA
- active site: Y54 (= Y75), E56 (= E77), D200 (= D252), T226 (= T281), K229 (= K284), R235 (= R290)
- binding malonate ion: S34 (= S55), Y54 (= Y75), E56 (= E77), Y64 (= Y85), H125 (= H177), H203 (= H255), K229 (= K284), R361 (= R414)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: Y54 (= Y75), S96 (= S117), G97 (= G118), A98 (≠ I119), H125 (= H177), Y174 (= Y226), S175 (= S227), D200 (= D252), A202 (= A254), T226 (= T281), K229 (= K284), G261 (= G314)
4n0wA X-ray crystal structure of a serine hydroxymethyltransferase from burkholderia cenocepacia with covalently attached pyridoxal phosphate
43% identity, 94% coverage: 24:482/487 of query aligns to 6:415/416 of 4n0wA
- active site: Y57 (= Y75), E59 (= E77), D202 (= D252), T228 (= T281), K231 (= K284), R237 (= R290)
- binding pyridoxal-5'-phosphate: S99 (= S117), G100 (= G118), S101 (≠ I119), H128 (= H177), D202 (= D252), A204 (= A254), H205 (= H255), K231 (= K284)
4ot8A X-ray crystal structure of serine hydroxymethyl transferase from burkholderia cenocepacia bound to plp and serine
43% identity, 94% coverage: 24:482/487 of query aligns to 4:413/414 of 4ot8A
- active site: Y55 (= Y75), E57 (= E77), D200 (= D252), T226 (= T281), K229 (= K284), R235 (= R290)
- binding pyridoxal-5'-phosphate: S97 (= S117), G98 (= G118), S99 (≠ I119), H126 (= H177), D200 (= D252), A202 (= A254), H203 (= H255), K229 (= K284)
- binding serine: S35 (= S55), E57 (= E77), Y65 (= Y85), H126 (= H177), H203 (= H255), R360 (= R414)
4otlA X-ray crystal structure of serine hydroxymethyl transferase from burkholderia cenocepacia bound to plp and glycine
44% identity, 93% coverage: 28:482/487 of query aligns to 3:408/409 of 4otlA
- active site: Y50 (= Y75), E52 (= E77), D195 (= D252), T221 (= T281), K224 (= K284), R230 (= R290)
- binding glycine: S30 (= S55), Y50 (= Y75), Y60 (= Y85), H121 (= H177), K224 (= K284), R355 (= R414)
- binding pyridoxal-5'-phosphate: S92 (= S117), G93 (= G118), S94 (≠ I119), H121 (= H177), S170 (= S227), D195 (= D252), A197 (= A254), H198 (= H255), K224 (= K284)
7x5oB Crystal structure of e. Faecium shmt in complex with me-thf and plp- gly (see paper)
47% identity, 85% coverage: 29:442/487 of query aligns to 4:386/412 of 7x5oB
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S30 (= S55), Y50 (= Y75), Y60 (= Y85), S92 (= S117), G93 (= G118), S94 (≠ I119), H121 (= H177), S171 (= S227), D196 (= D252), A198 (= A254), H199 (= H255), K225 (= K284), R358 (= R414)
- binding n-[4-({[(6s)-2-amino-4-hydroxy-5-methyl-5,6,7,8-tetrahydropteridin-6-yl]methyl}amino)benzoyl]-l-glutamic acid: E52 (= E77), Y59 (≠ F84), L116 (= L172), G119 (= G175), G120 (= G176), H121 (= H177), S171 (= S227), P252 (= P309), N342 (= N398), P351 (≠ A407)
7x5nA Crystal structure of e. Faecium shmt in complex with (+)-shin-1 and plp-ser (see paper)
47% identity, 85% coverage: 29:442/487 of query aligns to 3:385/409 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 (= E77), Y58 (≠ F84), Y59 (= Y85), L115 (= L172), G119 (= G176), H120 (= H177), L121 (= L178), K340 (≠ R397), N341 (= N398), S342 (≠ A399), P350 (≠ A407), F351 (≠ W408), R357 (= R414)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: S29 (= S55), Y49 (= Y75), E51 (= E77), Y59 (= Y85), S91 (= S117), G92 (= G118), S93 (≠ I119), H120 (= H177), S170 (= S227), D195 (= D252), A197 (= A254), H198 (= H255), K224 (= K284), R357 (= R414)
7v3dA Complex structure of serine hydroxymethyltransferase from enterococcus faecium and its inhibitor (see paper)
47% identity, 85% coverage: 29:442/487 of query aligns to 3:385/409 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 (= E77), Y58 (≠ F84), L115 (= L172), G119 (= G176), H120 (= H177), L121 (= L178), K340 (≠ R397), S342 (≠ A399), P350 (≠ A407), F351 (≠ W408), R357 (= R414)
- binding pyridoxal-5'-phosphate: Y49 (= Y75), S91 (= S117), G92 (= G118), S93 (≠ I119), H120 (= H177), S170 (= S227), D195 (= D252), A197 (= A254), K224 (= K284), G255 (= G313)
6uldA Crystal structure of serine hydroxymethyltransferase from mycobacterium tuberculosis with bound plp forming a schiff base with substrate serine in one monomer and plp forming a schiff base with product glycine in the other monomer
44% identity, 94% coverage: 28:485/487 of query aligns to 7:420/428 of 6uldA
- binding glycine: S34 (= S55), H125 (= H177), H203 (= H255), R365 (= R414)
- binding pyridoxal-5'-phosphate: Y54 (= Y75), S96 (= S117), G97 (= G118), A98 (≠ I119), H125 (= H177), W174 (≠ Y226), S175 (= S227), D200 (= D252), A202 (= A254), H203 (= H255), T226 (= T281), H228 (= H283), K229 (= K284), G259 (= G313)
- binding serine: Y54 (= Y75), E56 (= E77), Y64 (= Y85)
Q5SI56 Serine hydroxymethyltransferase; SHMT; Serine methylase; EC 2.1.2.1 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
48% identity, 80% coverage: 46:437/487 of query aligns to 22:381/407 of Q5SI56
- Y51 (= Y75) binding pyridoxal 5'-phosphate
- GS 94:95 (≠ GI 118:119) binding pyridoxal 5'-phosphate
- S172 (= S227) binding pyridoxal 5'-phosphate
- H200 (= H255) binding pyridoxal 5'-phosphate
- H225 (= H283) binding pyridoxal 5'-phosphate
- K226 (= K284) modified: N6-(pyridoxal phosphate)lysine
- G258 (= G314) 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)
48% identity, 80% coverage: 46:437/487 of query aligns to 17:376/402 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)
48% identity, 80% coverage: 46:437/487 of query aligns to 17:376/402 of 8ssyA
2dkjA Crystal structure of t.Th.Hb8 serine hydroxymethyltransferase
48% identity, 80% coverage: 46:437/487 of query aligns to 17:376/402 of 2dkjA
- active site: Y46 (= Y75), E48 (= E77), D192 (= D252), T218 (= T281), K221 (= K284), R227 (= R290)
- binding pyridoxal-5'-phosphate: S88 (= S117), G89 (= G118), S90 (≠ I119), H117 (= H177), S167 (= S227), D192 (= D252), A194 (= A254), H220 (= H283), K221 (= K284)
Query Sequence
>WP_011781806.1 NCBI__GCF_000015305.1:WP_011781806.1
MTSSSPSGQGADYAATASEAYRAALRVIESVEPRVAEATRKELADQRGSLKLIASENYAS
PAVLLTMGTWFSDKYAEGTVGHRFYAACQNVDTVEALAAEHARELFGAPYAYAQPHSGID
ANLVAYWAILATRVEAPGLAELGAKHVNDLSEGDWEKLRAKLGNQRLLGMSLDTGGHLTH
GFRPNISGKMFHQRQYGTDPATGFIDYDAVAAAAREFKPLVLVAGYSAYPRRVNFAKMRE
IADEVGATLMVDMAHFAGLVAGKVFTGDEDPVPHAHITTTTTHKSLRGPRGGLVLATEEY
APAVDKGCPMVLGGPLSHVMAAKAVALAEARRPEFRAYAQAVADNAQALADGFIKRDGSL
VTGGTDNHLVLLDVTSFGLTGRQAESALLDSGIVTNRNAVPADPNGAWYTSGIRFGSPAL
TTRGFGADDFDRVAELVVEVLSNTQPAAGPNGPSKAKYTLADGTAERVRAAAAELLDANP
LYPGLTL
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