ID GLYA_YERPS Reviewed; 417 AA.
AC Q667X1;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 01-MAY-2013, entry version 66.
DE RecName: Full=Serine hydroxymethyltransferase;
DE Short=SHMT;
DE Short=Serine methylase;
DE EC=2.1.2.1;
GN Name=glyA; OrderedLocusNames=YPTB2869;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
CC -!- FUNCTION: Catalyzes the reversible interconversion of serine and
CC glycine with tetrahydrofolate (THF) serving as the one-carbon
CC carrier. This reaction serves as the major source of one-carbon
CC groups required for the biosynthesis of purines, thymidylate,
CC methionine, and other important biomolecules. Also exhibits THF-
CC independent aldolase activity toward beta-hydroxyamino acids,
CC producing glycine and aldehydes, via a retro-aldol mechanism (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + glycine +
CC H(2)O = tetrahydrofolate + L-serine.
CC -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine
CC from L-serine: step 1/1.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the SHMT family.
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DR EMBL; BX936398; CAH22107.1; -; Genomic_DNA.
DR RefSeq; YP_071376.1; NC_006155.1.
DR ProteinModelPortal; Q667X1; -.
DR SMR; Q667X1; 1-417.
DR STRING; 273123.YPTB2869; -.
DR EnsemblBacteria; CAH22107; CAH22107; YPTB2869.
DR GeneID; 2955727; -.
DR KEGG; yps:YPTB2869; -.
DR PATRIC; 18644873; VBIYerPse22266_3487.
DR eggNOG; COG0112; -.
DR HOGENOM; HOG000239404; -.
DR KO; K00600; -.
DR OMA; GKIDYED; -.
DR ProtClustDB; PRK00011; -.
DR UniPathway; UPA00193; -.
DR UniPathway; UPA00288; UER01023.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:HAMAP.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:HAMAP.
DR GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:HAMAP.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00051; SHMT; 1; -.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR InterPro; IPR001085; Ser_HO-MeTrfase.
DR InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS.
DR PANTHER; PTHR11680; PTHR11680; 1.
DR Pfam; PF00464; SHMT; 1.
DR PIRSF; PIRSF000412; SHMT; 1.
DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR PROSITE; PS00096; SHMT; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Complete proteome; Cytoplasm;
KW One-carbon metabolism; Pyridoxal phosphate; Transferase.
FT CHAIN 1 417 Serine hydroxymethyltransferase.
FT /FTId=PRO_0000113706.
FT REGION 125 127 Substrate binding (By similarity).
FT REGION 355 357 Substrate binding (By similarity).
FT BINDING 35 35 Pyridoxal phosphate (By similarity).
FT BINDING 55 55 Pyridoxal phosphate (By similarity).
FT BINDING 57 57 Substrate (By similarity).
FT BINDING 64 64 Substrate (By similarity).
FT BINDING 65 65 Pyridoxal phosphate (By similarity).
FT BINDING 99 99 Pyridoxal phosphate (By similarity).
FT BINDING 121 121 Substrate; via carbonyl oxygen (By
FT similarity).
FT BINDING 175 175 Pyridoxal phosphate (By similarity).
FT BINDING 203 203 Pyridoxal phosphate (By similarity).
FT BINDING 228 228 Pyridoxal phosphate (By similarity).
FT BINDING 235 235 Pyridoxal phosphate (By similarity).
FT BINDING 263 263 Pyridoxal phosphate; via amide nitrogen
FT and carbonyl oxygen (By similarity).
FT BINDING 363 363 Pyridoxal phosphate (By similarity).
FT MOD_RES 229 229 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 417 AA; 45422 MW; 6B5DE183D921C704 CRC64;
MLKREMNIAD YDADLWRAME QEVVRQEEHI ELIASENYTS PRVMQAQGSQ LTNKYAEGYP
GKRYYGGCEY VDVVEQLAID RAKALFGADY ANVQPHSGSQ ANVAVYSALL KPGDTVLGMN
LAHGGHLTHG SPVNFSGKLY NIVPYGIDES GQIDYEDLAR QAEIHKPKMI IGGFSAYSGI
VDWAKMREIA DSIDAWFFVD MAHVAGLVAA GVYPNPVPHA HIVTTTTHKT LAGPRGGLIL
AKGGDEDLYK KLNSSVFPGN QGGPLMHVIA GKAVALKEAM EPEFKIYQQQ VAKNAKAMVA
VFLERGYKVV SGGTDNHLFL LDLVDKDITG KDADAALGRA NITVNKNSVP NDPKSPFVTS
GVRIGSPAIT RRGFKEAESR ELAGWMCDVL DNINDEATIE RVKQKVLAIC ARLPVYA
//
