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Database: UniProt
Entry: Q667X1
LinkDB: Q667X1
Original site: Q667X1 
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   26-NOV-2014, entry version 74.
DE   RecName: Full=Serine hydroxymethyltransferase {ECO:0000255|HAMAP-Rule:MF_00051};
DE            Short=SHMT {ECO:0000255|HAMAP-Rule:MF_00051};
DE            Short=Serine methylase {ECO:0000255|HAMAP-Rule:MF_00051};
DE            EC=2.1.2.1 {ECO:0000255|HAMAP-Rule:MF_00051};
GN   Name=glyA {ECO:0000255|HAMAP-Rule:MF_00051};
GN   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.
CC       {ECO:0000255|HAMAP-Rule:MF_00051}.
CC   -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + glycine +
CC       H(2)O = tetrahydrofolate + L-serine. {ECO:0000255|HAMAP-
CC       Rule:MF_00051}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00051};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000255|HAMAP-Rule:MF_00051}.
CC   -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine
CC       from L-serine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00051}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00051}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00051}.
CC   -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000255|HAMAP-
CC       Rule:MF_00051}.
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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; RQNHFIN; -.
DR   OrthoDB; EOG6Z0QB2; -.
DR   BioCyc; YPSE273123:GI1M-2963-MONOMER; -.
DR   UniPathway; UPA00193; -.
DR   UniPathway; UPA00288; UER01023.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:UniProtKB-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; SSF53383; 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. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   REGION      355    357       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      35     35       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      55     55       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      57     57       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      64     64       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      65     65       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING      99     99       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     121    121       Substrate; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00051}.
FT   BINDING     175    175       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     203    203       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     228    228       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     235    235       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     263    263       Pyridoxal phosphate; via amide nitrogen
FT                                and carbonyl oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   BINDING     363    363       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00051}.
FT   MOD_RES     229    229       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00051}.
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
//
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