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GLYA2_BURPS
ID   GLYA2_BURPS             Reviewed;         424 AA.
AC   Q63MV1;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Serine hydroxymethyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00051};
DE            Short=SHMT 2 {ECO:0000255|HAMAP-Rule:MF_00051};
DE            Short=Serine methylase 2 {ECO:0000255|HAMAP-Rule:MF_00051};
DE            EC=2.1.2.1 {ECO:0000255|HAMAP-Rule:MF_00051};
GN   Name=glyA2 {ECO:0000255|HAMAP-Rule:MF_00051}; OrderedLocusNames=BPSS0547;
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243;
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA   Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA   Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA   Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA   Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA   Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA   Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA   Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA   Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT   pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC   -!- FUNCTION: Catalyzes the reversible interconversion of serine and
CC       glycine with tetrahydrofolate (THF) serving as the one-carbon carrier.
CC       This reaction serves as the major source of one-carbon groups required
CC       for the biosynthesis of purines, thymidylate, methionine, and other
CC       important biomolecules. Also exhibits THF-independent aldolase activity
CC       toward beta-hydroxyamino acids, producing glycine and aldehydes, via a
CC       retro-aldol mechanism. {ECO:0000255|HAMAP-Rule:MF_00051}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O =
CC         (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1;
CC         Evidence={ECO:0000255|HAMAP-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 from L-
CC       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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAH38004.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX571966; CAH38004.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_004523136.1; NZ_CP009537.1.
DR   RefSeq; YP_110568.1; NC_006351.1.
DR   AlphaFoldDB; Q63MV1; -.
DR   SMR; Q63MV1; -.
DR   STRING; 272560.BPSS0547; -.
DR   EnsemblBacteria; CAH38004; CAH38004; BPSS0547.
DR   GeneID; 56531003; -.
DR   KEGG; bps:BPSS0547; -.
DR   PATRIC; fig|272560.51.peg.6715; -.
DR   eggNOG; COG0112; Bacteria.
DR   OMA; RCQHSEV; -.
DR   UniPathway; UPA00193; -.
DR   UniPathway; UPA00288; UER01023.
DR   Proteomes; UP000000605; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:UniProtKB-UniRule.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR   CDD; cd00378; SHMT; 1.
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.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR001085; Ser_HO-MeTrfase.
DR   InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS.
DR   InterPro; IPR039429; SHMT-like_dom.
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; Cytoplasm; One-carbon metabolism;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..424
FT                   /note="Serine hydroxymethyltransferase 2"
FT                   /id="PRO_0000113553"
FT   BINDING         125
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   BINDING         129..131
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   BINDING         250
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   SITE            233
FT                   /note="Plays an important role in substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   MOD_RES         234
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
SQ   SEQUENCE   424 AA;  45441 MW;  56789A4FFDDFC41F CRC64;
     MSNANPFFSQ SLAERDASVR GAILKELERQ QSQVELIASE NIVSRAVLDA QGSVLTNKYA
     EGYPGKRYYG GCEFADEVEA LAIERVKRLF NAGHANVQPH SGAQANGAVM LALAKPGDTV
     LGMSLDAGGH LTHGAKPALS GKWFNALQYG VSRDTMLIDY DQVEALAQQH KPSLIIAGFS
     AYPRKLDFAR FRAIADSVGA KLMVDMAHIA GVIAAGRHAN PVEHAHVVTS TTHKTLRGPR
     GGFVLTNDEE IAKKINSAVF PGLQGGPLMH VIAGKAVAFG EALTDDFKTY IDRVLANAQA
     LGDVLKAGGV DLVTGGTDNH LLLVDLRPKG LKGAQVEQAL ERAGITCNKN GIPFDPEKPT
     ITSGIRLGTP AGTTRGFGAA EFREVGRLIL EVFEALRTNP EGDHATEQRV RREIFALCER
     FPIY
 
 
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