ID   GLYA_THEON              Reviewed;         427 AA.
AC   B6YVY6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   03-AUG-2022, entry version 88.
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.- {ECO:0000255|HAMAP-Rule:MF_00051};
GN   Name=glyA {ECO:0000255|HAMAP-Rule:MF_00051}; OrderedLocusNames=TON_0821;
OS   Thermococcus onnurineus (strain NA1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=523850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1;
RX   PubMed=18790866; DOI=10.1128/jb.00746-08;
RA   Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA   Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA   Colwell R.R., Kim S.-J., Lee J.-H.;
RT   "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT   mixed heterotrophic and carboxydotrophic metabolism.";
RL   J. Bacteriol. 190:7491-7499(2008).
CC   -!- FUNCTION: Catalyzes the reversible interconversion of serine and
CC       glycine with a modified folate serving as the one-carbon carrier. Also
CC       exhibits a pteridine-independent aldolase activity toward beta-
CC       hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol
CC       mechanism. {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: 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}.
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DR   EMBL; CP000855; ACJ16309.1; -; Genomic_DNA.
DR   RefSeq; WP_012571781.1; NC_011529.1.
DR   AlphaFoldDB; B6YVY6; -.
DR   SMR; B6YVY6; -.
DR   STRING; 523850.TON_0821; -.
DR   EnsemblBacteria; ACJ16309; ACJ16309; TON_0821.
DR   GeneID; 7017124; -.
DR   KEGG; ton:TON_0821; -.
DR   PATRIC; fig|523850.10.peg.828; -.
DR   eggNOG; arCOG00070; Archaea.
DR   HOGENOM; CLU_022477_2_1_2; -.
DR   OMA; SHPAGLI; -.
DR   OrthoDB; 22518at2157; -.
DR   UniPathway; UPA00288; UER01023.
DR   Proteomes; UP000002727; Chromosome.
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:InterPro.
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; Transferase.
FT   CHAIN           1..427
FT                   /note="Serine hydroxymethyltransferase"
FT                   /id="PRO_0000369977"
FT   BINDING         122..124
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   SITE            227
FT                   /note="Plays an important role in substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
FT   MOD_RES         228
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00051"
SQ   SEQUENCE   427 AA;  47746 MW;  F0D767E320D5D514 CRC64;
     MENGYKTYRD KVIEYLEAHE KWRSSTINLI ASENVTSPSV NRAVSSGFMH KYAEGWPRQR
     YYQGCKYVDE VELIGVDLFC KLFGSDFADL RPISGTNANQ AVFFGLTQPG DKAIVLHTSH
     GGHISHMPFG AAGMRGLEVH TWPFDNEEFN IDVDKAAQLI RELEPRIVVF GGSLFPFPHP
     VKELAPVAKE VGAYVMYDAA HVLGLIAGKQ FQNPLREGVD IMTASTHKTF PGPQGGIILY
     KNFGDDVAKL QWAIFPGVLS NHHLHHMAGK VITAAEMLEF GERYAAQIVK NAKALAEALA
     EEGFKVIGED KDYTESHQVI VDVSDLHEAA GGWAAPLLEE AGIILNKNLL PWDPLEKVNT
     PSGLRIGVQE MTRVGMLEDN MKDIAVFMRR VLIDKEDPKK VEKEVAEYRK EYQKVYYSFD
     HGLPMKE