ID   GLYC_CANGA              Reviewed;         469 AA.
AC   Q6FUP6;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Serine hydroxymethyltransferase, cytosolic;
DE            Short=SHMT;
DE            EC=2.1.2.1;
DE   AltName: Full=Glycine hydroxymethyltransferase;
DE   AltName: Full=Serine methylase;
GN   Name=SHM2; OrderedLocusNames=CAGL0F01749g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Interconversion of serine and glycine. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR380952; CAG58972.1; -; Genomic_DNA.
DR   RefSeq; XP_446048.1; XM_446048.1.
DR   AlphaFoldDB; Q6FUP6; -.
DR   SMR; Q6FUP6; -.
DR   STRING; 5478.XP_446048.1; -.
DR   PRIDE; Q6FUP6; -.
DR   EnsemblFungi; CAG58972; CAG58972; CAGL0F01749g.
DR   GeneID; 2887952; -.
DR   KEGG; cgr:CAGL0F01749g; -.
DR   CGD; CAL0131260; SHM2.
DR   VEuPathDB; FungiDB:CAGL0F01749g; -.
DR   eggNOG; KOG2467; Eukaryota.
DR   HOGENOM; CLU_022477_0_0_1; -.
DR   InParanoid; Q6FUP6; -.
DR   OMA; SHPAGLI; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000002428; Chromosome F.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR   GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:InterPro.
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   Cytoplasm; One-carbon metabolism; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..469
FT                   /note="Serine hydroxymethyltransferase, cytosolic"
FT                   /id="PRO_0000113512"
FT   MOD_RES         248
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   469 AA;  52304 MW;  D07B42FC13D30951 CRC64;
     MPYALSDKHL KMVSGHLSET DPEVEQIIKD EVDRQKHSID LIASENFTTT SVFDALGTPL
     CNKYSEGYPG ARYYGGNEHI DRIERLCQQR ALEAFHVTPD RWGVNVQTLS GSPANLQVYQ
     ALMKPHERLM GLYLPDGGHL SHGYATENRK ISAVSTYFES FPYRVNPETG IIDYDTLEKN
     AILYRPKILV AGTSAYCRLI DYKRMREIAD KCGAYLMVDM AHISGLVAAG VIPSPFEYAD
     IVTTTTHKSL RGPRGAMIFF RRGIRSVNQK TGKEIPYDLE NPINFSVFPG HQGGPHNHTI
     AALATALKQA ATPEFKEYQT QVLKNAKALE NEFQTLGYRL VSNGTDSHMV LVSLREKGVD
     GARVEYVCEK INIALNKNSI PGDKSALVPG GVRIGAPAMT TRGMGEEDFH RIVRYIDQAV
     KFAEQTQSSL PKEANKLKDF KAKVDEIADQ LAPLKKEIYD WTAEYPLAV