ID   GLYM_CANAX              Reviewed;         493 AA.
AC   O13425;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Serine hydroxymethyltransferase, mitochondrial;
DE            Short=SHMT;
DE            EC=2.1.2.1;
DE   AltName: Full=Glycine hydroxymethyltransferase;
DE   AltName: Full=Serine methylase;
DE   Flags: Precursor;
GN   Name=SHM1;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10641038;
RX   DOI=10.1002/(sici)1097-0061(20000130)16:2<167::aid-yea519>3.0.co;2-1;
RA   McNeil J.B., Flynn J., Tsao N., Monschau N., Stahmann K., Haynes R.H.,
RA   McIntosh E.M., Pearlman R.E.;
RT   "Glycine metabolism in Candida albicans: characterization of the serine
RT   hydroxymethyltransferase (SHM1, SHM2) and threonine aldolase (GLY1)
RT   genes.";
RL   Yeast 16:167-175(2000).
CC   -!- FUNCTION: Interconversion of serine and glycine.
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: Mitochondrion.
CC   -!- MISCELLANEOUS: In eukaryotes there are two forms of the enzymes: a
CC       cytosolic one and a mitochondrial one.
CC   -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000305}.
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DR   EMBL; AF009965; AAB64196.1; -; Genomic_DNA.
DR   AlphaFoldDB; O13425; -.
DR   SMR; O13425; -.
DR   PRIDE; O13425; -.
DR   VEuPathDB; FungiDB:C7_03330C_A; -.
DR   VEuPathDB; FungiDB:CAWG_05666; -.
DR   UniPathway; UPA00193; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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   Mitochondrion; One-carbon metabolism; Pyridoxal phosphate; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..493
FT                   /note="Serine hydroxymethyltransferase, mitochondrial"
FT                   /id="PRO_0000032565"
FT   MOD_RES         270
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   493 AA;  54508 MW;  4EBBEA854DF90FDA CRC64;
     MLSSTLRRSV RAQSKNLPAF ARRTYAVSPS AQALISKSVQ DVDPEMADIL NQERTRQKNS
     ITLIPSENFT SKAVMDLLGS EMQNKYSEGY PGERYYGGNE IIDKAEALCQ KRALEAFGLD
     PSQWGVNVQP LSGAPANLYA YSAILEVGDR IMGLDLPHGG HLSHGYQTKT TKISYISKYF
     QTMPYRLNEE TGIIDYDTLE KNAQLFRPKV IVAGASAYSR VIDYKRMRQL SIRLGAYLLS
     DMAHISGLVS AVVTDSPFPY SDIVTTTTHK SLRGPRGAMI FFRKGIRKVT TKGKEIPYEL
     ERKINFLVFP GHQGGPHNHT ISALAVALKQ CTEPEYVKYQ QEVVSNAKHF ADALVSKGFK
     LVSDGTDTHL ILVDLRSRNI DGARVEAVLE RANIAANKNT VPGDVSALFP SGLRVGTPAM
     TTRGFGPEEF DKVAEFIDQA VNIAIELKAQ EQGKVPKELL ASFKKLADES DKVKQLDKEV
     VSWVSKYPVP GEL