ID   A0A0X8HQP7_9SACH        Unreviewed;       469 AA.
AC   A0A0X8HQP7;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|RuleBase:RU000585};
DE            EC=2.1.2.1 {ECO:0000256|RuleBase:RU000585};
GN   ORFNames=AW171_hschr42100 {ECO:0000313|EMBL:AMD20216.1};
OS   Eremothecium sinecaudum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=45286 {ECO:0000313|EMBL:AMD20216.1, ECO:0000313|Proteomes:UP000243052};
RN   [1] {ECO:0000313|EMBL:AMD20216.1, ECO:0000313|Proteomes:UP000243052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58844 {ECO:0000313|EMBL:AMD20216.1,
RC   ECO:0000313|Proteomes:UP000243052};
RA   Dietrich F.S.;
RT   "Genome sequence of the yeast Holleya sinecauda.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Interconversion of serine and glycine.
CC       {ECO:0000256|ARBA:ARBA00002224, ECO:0000256|RuleBase:RU000585}.
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:0000256|ARBA:ARBA00001528,
CC         ECO:0000256|RuleBase:RU000585};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR000412-50, ECO:0000256|RuleBase:RU000585};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000256|ARBA:ARBA00004777, ECO:0000256|RuleBase:RU000585}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000256|ARBA:ARBA00006376,
CC       ECO:0000256|RuleBase:RU000585}.
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DR   EMBL; CP014244; AMD20216.1; -; Genomic_DNA.
DR   RefSeq; XP_017987212.1; XM_018132210.1.
DR   AlphaFoldDB; A0A0X8HQP7; -.
DR   STRING; 45286.A0A0X8HQP7; -.
DR   GeneID; 28723454; -.
DR   OrthoDB; 5358603at2759; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000243052; Chromosome iv.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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; SERINE HYDROXYMETHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11680:SF66; SERINE HYDROXYMETHYLTRANSFERASE, CYTOSOLIC; 1.
DR   Pfam; PF00464; SHMT; 1.
DR   PIRSF; PIRSF000412; SHMT; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00096; SHMT; 1.
PE   3: Inferred from homology;
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563,
KW   ECO:0000256|RuleBase:RU000585};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000412-50};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000585}.
FT   DOMAIN          17..416
FT                   /note="Serine hydroxymethyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00464"
FT   MOD_RES         248
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000412-50"
SQ   SEQUENCE   469 AA;  51890 MW;  78F5923F93D6F43D CRC64;
     MTYALSESHK KLISTSLQES DPEVADIIKD EIERQKHSLV LIASENFTSS AVFGALGSPM
     CNKYSEGYPG ARYYGGNEHI DRMELLCQKR ALEAFHLSSD KWGVNVQSLS GSPANLQVYQ
     ALMKPHERLM GLFLPDGGHL SHGYQTENRK ISAVSTYFES FPYRVDPKTG IIDYDTLEQN
     AILYRPKILV AGTSAYCRLI DYKRMREIAD KVGAYLMVDM AHISGLIAAG VIPSPFEYAD
     IVTTTTHKSL RGPRGAMIFF RRGVRSVNQK TGKEVMYDLE APINFSVFPG HQGGPHNHTI
     SALAAALKQA ATPEFKEYQE QVLKNAKALE VGFKKLDYRL VSDGTDSHMV LVSLREKGVD
     GARVEYVCDK INIALNKNSI PGDKSALVPG GIRIGAPAMT TRGMGEEDFA RIVTYIDNAV
     QVAHKVQHSL PKEANRLKDF KAVIDAGVPE IDQLSKEIYE WTGSFPLPV
//