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Database: UniProt
Entry: A0A1B8CXY6_9PEZI
LinkDB: A0A1B8CXY6_9PEZI
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ID   A0A1B8CXY6_9PEZI        Unreviewed;       473 AA.
AC   A0A1B8CXY6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|RuleBase:RU000585};
DE            EC=2.1.2.1 {ECO:0000256|RuleBase:RU000585};
GN   ORFNames=VE04_05880 {ECO:0000313|EMBL:OBT51703.1};
OS   Pseudogymnoascus sp. 24MN13.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1622150 {ECO:0000313|EMBL:OBT51703.1, ECO:0000313|Proteomes:UP000092157};
RN   [1] {ECO:0000313|EMBL:OBT51703.1, ECO:0000313|Proteomes:UP000092157}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=24MN13 {ECO:0000313|EMBL:OBT51703.1,
RC   ECO:0000313|Proteomes:UP000092157};
RA   Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT   "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT   white-nose syndrome of bats.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000092157}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=24MN13 {ECO:0000313|Proteomes:UP000092157};
RX   PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA   Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT   "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT   white-nose syndrome of bats.";
RL   Nat. Commun. 9:35-35(2018).
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; KV456757; OBT51703.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B8CXY6; -.
DR   STRING; 1622150.A0A1B8CXY6; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000092157; Unassembled WGS sequence.
DR   GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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:0032259; P:methylation; IEA:UniProtKB-KW.
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   Methyltransferase {ECO:0000313|EMBL:OBT51703.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000092157};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000585}.
FT   DOMAIN          25..411
FT                   /note="Serine hydroxymethyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00464"
FT   MOD_RES         243
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000412-50"
SQ   SEQUENCE   473 AA;  51965 MW;  48566BFFCD6B10ED CRC64;
     MASTTQPTYA LSQAHKDSLE KSLLETDPEI AAIMEKEIQR QRESIILIAS ENVTSRAVFD
     ALGSPMSNKY SEGYPGARYY GGNEHIDAIE LTCQARALTA FNLDKAKWGV NVQCLSGSPA
     NLQVYQAIMR PHERLMGLDL PHGGHLSHGY QTAQRKISAV STYFETFPYR VNIETGIIDY
     EQLEQNALMY RPKVLVAAHA PMIADKVGAD RVVDMAHISG LIAAGVIPSP FEYADIVTTT
     THKSLRGPRG AMIFFRRGVR STDAKTGKDI LYDLENPINF SVFPGHQGGP HNHTITALAV
     ALKQANTPEF KQYQEQVVKN AKAIEVELKR LGYKLVADGT DSHMVLMDLR AQSLDGARVE
     AVLEQINIAC NKNAIPGDKS ALSPCGIRIG TPAMTSRGFG EEDFKRVASY IDQTIQICKE
     VQAALPKPDN KLKDFRAKVA GGEIEKINAL RKEIASWASS FPLPVEGWRA EKA
//
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