ID A0A2W1G404_9PLEO Unreviewed; 524 AA.
AC A0A2W1G404;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|RuleBase:RU000585};
DE EC=2.1.2.1 {ECO:0000256|RuleBase:RU000585};
GN ORFNames=Ptr86124_003130 {ECO:0000313|EMBL:KAI1517829.1}, PtrM4_027250
GN {ECO:0000313|EMBL:KAF7578485.1}, PtrM4_08305
GN {ECO:0000313|EMBL:PWO11015.1};
OS Pyrenophora tritici-repentis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=45151 {ECO:0000313|EMBL:PWO11015.1};
RN [1] {ECO:0000313|EMBL:PWO11015.1, ECO:0000313|Proteomes:UP000245464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M4 {ECO:0000313|EMBL:PWO11015.1,
RC ECO:0000313|Proteomes:UP000245464};
RX PubMed=29685100; DOI=10.1186/s12864-018-4680-3;
RA Moolhuijzen P., See P.T., Hane J.K., Shi G., Liu Z., Oliver R.P.,
RA Moffat C.S.;
RT "Comparative genomics of the wheat fungal pathogen Pyrenophora tritici-
RT repentis reveals chromosomal variations and genome plasticity.";
RL BMC Genomics 19:279-279(2018).
RN [2] {ECO:0000313|EMBL:KAI1517829.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=86-124 {ECO:0000313|EMBL:KAI1517829.1};
RA Moolhuijzen P.M., Moffat C.S.;
RL Submitted (MAY-2021) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAI1517829.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=86-124 {ECO:0000313|EMBL:KAI1517829.1};
RA Moolhuijzen P., See P.T., Shi G., Powell H.R., Cockram J., Jorgensen L.N.,
RA Benslimane H., Strelkov S.E., Turner J., Liu Z., Moffat C.S.;
RT "A global pangenome for the wheat fungal pathogen Pyrenophora tritici-
RT repentis and prediction of effector protein structural homology.";
RL bioRxiv 0:0-0(2022).
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 -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000256|ARBA:ARBA00006376,
CC ECO:0000256|RuleBase:RU000585}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWO11015.1}.
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DR EMBL; NQIK02000001; KAF7578485.1; -; Genomic_DNA.
DR EMBL; NRDI02000003; KAI1517829.1; -; Genomic_DNA.
DR EMBL; NQIK01000006; PWO11015.1; -; Genomic_DNA.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000245464; Unassembled WGS sequence.
DR Proteomes; UP000249757; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
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:SF64; SERINE HYDROXYMETHYLTRANSFERASE, MITOCHONDRIAL; 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:PWO11015.1};
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000585}.
FT DOMAIN 53..456
FT /note="Serine hydroxymethyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF00464"
FT MOD_RES 284
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000412-50"
SQ SEQUENCE 524 AA; 57739 MW; 4C2DE686E37F9585 CRC64;
MANLRAACRT PLRQLTSRPT AAIPTNHSRL LQRQWRGYAT SLDAQQKILS QDLEHADPTV
YEIINREKNR QKHFINLIPS ENFTSQAVLD ALGSVMQNKY SEGYPGARYY GGNEHIDEAE
RLCQQRALKA FGLSPDEWGV NVQALSGSPA NLYAYSAILN THDRILSLDL PHGGHLSHGY
QTPTKKISAV SKYFETLPYR LNEKTGIIDY EKMAELAHLY RPKVIVAGTS AYSRLIEYER
MRKLADEVGA YLLSDMAHIS GLVAAGVIPS PFPHSDIVTT TTHKSLRGPR GAMIFYRKGV
RKVDKKGKQE MYDLEGPINA SVFPGHQGGP HNHTITALAV ALQQASSKEF KDYQQQVLEN
AKALAHRLGA SKDSGGLGYN IVSGGTDNHL VLVDLKDRGV DGARVERILE LVGVASNKNT
VPGDKSAMKP GGLRLGTPAM TTRGFQADDF KRVADVVHRA VGITQKLDTD ARKKAEDMGR
KNPGSVAAFK EYVGEGEDIT EIIELKKEVA DWVSTFALPW DKAQ
//
