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Database: UniProt
Entry: A0A0W8C5L8_PHYNI
LinkDB: A0A0W8C5L8_PHYNI
Original site: A0A0W8C5L8_PHYNI 
ID   A0A0W8C5L8_PHYNI        Unreviewed;       502 AA.
AC   A0A0W8C5L8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|RuleBase:RU000585};
DE            EC=2.1.2.1 {ECO:0000256|RuleBase:RU000585};
GN   ORFNames=AM587_10002038 {ECO:0000313|EMBL:KUG00398.1}, AM587_10007048
GN   {ECO:0000313|EMBL:KUF79369.1};
OS   Phytophthora nicotianae (Buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF79369.1, ECO:0000313|Proteomes:UP000052943};
RN   [1] {ECO:0000313|EMBL:KUF79369.1, ECO:0000313|Proteomes:UP000052943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943}, and Race 0
RC   {ECO:0000313|EMBL:KUF79369.1};
RA   Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT   "Genomes and virulence difference between two physiological races of
RT   Phytophthora nicotianae.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Interconversion of serine and glycine.
CC       {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|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:KUF79369.1}.
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DR   EMBL; LNFO01004853; KUF79369.1; -; Genomic_DNA.
DR   EMBL; LNFO01000688; KUG00398.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W8C5L8; -.
DR   STRING; 4790.A0A0W8C5L8; -.
DR   EnsemblProtists; KUF79369; KUF79369; AM587_10007048.
DR   EnsemblProtists; KUG00398; KUG00398; AM587_10002038.
DR   OMA; SRQKHFI; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000052943; 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: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:KUF79369.1};
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:UP000052943};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000585}.
FT   DOMAIN          35..435
FT                   /note="Serine hydroxymethyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00464"
FT   MOD_RES         266
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000412-50"
SQ   SEQUENCE   502 AA;  55074 MW;  852BADCD99F84BDE CRC64;
     MLGFLRAPTR RAALLSRRHA STESLQWAAA MNKPLAESDP QLFDIIEREK QRQRDCISLI
     ASENCTSVSV LDALGSVMSN KYSEGYPGQR YYGGNQIIDQ AEELCRARAL EAFNLDPEQW
     GVNVQSLSGS PANFQVYTAL LAPHDRIMAL DLPHGGHLSH GYQLGRKKIS ATSIFFESMP
     YRLDESTGLI DYDGLEKTAA LFRPKLIVAG TSAYSRSIDY ARMREICDQQ DAVLLADMAH
     ISGLVAAGVV PSPFEYADVV TTTTHKSLRG PRGAMIFYRK GVQSVDKKSG KEVMYDLQQK
     IDFAVFPGLQ GGPHNHTIAA LSTALLQAQS PEFKAYQSQV IANSRAMVAE LMKRGYDVVS
     NGTDNHLALV DVKKSRGVDG ARVEFVLESA NMVVNKNTVP GDKSAFVPGG IRLGAPALTT
     RGCTEENFQQ VAAFIDDGVK LTAELNERAR GQGVKKVKDF KDFVADDAEA QQKVDALKSE
     VTAFVRQFPT IGFSEEDMKY KN
//
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