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Database: UniProt
Entry: R0HF33_9BRAS
LinkDB: R0HF33_9BRAS
Original site: R0HF33_9BRAS 
ID   R0HF33_9BRAS            Unreviewed;       519 AA.
AC   R0HF33;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|RuleBase:RU000585};
DE            EC=2.1.2.1 {ECO:0000256|RuleBase:RU000585};
GN   ORFNames=CARUB_v10003023mg {ECO:0000313|EMBL:EOA22388.1};
OS   Capsella rubella.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX   NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA22388.1, ECO:0000313|Proteomes:UP000029121};
RN   [1] {ECO:0000313|Proteomes:UP000029121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX   PubMed=23749190; DOI=10.1038/ng.2669;
RA   Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA   Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA   Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA   Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA   Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA   Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT   "The Capsella rubella genome and the genomic consequences of rapid mating
RT   system evolution.";
RL   Nat. Genet. 45:831-835(2013).
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}.
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DR   EMBL; KB870810; EOA22388.1; -; Genomic_DNA.
DR   RefSeq; XP_006289490.1; XM_006289428.1.
DR   AlphaFoldDB; R0HF33; -.
DR   STRING; 81985.R0HF33; -.
DR   GeneID; 17882962; -.
DR   KEGG; crb:17882962; -.
DR   eggNOG; KOG2467; Eukaryota.
DR   OrthoDB; 5358603at2759; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000029121; Unassembled WGS sequence.
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: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   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:UP000029121};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000585}.
FT   DOMAIN          57..454
FT                   /note="Serine hydroxymethyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00464"
FT   MOD_RES         288
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000412-50"
SQ   SEQUENCE   519 AA;  57602 MW;  E960B291F194375B CRC64;
     MALALRRLSS SVKKPISRLY SNGGDSLRFM SSSVSASAMA DSEKPRSIWI KQLNASLDEI
     DPEVADIIEL EKARQWKGFE LIPSENFTSL SVMQAVGSVM TNKYSEGYPG ARYYGGNEYI
     DMAESLCQKR ALEAFQLDPS KWGVNVQSLS GSPANFQVYT ALLKPHERIM ALDLPHGGHL
     SHGYQTDTKK ISAVSIFFET MPYRLDENTG YIDYDQLEKS AVLFRPKLIV AGASAYARLY
     DYARIRKVCD KQKAVMLADM AHISGLVAAG VIPSPFEYAD VVTTTTHKSL RGPRGAMIFF
     RKGLKEINKQ GKEVMYDYED RINQAVFPGL QGGPHNHTIT GLAVALKQAR TPEYKAYQDQ
     VLRNCSKFAE TLLAKGYDLV SGGTDNHLVL VNLKNKGIDG SRVEKVLESV HIAANKNTVP
     GDVSAMVPGG IRMGTPALTS RGFIEEDFAR VADYFDLAVK IALKIKAESQ GTKLKDFVAT
     MQSNEKLKSE MAKLREMVEE YAKQFPTIGF EKESMRYKE
//
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