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Database: UniProt
Entry: F7FV99_MACMU
LinkDB: F7FV99_MACMU
Original site: F7FV99_MACMU 
ID   F7FV99_MACMU            Unreviewed;       483 AA.
AC   F7FV99; F6WIE8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|RuleBase:RU000585};
DE            EC=2.1.2.1 {ECO:0000256|RuleBase:RU000585};
GN   Name=SHMT1 {ECO:0000313|EMBL:AFE79689.1,
GN   ECO:0000313|Ensembl:ENSMMUP00000017801.4,
GN   ECO:0000313|VGNC:VGNC:103864};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000017801.4, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA   Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA   Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA   Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA   Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA   Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA   Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA   Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA   Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA   Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA   Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA   Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA   Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA   Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA   Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA   Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA   Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA   Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA   Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA   Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA   Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA   Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA   Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA   Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA   Kuhn R.M., Smith K.E., Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|EMBL:AFE79689.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Caudate {ECO:0000313|EMBL:AFE79689.1}, and Thymus
RC   {ECO:0000313|EMBL:AFH28105.1};
RX   PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA   Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA   Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA   Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA   Yorke J.A., Norgren R.B.Jr.;
RT   "A new rhesus macaque assembly and annotation for next-generation
RT   sequencing analyses.";
RL   Biol. Direct 9:20-20(2014).
RN   [3] {ECO:0000313|Ensembl:ENSMMUP00000017801.4}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000017801.4};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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; JU335936; AFE79689.1; -; mRNA.
DR   EMBL; JU471301; AFH28105.1; -; mRNA.
DR   RefSeq; NP_001244360.1; NM_001257431.1.
DR   RefSeq; XP_014974168.1; XM_015118682.1.
DR   RefSeq; XP_014974169.1; XM_015118683.1.
DR   RefSeq; XP_014974170.1; XM_015118684.1.
DR   STRING; 9544.ENSMMUP00000017801; -.
DR   PaxDb; 9544-ENSMMUP00000035136; -.
DR   Ensembl; ENSMMUT00000019005.4; ENSMMUP00000017801.4; ENSMMUG00000013535.4.
DR   GeneID; 701186; -.
DR   KEGG; mcc:701186; -.
DR   CTD; 6470; -.
DR   VEuPathDB; HostDB:ENSMMUG00000013535; -.
DR   VGNC; VGNC:103864; SHMT1.
DR   GeneTree; ENSGT00390000002762; -.
DR   OMA; CATTHKV; -.
DR   OrthoDB; 5358603at2759; -.
DR   TreeFam; TF314667; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000006718; Chromosome 16.
DR   Bgee; ENSMMUG00000013535; Expressed in liver and 21 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0048027; F:mRNA 5'-UTR binding; IBA:GO_Central.
DR   GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0070905; F:serine binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IBA:GO_Central.
DR   GO; GO:1904482; P:cellular response to tetrahydrofolate; IEA:Ensembl.
DR   GO; GO:0046655; P:folic acid metabolic process; IBA:GO_Central.
DR   GO; GO:0019264; P:glycine biosynthetic process from serine; IBA:GO_Central.
DR   GO; GO:0006565; P:L-serine catabolic process; IBA:GO_Central.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0051289; P:protein homotetramerization; IBA:GO_Central.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IBA:GO_Central.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IBA:GO_Central.
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:SF35; 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   2: Evidence at transcript level;
KW   Methyltransferase {ECO:0000313|EMBL:AFE79689.1};
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:UP000006718};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000585}.
FT   DOMAIN          26..425
FT                   /note="Serine hydroxymethyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00464"
FT   MOD_RES         257
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000412-50"
SQ   SEQUENCE   483 AA;  53141 MW;  D2026D6660587D93 CRC64;
     METPVNGAHK DADLWSSHDK MLAQPLKDSD VEVYNIIKKE SNRQRVGLEL IASENFASRA
     VLEALGSCLN NKYSEGYPGQ RYYGGTEFID ELETLCQKRA LQAYKLDPQC WGVNVQPYSG
     SPANFAVYTA LVEPHGRIMG LDLPDGGHLT HGFMTDKKKI SATSIFFESM PYKVNPDTGY
     INYDQLEENA RLFHPKLIIA GTSCYSRNLD YARLRKIADE NGAYLMADMA HISGLVVAGV
     VPSPFEHCHV VTTTTHKTLR GCRAGMIFYR KGVKNVDPKT GKEILYNLES LINSAVFPGL
     QGGPHNHAIA GVAVALKQAM TLEFKVYQHQ VVANCRALSE ALMELGYKIV TGGSDNHLIL
     VDLRSKGTDG GRAEKVLEAC SIACNKNTCP GDRSALRPSG LRLGTPALTS RGLLEKDFQK
     VAQFIHRGIE LTLQIQSDIG VRATLKEFKE RLAGDKYQGA VQALREEVES FASLFPLPGL
     PDF
//
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