GLYC_SHEEP
ID GLYC_SHEEP Reviewed; 484 AA.
AC P35623;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Serine hydroxymethyltransferase, cytosolic;
DE Short=SHMT;
DE EC=2.1.2.1 {ECO:0000269|PubMed:7607226};
DE AltName: Full=Glycine hydroxymethyltransferase;
DE AltName: Full=Serine methylase;
GN Name=SHMT1;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-15, SEQUENCE REVISION,
RP CATALYTIC ACTIVITY, FUNCTION, AND SUBUNIT.
RC TISSUE=Liver;
RX PubMed=7607226; DOI=10.1111/j.1432-1033.1995.0533h.x;
RA Jagath-Reddy J., Ganesan K., Savithri H.S., Datta A., Rao N.A.;
RT "cDNA cloning, overexpression in Escherichia coli, purification and
RT characterization of sheep liver cytosolic serine
RT hydroxymethyltransferase.";
RL Eur. J. Biochem. 230:533-537(1995).
RN [2]
RP SEQUENCE REVISION.
RA Rao N.A.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-484, AND COFACTOR.
RC TISSUE=Liver;
RX PubMed=8305478; DOI=10.1016/0167-4838(94)90035-3;
RA Usha R., Savithri H.S., Rao N.A.;
RT "The primary structure of sheep liver cytosolic serine
RT hydroxymethyltransferase and an analysis of the evolutionary relationships
RT among serine hydroxymethyltransferases.";
RL Biochim. Biophys. Acta 1204:75-83(1994).
CC -!- FUNCTION: Interconversion of serine and glycine.
CC {ECO:0000269|PubMed:7607226}.
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:0000269|PubMed:7607226};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|Ref.2};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000305}.
CC -!- SUBUNIT: Homotetramer (PubMed:7607226). Identified in complex with
CC ABRAXAS2 and the other subunits of the BRISC complex, at least composed
CC of ABRAXAS2, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1.
CC {ECO:0000250|UniProtKB:P34896, ECO:0000269|PubMed:7607226}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: In eukaryotes there are two forms of the enzymes: a
CC cytosolic one and a mitochondrial one. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000305}.
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DR EMBL; X80024; CAA56326.1; -; mRNA.
DR PIR; S65688; A40202.
DR RefSeq; NP_001009469.1; NM_001009469.1.
DR AlphaFoldDB; P35623; -.
DR SMR; P35623; -.
DR STRING; 9940.ENSOARP00000019916; -.
DR Ensembl; ENSOART00020041479; ENSOARP00020034441; ENSOARG00020026362.
DR GeneID; 443544; -.
DR KEGG; oas:443544; -.
DR CTD; 6470; -.
DR eggNOG; KOG2467; Eukaryota.
DR OrthoDB; 372408at2759; -.
DR SABIO-RK; P35623; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; ISS:UniProtKB.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IEA:Ensembl.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR GO; GO:0070905; F:serine binding; IEA:Ensembl.
DR GO; GO:1904482; P:cellular response to tetrahydrofolate; IEA:Ensembl.
DR GO; GO:0046655; P:folic acid metabolic process; IEA:Ensembl.
DR GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:InterPro.
DR GO; GO:0006544; P:glycine metabolic process; ISS:UniProtKB.
DR GO; GO:0006565; P:L-serine catabolic process; IEA:Ensembl.
DR GO; GO:0006563; P:L-serine metabolic process; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:Ensembl.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR GO; GO:0046653; P:tetrahydrofolate metabolic process; ISS:UniProtKB.
DR CDD; cd00378; SHMT; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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; PTHR11680; 1.
DR Pfam; PF00464; SHMT; 1.
DR PIRSF; PIRSF000412; SHMT; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00096; SHMT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; One-carbon metabolism;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P07511,
FT ECO:0000269|PubMed:7607226, ECO:0000269|PubMed:8305478"
FT CHAIN 2..484
FT /note="Serine hydroxymethyltransferase, cytosolic"
FT /id="PRO_0000113507"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P07511"
FT MOD_RES 257
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P34896"
FT VARIANT 468
FT /note="E -> V"
FT VARIANT 474
FT /note="T -> A"
SQ SEQUENCE 484 AA; 53025 MW; 6EAF599F23D3B77F CRC64;
MAAPVNKAPR DADLWSLHEK MLAQPLKDND VEVYNIIKKE SNRQRVGLEL IASENFASRA
VLEALGSCLN NKYSEGYPGQ RYYGGTEFID ELEVLCQKRA LQVYGLDPEC WGVNVQPYSG
SPANFAVYTA LVEPHGRIMG LDLPDGGHLT HGFMTDKKKI SATSIFFESM PYKVNPDTGY
INYDQLEENA RLFHPRLIIA GTSCYSRNLD YARLRKIADD NGAYLMADMA HISGLVAAGV
VPSPFEHCHV VSTTTHKTLR GCRAGMIFYR KGVRSVDPKT GKETRYNLES LINSAVFPGL
QGGPHNHAIA GVAVALKQAM TPEFRAYQRQ VVANCRALAE ALMGLGYRVV TGGSDNHLIL
VDLRSKGTDG GRAEKVLEAC SIACNKNTCP GDKSALRPSG LRLGTPALTS RGLLEEDFRK
VAHFIHRGIE LTLQIQDAVG VKATLKEFME KLAGAEEHQR AVTALRAEVE SFATLFPLPG
LPGF
