ID   GLYM_PEA                Reviewed;         518 AA.
AC   P34899;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Serine hydroxymethyltransferase, mitochondrial;
DE            Short=SHMT;
DE            EC=2.1.2.1;
DE   AltName: Full=Glycine hydroxymethyltransferase;
DE   AltName: Full=Serine methylase;
DE   Flags: Precursor;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=1618853; DOI=10.1016/s0021-9258(18)42243-0;
RA   Turner S.R., Ireland R., Morgan C., Rawsthorne S.;
RT   "Identification and localization of multiple forms of serine
RT   hydroxymethyltransferase in pea (Pisum sativum) and characterization of a
RT   cDNA encoding a mitochondrial isoform.";
RL   J. Biol. Chem. 267:13528-13534(1992).
CC   -!- FUNCTION: Catalyzes the interconversion of serine and glycine.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000305}.
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DR   EMBL; M87649; AAA33687.1; -; mRNA.
DR   PIR; A42906; A42906.
DR   AlphaFoldDB; P34899; -.
DR   SMR; P34899; -.
DR   IntAct; P34899; 1.
DR   PRIDE; P34899; -.
DR   EnsemblPlants; Psat2g133920.1; Psat2g133920.1.cds; Psat2g133920.
DR   Gramene; Psat2g133920.1; Psat2g133920.1.cds; Psat2g133920.
DR   UniPathway; UPA00193; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; 3.40.640.10; -; 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   Direct protein sequencing; Mitochondrion; One-carbon metabolism;
KW   Pyridoxal phosphate; Transferase; Transit peptide.
FT   TRANSIT         1..31
FT                   /note="Mitochondrion"
FT   CHAIN           32..518
FT                   /note="Serine hydroxymethyltransferase, mitochondrial"
FT                   /id="PRO_0000032570"
FT   MOD_RES         287
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   518 AA;  57293 MW;  F96DA281FEBE592B CRC64;
     MAMAMALRKL SSSVNKSSRP LFSASSLYYK SSLPDEAVYD KENPRVTWPK QLNSPLEVID
     PEIADIIELE KARQWKGLEL IPSENFTSLS VMQAVGSVMT NKYSEGYPGA RYYGGNEYID
     MAETLCQKRA LEAFRLDPAK WGVNVQPLSG SPSNFQVYTA LLKPHDRIMA LDLPHGGHLS
     HGYQTDTKKI SAVSIFFETM PYRLDESTGY IDYDQLEKSA TLFRPKLIVA GASAYARLYD
     YARIRKVCDK QKAVLLADMA HISGLVAAGV IPSPFDYADV VTTTTHKSLR GPRGAMIFFR
     KGLKEVNKQG KEVFYDYEDK INQAVFPGLQ GGPHNHTITG LAVALKQATT PEYRAYQEQV
     LSNSSKFAKA LSEKGYDLVS GGTENHLVLV NLKNKGIDGS RVEKVLELVH IAANKNTVPG
     DVSAMVPGGI RMGTPALTSR GFVEEDFVKV AEYFDAAVSL ALKVKAESKG TKLKDFVEAL
     QTSSYVQSEI SKLKHDVEEF AKQFPTIGFE KATMKYNK