ID   GLYM2_FLAPR             Reviewed;         517 AA.
AC   P49358;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Serine hydroxymethyltransferase 2, mitochondrial;
DE            Short=SHMT2;
DE            EC=2.1.2.1;
DE   AltName: Full=Glycine hydroxymethyltransferase 2;
DE   AltName: Full=Serine methylase 2;
DE   Flags: Precursor;
OS   Flaveria pringlei.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Tageteae; Flaveria.
OX   NCBI_TaxID=4226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RA   Kopriva S., Bauwe H.;
RT   "Cloning and sequencing of two isoforms of serine hydroxymethyltransferase
RT   from Flaveria pringlei.";
RL   (er) Plant Gene Register PGR98-051(1998).
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; Z25860; CAA81079.1; -; mRNA.
DR   PIR; S40213; S40213.
DR   AlphaFoldDB; P49358; -.
DR   SMR; P49358; -.
DR   PRIDE; P49358; -.
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   2: Evidence at transcript level;
KW   Mitochondrion; One-carbon metabolism; Pyridoxal phosphate; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..31
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           32..517
FT                   /note="Serine hydroxymethyltransferase 2, mitochondrial"
FT                   /id="PRO_0000032572"
FT   MOD_RES         287
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   517 AA;  56933 MW;  8D007DB76E5AED3F CRC64;
     MAMASALRRL SSSSNKPLQR LFNGGHLYSM SSLPSEAVYE KERPGVTWPK QLNAPLEVGD
     PEIADIIELE KARQWKGLEL ILSENFTSLS VMQAVGSVMT NKYSEGYPGA RYYGGNEYID
     MAETLCQKRA LEAFRLDAAK WGVNVQPLSG SPANFHVYTA LLKAHDRIMA LDLPHGGHLS
     HGYQTDTKKI SAVSIFFETM PYRLNESTGY IDYDQLEKSA TLFRPKLIVA GASAYARLYD
     YARIRKVCDK QKAILLADMA HISGLVAAGV IPSPFDYADV VTTTTHKSLR GPRGAMIFFR
     KGVKEVNKQG KEVLYDYEDK INQAVFPGLQ GGPHNHTITG LAVALKQATT AEYKAYQEQV
     MSNCAKFAET LVKSGYELVS GGTENHLVLV NLKNKGIDGS RVEKVLEAVH IAANKNTVPG
     DVSAMVPGGI RMGTPALTSR GFVEEDFAKV AYLFDLAVKL AVKIKGEAQG TKLKDFVAAM
     QSSAFQSEIS KLRHDVEEYA KQFPTIGFEK ETMKYKN