GLYM1_FLAPR
ID GLYM1_FLAPR Reviewed; 517 AA.
AC P49357;
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 1, mitochondrial;
DE Short=SHMT1;
DE EC=2.1.2.1;
DE AltName: Full=Glycine hydroxymethyltransferase 1;
DE AltName: Full=Serine methylase 1;
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; Z25859; CAA81078.1; -; mRNA.
DR PIR; S40212; S40212.
DR AlphaFoldDB; P49357; -.
DR SMR; P49357; -.
DR PRIDE; P49357; -.
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 1, mitochondrial"
FT /id="PRO_0000032571"
FT MOD_RES 287
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 517 AA; 57049 MW; C95386CC3FCF6350 CRC64;
MAMALALRRL SSSADKPLQR LFNGGHLYSM SSLPSEAVYE KERPGVTWPK QLNAPLEVVD
PEIADIIELE KARQWKGLEL IPSENFTSLS VMQAVGSVMT NKYSEGYPGA RYYGGNEYID
MAETLCQKRA LEAFRLDPAK WGVNVQPLSG SPANFHVYTA LLKAHDRIMA LDLPHGGHLS
HGYQTDTKKI SAVSIFFETM PYRLNESTGY IDYDQLEKSA TLFRPKLIVA GASAYARLYD
YARIRKVCDK QKAIMLADMA HISGLVAAGV IPSPFDYADV VTTTTHKSLR GPRGAMIFFR
KGLKEVNKQG KEVFYDYEDK INQAVFPGLQ GGPHNHTITG LAVALKQATT AEYKAYQEQV
MSNSAKFAET LVKSGYELVS GGTENHLVLV NLKNKGIDGS KVEKVLEAVH IAANKNTVPG
DVSAMVPGGI RMGTPALTSR GFVEEDFAKV AYFFDLAVKL AVKIKGEAKG TKLKDFVTAM
ESSAIQSEIS KLRHDVEEYA KQFPTIGFEK ETMKYKN
