ID   FTHS_SPIOL              Reviewed;         637 AA.
AC   P28723;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-NOV-2023, entry version 86.
DE   RecName: Full=Formate--tetrahydrofolate ligase;
DE            EC=6.3.4.3;
DE   AltName: Full=10-formyletrahydrofolate synthetase;
DE            Short=FHS;
DE            Short=FTHFS;
DE   AltName: Full=Formyltetrahydrofolate synthetase;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1644815; DOI=10.1016/s0021-9258(18)41999-0;
RA   Nour J.M., Rabinowitz J.C.;
RT   "Isolation and sequencing of the cDNA coding for spinach 10-
RT   formyltetrahydrofolate synthetase. Comparisons with the yeast, mammalian,
RT   and bacterial proteins.";
RL   J. Biol. Chem. 267:16292-16296(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-36.
RC   TISSUE=Leaf;
RX   PubMed=1917961; DOI=10.1016/s0021-9258(18)55279-0;
RA   Nour J.M., Rabinowitz J.C.;
RT   "Isolation, characterization, and structural organization of 10-
RT   formyltetrahydrofolate synthetase from spinach leaves.";
RL   J. Biol. Chem. 266:18363-18369(1991).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6R)-10-
CC         formyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:20221,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57453, ChEBI:CHEBI:195366, ChEBI:CHEBI:456216;
CC         EC=6.3.4.3;
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the formate--tetrahydrofolate ligase family.
CC       {ECO:0000305}.
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DR   EMBL; M83940; AAA34046.1; -; mRNA.
DR   PIR; A40948; A40948.
DR   PIR; A43350; A43350.
DR   AlphaFoldDB; P28723; -.
DR   SMR; P28723; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP001155700; Unplaced.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004329; F:formate-tetrahydrofolate ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR   CDD; cd00477; FTHFS; 1.
DR   Gene3D; 1.10.8.770; -; 1.
DR   Gene3D; 3.10.410.10; Formyltetrahydrofolate synthetase, domain 3; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   HAMAP; MF_01543; FTHFS; 1.
DR   InterPro; IPR000559; Formate_THF_ligase.
DR   InterPro; IPR020628; Formate_THF_ligase_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF01268; FTHFS; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00721; FTHFS_1; 1.
DR   PROSITE; PS00722; FTHFS_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Ligase; Nucleotide-binding;
KW   One-carbon metabolism; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1917961"
FT   CHAIN           2..637
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_0000199418"
FT   BINDING         81..88
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   637 AA;  67855 MW;  AAF08ABA23C54B9E CRC64;
     MGGSSKTVRK LEVATPVPAD IDIANAVEPL HIADIAADLN LSPRHYDLYG KYKAKVLLSV
     LDEVQETQDG YYVVVGGITP TPLGEGKSTT TVGLCQALGA FLDKKVVTCL RQPSQGPTFG
     IKGGAAGGGY SQVIPMDEFN LHLTGDIHAI TASNNLLAAA IDTRMFHEST QSDKALFNRL
     CPPNKEGKRT FCNIMHRRLK KLGIDKTNPD DLTPEEVTKF ARLDIDPDSI TWRRVMDVND
     RFLRKISVGQ GPDEKGMVRE TGFDISVASE IMAVLALTTS LADMRERLGK MVIGNSKAGE
     PITADDLGLG GALTVLMKDA INPTLMQTLE GTPVLVHAGP FANIAHGNSS IVADKIALKL
     VGPGGFVVTE AGFGSDIGTE KFMNIKCRYS GLTPQCAIVV ATVRALKMHG GGPQVVAGKP
     LDRAYLTENV GLVEAGCVNL ARHIINTKAY GSNVVVAINM FSSDTEAELN AVKKAAMDAG
     AFDAVICTHH AHGGKGAVDL GIAVQKACEN VTQPLRFLYP LDISIKEKIE AIAKSYGAAG
     VEYSEQAEKK IEMYSKQGFS NLPICMAKTQ YSFSHNAAEK GAPSGFILPI RDVRGSIGAG
     FIYPLVGTMS TMPGLPTRPC FFDIDLDTTT GKVIGLS
//