FTHS_SPIOL
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 03-AUG-2022, entry version 82.
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 = (6S)-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:57454, ChEBI:CHEBI:456216; 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 PRIDE; P28723; -.
DR UniPathway; UPA00193; -.
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; 3.40.50.300; -; 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; SSF52540; 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.
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
