ID   FTHS_ALIFM              Reviewed;         582 AA.
AC   B5FG96;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Formate--tetrahydrofolate ligase {ECO:0000255|HAMAP-Rule:MF_01543};
DE            EC=6.3.4.3 {ECO:0000255|HAMAP-Rule:MF_01543};
DE   AltName: Full=Formyltetrahydrofolate synthetase {ECO:0000255|HAMAP-Rule:MF_01543};
DE            Short=FHS {ECO:0000255|HAMAP-Rule:MF_01543};
DE            Short=FTHFS {ECO:0000255|HAMAP-Rule:MF_01543};
GN   Name=fhs {ECO:0000255|HAMAP-Rule:MF_01543}; OrderedLocusNames=VFMJ11_1925;
OS   Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=388396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11;
RA   Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT   "Complete sequence of Vibrio fischeri strain MJ11.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01543};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000255|HAMAP-Rule:MF_01543}.
CC   -!- SIMILARITY: Belongs to the formate--tetrahydrofolate ligase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01543}.
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DR   EMBL; CP001139; ACH66842.1; -; Genomic_DNA.
DR   RefSeq; WP_012534022.1; NC_011184.1.
DR   AlphaFoldDB; B5FG96; -.
DR   SMR; B5FG96; -.
DR   EnsemblBacteria; ACH66842; ACH66842; VFMJ11_1925.
DR   KEGG; vfm:VFMJ11_1925; -.
DR   HOGENOM; CLU_003601_3_3_6; -.
DR   OMA; CGEIMTM; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000001857; Chromosome I.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004329; F:formate-tetrahydrofolate ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR   CDD; cd00477; FTHFS; 1.
DR   Gene3D; 3.40.50.300; -; 1.
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   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; One-carbon metabolism.
FT   CHAIN           1..582
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_1000146710"
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   582 AA;  62374 MW;  C11574C527FCBFEB CRC64;
     MKSDIEICQT ATLTRMKTIA SNLGLHDDDI TPQGPFKAKV NIDALKRLKS EPNGKLILVS
     AITPTPLGEG KTVTTIGLAQ GLAKLGESVS ACIRQPSMGP VFGVKGGAAG GGYSQVAPME
     ELNLHLTGDI HAITAAHNLA SAAIDARIYH EQRLGYDVFS EKNQLPALRI DPQRVVWKRV
     MDHNDRALRM VTIGKNEDGK TINGYEREDG FDITAASELM AILALATDLQ DLRQRIGRIV
     VAYNLDGEPV TTEDLQVAGA MTVTMKFAIN PTLMQTLEGV PTFVHSGPFA NIAHGNSSII
     ADNIALKLTD YTVTEGGFGS DMGFEKACNI KAPLSEKSPD CAVLVATLRG IKANSGLFPL
     SPGQSLPKEL FAPNKEALDA GLDNLLWHIN NCAKYGLPVV VAINRFPEDT QEELDSLLNW
     VSNLDINVDV AISEAFVKGG NGTLELAEKV IKACQQETQF TPLYTSEMSL FDKLNAVAIK
     GYGAERIELS EKAQQQLATF EKLGYQSLSV CMAKTPASIS TDGNIKGAPT DFVVPIRELK
     LCAGAGFIYA LCGNVMTMPG LPEKPAFMNL DIDGDGNIVG LS