ID   FTHS_ALIF1              Reviewed;         582 AA.
AC   Q5E3V8;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=VF_1793;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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; CP000020; AAW86288.1; -; Genomic_DNA.
DR   RefSeq; WP_011262325.1; NC_006840.2.
DR   RefSeq; YP_205176.1; NC_006840.2.
DR   AlphaFoldDB; Q5E3V8; -.
DR   SMR; Q5E3V8; -.
DR   STRING; 312309.VF_1793; -.
DR   EnsemblBacteria; AAW86288; AAW86288; VF_1793.
DR   KEGG; vfi:VF_1793; -.
DR   PATRIC; fig|312309.11.peg.1820; -.
DR   eggNOG; COG2759; Bacteria.
DR   HOGENOM; CLU_003601_3_3_6; -.
DR   OMA; CGEIMTM; -.
DR   OrthoDB; 177859at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000000537; 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;
KW   Reference proteome.
FT   CHAIN           1..582
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_0000199408"
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;  62388 MW;  4AEA0318FE978295 CRC64;
     MKSDIEICQT ATLTRMKTIA SNLGLHDDDI TPQGPFKAKV NIDALKRLKS EPNGKLILVS
     AITPTPLGEG KTVTTIGLAQ GLAKLGESVS ACIRQPSMGP VFGVKGGAAG GGYSQVAPME
     ELNLHLTGDI HAITAAHNLA SAAIDARIYH EQRLGYDVFS EKNELPALRI DPQHVVWKRV
     MDHNDRALRM VTIGKNEDGK TINGYEREDG FDITAASELM AILALATDLQ DLRQRIGRIV
     VAYNLDGEPV TTEDLQVAGA MTVTMKFAIN PTLMQTLEGV PTFVHSGPFA NIAHGNSSII
     ADNIALKLTD YTVTEGGFGS DMGFEKACNI KAPLSEKSPD CAVLVATLRG IKANSGLFPL
     SPGQSLPKEL FAPNKEALDA GLDNLLWHIN NCAKYGLPVV VAINRFPEDT QEELDSLLNW
     VSNLDMNVDV AISEAFVKGG NGTLELAEKV IKACQQETQF TPLYTSEMSL FDKLNAVAIK
     GYGAERIELS EKAQQQLATF EKLGYQSLSV CMAKTPASIS TDGNIKGAPT DFIVPIRELK
     LCAGAGFIYA LCGNVMTMPG LPEKPAFMNL DIDGDGNIVG LS