ID   FTHS_METEA              Reviewed;         557 AA.
AC   Q83WS0; C5AS46;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Formate--tetrahydrofolate ligase;
DE            EC=6.3.4.3;
DE   AltName: Full=Formyltetrahydrofolate synthetase;
DE            Short=FHS;
DE            Short=FTHFS;
GN   Name=fhs; Synonyms=ftfL; OrderedLocusNames=MexAM1_META1p0329;
OS   Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS   9133 / AM1) (Methylobacterium extorquens).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=272630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13, CATALYTIC
RP   ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX   PubMed=14645277; DOI=10.1128/jb.185.24.7169-7175.2003;
RA   Marx C.J., Laukel M., Vorholt J.A., Lidstrom M.E.;
RT   "Purification of the formate-tetrahydrofolate ligase from Methylobacterium
RT   extorquens AM1 and demonstration of its requirement for methylotrophic
RT   growth.";
RL   J. Bacteriol. 185:7169-7175(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX   PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA   Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA   Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA   Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA   Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA   Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA   Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA   Lidstrom M.E.;
RT   "Methylobacterium genome sequences: a reference blueprint to investigate
RT   microbial metabolism of C1 compounds from natural and industrial sources.";
RL   PLoS ONE 4:E5584-E5584(2009).
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:0000269|PubMed:14645277};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=22 mM for formate {ECO:0000269|PubMed:14645277};
CC         KM=0.8 mM for tetrahydrofolate {ECO:0000269|PubMed:14645277};
CC         KM=21 uM for ATP {ECO:0000269|PubMed:14645277};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:14645277}.
CC   -!- SIMILARITY: Belongs to the formate--tetrahydrofolate ligase family.
CC       {ECO:0000305}.
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DR   EMBL; AY279316; AAP33693.1; -; Genomic_DNA.
DR   EMBL; CP001510; ACS38281.1; -; Genomic_DNA.
DR   RefSeq; WP_003606333.1; NC_012808.1.
DR   AlphaFoldDB; Q83WS0; -.
DR   SMR; Q83WS0; -.
DR   STRING; 272630.MexAM1_META1p0329; -.
DR   EnsemblBacteria; ACS38281; ACS38281; MexAM1_META1p0329.
DR   KEGG; mea:Mex_1p0329; -.
DR   eggNOG; COG2759; Bacteria.
DR   HOGENOM; CLU_003601_3_3_5; -.
DR   OMA; CGEIMTM; -.
DR   OrthoDB; 177859at2; -.
DR   BioCyc; MetaCyc:MON-3942; -.
DR   BRENDA; 6.3.4.3; 3296.
DR   SABIO-RK; Q83WS0; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000009081; Chromosome.
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   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:14645277"
FT   CHAIN           2..557
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_0000199359"
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   557 AA;  59391 MW;  D0DB51A90971072A CRC64;
     MPSDIEIARA ATLKPIAQVA EKLGIPDEAL HNYGKHIAKI DHDFIASLEG KPEGKLVLVT
     AISPTPAGEG KTTTTVGLGD ALNRIGKRAV MCLREPSLGP CFGMKGGAAG GGKAQVVPME
     QINLHFTGDF HAITSAHSLA AALIDNHIYW ANELNIDVRR IHWRRVVDMN DRALRAINQS
     LGGVANGFPR EDGFDITVAS EVMAVFCLAK NLADLEERLG RIVIAETRDR KPVTLADVKA
     TGAMTVLLKD ALQPNLVQTL EGNPALIHGG PFANIAHGCN SVIATRTGLR LADYTVTEAG
     FGADLGAEKF IDIKCRQTGL KPSAVVIVAT IRALKMHGGV NKKDLQAENL DALEKGFANL
     ERHVNNVRSF GLPVVVGVNH FFQDTDAEHA RLKELCRDRL QVEAITCKHW AEGGAGAEAL
     AQAVVKLAEG EQKPLTFAYE TETKITDKIK AIATKLYGAA DIQIESKAAT KLAGFEKDGY
     GGLPVCMAKT QYSFSTDPTL MGAPSGHLVS VRDVRLSAGA GFVVVICGEI MTMPGLPKVP
     AADTIRLDAN GQIDGLF