ID   FTHS_STAA2              Reviewed;         555 AA.
AC   A6U2J8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=SaurJH1_1822;
OS   Staphylococcus aureus (strain JH1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=359787;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JH1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Tomasz A., Richardson P.;
RT   "Complete sequence of chromosome of Staphylococcus aureus subsp. aureus
RT   JH1.";
RL   Submitted (JUN-2007) 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; CP000736; ABR52666.1; -; Genomic_DNA.
DR   RefSeq; WP_000149407.1; NC_009632.1.
DR   AlphaFoldDB; A6U2J8; -.
DR   SMR; A6U2J8; -.
DR   KEGG; sah:SaurJH1_1822; -.
DR   HOGENOM; CLU_003601_3_3_9; -.
DR   OMA; CGEIMTM; -.
DR   UniPathway; UPA00193; -.
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..555
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_1000087659"
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   555 AA;  59872 MW;  E71E884FF0368174 CRC64;
     MTHLSDLDIA NQSTLQPIKD IAASVGISED ALEPYGHYKA KIDINKITPR ENKGKVVLVT
     AMSPTPAGEG KSTVTVGLAD AFHELNKNVM VALREPALGP TFGIKGGATG GGYAQVLPME
     DINLHFNGDF HAITTANNAL SAFIDNHIHQ GNELGIDQRR IEWKRVLDMN DRALRHVNVG
     LGGPTNGVPR EDGFNITVAS EIMAILCLSR SIKDLKDKIS RITIGYTRDR KPVTVADLKV
     QGALAMILKD AIKPNLVQSI EGTPALVHGG PFANIAHGCN SILATETARD LADIVVTEAG
     FGSDLGAEKF MDIKAREAGF DLAAVVVVAT IRALKMHGGV AKDNLKEENV EAVKAGIVNL
     ERHVNNIKKF GVEPVVAINA FIHDTDAEVE YVKSWAKENN VRIALTEVWE KGGKGGVDLA
     NEVLEVIDQP NSFKPLYELE LPLEQKIEKI VTEIYGGSKV TFSSKAQKQL KQFKENGWDN
     YPVCMAKTQY SFSDDQTLLG APSGFEITIR ELEAKTGAGF IVALTGAIMT MPGLPKKPAA
     LNMDVTDDGH AIGLF