ID   FTHS_GRABC              Reviewed;         572 AA.
AC   Q0BW57;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 89.
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};
GN   OrderedLocusNames=GbCGDNIH1_0047;
OS   Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Granulibacter.
OX   NCBI_TaxID=391165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1260 / CGDNIH1;
RX   PubMed=17827295; DOI=10.1128/jb.00793-07;
RA   Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA   Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT   "Genome sequence analysis of the emerging human pathogenic acetic acid
RT   bacterium Granulibacter bethesdensis.";
RL   J. Bacteriol. 189:8727-8736(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6R)-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:195366, ChEBI:CHEBI:456216;
CC         EC=6.3.4.3; 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; CP000394; ABI60945.1; -; Genomic_DNA.
DR   RefSeq; WP_011630755.1; NC_008343.2.
DR   AlphaFoldDB; Q0BW57; -.
DR   SMR; Q0BW57; -.
DR   STRING; 391165.GbCGDNIH1_0047; -.
DR   KEGG; gbe:GbCGDNIH1_0047; -.
DR   eggNOG; COG2759; Bacteria.
DR   HOGENOM; CLU_003601_3_3_5; -.
DR   OrthoDB; 9761733at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000001963; 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; 3.30.1510.10; Domain 2, N(10)-formyltetrahydrofolate synthetase; 1.
DR   Gene3D; 3.10.410.10; Formyltetrahydrofolate synthetase, domain 3; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; P-loop containing nucleoside triphosphate hydrolases; 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..572
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_0000293036"
FT   BINDING         81..88
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   572 AA;  60606 MW;  6D804024DA30ADD2 CRC64;
     MSTEANKPRG NQHQEAKSDA EIAQAAFMRP IVDVAAEKLG IAAEHLAPYG HYKAKIDLNY
     LSSLDSRPDG KLVLVTAISP TPAGEGKTTT TVGLTDALNH IGKKAVACLR EPSLGPCFGV
     KGGAAGGGYA QVVPMEDINL HFTGDFHAIG AANNLLAALI DNHVYWGNEL GIDPRRIGWR
     RAVDMNDRAL RSIVSSLGGV SNGYPREDGF DITVASEVMA IFCLATDLDD LQRRLGNIIV
     GHTKDRKPIR ASELSAAGSM AVLLKDAIAP NLVQTLEHNP AFIHGGPFAN IAHGCNSVIA
     TRAALKLSDY VVTEAGFGAD LGAEKFFDIK CRKAGLSPSA VVIVATVRAL KMHGGVAKDA
     LKTENVEAVQ KGFANLERHI QNVRKFGVPV VVGVNKFSAD TDAEFQMLHD LCAKMGVPCV
     SSDHWANGGA GAADLAHEVV KLVEGGSADF KPLYPEDMPL WDKLRTIATE IYGASDITAD
     AAVRKRFDEL QKEGFGHLPI CVAKTQYSFS TDANLRGAPS GHVIPVRDLR LSAGAEFVVA
     ICGDIMTMPG LPKVPAANAI RLASNGTIAG LF
//