ID   FTHS_CERS5              Reviewed;         557 AA.
AC   A4WQ11;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Rsph17025_0569;
OS   Cereibacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=349102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17025 / ATH 2.4.3;
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   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M.,
RA   Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome of Rhodobacter sphaeroides ATCC 17025.";
RL   Submitted (APR-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; CP000661; ABP69475.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4WQ11; -.
DR   SMR; A4WQ11; -.
DR   STRING; 349102.Rsph17025_0569; -.
DR   PRIDE; A4WQ11; -.
DR   EnsemblBacteria; ABP69475; ABP69475; Rsph17025_0569.
DR   KEGG; rsq:Rsph17025_0569; -.
DR   eggNOG; COG2759; Bacteria.
DR   HOGENOM; CLU_003601_3_3_5; -.
DR   OMA; CGEIMTM; -.
DR   OrthoDB; 177859at2; -.
DR   BioCyc; RSPH349102:G1G8M-586-MON; -.
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..557
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_1000068791"
FT   BINDING         67..74
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   557 AA;  59748 MW;  C4CD3642735EADAE CRC64;
     MTFQSDIEIA RAANKLPIQE IGARLGIPSG DLIPYGHDKA KVSQGFIRGL ADRPDGKLIL
     VTAINPTPAG EGKTTTTVGL GDGLNRIGKR AVICIREASL GPNFGMKGGA AGGGRSQVVP
     MEDMNLHFTG DFHAITSAHN LLSAMIDNHI YWGNDLGLDA RRITWRRVMD MNDRALRDMV
     VNLGGVSNGF PRQTGFDITV ASEVMAILCL AEDLEDLERR LGGIVVGYRR DRSPVFCRDL
     KADGAMAVLL KDAMQPNLVQ TIENNPAFVH GGPFANIAHG CNSVIATRTA LKLADYVVTE
     AGFGADLGAE KFFDIKCRKA GLKPSAAVVV ATVRALKMNG GVAREDLGRE DVAALKRGCA
     NLGRHIANVK GFGVPVVVAI NHFTTDTEAE IEAVRAYAAG QGAEAILCRH WADGSAGIED
     LARKVVQLAE TPSMFAPLYP DEMPLFEKME TVARRIYHAH DVIADHVIRD QLRAWEDAGY
     GALPVCMAKT QYSFTTDAAI RGAPEGHSVP IREVRLSAGA GFVVAICGEI RTMPGLPREP
     AAEVIRLNGE GRIEGLF