ID FTHS_CORDI Reviewed; 550 AA. AC Q6NH87; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 102. 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=DIP1253; OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype OS gravis). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=257309; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis; RX PubMed=14602910; DOI=10.1093/nar/gkg874; RA Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G., RA Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D., RA De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N., RA Holroyd S., Jagels K., Moule S., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G., RA Parkhill J.; RT "The complete genome sequence and analysis of Corynebacterium diphtheriae RT NCTC13129."; RL Nucleic Acids Res. 31:6516-6523(2003). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX248357; CAE49782.1; -; Genomic_DNA. DR RefSeq; WP_010934929.1; NC_002935.2. DR AlphaFoldDB; Q6NH87; -. DR SMR; Q6NH87; -. DR STRING; 257309.DIP1253; -. DR KEGG; cdi:DIP1253; -. DR HOGENOM; CLU_003601_3_3_11; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000002198; 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..550 FT /note="Formate--tetrahydrofolate ligase" FT /id="PRO_0000199342" FT BINDING 62..69 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543" SQ SEQUENCE 550 AA; 58098 MW; 27D7F2392BABA05D CRC64; MPTDVEIAQA HTLEPITDIA NRAGVPSDAL IPYGFTKAKI DINRIASENT GKLVLVTGIS PTPAGEGKST VLIGLSDAMR LRGHNSIVAI REPSLGPVMG IKGGAAGGGY SQIVPMEDIN LHFTGDFHAI TAANNTLAAM IDNHIHQGNT LGIDVRRITW QRCLDVNDRC LRKVVTGLGG KAHGVPTETG FTITAASEIM AILCLALDLT DLEARLARIV VGQTFSSEPV TVGQLNAQGA LAALLRDAVN PNLVQTLGGT PALCHGGPFA NIAHGCNSLI ATKTALSLGD VVLTEAGFGS DLGAEKFFDI KSRVGDLNVA ATVVVATVRS LKYNAGVPKD ELTTENLEAL ASGVVNLERH VENIRAFGIE PIVALNKFAS DTDAEINQLK AWAETMSVQL IPVEVWAHGG QGALELADAV AVSMQNQTSH HLYDPELGIE ASLLTIAQKI YGAADVELSK QARQDLAYLQ ENGWDRLPVC ISKTQYSFSD DPSQLGRPEG HTLHVRNLLP RIGAGFIVAL TGDVMTMPGL PKKPAAENIG VENGEIKGLF //