ID FTHS_CAMC5 Reviewed; 550 AA. AC A7GZZ0; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 1. DT 27-MAR-2024, entry version 85. 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=Ccur92_14780; ORFNames=CCV52592_0358; OS Campylobacter curvus (strain 525.92). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=360105; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=525.92; RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., RA Mandrell R.E., Lastovica A.J., Nelson K.E.; RT "Genome sequence of Campylobacter curvus 525.92 isolated from human RT feces."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. 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; CP000767; EAT99584.1; -; Genomic_DNA. DR RefSeq; WP_011992625.1; NC_009715.2. DR AlphaFoldDB; A7GZZ0; -. DR SMR; A7GZZ0; -. DR STRING; 360105.CCV52592_0358; -. DR KEGG; ccv:CCV52592_0358; -. DR HOGENOM; CLU_003601_3_3_7; -. DR OrthoDB; 9761733at2; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000006380; 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_1000068789" FT BINDING 60..67 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543" SQ SEQUENCE 550 AA; 59241 MW; C88B170DDC4A8D78 CRC64; MLSDIEITHL AKLDHISKIG AKLGLGEDDM ELYGKFKAKI EPRLDGSNSK LILVTATSPT PFGEGKTTMS IGLADALNRL VKKVCLALRE PSLGPVFGIK GGAAGGGYSQ LAPMEDLNLH FTGDFHAITS ANNLISAMID NSLYQENPLN IDKILWKRCM DMNDRALRFI TVGQGGKADG VEREDGFNIT AASEIMAILC LATSLADLKE RIANIMVAYN DRGEPIYVRD LGCEDAVCIL LKDAMKPNLF QTIEHTPTLV HGGPFANIAH GCNSIIATKT ALNLADFVIT EAGFGSELGA EKFIDIKCRV AGIAPDAVVL VSTIRSLKYN GGADKESITK PNMSALEVGI ANLGGHIENL KQKFGLNVVV ALNKFGFDED SEIDFVRDYC AKFGVKMAVC ENFVKGGEGA LELANFVLEE LKKPNDMKFA YETSDDTKSK ITKIATEIYG AGEVVFEEAA QKALEKIKKL GLEKLPVCIA KTQYSFSDDA KLLGRAKGFK FSVKDLQIRT GAGFIVAVCG KIMLMPGLPK TPSALNMHID TKTGEISGLA //