ID FTHS_DEHMC Reviewed; 597 AA. AC Q3ZX40; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2005, sequence version 1. DT 27-MAR-2024, entry version 95. 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=cbdbA660; OS Dehalococcoides mccartyi (strain CBDB1). OC Bacteria; Chloroflexota; Dehalococcoidia; Dehalococcoidales; OC Dehalococcoidaceae; Dehalococcoides. OX NCBI_TaxID=255470; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBDB1; RX PubMed=16116419; DOI=10.1038/nbt1131; RA Kube M., Beck A., Zinder S.H., Kuhl H., Reinhardt R., Adrian L.; RT "Genome sequence of the chlorinated compound-respiring bacterium RT Dehalococcoides species strain CBDB1."; RL Nat. Biotechnol. 23:1269-1273(2005). 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; AJ965256; CAI82827.1; -; Genomic_DNA. DR AlphaFoldDB; Q3ZX40; -. DR SMR; Q3ZX40; -. DR KEGG; deh:cbdbA660; -. DR HOGENOM; CLU_003601_3_3_0; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000000433; 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. FT CHAIN 1..597 FT /note="Formate--tetrahydrofolate ligase" FT /id="PRO_0000199345" FT BINDING 84..91 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543" SQ SEQUENCE 597 AA; 64493 MW; 775FDB2876B52CB5 CRC64; MAVNDREFHL KELDPVLMKD WEIAEKAEDF LKPVKVLAME LGLTEDEIIP HGKYIAKVDF AGVLARLKDR PNGKYIDVTA ITPTPLGEGK STTTMGLVQG LGKLGKKVTG AIRQPSSGPT FNIKGSAAGG GLSQCLPLSP FSLGLTGDID AVTNSHNLAM VALQARLQHE ANNTDEFLSS RHLTRLDIDP SRVEMKWAMD FCAQSLREII MGIGGKTDGY RMPSGFGISV SSEVMAILSV FTSLSDLRER MGKIIVAYRK NDEPVTTADL EVDGAMTALL LRAVNPNLLQ TIEGQPVFVH AGPFANIAIG QSSIVADRLA LKLADYHVTE SGFGADIGFE KFWNIKCRLS GLKPDCAVIV VTARALKMHG GGPKVTPGAP LDPAYTTPNT KLVEKGCQNM LAHIQTVKTA GINPVVCINH FAADTHEEID IIRRTAEQAE ARVAVSHHWA KGGDGATELA EAVTDACNEP NNFHFLYPEN MPLKKRIETI ARKVYGANGV SYTPIAMEKL ARIESMGDTQ FMPTCMVKTH LSLSHDPALK GRPSGFTLPI RDILTYMGAG LVVPVAGDIK LMPGTSSDPN FKRIDVDTQT GKVKGLF //