ID FTHS_ALIFM Reviewed; 582 AA. AC B5FG96; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 14-OCT-2008, sequence version 1. DT 27-MAR-2024, entry version 70. 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=VFMJ11_1925; OS Aliivibrio fischeri (strain MJ11) (Vibrio fischeri). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Aliivibrio. OX NCBI_TaxID=388396; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MJ11; RA Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S., RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.; RT "Complete sequence of Vibrio fischeri strain MJ11."; RL Submitted (AUG-2008) 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; CP001139; ACH66842.1; -; Genomic_DNA. DR RefSeq; WP_012534022.1; NC_011184.1. DR AlphaFoldDB; B5FG96; -. DR SMR; B5FG96; -. DR GeneID; 77253063; -. DR KEGG; vfm:VFMJ11_1925; -. DR HOGENOM; CLU_003601_3_3_6; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000001857; Chromosome I. 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..582 FT /note="Formate--tetrahydrofolate ligase" FT /id="PRO_1000146710" FT BINDING 65..72 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543" SQ SEQUENCE 582 AA; 62374 MW; C11574C527FCBFEB CRC64; MKSDIEICQT ATLTRMKTIA SNLGLHDDDI TPQGPFKAKV NIDALKRLKS EPNGKLILVS AITPTPLGEG KTVTTIGLAQ GLAKLGESVS ACIRQPSMGP VFGVKGGAAG GGYSQVAPME ELNLHLTGDI HAITAAHNLA SAAIDARIYH EQRLGYDVFS EKNQLPALRI DPQRVVWKRV MDHNDRALRM VTIGKNEDGK TINGYEREDG FDITAASELM AILALATDLQ DLRQRIGRIV VAYNLDGEPV TTEDLQVAGA MTVTMKFAIN PTLMQTLEGV PTFVHSGPFA NIAHGNSSII ADNIALKLTD YTVTEGGFGS DMGFEKACNI KAPLSEKSPD CAVLVATLRG IKANSGLFPL SPGQSLPKEL FAPNKEALDA GLDNLLWHIN NCAKYGLPVV VAINRFPEDT QEELDSLLNW VSNLDINVDV AISEAFVKGG NGTLELAEKV IKACQQETQF TPLYTSEMSL FDKLNAVAIK GYGAERIELS EKAQQQLATF EKLGYQSLSV CMAKTPASIS TDGNIKGAPT DFVVPIRELK LCAGAGFIYA LCGNVMTMPG LPEKPAFMNL DIDGDGNIVG LS //