ID FTHS_ALLAM Reviewed; 555 AA. AC B9JZN5; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 65. 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=Avi_3272; OS Allorhizobium ampelinum (strain ATCC BAA-846 / DSM 112012 / S4) OS (Agrobacterium vitis (strain S4)). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Allorhizobium; OC Allorhizobium ampelinum. OX NCBI_TaxID=311402; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-846 / DSM 112012 / S4; RX PubMed=19251847; DOI=10.1128/jb.01779-08; RA Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K., RA Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., Otten L., RA Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., Du Z., Ewing A., RA Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., Miller N.M., RA Norton S., Chen Q., Phoolcharoen W., Ohlin V., Ondrusek D., Pride N., RA Stricklin S.L., Sun J., Wheeler C., Wilson L., Zhu H., Wood D.W.; RT "Genome sequences of three Agrobacterium biovars help elucidate the RT evolution of multichromosome genomes in bacteria."; RL J. Bacteriol. 191:2501-2511(2009). 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; CP000633; ACM37345.1; -; Genomic_DNA. DR RefSeq; WP_015916764.1; NC_011989.1. DR AlphaFoldDB; B9JZN5; -. DR SMR; B9JZN5; -. DR STRING; 311402.Avi_3272; -. DR KEGG; avi:Avi_3272; -. DR eggNOG; COG2759; Bacteria. DR HOGENOM; CLU_003601_3_3_5; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000001596; Chromosome 1. 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..555 FT /note="Formate--tetrahydrofolate ligase" FT /id="PRO_1000185242" FT BINDING 64..71 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543" SQ SEQUENCE 555 AA; 59093 MW; D56E7BD0AA301A7C CRC64; MSDIEIARAA SKLAITQIGE RLGISPGDLQ PYGHDKAKIS ASFLHSLEDR KDGKLILVTA INPTPAGEGK TTTTVGLVDG LNRIGAKAMV CVREPSLGPC FGVKGGAAGG GRAQVVPMED INLHFTGDFH AITSAHNLLA AMIDNHIYWG NEQDLDTRRI AWRRVVDMND RALREMVGAL GGVRNGFPRE TGFDITVASE VMAILCLARD LADLEERLGQ IVIGYRRDKT PVHARDIKAH QAMTVLLKEA MQPNLVQTLE NNPALVHGGP FANIAHGCNS VVATRAALKL ADYVVTEAGF GADLGAEKFF DIKCRKAGLR PAAAVIVATV RALKMNGGVA KTELGHEDVA ALVRGAVNLG RHVENVRGFG VPVIVAINHF LSDTPAEIAA LQDYAASIGV EAVLCRHWAE GGAGIEELAR KVAAMADSGI ADFQPLYPDD MPLFAKIETV AKRIYRAGSV TADRAVIDQL SQFEAMGYGD LPVCIAKTQY SFSTDPSLLG APDGHEVHVR DVRLSAGAGF VVAITGDIMT MPGLPRKPAA ETIRLDDDGL VEGLF //