ID FTHS_SHELP Reviewed; 564 AA. AC A3QA17; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 17-APR-2007, sequence version 1. DT 27-MAR-2024, entry version 97. 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=Shew_0443; OS Shewanella loihica (strain ATCC BAA-1088 / PV-4). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=323850; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1088 / PV-4; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G., RA Fredrickson J., Tiedje J., Richardson P.; RT "Complete sequence of Shewanella loihica PV-4."; RL Submitted (MAR-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; CP000606; ABO22315.1; -; Genomic_DNA. DR RefSeq; WP_011864249.1; NC_009092.1. DR AlphaFoldDB; A3QA17; -. DR SMR; A3QA17; -. DR STRING; 323850.Shew_0443; -. DR KEGG; slo:Shew_0443; -. DR eggNOG; COG2759; Bacteria. DR HOGENOM; CLU_003601_3_3_6; -. DR OrthoDB; 9761733at2; -. DR UniPathway; UPA00193; -. DR Proteomes; UP000001558; 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. PE 3: Inferred from homology; KW ATP-binding; Ligase; Nucleotide-binding; One-carbon metabolism; KW Reference proteome. FT CHAIN 1..564 FT /note="Formate--tetrahydrofolate ligase" FT /id="PRO_0000300537" FT BINDING 65..72 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543" SQ SEQUENCE 564 AA; 59785 MW; 4D1C5024D1BF473A CRC64; MLTDIEISRQ ASLQPIESIA TAFGILPHEL SPYGRTKAKV DLAITNRIKD NKHGKLVIVT AVTPTPFGEG KTVTSIGLTQ GLQAIGKKSC ACIRQPSMGP VFGIKGGAAG GGLAQVVPME DLNLHLTGDI HAVTSAHNLA AAAIDARLYH EQRLGCEAFR EQSGLAPLDI DPEKILWRRV VDQNERSLRT ITVGLGEVNG PVHQGGFDIS AASELMAILA LSRDLKDLRA RIGRIVLAQN KQGDYISAED LGVAGAMTAI MSQAISPTLM QTLSGAPCLI HAGPFANIAH GNSSIIADDI ALRLADIVVT EGGFGSDMGF EKFCNIKTRQ SGNAPDAAVL VVTVKALKSH NPDAGSEMDK LAAGYANLSW HISNVAKYGL PLVVAINRFA EDTQEELEWL KARVLQEGVF ACEVCEAFTQ GAEGAMALAR AVVRATEQPS QFRYLYETKQ SIEAKLLTIA EAGYGANGIS LSDTAKAQLA QLQRQGFDKL ALCIAKTPMS VSHDPKLKGA PQGFELPIAE LKLNAGAGFI TALVGKVMTM PGLGIRPGYL NIDIDERGEI TGLA //