FTHS_BART1
ID FTHS_BART1 Reviewed; 557 AA.
AC A9IM41;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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}; OrderedLocusNames=BT_0147;
OS Bartonella tribocorum (strain CIP 105476 / IBS 506).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=382640;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 105476 / IBS 506;
RX PubMed=18037886; DOI=10.1038/ng.2007.38;
RA Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G.,
RA Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.;
RT "Genomic analysis of Bartonella identifies type IV secretion systems as
RT host adaptability factors.";
RL Nat. Genet. 39:1469-1476(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-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:57454, ChEBI:CHEBI:456216; EC=6.3.4.3;
CC 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}.
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DR EMBL; AM260525; CAK00634.1; -; Genomic_DNA.
DR RefSeq; WP_012230481.1; NC_010161.1.
DR AlphaFoldDB; A9IM41; -.
DR SMR; A9IM41; -.
DR STRING; 382640.BT_0147; -.
DR EnsemblBacteria; CAK00634; CAK00634; BT_0147.
DR KEGG; btr:BT_0147; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_5; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001592; 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; 3.40.50.300; -; 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; SSF52540; 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..557
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000333312"
FT BINDING 66..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 557 AA; 60207 MW; D3970AB1B11E2183 CRC64;
MHKTDIEIAH TAKKQHITEI AQKIGIAHEN LIPYGHDKAK ISSSYIKSLN NNPDGKLILV
TAINPTPAGE GKTTTTVGLS DALNLIGKKT IATLREPSLG PCFGVKGGAA GGGYAQVIPM
DDLNLHFTGD FHAITAAHNL LAAMIDNHIY WGNPLNIDPR RIVWKRVLDM NDRALRDIVI
SLGGITNGFP RQTGFDITVA SEIMALLCLS ENLENLTQRL KKIIVAYRHD KTPVTVADLN
AEGAMAVLLK DAIQPNLVQT IENNPVLVHG GPFANIAHGC NSVIATKTAL KLADYVVTEA
GFGADLGAEK FFNIKCRQTG IVPNATVIVA TIRALKMNGG VDKNNLTEEN ITALEKGAAN
LVRHIKNMAL YGIPCVVAIN HFDSDSDAEI RTLQKIVATT GHKALICKHW EQGGKGAVAL
AQELVTLIEK QDSDFKVLYQ DDIPLVQKIN CIITKLYGGR GAIISATILK QLESWEKEGF
GTYPICMAKT PYSFSADPKQ YGAPVDFEIP VREVRLCAGA GFIVVICGDV MTMPGLPHYP
AAEKIHLDEN DQIQGLS
