FTHS_STRPJ
ID FTHS_STRPJ Reviewed; 556 AA.
AC B8ZJQ0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, 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}; OrderedLocusNames=SPN23F11250;
OS Streptococcus pneumoniae (strain ATCC 700669 / Spain 23F-1).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=561276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700669 / Spain 23F-1;
RX PubMed=19114491; DOI=10.1128/jb.01343-08;
RA Croucher N.J., Walker D., Romero P., Lennard N., Paterson G.K., Bason N.C.,
RA Mitchell A.M., Quail M.A., Andrew P.W., Parkhill J., Bentley S.D.,
RA Mitchell T.J.;
RT "Role of conjugative elements in the evolution of the multidrug-resistant
RT pandemic clone Streptococcus pneumoniae Spain23F ST81.";
RL J. Bacteriol. 191:1480-1489(2009).
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; FM211187; CAR68934.1; -; Genomic_DNA.
DR RefSeq; WP_000845292.1; NC_011900.1.
DR AlphaFoldDB; B8ZJQ0; -.
DR SMR; B8ZJQ0; -.
DR GeneID; 60232711; -.
DR KEGG; sne:SPN23F11250; -.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; CGEIMTM; -.
DR UniPathway; UPA00193; -.
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..556
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_1000185266"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 556 AA; 59630 MW; 025035A325CF97FF CRC64;
MKTDIEIAQS IELKPIVDVV EKLGISYDDL ELYGKYKAKL SFDKIRAVES NPVGKLILVT
AINPTPAGEG KSTLTIGLAD ALNKIGKKTM IAIREPSLGP VMGIKGGAAG GGYAQVLPME
DINLHFTGDM HAITTANNAL SALIDNHLHQ GNELGIDQRR ILWKRVVDLN DRALRHVTVG
LGGPLNGIPR EDGFDITVAS EIMAILCLAT DIEDLKRRLA NIVIGYRYDR TPVSVGDLQV
EGALALILKD AIKPNLVQTI YGTPAFVHGG PFANIAHGCN SVLATTTALH LADYTVTEAG
FGADLGAEKF LDIKTPNLPT SPDAVVIVAT LRALKMNGGV AKDALTEENV EAVRAGFANL
KRHVENIRKF GIPAVVAINE FVSDTEAEIA VLKELCASID VPVELASVWA DGAEGGVALA
ETVVKTIAEN PANYKRLYDN DLSVQEKIEK IVTEIYRGSK VNFEKKSQTQ IAQIVQNGWD
KLPICMAKTQ YSFSDNPNAL GAPENFEITI RELVPKLGAG FIVALTGDVM TMPGLPKRPA
ALNMDVESDG TVLGLF