FTHS_STRP2
ID FTHS_STRP2 Reviewed; 556 AA.
AC Q04K90;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=SPD_1087;
OS Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=373153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D39 / NCTC 7466;
RX PubMed=17041037; DOI=10.1128/jb.01148-06;
RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT pneumoniae and comparison with that of unencapsulated laboratory strain
RT R6.";
RL J. Bacteriol. 189:38-51(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; CP000410; ABJ55341.1; -; Genomic_DNA.
DR RefSeq; WP_000845292.1; NC_008533.2.
DR AlphaFoldDB; Q04K90; -.
DR SMR; Q04K90; -.
DR STRING; 373153.SPD_1087; -.
DR EnsemblBacteria; ABJ55341; ABJ55341; SPD_1087.
DR GeneID; 60232711; -.
DR KEGG; spd:SPD_1087; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR BioCyc; SPNE373153:G1G6V-1178-MON; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001452; 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..556
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000300547"
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