FTHS_LIMF3
ID FTHS_LIMF3 Reviewed; 553 AA.
AC B2GF64;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=LAF_0117;
OS Limosilactobacillus fermentum (strain NBRC 3956 / LMG 18251) (Lactobacillus
OS fermentum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=334390;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 3956 / LMG 18251;
RX PubMed=18487258; DOI=10.1093/dnares/dsn009;
RA Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T.,
RA Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T.,
RA Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T.,
RA Hattori M.;
RT "Comparative genome analysis of Lactobacillus reuteri and Lactobacillus
RT fermentum reveal a genomic island for reuterin and cobalamin production.";
RL DNA Res. 15:151-161(2008).
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; AP008937; BAG26453.1; -; Genomic_DNA.
DR RefSeq; WP_012390743.1; NC_010610.1.
DR AlphaFoldDB; B2GF64; -.
DR SMR; B2GF64; -.
DR EnsemblBacteria; BAG26453; BAG26453; LAF_0117.
DR GeneID; 61201210; -.
DR KEGG; lfe:LAF_0117; -.
DR PATRIC; fig|334390.5.peg.122; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001697; 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..553
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_1000196811"
FT BINDING 63..70
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 553 AA; 59287 MW; 8BED7428F0A9E7AA CRC64;
MLTDIEIADQ AQLTPINEIA AQLGLDEDAI EQYGKYKAKI NLPVQATPEK KHKLVLVTSI
NPTPAGEGKS TVLVGLGDAL SLLHHQTVIA MREPSMGPVF GMKGGATGGG YSQVVPMEDI
NLHFTGDFHA LTSANNTLAA LIDNYLMRGN ELGLDPRRVI WKRVEDVNDR ALRDVVTGLG
GIMQGVPRQT GFDITPASEL MAILCLATDL SDLKARVSRI VVGYTYDKEP VTVGQLGFEE
AVTILLKDAI KPNLVQTLGH TPAIVHGGPF ANIAHGCNSV LATKTALQLA DYTVTEAGFG
ADLGAEKFLD IKRPVLGKTP DAVVIVATVR ALEYNGGASL QALKDENLTE LENGLQNLNR
HIANMQRYGL PLVVAINHFA TDTPAEIKLI EDNCKARGVN VVVADAWAKG GAGTLDLAKE
VVALAEQEAS FTPLYDYQAT PKEKVETIAT KVYGAGRVAF SKKALNQLKQ FEKLGWNDLP
ICIAKTQYSF TDDQTQLGAP EGFTFHIREF VPKLGAGFIV ALAGNMLTMP GLPKVPAAVK
MTIDSEGKIT GLF