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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
 
 
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