NFI_ECOLI
ID NFI_ECOLI Reviewed; 223 AA.
AC P68739; P32679; Q2M8T5;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Endonuclease V {ECO:0000255|HAMAP-Rule:MF_00801};
DE Short=EndoV;
DE EC=3.1.21.7 {ECO:0000255|HAMAP-Rule:MF_00801};
DE AltName: Full=Deoxyinosine 3'endonuclease {ECO:0000255|HAMAP-Rule:MF_00801};
DE AltName: Full=Deoxyribonuclease V {ECO:0000255|HAMAP-Rule:MF_00801};
DE Short=DNase V {ECO:0000255|HAMAP-Rule:MF_00801};
GN Name=nfi {ECO:0000255|HAMAP-Rule:MF_00801}; Synonyms=yjaF;
GN OrderedLocusNames=b3998, JW5547;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PROTEIN SEQUENCE OF 1-11, AND IDENTIFICATION.
RX PubMed=8990280; DOI=10.1128/jb.179.2.310-316.1997;
RA Guo G., Ding Y., Weiss B.;
RT "nfi, the gene for endonuclease V in Escherichia coli K-12.";
RL J. Bacteriol. 179:310-316(1997).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=6246346; DOI=10.1016/s0076-6879(80)65031-9;
RA Demple B., Gates F.T., Linn S.;
RT "Purification and properties of Escherichia coli endodeoxyribonuclease V.";
RL Methods Enzymol. 65:224-231(1980).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RX PubMed=8206931; DOI=10.1016/s0021-9258(17)34002-4;
RA Yao M., Hatahet Z., Melamede R.J., Kow Y.W.;
RT "Purification and characterization of a novel deoxyinosine-specific enzyme,
RT deoxyinosine 3' endonuclease, from Escherichia coli.";
RL J. Biol. Chem. 269:16260-16268(1994).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9388217; DOI=10.1074/jbc.272.49.30774;
RA Yao M., Kow Y.W.;
RT "Further characterization of Escherichia coli endonuclease V. Mechanism of
RT recognition for deoxyinosine, deoxyuridine, and base mismatches in DNA.";
RL J. Biol. Chem. 272:30774-30779(1997).
RN [8]
RP FUNCTION.
RX PubMed=11104906; DOI=10.1016/s0921-8777(00)00062-8;
RA Weiss B.;
RT "Endonuclease V of Escherichia coli prevents mutations from nitrosative
RT deamination during nitrate/nitrite respiration.";
RL Mutat. Res. 461:301-309(2001).
RN [9]
RP FUNCTION IN CLEAVAGE OF RNA, AND MUTAGENESIS OF ASP-35.
RX PubMed=23912683; DOI=10.1038/ncomms3271;
RA Sebastian Vik E., Sameen Nawaz M., Strom Andersen P., Fladeby C.,
RA Bjoras M., Dalhus B., Alseth I.;
RT "Endonuclease V cleaves at inosines in RNA.";
RL Nat. Commun. 4:2271-2271(2013).
CC -!- FUNCTION: DNA repair enzyme involved in the repair of deaminated bases.
CC Selectively cleaves double-stranded DNA at the second phosphodiester
CC bond 3' to a deoxyinosine leaving behind the intact lesion on the
CC nicked DNA. Has a wide substrate spectrum. In addition to deoxyinosine-
CC containing DNA, the enzyme cleaves DNA containing urea residues, AP
CC sites, base mismatches, insertion/deletion mismatches, flaps, and
CC pseudo-Y structures. Participates in the excision repair of
CC hypoxanthine and xanthine (deaminated adenine and guanine) in DNA. It
CC thereby reduces the mutagenic effects of nitrous acid by attacking
CC lesions caused by nitrosative deamination. Also active on inosines in
CC single- and double-stranded RNA. May cleave tRNA(Arg2), which contains
CC inosine at the wobble position. {ECO:0000255|HAMAP-Rule:MF_00801,
CC ECO:0000269|PubMed:11104906, ECO:0000269|PubMed:23912683,
CC ECO:0000269|PubMed:6246346, ECO:0000269|PubMed:8206931,
CC ECO:0000269|PubMed:9388217}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage at apurinic or apyrimidinic sites to
CC products with a 5'-phosphate.; EC=3.1.21.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00801,
CC ECO:0000269|PubMed:6246346, ECO:0000269|PubMed:8206931,
CC ECO:0000269|PubMed:9388217};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00801,
CC ECO:0000269|PubMed:8206931, ECO:0000269|PubMed:9388217};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0-7.5. {ECO:0000269|PubMed:8206931,
CC ECO:0000269|PubMed:9388217};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8206931}.
CC -!- INTERACTION:
CC P68739; P00914: phrB; NbExp=2; IntAct=EBI-551698, EBI-555781;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the endonuclease V family. {ECO:0000255|HAMAP-
CC Rule:MF_00801}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC43096.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U00006; AAC43096.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76972.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77321.1; -; Genomic_DNA.
DR PIR; A65207; A65207.
DR RefSeq; NP_418426.2; NC_000913.3.
DR RefSeq; WP_000362388.1; NZ_STEB01000045.1.
DR PDB; 4XPU; X-ray; 2.40 A; A/B=1-214.
DR PDBsum; 4XPU; -.
DR AlphaFoldDB; P68739; -.
DR SMR; P68739; -.
DR BioGRID; 4263468; 110.
DR BioGRID; 852796; 1.
DR DIP; DIP-47986N; -.
DR IntAct; P68739; 30.
DR STRING; 511145.b3998; -.
DR jPOST; P68739; -.
DR PaxDb; P68739; -.
DR PRIDE; P68739; -.
DR DNASU; 948502; -.
DR EnsemblBacteria; AAC76972; AAC76972; b3998.
DR EnsemblBacteria; BAE77321; BAE77321; BAE77321.
DR GeneID; 948502; -.
DR KEGG; ecj:JW5547; -.
DR KEGG; eco:b3998; -.
DR PATRIC; fig|1411691.4.peg.2713; -.
DR EchoBASE; EB1859; -.
DR eggNOG; COG1515; Bacteria.
DR HOGENOM; CLU_047631_1_0_6; -.
DR InParanoid; P68739; -.
DR OMA; RIHFRQA; -.
DR PhylomeDB; P68739; -.
DR BioCyc; EcoCyc:EG11915-MON; -.
DR BioCyc; MetaCyc:EG11915-MON; -.
DR BRENDA; 3.1.21.7; 2026.
DR PRO; PR:P68739; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043737; F:deoxyribonuclease V activity; IDA:EcoCyc.
DR GO; GO:0016891; F:endoribonuclease activity, producing 5'-phosphomonoesters; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IDA:EcoCyc.
DR CDD; cd06559; Endonuclease_V; 1.
DR HAMAP; MF_00801; Endonuclease_5; 1.
DR InterPro; IPR007581; Endonuclease-V.
DR PANTHER; PTHR28511; PTHR28511; 1.
DR Pfam; PF04493; Endonuclease_5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; DNA damage; DNA repair;
KW Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome.
FT CHAIN 1..223
FT /note="Endonuclease V"
FT /id="PRO_0000159660"
FT BINDING 35
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
FT SITE 73
FT /note="Interaction with target DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
FT MUTAGEN 35
FT /note="D->A: Lack of activity on RNA."
FT /evidence="ECO:0000269|PubMed:23912683"
SQ SEQUENCE 223 AA; 24673 MW; A876DEED5EB848E4 CRC64;
MDLASLRAQQ IELASSVIRE DRLDKDPPDL IAGADVGFEQ GGEVTRAAMV LLKYPSLELV
EYKVARIATT MPYIPGFLSF REYPALLAAW EMLSQKPDLV FVDGHGISHP RRLGVASHFG
LLVDVPTIGV AKKRLCGKFE PLSSEPGALA PLMDKGEQLA WVWRSKARCN PLFIATGHRV
SVDSALAWVQ RCMKGYRLPE PTRWADAVAS ERPAFVRYTA NQP
