EX1_BUCBP
ID EX1_BUCBP Reviewed; 481 AA.
AC Q89A43;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Exodeoxyribonuclease I;
DE Short=ExoI;
DE Short=Exonuclease I;
DE EC=3.1.11.1 {ECO:0000250|UniProtKB:P04995};
DE AltName: Full=DNA deoxyribophosphodiesterase;
DE Short=dRPase;
GN Name=sbcB; OrderedLocusNames=bbp_503;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
CC -!- FUNCTION: Degrades single-stranded DNA (ssDNA) in a highly processive
CC manner. Also functions as a DNA deoxyribophosphodiesterase that
CC releases deoxyribose-phosphate moieties following the cleavage of DNA
CC at an apurinic/apyrimidinic (AP) site by either an AP endonuclease or
CC AP lyase. {ECO:0000250|UniProtKB:P04995}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.11.1;
CC Evidence={ECO:0000250|UniProtKB:P04995};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P04995};
CC Note=Binds 2 Mg(2+) ions per monomer. {ECO:0000250|UniProtKB:P04995};
CC -!- SUBUNIT: Monomer. Interacts with ssb (via C-terminus); this interaction
CC stimulates the exonuclease activity by recruiting the enzyme to its
CC substrate. {ECO:0000250|UniProtKB:P04995}.
CC -!- DOMAIN: The N-terminal exonuclease domain and the exonuclease C-
CC terminal domain form a central positively charged groove which binds
CC the DNA. {ECO:0000250|UniProtKB:P04995}.
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DR EMBL; AE016826; AAO27208.1; -; Genomic_DNA.
DR AlphaFoldDB; Q89A43; -.
DR SMR; Q89A43; -.
DR STRING; 224915.bbp_503; -.
DR EnsemblBacteria; AAO27208; AAO27208; bbp_503.
DR KEGG; bab:bbp_503; -.
DR eggNOG; COG2925; Bacteria.
DR HOGENOM; CLU_043508_1_1_6; -.
DR OMA; FIYVNRC; -.
DR Proteomes; UP000000601; Chromosome.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:InterPro.
DR GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; ISS:UniProtKB.
DR GO; GO:0008852; F:exodeoxyribonuclease I activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0008310; F:single-stranded DNA 3'-5' exodeoxyribonuclease activity; ISS:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0000738; P:DNA catabolic process, exonucleolytic; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1520.20; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR023607; Exodeoxyribonuclease_I.
DR InterPro; IPR034748; EXOI_C.
DR InterPro; IPR034747; EXOI_SH3.
DR InterPro; IPR038649; EXOI_SH3_sf.
DR InterPro; IPR013620; Exonuc_1_C.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR022894; Oligoribonuclease.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR11046; PTHR11046; 1.
DR Pfam; PF08411; Exonuc_X-T_C; 1.
DR Pfam; PF00929; RNase_T; 1.
DR PIRSF; PIRSF000977; Exodeoxyribonuclease_I; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS51785; EXOI_C; 1.
DR PROSITE; PS51784; EXOI_SH3; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; DNA-binding; Exonuclease; Hydrolase; Magnesium;
KW Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..481
FT /note="Exodeoxyribonuclease I"
FT /id="PRO_0000087109"
FT DOMAIN 12..193
FT /note="Exonuclease"
FT /evidence="ECO:0000255"
FT DOMAIN 202..350
FT /note="ExoI SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01120"
FT DOMAIN 356..471
FT /note="ExoI C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01121"
FT BINDING 15
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT BINDING 17
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT BINDING 17
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT BINDING 186
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 113
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 124
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 128
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 142
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 148
FT /note="Important for interaction with ssb"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 181
FT /note="Important for activity"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 214
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 257
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 299
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 365
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 368
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
SQ SEQUENCE 481 AA; 57404 MW; F83819117CA68E34 CRC64;
MDIQKNTSLT FLFYDYETFG KNPALDKPSQ FSCIQTDIDF NIIGSIQEIF CYPSVDYLPD
PESVLITGIS PKYTSLFGVN EFEFAKKIYS LFMKSDTCII GYNNIYFDDE FTRNIFYRNF
LNSYEWSWKN GNSRWDMLDL LRACYVLRPE GINWPRNEDN SVSLRLSDIS LANNIVHNVA
HNASSDVYAT MNIAKLIKQK KPKLFNFFFK YRTKKAILTL IDVNSLNPIV YISRFFGVVN
RYISYIVPIL WHPINSNILV SIDLSQDVQK ILNFFKRNSI LNVNYKEIFL MGIRFIYVNR
CPILIPTNVI RMKDRIRLRI NYKLFQNNLV LLRKNIFLKK KLKKFLCSIA EAPKYNGSNV
DLKMYNSFFS YIDNNVIKNI HSTLPKRIKI NFMKYDNRIN QLFILFLARY RPDMLDYSEK
YFWIQRYLNI FSYANIQKYE NKILKLIVKY KNHVRNVQLL EELFEYVKYT RKNFLKSIFT
N
