ID Q28VF0_JANSC Unreviewed; 345 AA.
AC Q28VF0;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 04-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Adenine DNA glycosylase {ECO:0000256|ARBA:ARBA00022023, ECO:0000256|RuleBase:RU365096};
DE EC=3.2.2.31 {ECO:0000256|ARBA:ARBA00012045, ECO:0000256|RuleBase:RU365096};
GN OrderedLocusNames=Jann_0395 {ECO:0000313|EMBL:ABD53312.1};
OS Jannaschia sp. (strain CCS1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=290400 {ECO:0000313|EMBL:ABD53312.1, ECO:0000313|Proteomes:UP000008326};
RN [1] {ECO:0000313|Proteomes:UP000008326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCS1 {ECO:0000313|Proteomes:UP000008326};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W.,
RA Buchan A., Gonzalez J.M., Schell M.A., Richardson P.;
RT "Complete sequence of chromosome of Jannaschia sp. CCS1.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABD53312.1, ECO:0000313|Proteomes:UP000008326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCS1 {ECO:0000313|EMBL:ABD53312.1,
RC ECO:0000313|Proteomes:UP000008326};
RX PubMed=17526795; DOI=10.1128/AEM.02580-06;
RA Moran M.A., Belas R., Schell M.A., Gonzalez J.M., Sun F., Sun S.,
RA Binder B.J., Edmonds J., Ye W., Orcutt B., Howard E.C., Meile C.,
RA Palefsky W., Goesmann A., Ren Q., Paulsen I., Ulrich L.E., Thompson L.S.,
RA Saunders E., Buchan A.;
RT "Ecological genomics of marine Roseobacters.";
RL Appl. Environ. Microbiol. 73:4559-4569(2007).
CC -!- FUNCTION: Adenine glycosylase active on G-A mispairs. MutY also
CC corrects error-prone DNA synthesis past GO lesions which are due to the
CC oxidatively damaged form of guanine: 7,8-dihydro-8-oxoguanine (8-oxo-
CC dGTP). {ECO:0000256|ARBA:ARBA00002933}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes free adenine bases from 7,8-dihydro-8-
CC oxoguanine:adenine mismatched double-stranded DNA, leaving an
CC apurinic site.; EC=3.2.2.31; Evidence={ECO:0000256|ARBA:ARBA00000843,
CC ECO:0000256|RuleBase:RU365096};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|RuleBase:RU365096};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|RuleBase:RU365096};
CC -!- SIMILARITY: Belongs to the Nth/MutY family.
CC {ECO:0000256|ARBA:ARBA00008343, ECO:0000256|RuleBase:RU365096}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000264; ABD53312.1; -; Genomic_DNA.
DR AlphaFoldDB; Q28VF0; -.
DR STRING; 290400.Jann_0395; -.
DR KEGG; jan:Jann_0395; -.
DR eggNOG; COG1194; Bacteria.
DR HOGENOM; CLU_012862_0_2_5; -.
DR OrthoDB; 9802365at2; -.
DR Proteomes; UP000008326; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000701; F:purine-specific mismatch base pair DNA N-glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006284; P:base-excision repair; IEA:UniProtKB-UniRule.
DR CDD; cd03431; DNA_Glycosylase_C; 1.
DR CDD; cd00056; ENDO3c; 1.
DR Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR005760; A/G_AdeGlyc_MutY.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR004036; Endonuclease-III-like_CS2.
DR InterPro; IPR003651; Endonuclease3_FeS-loop_motif.
DR InterPro; IPR004035; Endouclease-III_FeS-bd_BS.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR InterPro; IPR000445; HhH_motif.
DR InterPro; IPR044298; MIG/MutY.
DR InterPro; IPR029119; MutY_C.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR NCBIfam; TIGR01084; mutY; 1.
DR PANTHER; PTHR42944; ADENINE DNA GLYCOSYLASE; 1.
DR PANTHER; PTHR42944:SF1; ADENINE DNA GLYCOSYLASE; 1.
DR Pfam; PF10576; EndIII_4Fe-2S; 1.
DR Pfam; PF00633; HHH; 1.
DR Pfam; PF00730; HhH-GPD; 1.
DR Pfam; PF14815; NUDIX_4; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SUPFAM; SSF48150; DNA-glycosylase; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS00764; ENDONUCLEASE_III_1; 1.
DR PROSITE; PS01155; ENDONUCLEASE_III_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU365096};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU365096};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABD53312.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU365096};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008326}.
FT DOMAIN 35..184
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
SQ SEQUENCE 345 AA; 37761 MW; 0B865453F66BB877 CRC64;
MLDWYDVHAR DLPWRVPPLS GLDADPYRVW LSEIMLQQTT VAAVKAYFQR FTALWPTVGD
LAAAEDAAVM GEWAGLGYYA RARNLLKCAR VVVEEHGGQF PRTEAELLEL PGIGPYTAAA
VASIAFQQPA PVMDGNIERV MARLFAVEDP LPGCKSVLKE HATRLTPNDR PGDHAQALMD
LGATICTPKN PACGICPVME ACTAHKRGIA ADLPKKAPKK AKPTRLGYVY VARQEDGSVL
LETREEKGLL GGMLAFPTSD WSEAPTDVPP FAADWHDPGL EVRHTFTHFH LRLALRVTNA
ASDTSPQRGE FLPRALFKPS SLPTLMRKAH DLSVGHFTGD DHDLG
//
