ID B2UR57_AKKM8 Unreviewed; 305 AA.
AC B2UR57;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Type-4 uracil-DNA glycosylase {ECO:0000256|ARBA:ARBA00019403};
DE EC=3.2.2.27 {ECO:0000256|ARBA:ARBA00012030};
GN OrderedLocusNames=Amuc_1116 {ECO:0000313|EMBL:ACD04942.1};
OS Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC
OS 81048 / CCUG 64013 / CIP 107961 / Muc).
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC Akkermansiaceae; Akkermansia.
OX NCBI_TaxID=349741 {ECO:0000313|EMBL:ACD04942.1, ECO:0000313|Proteomes:UP000001031};
RN [1] {ECO:0000313|Proteomes:UP000001031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013
RC / CIP 107961 / Muc {ECO:0000313|Proteomes:UP000001031};
RX PubMed=21390229; DOI=10.1371/journal.pone.0016876;
RA van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M.,
RA Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.;
RT "The genome of Akkermansia muciniphila, a dedicated intestinal mucin
RT degrader, and its use in exploring intestinal metagenomes.";
RL PLoS ONE 6:E16876-E16876(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes single-stranded DNA or mismatched double-stranded
CC DNA and polynucleotides, releasing free uracil.; EC=3.2.2.27;
CC Evidence={ECO:0000256|ARBA:ARBA00001400};
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC Type 4 (UDGa) family. {ECO:0000256|ARBA:ARBA00006521}.
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DR EMBL; CP001071; ACD04942.1; -; Genomic_DNA.
DR RefSeq; WP_012420157.1; NZ_CP071807.1.
DR AlphaFoldDB; B2UR57; -.
DR STRING; 349741.Amuc_1116; -.
DR PaxDb; 349741-Amuc_1116; -.
DR KEGG; amu:Amuc_1116; -.
DR eggNOG; COG1573; Bacteria.
DR HOGENOM; CLU_044815_1_0_0; -.
DR BioCyc; AMUC349741:G1GBX-1191-MONOMER; -.
DR Proteomes; UP000001031; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004844; F:uracil DNA N-glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd10030; UDG-F4_TTUDGA_SPO1dp_like; 1.
DR Gene3D; 3.40.470.10; Uracil-DNA glycosylase-like domain; 1.
DR InterPro; IPR005273; Ura-DNA_glyco_family4.
DR InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR NCBIfam; TIGR00758; UDG_fam4; 1.
DR PANTHER; PTHR33693:SF1; TYPE-4 URACIL-DNA GLYCOSYLASE; 1.
DR PANTHER; PTHR33693; TYPE-5 URACIL-DNA GLYCOSYLASE; 1.
DR Pfam; PF03167; UDG; 1.
DR SMART; SM00986; UDG; 1.
DR SMART; SM00987; UreE_C; 1.
DR SUPFAM; SSF52141; Uracil-DNA glycosylase-like; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001031}.
FT DOMAIN 129..283
FT /note="Uracil-DNA glycosylase-like"
FT /evidence="ECO:0000259|SMART:SM00986"
FT REGION 44..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 305 AA; 33844 MW; 46FB6FC5A7D708CD CRC64;
MSATPNSLFR HYLDSLIQQG TTRTSLTDEA RNVLRTWYVA SRQGGRPAAS APASPEPPPL
QAAAPASAPA SAPAGKPEPP ELFPQNREPA SAITLPEGTM EDKLQYLRNL AQNWKPAREL
NSLRDTMVFA TGNPHTKLML IGEAPGYYEE VQQEPFVGRA GEKLNQILRA MGLSRDMVYI
SNIVKFRPAL PNQRTNNRAP TPEEIEACLP IIMHEIRVIQ PKMIVALGGT AAVGLLGEQG
SVSSMRGRFH DLNGIPVRVT YHPSYLLRSD SPREKRKVWE DMLAVMERLD MPISEKQRGY
FLPRA
//