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Formamidopyrimidine-DNA glycosylase (Fapy-DNA glycosylase) (EC 3.2.2.23) (DNA-(apurinic or apyrimidinic site) lyase MutM) (AP lyase MutM) (EC 4.2.99.18)

 A0A1J0H0N9_VIRHA        Unreviewed;       275 AA.
A0A1J0H0N9;
15-FEB-2017, integrated into UniProtKB/TrEMBL.
15-FEB-2017, sequence version 1.
23-MAY-2018, entry version 11.
RecName: Full=Formamidopyrimidine-DNA glycosylase {ECO:0000256|HAMAP-Rule:MF_00103};
Short=Fapy-DNA glycosylase {ECO:0000256|HAMAP-Rule:MF_00103};
EC=3.2.2.23 {ECO:0000256|HAMAP-Rule:MF_00103};
AltName: Full=DNA-(apurinic or apyrimidinic site) lyase MutM {ECO:0000256|HAMAP-Rule:MF_00103};
Short=AP lyase MutM {ECO:0000256|HAMAP-Rule:MF_00103};
EC=4.2.99.18 {ECO:0000256|HAMAP-Rule:MF_00103};
Name=mutM {ECO:0000256|HAMAP-Rule:MF_00103};
Synonyms=fpg {ECO:0000256|HAMAP-Rule:MF_00103};
ORFNames=BME96_07650 {ECO:0000313|EMBL:APC48055.1};
Virgibacillus halodenitrificans (Bacillus halodenitrificans).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
NCBI_TaxID=1482 {ECO:0000313|EMBL:APC48055.1, ECO:0000313|Proteomes:UP000182945};
[1] {ECO:0000313|EMBL:APC48055.1, ECO:0000313|Proteomes:UP000182945}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=PDB-F2 {ECO:0000313|EMBL:APC48055.1,
ECO:0000313|Proteomes:UP000182945};
Sun Z., Zhou Y., Li H.;
"Complete genome sequencing of Virgibacillus halodenitrificans PDB-
F2.";
Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Involved in base excision repair of DNA damaged by
oxidation or by mutagenic agents. Acts as DNA glycosylase that
recognizes and removes damaged bases. Has a preference for
oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has
AP (apurinic/apyrimidinic) lyase activity and introduces nicks in
the DNA strand. Cleaves the DNA backbone by beta-delta elimination
to generate a single-strand break at the site of the removed base
with both 3'- and 5'-phosphates. {ECO:0000256|HAMAP-Rule:MF_00103,
ECO:0000256|SAAS:SAAS00635477}.
-!- CATALYTIC ACTIVITY: Hydrolysis of DNA containing ring-opened 7-
methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-
methyl)formamidopyrimidine. {ECO:0000256|HAMAP-Rule:MF_00103,
ECO:0000256|SAAS:SAAS00635490}.
-!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
apyrimidinic site in DNA is broken by a beta-elimination reaction,
leaving a 3'-terminal unsaturated sugar and a product with a
terminal 5'-phosphate. {ECO:0000256|HAMAP-Rule:MF_00103,
ECO:0000256|SAAS:SAAS00909191}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000256|HAMAP-Rule:MF_00103};
Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
Rule:MF_00103};
-!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00103,
ECO:0000256|SAAS:SAAS00635466}.
-!- SIMILARITY: Belongs to the FPG family. {ECO:0000256|HAMAP-
Rule:MF_00103, ECO:0000256|SAAS:SAAS00643420}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00103}.
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EMBL; CP017962; APC48055.1; -; Genomic_DNA.
RefSeq; WP_071648806.1; NZ_CP017962.1.
KEGG; vhl:BME96_07650; -.
KO; K10563; -.
Proteomes; UP000182945; Chromosome.
GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
GO; GO:0006284; P:base-excision repair; IEA:InterPro.
GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
Gene3D; 3.20.190.10; -; 1.
HAMAP; MF_00103; Fapy_DNA_glycosyl; 1.
InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
InterPro; IPR015887; DNA_glyclase_Znf_dom_DNA_BS.
InterPro; IPR020629; Formamido-pyr_DNA_Glyclase.
InterPro; IPR012319; FPG_cat.
InterPro; IPR035937; MutM-like_N-ter.
InterPro; IPR010979; Ribosomal_S13-like_H2TH.
InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
InterPro; IPR010663; Znf_FPG/IleRS.
Pfam; PF01149; Fapy_DNA_glyco; 1.
Pfam; PF06831; H2TH; 1.
Pfam; PF06827; zf-FPG_IleRS; 1.
SMART; SM00898; Fapy_DNA_glyco; 1.
SMART; SM01232; H2TH; 1.
SUPFAM; SSF46946; SSF46946; 1.
SUPFAM; SSF81624; SSF81624; 1.
TIGRFAMs; TIGR00577; fpg; 1.
PROSITE; PS51068; FPG_CAT; 1.
PROSITE; PS01242; ZF_FPG_1; 1.
PROSITE; PS51066; ZF_FPG_2; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000182945};
DNA damage {ECO:0000256|HAMAP-Rule:MF_00103,
ECO:0000256|SAAS:SAAS00909150};
DNA repair {ECO:0000256|HAMAP-Rule:MF_00103,
ECO:0000256|SAAS:SAAS00909150};
DNA-binding {ECO:0000256|HAMAP-Rule:MF_00103,
ECO:0000256|SAAS:SAAS00909149};
Glycosidase {ECO:0000256|HAMAP-Rule:MF_00103,
ECO:0000256|SAAS:SAAS00909132};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_00103,
ECO:0000256|SAAS:SAAS00909132};
Lyase {ECO:0000256|HAMAP-Rule:MF_00103,
ECO:0000256|SAAS:SAAS00909168};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00103, ECO:0000256|PROSITE-
ProRule:PRU00391, ECO:0000256|SAAS:SAAS00640308};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00103,
ECO:0000256|SAAS:SAAS00909184};
Zinc {ECO:0000256|HAMAP-Rule:MF_00103, ECO:0000256|PROSITE-
ProRule:PRU00391, ECO:0000256|SAAS:SAAS00640308};
Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00103, ECO:0000256|PROSITE-
ProRule:PRU00391, ECO:0000256|SAAS:SAAS00640308}.
DOMAIN 2 115 FPG_CAT. {ECO:0000259|PROSITE:PS51068}.
DOMAIN 240 274 FPG-type. {ECO:0000259|PROSITE:PS51066}.
ACT_SITE 2 2 Schiff-base intermediate with DNA.
{ECO:0000256|HAMAP-Rule:MF_00103}.
ACT_SITE 3 3 Proton donor. {ECO:0000256|HAMAP-
Rule:MF_00103}.
ACT_SITE 60 60 Proton donor; for beta-elimination
activity. {ECO:0000256|HAMAP-
Rule:MF_00103}.
ACT_SITE 264 264 Proton donor; for delta-elimination
activity. {ECO:0000256|HAMAP-
Rule:MF_00103}.
BINDING 93 93 DNA. {ECO:0000256|HAMAP-Rule:MF_00103}.
BINDING 112 112 DNA. {ECO:0000256|HAMAP-Rule:MF_00103}.
SEQUENCE 275 AA; 31550 MW; 06994E80B15999D4 CRC64;
MPELPEVETI RKTLKNLVLN KKIEKVKVYW PKIIKQPDDV EEFKHILSGQ TIRDIKRKGK
FLLFQLDDYY LVSHLRMEGK YSVNKPIEPV KKHTHIVFYF EDGDELRYND VRKFGTMHVY
PIGEELNEKP LNQLGPDPFE DAFTFDYFYS KLKKTDRTIK AALLDQSILA GLGNIYVDET
LFKAGIHPLK RSSKLTKKEI KAIQEAAIYT LAGAVKLGGT TIRSYVNGQG QMGMFQQELF
VYGQENKPCK TCGKPIVKMK VGGRGTHICP TCQKN


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