(data stored in ACNUC29543 zone)

SWISSPROT: A5GR44_SYNR3

ID   A5GR44_SYNR3            Unreviewed;       282 AA.
AC   A5GR44;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 89.
DE   RecName: Full=Formamidopyrimidine-DNA glycosylase {ECO:0000256|HAMAP-Rule:MF_00103};
DE            Short=Fapy-DNA glycosylase {ECO:0000256|HAMAP-Rule:MF_00103};
DE            EC=3.2.2.23 {ECO:0000256|HAMAP-Rule:MF_00103};
DE   AltName: Full=DNA-(apurinic or apyrimidinic site) lyase MutM {ECO:0000256|HAMAP-Rule:MF_00103};
DE            Short=AP lyase MutM {ECO:0000256|HAMAP-Rule:MF_00103};
DE            EC=4.2.99.18 {ECO:0000256|HAMAP-Rule:MF_00103};
GN   Name=mutM {ECO:0000256|HAMAP-Rule:MF_00103,
GN   ECO:0000313|EMBL:CAK27353.1};
GN   Synonyms=fpg {ECO:0000256|HAMAP-Rule:MF_00103};
GN   OrderedLocusNames=SynRCC307_0450 {ECO:0000313|EMBL:CAK27353.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27353.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|EMBL:CAK27353.1, ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in base excision repair of DNA damaged by
CC       oxidation or by mutagenic agents. Acts as DNA glycosylase that
CC       recognizes and removes damaged bases. Has a preference for
CC       oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has
CC       AP (apurinic/apyrimidinic) lyase activity and introduces nicks in
CC       the DNA strand. Cleaves the DNA backbone by beta-delta elimination
CC       to generate a single-strand break at the site of the removed base
CC       with both 3'- and 5'-phosphates. {ECO:0000256|HAMAP-Rule:MF_00103,
CC       ECO:0000256|SAAS:SAAS00020861}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of DNA containing ring-opened 7-methylguanine
CC         residues, releasing 2,6-diamino-4-hydroxy-5-(N-
CC         methyl)formamidopyrimidine.; EC=3.2.2.23;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00103,
CC         ECO:0000256|SAAS:SAAS01116288};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=The C-O-P bond 3' to the apurinic or apyrimidinic site in
CC         DNA is broken by a beta-elimination reaction, leaving a 3'-
CC         terminal unsaturated sugar and a product with a terminal 5'-
CC         phosphate.; EC=4.2.99.18; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00103, ECO:0000256|SAAS:SAAS01121890};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00103};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00103};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00103,
CC       ECO:0000256|SAAS:SAAS00041892}.
CC   -!- SIMILARITY: Belongs to the FPG family. {ECO:0000256|HAMAP-
CC       Rule:MF_00103, ECO:0000256|SAAS:SAAS00557294}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00103}.
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DR   EMBL; CT978603; CAK27353.1; -; Genomic_DNA.
DR   RefSeq; WP_011934868.1; NC_009482.1.
DR   STRING; 316278.SynRCC307_0450; -.
DR   EnsemblBacteria; CAK27353; CAK27353; SynRCC307_0450.
DR   KEGG; syr:SynRCC307_0450; -.
DR   eggNOG; ENOG4105ERD; Bacteria.
DR   eggNOG; COG0266; LUCA.
DR   HOGENOM; HOG000020884; -.
DR   KO; K10563; -.
DR   OMA; GVHLRMT; -.
DR   OrthoDB; 1162346at2; -.
DR   BioCyc; SSP316278:G1GJL-448-MONOMER; -.
DR   Proteomes; UP000001115; Chromosome.
DR   GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   Gene3D; 3.20.190.10; -; 1.
DR   HAMAP; MF_00103; Fapy_DNA_glycosyl; 1.
DR   InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR   InterPro; IPR015887; DNA_glyclase_Znf_dom_DNA_BS.
DR   InterPro; IPR020629; Formamido-pyr_DNA_Glyclase.
DR   InterPro; IPR012319; FPG_cat.
DR   InterPro; IPR035937; MutM-like_N-ter.
DR   InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR   InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
DR   InterPro; IPR010663; Znf_FPG/IleRS.
DR   Pfam; PF01149; Fapy_DNA_glyco; 1.
DR   Pfam; PF06831; H2TH; 1.
DR   Pfam; PF06827; zf-FPG_IleRS; 1.
DR   SMART; SM00898; Fapy_DNA_glyco; 1.
DR   SMART; SM01232; H2TH; 1.
DR   SUPFAM; SSF46946; SSF46946; 1.
DR   SUPFAM; SSF81624; SSF81624; 1.
DR   TIGRFAMs; TIGR00577; fpg; 1.
DR   PROSITE; PS51068; FPG_CAT; 1.
DR   PROSITE; PS01242; ZF_FPG_1; 1.
DR   PROSITE; PS51066; ZF_FPG_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5GR44.
DR   SWISS-2DPAGE; A5GR44.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00103,
KW   ECO:0000256|SAAS:SAAS01087016};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00103,
KW   ECO:0000256|SAAS:SAAS01087019};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00103,
KW   ECO:0000256|SAAS:SAAS01087047};
KW   Glycosidase {ECO:0000256|HAMAP-Rule:MF_00103,
KW   ECO:0000256|SAAS:SAAS01087011, ECO:0000313|EMBL:CAK27353.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00103,
KW   ECO:0000256|SAAS:SAAS01087030, ECO:0000313|EMBL:CAK27353.1};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00103,
KW   ECO:0000256|SAAS:SAAS01087025};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00103,
KW   ECO:0000256|SAAS:SAAS00551678};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00103,
KW   ECO:0000256|SAAS:SAAS01087023};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00103, ECO:0000256|SAAS:SAAS00551670};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00103, ECO:0000256|PROSITE-
KW   ProRule:PRU00391, ECO:0000256|SAAS:SAAS00551733}.
FT   DOMAIN        2    121       FPG_CAT. {ECO:0000259|PROSITE:PS51068}.
FT   DOMAIN      248    282       FPG-type. {ECO:0000259|PROSITE:PS51066}.
FT   ACT_SITE      2      2       Schiff-base intermediate with DNA.
FT                                {ECO:0000256|HAMAP-Rule:MF_00103}.
FT   ACT_SITE      3      3       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00103}.
FT   ACT_SITE     61     61       Proton donor; for beta-elimination
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_00103}.
FT   ACT_SITE    272    272       Proton donor; for delta-elimination
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_00103}.
FT   BINDING     100    100       DNA. {ECO:0000256|HAMAP-Rule:MF_00103}.
FT   BINDING     118    118       DNA. {ECO:0000256|HAMAP-Rule:MF_00103}.
SQ   SEQUENCE   282 AA;  31099 MW;  5B2E1CC28F6B7A75 CRC64;
     MPELPEVETV RRGLELQVGR FPIGETIVCR SRAVAAPKGD PDGFTAALRG CELAGWRRRG
     KYLVAKLERD GAPAGELGVH LRMTGQFQWL QREERPPCPH TRVRFLSEKH ELRFVDVRSF
     GELWFVPLGT PTEQVITGLT RLGPEPFSDA FNANYLRQRL KGSSRPIKNA LLDQALVAGV
     GNIYADESLF MAGIRPHTPS GSVSAARLEK LRAALVKVLE LSIGAGGTTF SDFRDLTGTN
     GNYGGQARVY RRGGEPCRQC GTILRRDTLG GRSSHWCPSC QR
//

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