(data stored in ACNUC27125 zone)

HOGENOM: ACAM1_1_PE2419

ID   ACAM1_1_PE2419                       STANDARD;      PRT;   284 AA.
AC   ACAM1_1_PE2419; B0C5D4;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Formamidopyrimidine-DNA glycosylase; Short=Fapy-DNA
DE   glycosylase; EC=3.2.2.23;AltName: Full=DNA-(apurinic or apyrimidinic
DE   site) lyase mutM; Short=AP lyase mutM; EC=4.2.99 18; (ACAM1_1.PE2419).
GN   Name=mutM; Synonyms=fpg; OrderedLocusNames=AM1_2501;
OS   ACARYOCHLORIS MARINA MBIC11017.
OC   Bacteria; Cyanobacteria; Acaryochloris.
OX   NCBI_TaxID=329726;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACAM1_1.PE2419.
CC       Acaryochloris marina MBIC11017, complete genome.
CC   -!- ANNOTATIONS ORIGIN:FPG_ACAM1
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of DNA containing ring-opened 7-
CC       methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-
CC       methyl)formamidopyrimidine.
CC   -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
CC       apyrimidinic site in DNA is broken by a beta-elimination reaction,
CC       leaving a 3'-terminal unsaturated sugar and a product with a
CC       terminal 5'-phosphate.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SIMILARITY: Belongs to the FPG family.
CC   -!- SIMILARITY: Contains 1 FPG-type zinc finger.
CC   -!- GENE_FAMILY: HOG000020884 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B0C5D4; -.
DR   EMBL; CP000828; ABW27510.1; -; Genomic_DNA.
DR   RefSeq; YP_001516824.1; NC_009925.1.
DR   ProteinModelPortal; B0C5D4; -.
DR   STRING; B0C5D4; -.
DR   GeneID; 5681314; -.
DR   GenomeReviews; CP000828_GR; AM1_2501.
DR   KEGG; amr:AM1_2501; -.
DR   OMA; RMTGQLL; -.
DR   ProtClustDB; PRK13945; -.
DR   BioCyc; AMAR329726:AM1_2501-MON; -.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0008534; F:oxidized purine base lesion DNA N-glycosylase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
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; IPR000191; DNA_glycosylase/AP_lyase.
DR   InterPro; IPR012319; DNA_glycosylase/AP_lyase_cat.
DR   InterPro; IPR020629; Formamido-pyr_DNA_Glyclase.
DR   InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR   InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
DR   InterPro; IPR010663; Znf_DNA_glyclase/IsotRNA_synth.
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   SUPFAM; SSF81624; Form_DNAglyc_cat; 1.
DR   SUPFAM; SSF46946; Ribosomal_H2TH; 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.
DR   HOGENOMDNA; ACAM1_1.PE2419; -.
KW   formamidopyrimidine-DNA glycosylase;
KW   Complete proteome; DNA damage; DNA repair; DNA-binding; Glycosidase;
KW   Hydrolase; Lyase; Metal-binding; Multifunctional enzyme; Zinc;
KW   Zinc-finger.
SQ   SEQUENCE   284 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MPELPEVETV RLGLEKVTVG MQIMGGEVLY PRTIAHPQSP QVFIQGLQDA TFLSWMRRGK
     YLLSQLSFST QQPSGWLGVH LRMTGQLLWV AQDEPVQKHT RVRLFFVNNR ELRFVDQRTF
     GQMWWVAPTE DPKQVISGLQ KLGPEPFSEE FSVDYFWESL QGRKRSIKSA LLDQALVAGV
     GNIYADEALF MSEIRPTTAC HQLQTEQVQR LRTAIIEVLS TSIGAGGTTF SDFRDLKGVN
     GNYGGMAWVY GRQGQPCRTC GQTIERIKLV GRSTHFCPQC QPES
//

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