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C7JHC7 (C7JHC7_ACEP3) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103
Short name=Fapy-DNA glycosylase HAMAP-Rule MF_00103
EC=3.2.2.23 HAMAP-Rule MF_00103
Alternative name(s):
DNA-(apurinic or apyrimidinic site) lyase MutM HAMAP-Rule MF_00103
Gene names
Name:mutM HAMAP-Rule MF_00103
Synonyms:fpg HAMAP-Rule MF_00103
Ordered Locus Names:APA01_12340 EMBL BAH99381.1
OrganismAcetobacter pasteurianus (strain NBRC 3283 / LMG 1513 / CCTM 1153) [Complete proteome] [HAMAP] EMBL BAH99381.1
Taxonomic identifier634452 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Acetobacter ›

Protein attributes

Sequence length279 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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 By similarity. HAMAP-Rule MF_00103 SAAS SAAS015886

Catalytic activity

Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine. HAMAP-Rule MF_00103 SAAS SAAS015886

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. HAMAP-Rule MF_00103 SAAS SAAS015886

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00103 SAAS SAAS000191

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00103 SAAS SAAS015886

Sequence similarities

Belongs to the FPG family. HAMAP-Rule MF_00103

Contains 1 FPG-type zinc finger. HAMAP-Rule MF_00103 SAAS SAAS015886

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Zinc finger238 – 27740FPG-type; degenerate By similarity HAMAP-Rule MF_00103

Sites

Active site21Schiff-base intermediate with DNA By similarity HAMAP-Rule MF_00103
Active site31Proton donor By similarity HAMAP-Rule MF_00103
Active site581Proton donor; for beta-elimination activity By similarity HAMAP-Rule MF_00103
Active site2671Proton donor (in delta-elimination) By similarity HAMAP-Rule MF_00103
Active site2671Proton donor; for delta-elimination activity By similarity HAMAP-Rule MF_00103
Binding site911DNA By similarity HAMAP-Rule MF_00103
Binding site1101DNA By similarity HAMAP-Rule MF_00103
Binding site1531DNA By similarity HAMAP-Rule MF_00103

Sequences

Sequence LengthMass (Da)Tools
C7JHC7 [UniParc].

Last modified October 13, 2009. Version 1.
Checksum: 8A9531626EB1BBE2

FASTA27930,978
        10         20         30         40         50         60 
MPELPEVETV MRGMQIALQN GTIKEAIVRR HDLRWRIPAD FSQTIKGRRI EGFRRRGKYI 

        70         80         90        100        110        120 
LMRLSGGMSI IWHLGMSGRV LLDSPTEPLP HEHVVLILQD GKRCGYIDPR RFGMLDLVPT 

       130        140        150        160        170        180 
DQEDTYPLLV GMGPEPLEPD FTPKTLLAAS KNRRMPIKPF LLDQKVVAGL GNIYVCEALF 

       190        200        210        220        230        240 
RAGIAPTMPA CNLTPPKACK LAQAIRDVLE EAIEAGGSSL KDYVRPEGGL GYFQHAWRVY 

       250        260        270 
GQTGKPCPNC PGTPACSGVQ QITQAGRSTF FCPQRQKNG

« Hide

References

[1]"Whole-genome analyses reveal genetic instability of Acetobacter pasteurianus."
Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., Harada T., Hirakawa H., Kuhara S., Matsushita K., Fujita N., Shirai M.
Nucleic Acids Res. 37:5768-5783(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NBRC 3283 / LMG 1513 / CCTM 1153.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP011121 Genomic DNA. Translation: BAH99381.1.
RefSeqYP_003187761.1. NC_013209.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING634452.APA01_12340.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAH99381; BAH99381; APA01_12340.
GeneID8435322.
KEGGapt:APA01_12340.
PATRIC20632854. VBIAcePas139226_1302.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020881.
KOK10563.
OMANIHASEA.

Enzyme and pathway databases

BioCycAPAS634452:GI0T-1497-MONOMER.

Family and domain databases

HAMAPMF_00103. Fapy_DNA_glycosyl.
InterProIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
IPR000191. DNA_glycosylase/AP_lyase.
IPR012319. DNA_glycosylase/AP_lyase_cat.
IPR020629. Formamido-pyr_DNA_Glyclase.
IPR010979. Ribosomal_S13-like_H2TH.
IPR000214. Znf_DNA_glyclase/AP_lyase.
[Graphical view]
PfamPF01149. Fapy_DNA_glyco. 1 hit.
PF06831. H2TH. 1 hit.
[Graphical view]
SMARTSM00898. Fapy_DNA_glyco. 1 hit.
[Graphical view]
SUPFAMSSF81624. Form_DNAglyc_cat. 1 hit.
SSF46946. Ribosomal_H2TH. 1 hit.
TIGRFAMsTIGR00577. fpg. 1 hit.
PROSITEPS51068. FPG_CAT. 1 hit.
PS51066. ZF_FPG_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC7JHC7_ACEP3
AccessionPrimary (citable) accession number: C7JHC7
Entry history
Integrated into UniProtKB/TrEMBL: October 13, 2009
Last sequence update: October 13, 2009
Last modified: May 1, 2013
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info