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B7K1T1 (FPG_CYAP8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Formamidopyrimidine-DNA glycosylase

Short name=Fapy-DNA glycosylase
EC=3.2.2.23
Alternative name(s):
DNA-(apurinic or apyrimidinic site) lyase MutM
Short name=AP lyase MutM
EC=4.2.99.18
Gene names
Name:mutM
Synonyms:fpg
Ordered Locus Names:PCC8801_0132
OrganismCyanothece sp. (strain PCC 8801) (Synechococcus sp. (strain PCC 8801 / RF-1)) [Complete proteome] [HAMAP]
Taxonomic identifier41431 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesCyanothece

Protein attributes

Sequence length282 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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

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

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

Cofactor

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

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00103

Sequence similarities

Belongs to the FPG family.

Contains 1 FPG-type zinc finger.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 282281Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103
PRO_1000117379

Regions

Zinc finger248 – 28235FPG-type HAMAP-Rule MF_00103

Sites

Active site21Schiff-base intermediate with DNA By similarity
Active site31Proton donor By similarity
Active site601Proton donor; for beta-elimination activity By similarity
Active site2721Proton donor; for delta-elimination activity By similarity
Binding site991DNA By similarity
Binding site1181DNA By similarity
Binding site1631DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
B7K1T1 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: E4DAA54A37F716B0

FASTA28231,224
        10         20         30         40         50         60 
MPELPEVETV CRGLNELTSG KVIKDAEVLL PRSLASPSSV DEFLSNIRGV IFGEWQRRGK 

        70         80         90        100        110        120 
YLLGTLVKES GEAAGWLGVH LRMTGQLLWV NQSEPLQIHT RLRLFCGENK ELRFVDIRTF 

       130        140        150        160        170        180 
GKVWCVPPKT TPETIITGLK KLGVEPFSDD FSDDYFTTKL NGRQRNIKTL LLDQEIVAGL 

       190        200        210        220        230        240 
GNIYADEALF KSGVHPTTLG KNLKPQQIEQ LRIAIIEVLE TAIEKGGTTF SDFKGVTGIN 

       250        260        270        280 
GNYGGTAWVY GRTGEPCRVC GTSIERLKLG GRSAHFCPRC QA 

« Hide

References

[1]"Novel metabolic attributes of the genus Cyanothece, comprising a group of unicellular nitrogen-fixing Cyanobacteria."
Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H., Sherman L.A., Pakrasi H.B.
MBio 2:E214-E214(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 8801.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001287 Genomic DNA. Translation: ACK64238.1.
RefSeqYP_002370394.1. NC_011726.1.

3D structure databases

ProteinModelPortalB7K1T1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING41431.PCC8801_0132.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACK64238; ACK64238; PCC8801_0132.
GeneID7104721.
KEGGcyp:PCC8801_0132.
PATRIC21572409. VBICyaSp125535_0248.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020885.
KOK10563.
OMAGWIIVHL.
OrthoDBEOG6QP131.
ProtClustDBPRK13945.

Enzyme and pathway databases

BioCycCSP41431:GHLK-132-MONOMER.

Family and domain databases

HAMAPMF_00103. Fapy_DNA_glycosyl.
InterProIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
IPR015887. DNA_glyclase_Znf_dom_DNA_BS.
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.
IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
[Graphical view]
PfamPF01149. Fapy_DNA_glyco. 1 hit.
PF06831. H2TH. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
SMARTSM00898. Fapy_DNA_glyco. 1 hit.
[Graphical view]
SUPFAMSSF46946. SSF46946. 1 hit.
SSF81624. SSF81624. 1 hit.
TIGRFAMsTIGR00577. fpg. 1 hit.
PROSITEPS51068. FPG_CAT. 1 hit.
PS01242. ZF_FPG_1. 1 hit.
PS51066. ZF_FPG_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFPG_CYAP8
AccessionPrimary (citable) accession number: B7K1T1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: February 19, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families