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A2BPD1 (FPG_PROMS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 57. 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:A9601_03541
OrganismProchlorococcus marinus (strain AS9601) [Complete proteome] [HAMAP]
Taxonomic identifier146891 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length292 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 – 292291Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103
PRO_1000008739

Regions

Zinc finger258 – 29235FPG-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 site2821Proton donor; for delta-elimination activity By similarity
Binding site1091DNA By similarity
Binding site1281DNA By similarity
Binding site1731DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
A2BPD1 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: 3AC5351E751EC002

FASTA29233,695
        10         20         30         40         50         60 
MPELPEVETV RRGLEQKLNN FIIKKVEICR YSTVAFPTNK EEFIKGLRNS LIYKWDRRGK 

        70         80         90        100        110        120 
YLIAQLKEVQ NEHTQLPLEN SQNNGFLVVH LRMTGYFKFI ENSSNPCKHT RVRFFDKNNN 

       130        140        150        160        170        180 
ELRYIDVRSF GQMWWINNDL SLNKIIKGLG SLGPEPFSKD FNANYLKKVI SKRTKSIKAI 

       190        200        210        220        230        240 
LLDQTIVAGI GNIYADESLY SAGISPFREA RTIKKNELIK LKESIVTVLK KSIGSGGTTF 

       250        260        270        280        290 
SDFRDLEGEN GNFGLQTNVY RRTGKECRKC GNLIERQKIT GRSTHWCPKC QK 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AS9601.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000551 Genomic DNA. Translation: ABM69642.1.
RefSeqYP_001008749.1. NC_008816.1.

3D structure databases

ProteinModelPortalA2BPD1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING146891.A9601_03541.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM69642; ABM69642; A9601_03541.
GeneID4717048.
KEGGpmb:A9601_03541.
PATRIC22982175. VBIProMar75723_0354.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020885.
KOK10563.
OMADHVDLKL.
OrthoDBEOG6QP131.

Enzyme and pathway databases

BioCycPMAR146891:GH90-367-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_PROMS
AccessionPrimary (citable) accession number: A2BPD1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 20, 2007
Last modified: May 14, 2014
This is version 57 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