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B1J2M4 (FPG_PSEPW) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:PputW619_0340
OrganismPseudomonas putida (strain W619) [Complete proteome] [HAMAP]
Taxonomic identifier390235 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length270 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 – 270269Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103
PRO_1000094064

Regions

Zinc finger236 – 27035FPG-type HAMAP-Rule MF_00103

Sites

Active site21Schiff-base intermediate with DNA By similarity
Active site31Proton donor By similarity
Active site581Proton donor; for beta-elimination activity By similarity
Active site2601Proton donor; for delta-elimination activity By similarity
Binding site911DNA By similarity
Binding site1101DNA By similarity
Binding site1511DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
B1J2M4 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 7DD3E19008C25CA0

FASTA27030,196
        10         20         30         40         50         60 
MPELPEVETT RRGIAPHLEG QRVSRVVVRD RRLRWPIPED LDVRLSGQRI LSVERRAKYL 

        70         80         90        100        110        120 
LINAEVGTLI SHLGMSGNLR LVQLGLPAAK HEHVDIELES GLMLRYTDPR RFGAMLWSLD 

       130        140        150        160        170        180 
PLNHELLLRL GPEPLTDLFD GERLFQLSRG RTMAVKPFIM DNAVVVGVGN IYATEALFAA 

       190        200        210        220        230        240 
GIDPRREAGG ISRTRYLKLA IEIKRVLAAA IEQGGTTLRD FIGGDGQPGY FQQELFVYGR 

       250        260        270 
GGMPCKLCGT TLREAKLGQR ASVYCPRCQR 

« Hide

References

[1]"Complete sequence of Pseudomonas putida W619."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Taghavi S., Vangronsveld D., van der Lelie D., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: W619.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000949 Genomic DNA. Translation: ACA70846.1.
RefSeqYP_001747215.1. NC_010501.1.

3D structure databases

ProteinModelPortalB1J2M4.
SMRB1J2M4. Positions 2-270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING390235.PputW619_0340.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA70846; ACA70846; PputW619_0340.
GeneID6109120.
KEGGppw:PputW619_0340.
PATRIC19950405. VBIPsePut93764_0344.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020881.
KOK10563.
OMAGWIIVHL.
OrthoDBEOG6QP131.
ProtClustDBPRK01103.

Enzyme and pathway databases

BioCycPPUT390235:GHHJ-341-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_PSEPW
AccessionPrimary (citable) accession number: B1J2M4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: February 19, 2014
This is version 45 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