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Q6NGH4 (FPG_CORDI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 79. 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:DIP1543
OrganismCorynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis) [Complete proteome] [HAMAP]
Taxonomic identifier257309 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length296 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 – 296295Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103
PRO_0000228427

Regions

Zinc finger260 – 29435FPG-type HAMAP-Rule MF_00103

Sites

Active site21Schiff-base intermediate with DNA By similarity
Active site31Proton donor By similarity
Active site611Proton donor; for beta-elimination activity By similarity
Active site2841Proton donor; for delta-elimination activity By similarity
Binding site1041DNA By similarity
Binding site1281DNA By similarity
Binding site1741DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6NGH4 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 6DC76CDA56AF5F20

FASTA29633,183
        10         20         30         40         50         60 
MPELPEVEVV RRGLTPYVLG ATITDVAVEH PRSIRTIEGG AAELIGSLQG REVTRIGRRG 

        70         80         90        100        110        120 
KFLWFELTGH GDYACGFPQQ GLLVHLGMSG QMLIKTQNSA LHPHRRIRTT IVRSDAQECF 

       130        140        150        160        170        180 
ELWFVDQRTF GYWAPTTFVE TAHGCVPEQI THIARDLLDP QLKRENLARL IRKKNSEIKR 

       190        200        210        220        230        240 
VLLNQEIVSG IGNIYADEML WAARIHPQTP ASHLSVAQLS NLLEHGQRVM NAALDQGGTS 

       250        260        270        280        290 
FDSLYVNVNG QSGYFDVSLH AYGQQGQACD RCGSNIIREK FANRSSHFCP RCQLMH 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248358 Genomic DNA. Translation: CAE50068.1.
RefSeqNP_939885.1. NC_002935.2.

3D structure databases

ProteinModelPortalQ6NGH4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257309.DIP1543.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE50068; CAE50068; DIP1543.
GeneID2650732.
KEGGcdi:DIP1543.
PATRIC21484294. VBICorDip47633_1523.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020884.
KOK10563.
OMAFHHARSK.
OrthoDBEOG6QP131.
ProtClustDBPRK01103.

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_CORDI
AccessionPrimary (citable) accession number: Q6NGH4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 79 of the entry and version 3 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