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Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Bordetella avium (strain 197N)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.UniRule annotation
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.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei2Schiff-base intermediate with DNAUniRule annotation1
Active sitei3Proton donorUniRule annotation1
Active sitei58Proton donor; for beta-elimination activityUniRule annotation1
Binding sitei91DNAUniRule annotation1
Binding sitei109DNAUniRule annotation1
Binding sitei154DNAUniRule annotation1
Active sitei264Proton donor; for delta-elimination activityUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri240 – 274FPG-typeUniRule annotationAdd BLAST35

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, Glycosidase, Hydrolase, Lyase, Multifunctional enzyme
Biological processDNA damage, DNA repair
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyciBAVI360910:G1GJZ-544-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Formamidopyrimidine-DNA glycosylaseUniRule annotation (EC:3.2.2.23UniRule annotation)
Short name:
Fapy-DNA glycosylaseUniRule annotation
Alternative name(s):
DNA-(apurinic or apyrimidinic site) lyase MutMUniRule annotation (EC:4.2.99.18UniRule annotation)
Short name:
AP lyase MutMUniRule annotation
Gene namesi
Name:mutMUniRule annotation
Synonyms:fpgUniRule annotation
Ordered Locus Names:BAV0533
OrganismiBordetella avium (strain 197N)
Taxonomic identifieri360910 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
Proteomesi
  • UP000001977 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_10000086772 – 275Formamidopyrimidine-DNA glycosylaseAdd BLAST274

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi360910.BAV0533

Structurei

3D structure databases

ProteinModelPortaliQ2KYB7
SMRiQ2KYB7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FPG family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri240 – 274FPG-typeUniRule annotationAdd BLAST35

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG4105ERD Bacteria
COG0266 LUCA
HOGENOMiHOG000020881
KOiK10563
OMAiRNSRLRW

Family and domain databases

Gene3Di3.20.190.10, 1 hit
HAMAPiMF_00103 Fapy_DNA_glycosyl, 1 hit
InterProiView protein in InterPro
IPR015886 DNA_glyclase/AP_lyase_DNA-bd
IPR015887 DNA_glyclase_Znf_dom_DNA_BS
IPR020629 Formamido-pyr_DNA_Glyclase
IPR012319 FPG_cat
IPR035937 MutM-like_N-ter
IPR010979 Ribosomal_S13-like_H2TH
IPR000214 Znf_DNA_glyclase/AP_lyase
IPR010663 Znf_FPG/IleRS
PfamiView protein in Pfam
PF01149 Fapy_DNA_glyco, 1 hit
PF06831 H2TH, 1 hit
PF06827 zf-FPG_IleRS, 1 hit
SMARTiView protein in SMART
SM00898 Fapy_DNA_glyco, 1 hit
SM01232 H2TH, 1 hit
SUPFAMiSSF46946 SSF46946, 1 hit
SSF81624 SSF81624, 1 hit
TIGRFAMsiTIGR00577 fpg, 1 hit
PROSITEiView protein in PROSITE
PS51068 FPG_CAT, 1 hit
PS01242 ZF_FPG_1, 1 hit
PS51066 ZF_FPG_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q2KYB7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPELPEVETT RRGIDPVITG QTLRRLVVRE PRMRWPIPAD LPSLLTDRPV
60 70 80 90 100
LATGRRGKYL LLRFEHGVQI VHLGMSGSLR RVAMDEAPRK HDHVDWVFDH
110 120 130 140 150
AILRLHDPRR FGAVLWHPNT DGPVEAHPLL IGLGIEPFDP RFDGKWLHDH
160 170 180 190 200
FRDKRVAVKQ ALLAGHAVVG VGNIYASECL FRAGIDPRTP AGKLSRPRCE
210 220 230 240 250
RLAQAVRATL ADALASGGST LRDYVGASGE PGAYFAIHAA VYERAGLACR
260 270
VCGTPIRRLV QGQRATYFCP HCQKR
Length:275
Mass (Da):30,633
Last modified:March 7, 2006 - v1
Checksum:iC72A0D038241A4D6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM167904 Genomic DNA Translation: CAJ48138.1
RefSeqiWP_012416229.1, NC_010645.1

Genome annotation databases

EnsemblBacteriaiCAJ48138; CAJ48138; BAV0533
KEGGibav:BAV0533

Similar proteinsi

Entry informationi

Entry nameiFPG_BORA1
AccessioniPrimary (citable) accession number: Q2KYB7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 7, 2006
Last modified: May 23, 2018
This is version 83 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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