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Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Yersinia pestis bv. Antiqua (strain Angola)
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 sitei57Proton donor; for beta-elimination activityUniRule annotation1
Binding sitei90DNAUniRule annotation1
Binding sitei109DNAUniRule annotation1
Binding sitei150DNAUniRule annotation1
Active sitei259Proton donor; for delta-elimination activityUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri235 – 269FPG-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

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:YpAngola_A0058
OrganismiYersinia pestis bv. Antiqua (strain Angola)
Taxonomic identifieri349746 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesYersiniaceaeYersinia

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_10000940892 – 269Formamidopyrimidine-DNA glycosylaseAdd BLAST268

Interactioni

Subunit structurei

Monomer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA9R677
SMRiA9R677
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FPG family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri235 – 269FPG-typeUniRule annotationAdd BLAST35

Keywords - Domaini

Zinc-finger

Phylogenomic databases

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.

A9R677-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPELPEVETS RRGIEPYLVG QTILYAVVRN ARLRWPVSDE ILTLSDQPVL
60 70 80 90 100
SVQRRAKYLL LELPKGWIII HLGMSGSLRV LSEETAAEKH DHVDLVVSNG
110 120 130 140 150
KILRYTDPRR FGAWLWAKDL ETSNVLAHLG PEPLSDEFTA QYLFDKSRNK
160 170 180 190 200
RTLIKPWLMD NKVVVGVGNI YASESLFAAG ILPDRAAGSL TDAESVLLVA
210 220 230 240 250
TIKAVLLHSI EQGGTTLRDF LQSDGKPGYF AQELQVYGRA GEPCRQCGHP
260
IEIAKHGQRS TFFCRHCQH
Length:269
Mass (Da):30,111
Last modified:February 5, 2008 - v1
Checksum:i659CBC9A7233857C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000901 Genomic DNA Translation: ABX85219.1
RefSeqiWP_002208989.1, NZ_CP009935.1

Genome annotation databases

EnsemblBacteriaiABX85219; ABX85219; YpAngola_A0058
KEGGiypg:YpAngola_A0058
PATRICifig|349746.12.peg.1001

Similar proteinsi

Entry informationi

Entry nameiFPG_YERPG
AccessioniPrimary (citable) accession number: A9R677
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 5, 2008
Last modified: May 23, 2018
This is version 70 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health