Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Xylella fastidiosa subsp. multiplex
Status
Unreviewed-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

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

Catalytic activityi

Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.UniRule annotationSAAS 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 annotationSAAS 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 sitei92DNAUniRule annotation1
Binding sitei111DNAUniRule annotation1
Binding sitei152DNAUniRule annotation1
Active sitei261Proton donor; for delta-elimination activityUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-bindingUniRule annotationSAAS annotation, GlycosidaseUniRule annotationSAAS annotation, Hydrolase, LyaseUniRule annotationSAAS annotation, Multifunctional enzymeUniRule annotationSAAS annotation
Biological processDNA damage, DNA repairUniRule annotationSAAS annotation
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
ORF Names:XYFPCFBP8417_09800Imported
OrganismiXylella fastidiosa subsp. multiplexImported
Taxonomic identifieri644357 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXylella
Proteomesi
  • UP000187297 Componenti: Unassembled WGS sequence

Interactioni

Subunit structurei

Monomer.UniRule annotationSAAS annotation

Structurei

3D structure databases

SMRiA0A1R2D5R8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 114FPG_CATInterPro annotationAdd BLAST113
Domaini237 – 271FPG-typeInterPro annotationAdd BLAST35

Sequence similaritiesi

Belongs to the FPG family.UniRule annotationSAAS annotation

Keywords - Domaini

Zinc-fingerUniRule annotationSAAS annotation

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
PfamiView protein in Pfam
PF01149 Fapy_DNA_glyco, 1 hit
PF06831 H2TH, 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.

A0A1R2D5R8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPELPEVETT LRGLLPYLTN QLIYSLTLRR RTLRWDIPSH IESRLPGHRI
60 70 80 90 100
TTVCRRAKYL LIDTNAGGSL IIHLGMSGTL RLLAPETPLR PHDHVDIMLN
110 120 130 140 150
NRRVLRFNDP RRFGCLLWQE DGQIHPLLQR LGCEPLSDSF NGDYLYQCSR
160 170 180 190 200
ARNVSVKTFL MDQRIVVGVG NIYAAESLFR AGISPLCEAD KISLQRYRRL
210 220 230 240 250
AEVVKDILLY AINRGGTTLR DFLSPDGRPG YFKQELFVYG RQQQPCKQCG
260 270
SLLRQTTIRQ RTTVWCGHCQ G
Length:271
Mass (Da):31,091
Last modified:April 12, 2017 - v1
Checksum:i3FF8AFA1617695DF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
LUYB01000031 Genomic DNA Translation: OMJ98601.1
RefSeqiWP_004085054.1, NZ_LUYB01000031.1

Genome annotation databases

GeneIDi1125693

Similar proteinsi

Entry informationi

Entry nameiA0A1R2D5R8_XYLFS
AccessioniPrimary (citable) accession number: A0A1R2D5R8
Entry historyiIntegrated into UniProtKB/TrEMBL: April 12, 2017
Last sequence update: April 12, 2017
Last modified: May 23, 2018
This is version 9 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health