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Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Xylella fastidiosa 32
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

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:B398_00735Imported
OrganismiXylella fastidiosa 32Imported
Taxonomic identifieri1214121 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXylella
Proteomesi
  • UP000018676 Componenti: Unassembled WGS sequence

Interactioni

Subunit structurei

Monomer.UniRule annotationSAAS annotation

Structurei

3D structure databases

SMRiA0A1S0VA06.
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.

A0A1S0VA06-1 [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
AWYH01000004 Genomic DNA. Translation: ETE36204.1.
RefSeqiWP_004085054.1. NZ_AWYH01000004.1.

Genome annotation databases

GeneIDi1125693.

Similar proteinsi

Entry informationi

Entry nameiA0A1S0VA06_XYLFS
AccessioniPrimary (citable) accession number: A0A1S0VA06
Entry historyiIntegrated into UniProtKB/TrEMBL: April 12, 2017
Last sequence update: April 12, 2017
Last modified: March 28, 2018
This is version 8 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

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

Keywords - Technical termi

Complete proteomeImported