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Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Corynebacterium glutamicum (Brevibacterium saccharolyticum)
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 annotationSAAS 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 sitei61Proton donor; for beta-elimination activityUniRule annotation1
Binding sitei103DNAUniRule annotation1
Binding sitei122DNAUniRule annotation1
Binding sitei164DNAUniRule annotation1
Active sitei274Proton 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:N24_2149Imported
OrganismiCorynebacterium glutamicum (Brevibacterium saccharolyticum)Imported
Taxonomic identifieri1718 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
Proteomesi
  • UP000218244 Componenti: Chromosome

Interactioni

Subunit structurei

Monomer.UniRule annotationSAAS annotation

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 125FPG_CATInterPro annotationAdd BLAST124
Domaini250 – 284FPG-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.
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.

A0A160PTN1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPELPEVEVV RRGLENHMVG HTIVSASVLH PRAARNQLGG GPEIEANIVG
60 70 80 90 100
LKVSAAKRRG KFLWLELIDE PSGDTPPDLG LLVHLGMSGQ MLIKEPDAPI
110 120 130 140 150
SPHLRAKVEL DSGDEVWFVD QRTFGYWWLG ELVDGVPQRV SHIATDLLDD
160 170 180 190 200
SFDFSAVARN LKSRKTEIKR LLLNQEIVSG IGNIYADEML WQAQIHPLQR
210 220 230 240 250
ADRLSLARLE ELLHAGKEVM IKALAQGGTS FDALYVNVNG NSGYFALSLN
260 270 280
AYGQTGEPCA RCGTPIIREN FMNRGSHFCP NCQKQR
Length:286
Mass (Da):31,682
Last modified:July 6, 2016 - v1
Checksum:iB4E8961E035357DD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP017369 Genomic DNA. Translation: BAU96411.1.

Similar proteinsi

Entry informationi

Entry nameiA0A160PTN1_CORGT
AccessioniPrimary (citable) accession number: A0A160PTN1
Entry historyiIntegrated into UniProtKB/TrEMBL: July 6, 2016
Last sequence update: July 6, 2016
Last modified: March 28, 2018
This is version 13 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported