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Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM_1

Organism
Mycobacterium smegmatis
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 sitei93DNAUniRule annotation1
Binding sitei112DNAUniRule annotation1
Binding sitei158DNAUniRule annotation1
Active sitei268Proton donor; for delta-elimination activityUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-bindingUniRule annotationSAAS annotation, GlycosidaseUniRule annotationSAAS annotationImported, 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:mutM_1Imported
Synonyms:fpgUniRule annotation, mutMUniRule annotation
ORF Names:ERS451418_02433Imported
OrganismiMycobacterium smegmatisImported
Taxonomic identifieri1772 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000062612 Componenti: Chromosome 1

Interactioni

Subunit structurei

Monomer.UniRule annotationSAAS annotation

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 115FPG_CATInterPro annotationAdd BLAST114
Domaini244 – 278FPG-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.

A0A0D6HUL2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPELPEVEVV RRGLAEHVTG KTITGVRVHH PRAVRRHEAG PADLTARLLD
60 70 80 90 100
VRITGTGRRG KYLWLTLDDS AALVVHLGMS GQMLLGPIRD TRHLRIAAVL
110 120 130 140 150
DDGTALSFVD QRTFGGWQLT EMVTVDGTDV PEPVAHIARD PLDPLFDRDR
160 170 180 190 200
VVTVLRGKHS EIKRQLLDQT VVSGIGNIYA DEALWRTKIN GARIAAALLR
210 220 230 240 250
RRLAELLDAA AEVMTDALGQ GGTSFDSLYV NVNGESGYFD RSLDAYGREG
260 270 280
EPCRRCGAIM RREKFMNRSS FYCPRCQPRP RVPRV
Length:285
Mass (Da):31,685
Last modified:May 27, 2015 - v1
Checksum:i89157DD8AECCA88C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
LN831039 Genomic DNA. Translation: CKH58835.1.
RefSeqiWP_058125900.1. NZ_LN831039.1.

Genome annotation databases

EnsemblBacteriaiCKH58835; CKH58835; ERS451418_02433.
PATRICifig|1772.19.peg.2470.

Similar proteinsi

Entry informationi

Entry nameiA0A0D6HUL2_MYCSM
AccessioniPrimary (citable) accession number: A0A0D6HUL2
Entry historyiIntegrated into UniProtKB/TrEMBL: May 27, 2015
Last sequence update: May 27, 2015
Last modified: March 28, 2018
This is version 19 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported