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Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Pontibacillus yanchengensis Y32
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 sitei60Proton donor; for beta-elimination activityUniRule annotation1
Binding sitei93DNAUniRule annotation1
Binding sitei112DNAUniRule annotation1
Active sitei264Proton 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:N782_16850Imported
OrganismiPontibacillus yanchengensis Y32Imported
Taxonomic identifieri1385514 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaePontibacillus
Proteomesi
  • UP000030147 Componenti: Unassembled WGS sequence

Interactioni

Subunit structurei

Monomer.UniRule annotationSAAS annotation

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 115FPG_CATInterPro annotationAdd BLAST114
Domaini240 – 274FPG-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.
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.
PS51066. ZF_FPG_2. 1 hit.

Sequencei

Sequence statusi: Complete.

A0A0A2TCC2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPELPEVETI KKTLEYMVIG KTIKNVSLYW PKMIKHPDDS EEFINLIKGQ
60 70 80 90 100
TINRLDRRGK FLLFYLDTHV LISHLRMEGK YGVFSSETPL AKHTHVRFLL
110 120 130 140 150
DDEQELRYQD VRKFGTLHLY NIGEEFSNPP LEQLGPEPFE EGFSIQYLHT
160 170 180 190 200
KLRRTNRHIK TALLDQTILA GLGNIYVDEA LFRAAIHPLR IASGISEKEV
210 220 230 240 250
RSLHRSIQQT LREAVDQGGT TIRSYVNTQG QIGMFQQQLN VYGREEESCK
260 270
ICSTPITKMK VGGRGTHVCL TCQKENV
Length:277
Mass (Da):31,872
Last modified:February 4, 2015 - v1
Checksum:i66F5DF8151BC769F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AVBF01000050 Genomic DNA. Translation: KGP71721.1.
RefSeqiWP_036822080.1. NZ_AVBF01000050.1.

Genome annotation databases

EnsemblBacteriaiKGP71721; KGP71721; N782_16850.

Similar proteinsi

Entry informationi

Entry nameiA0A0A2TCC2_9BACI
AccessioniPrimary (citable) accession number: A0A0A2TCC2
Entry historyiIntegrated into UniProtKB/TrEMBL: February 4, 2015
Last sequence update: February 4, 2015
Last modified: March 28, 2018
This is version 21 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.UniRule annotation
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 proteome, Reference proteomeImported