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Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
Status
Reviewed-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 (By similarity).By similarity

Catalytic activityi

Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.
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.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei2Schiff-base intermediate with DNABy similarity1
Active sitei3Proton donorBy similarity1
Active sitei58Proton donor; for beta-elimination activityBy similarity1
Binding sitei92DNABy similarity1
Binding sitei110DNABy similarity1
Active sitei261Proton donor; for delta-elimination activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri237 – 271FPG-typeAdd BLAST35

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, Glycosidase, Hydrolase, Lyase, Multifunctional enzyme
Biological processDNA damage, DNA repair
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyciLLAC272623:G1FZA-378-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Formamidopyrimidine-DNA glycosylase (EC:3.2.2.23)
Short name:
Fapy-DNA glycosylase
Alternative name(s):
DNA-(apurinic or apyrimidinic site) lyase MutM (EC:4.2.99.18)
Short name:
AP lyase MutM
Gene namesi
Name:mutM
Synonyms:fpg
Ordered Locus Names:LL0353
ORF Names:L0271
OrganismiLactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
Taxonomic identifieri272623 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus
Proteomesi
  • UP000002196 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001708292 – 272Formamidopyrimidine-DNA glycosylaseAdd BLAST271

Proteomic databases

PaxDbiQ9CIK4
PRIDEiQ9CIK4

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi272623.L0271

Structurei

3D structure databases

ProteinModelPortaliQ9CIK4
SMRiQ9CIK4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FPG family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri237 – 271FPG-typeAdd BLAST35

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG4105ERD Bacteria
COG0266 LUCA
HOGENOMiHOG000020885
KOiK10563
OMAiGVHLRMT

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9CIK4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPELPEVETV RRELEKRIVG QKIVSIEATY PRMVLTGFEQ LKKELTGKTI
60 70 80 90 100
HGISRRGKYL IFEIGEKDRL ISHLRMEGKY RLASLNVPME KHDHLALKFT
110 120 130 140 150
DEQLIYADVR KFGTWELIST DQVLPYFLKK NIGPEPTYET FDEQIFREKL
160 170 180 190 200
QKSTKKIKPF LLEQTLVAGL GNIYVDEVLW LAKIHPEKVA NQLTESSIHL
210 220 230 240 250
LHDSIIEILQ KAIKLGGSSI RTYSALGSTG KMQDELRVYG KTGEKCVRCG
260 270
NEIQKIKVAG RGTHFCPFCQ QK
Length:272
Mass (Da):31,215
Last modified:January 23, 2007 - v3
Checksum:i5E4F711CFFB297F2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005176 Genomic DNA Translation: AAK04451.1
PIRiA86669
RefSeqiNP_266509.1, NC_002662.1
WP_010905298.1, NC_002662.1

Genome annotation databases

EnsemblBacteriaiAAK04451; AAK04451; L0271
GeneIDi1113964
KEGGilla:L0271
PATRICifig|272623.7.peg.387

Similar proteinsi

Entry informationi

Entry nameiFPG_LACLA
AccessioniPrimary (citable) accession number: Q9CIK4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 120 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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