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Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
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 sitei57Proton donor; for beta-elimination activityBy similarity1
Binding sitei90DNABy similarity1
Binding sitei109DNABy similarity1
Binding sitei150DNABy similarity1
Active sitei259Proton donor; for delta-elimination activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri235 – 269FPG-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

BioCyciHINF71421:G1GJ1-986-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:HI_0946
OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifieri71421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
Proteomesi
  • UP000000579 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001708282 – 271Formamidopyrimidine-DNA glycosylaseAdd BLAST270

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi71421.HI0946

Structurei

3D structure databases

ProteinModelPortaliP44948
SMRiP44948
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FPG family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri235 – 269FPG-typeAdd BLAST35

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG4105ERD Bacteria
COG0266 LUCA
KOiK10563
OMAiRNSRLRW
PhylomeDBiP44948

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.

P44948-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPELPEVETA LRGISPYLKN FTIEKVVVRQ PKLRWAVSEE LITLKNVKIV
60 70 80 90 100
DLTRRAKYLI IHTEKGYIIG HLGMSGSVRI VPQDSAIDKH DHIDIVVNNG
110 120 130 140 150
KLLRYNDPRR FGAWLWTENL DDFHLFLKLG PEPLSDEFNA EYLFKKSRQK
160 170 180 190 200
STALKTFLMD NAVVVGVGNI YTNESLFICG IHPLKLAKNL TRNQCFSLVN
210 220 230 240 250
TIKDVLRKAI IQGGTTLKDF LQPDGRPGYF AQELLVYGNK DKPCPKCGGK
260 270
IESLIIGQRN SFFCPKCQKR G
Length:271
Mass (Da):30,772
Last modified:January 23, 2007 - v3
Checksum:i571E67EF1D0978E1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA Translation: AAC22606.1
PIRiA64104
RefSeqiNP_439106.1, NC_000907.1
WP_005693293.1, NC_000907.1

Genome annotation databases

EnsemblBacteriaiAAC22606; AAC22606; HI_0946
GeneIDi949949
KEGGihin:HI0946
PATRICifig|71421.8.peg.987

Similar proteinsi

Entry informationi

Entry nameiFPG_HAEIN
AccessioniPrimary (citable) accession number: P44948
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 130 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

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