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Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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 sitei95DNABy similarity1
Binding sitei114DNABy similarity1
Active sitei265Proton donor; for delta-elimination activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri241 – 275FPG-typeAdd BLAST35

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase, Lyase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

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:NMA1505
OrganismiNeisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Taxonomic identifieri122587 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
Proteomesi
  • UP000000626 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001708422 – 275Formamidopyrimidine-DNA glycosylaseAdd BLAST274

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP57014.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FPG family.Curated
Contains 1 FPG-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri241 – 275FPG-typeAdd BLAST35

Keywords - Domaini

Zinc-finger

Phylogenomic databases

HOGENOMiHOG000020881.
KOiK10563.
OMAiWHRRGKY.

Family and domain databases

HAMAPiMF_00103. Fapy_DNA_glycosyl. 1 hit.
InterProiIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
IPR015887. DNA_glyclase_Znf_dom_DNA_BS.
IPR020629. Formamido-pyr_DNA_Glyclase.
IPR012319. FPG_cat.
IPR010979. Ribosomal_S13-like_H2TH.
IPR000214. Znf_DNA_glyclase/AP_lyase.
IPR010663. Znf_FPG/IleRS.
[Graphical view]
PfamiPF01149. Fapy_DNA_glyco. 1 hit.
PF06831. H2TH. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
SMARTiSM00898. Fapy_DNA_glyco. 1 hit.
SM01232. H2TH. 1 hit.
[Graphical view]
SUPFAMiSSF46946. SSF46946. 1 hit.
SSF81624. SSF81624. 1 hit.
TIGRFAMsiTIGR00577. fpg. 1 hit.
PROSITEiPS51068. FPG_CAT. 1 hit.
PS01242. ZF_FPG_1. 1 hit.
PS51066. ZF_FPG_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P57014-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPELPEVETT LRGIAPHIEG KTVEAVVLRQ LKLRWQINPD LGEILSGRQV
60 70 80 90 100
LSCGRRAKYL IVRFQTGILL IHLGMSGSLR IFTPSDGRIG RSDRHDHVDI
110 120 130 140 150
VFSDGTVMRY RDPRKFGAIL WYEGIEEHHP LLEKLGPEPL SEAFCTDYLY
160 170 180 190 200
VRLKAQKRAV KLALMDNAVV VGVGNIYANE SLFRAGISPH RPANRLKKKE
210 220 230 240 250
CALLVETVKA VLRRAIETGG STLRDFVDSD GKSGYFQQEY TVYGRHNQPC
260 270
PQCGGLVVKE TLGQRGTFYC PNCQK
Length:275
Mass (Da):30,904
Last modified:January 23, 2007 - v3
Checksum:i5DD06DB8F7C423C9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL157959 Genomic DNA. Translation: CAM08656.1.
PIRiB81842.
RefSeqiWP_002245999.1. NC_003116.1.

Genome annotation databases

EnsemblBacteriaiCAM08656; CAM08656; NMA1505.
KEGGinma:NMA1505.
PATRICi20364072. VBINeiMen132687_1740.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL157959 Genomic DNA. Translation: CAM08656.1.
PIRiB81842.
RefSeqiWP_002245999.1. NC_003116.1.

3D structure databases

ProteinModelPortaliP57014.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAM08656; CAM08656; NMA1505.
KEGGinma:NMA1505.
PATRICi20364072. VBINeiMen132687_1740.

Phylogenomic databases

HOGENOMiHOG000020881.
KOiK10563.
OMAiWHRRGKY.

Family and domain databases

HAMAPiMF_00103. Fapy_DNA_glycosyl. 1 hit.
InterProiIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
IPR015887. DNA_glyclase_Znf_dom_DNA_BS.
IPR020629. Formamido-pyr_DNA_Glyclase.
IPR012319. FPG_cat.
IPR010979. Ribosomal_S13-like_H2TH.
IPR000214. Znf_DNA_glyclase/AP_lyase.
IPR010663. Znf_FPG/IleRS.
[Graphical view]
PfamiPF01149. Fapy_DNA_glyco. 1 hit.
PF06831. H2TH. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
SMARTiSM00898. Fapy_DNA_glyco. 1 hit.
SM01232. H2TH. 1 hit.
[Graphical view]
SUPFAMiSSF46946. SSF46946. 1 hit.
SSF81624. SSF81624. 1 hit.
TIGRFAMsiTIGR00577. fpg. 1 hit.
PROSITEiPS51068. FPG_CAT. 1 hit.
PS01242. ZF_FPG_1. 1 hit.
PS51066. ZF_FPG_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFPG_NEIMA
AccessioniPrimary (citable) accession number: P57014
Secondary accession number(s): A1ISA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.