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Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
Status
Reviewed-Annotation score: Annotation score: 4 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 sitei59Proton donor; for beta-elimination activityBy similarity1
Binding sitei97DNABy similarity1
Binding sitei116DNABy similarity1
Active sitei270Proton donor; for delta-elimination activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri246 – 280FPG-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:syc0230_c
OrganismiSynechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
Taxonomic identifieri269084 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesSynechococcaceaeSynechococcus
Proteomesi
  • UP000001175 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001708772 – 282Formamidopyrimidine-DNA glycosylaseAdd BLAST281

Proteomic databases

PRIDEiQ08079.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi269084.syc0230_c.

Structurei

3D structure databases

ProteinModelPortaliQ08079.
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 fingeri246 – 280FPG-typeAdd BLAST35

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG4105ERD. Bacteria.
COG0266. LUCA.
HOGENOMiHOG000020885.
KOiK10563.
OrthoDBiPOG091H01RH.

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.

Q08079-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPELPEVETV RRGLTQQTLQ RVCTGGEVLL SRTIATPTPE LFLVALQQTQ
60 70 80 90 100
IQEWRRRGKY LLADLSREGE PAGTWGVHLR MTGQFFWTEP ATPLTKHTRV
110 120 130 140 150
RLRFEGDREL RFIDIRSFGQ MWWVPPDRPV ESVITGLSKL GPEPFAPEFT
160 170 180 190 200
ARYLRDRLRR SQRPIKTALL DQSLVAGIGN IYADESLFRT GIHPTTPSDR
210 220 230 240 250
LTKIQAEKLR EAIVEVLTAS IGAGGTTFSD FRDLTGVNGN YGGQAWVYGR
260 270 280
KDQPCRTCGT PIQKLKLAGR SSHFCPRCQP CS
Length:282
Mass (Da):31,794
Last modified:January 23, 2007 - v4
Checksum:iD13CE1DCD43503B1
GO

Sequence cautioni

The sequence BAD78420 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008231 Genomic DNA. Translation: BAD78420.1. Different initiation.
M99432 Genomic DNA. Translation: AAA18569.2.
RefSeqiWP_011377983.1. NC_006576.1.

Genome annotation databases

EnsemblBacteriaiBAD78420; BAD78420; syc0230_c.
KEGGisyc:syc0230_c.
PATRICi32485994. VBISynElo117686_0274.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008231 Genomic DNA. Translation: BAD78420.1. Different initiation.
M99432 Genomic DNA. Translation: AAA18569.2.
RefSeqiWP_011377983.1. NC_006576.1.

3D structure databases

ProteinModelPortaliQ08079.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi269084.syc0230_c.

Proteomic databases

PRIDEiQ08079.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD78420; BAD78420; syc0230_c.
KEGGisyc:syc0230_c.
PATRICi32485994. VBISynElo117686_0274.

Phylogenomic databases

eggNOGiENOG4105ERD. Bacteria.
COG0266. LUCA.
HOGENOMiHOG000020885.
KOiK10563.
OrthoDBiPOG091H01RH.

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_SYNP6
AccessioniPrimary (citable) accession number: Q08079
Secondary accession number(s): Q5N5J8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 116 of the entry and version 4 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.