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Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Trichodesmium erythraeum (strain IMS101)
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.UniRule annotation

Catalytic activityi

Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.UniRule 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 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 sitei108DNAUniRule annotation1
Binding sitei136DNAUniRule annotation1
Binding sitei181DNAUniRule annotation1
Active sitei290Proton donor; for delta-elimination activityUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri266 – 300FPG-typeUniRule annotationAdd 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

BioCyciTERY203124:G1G6S-1003-MONOMER

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
Ordered Locus Names:Tery_1015
OrganismiTrichodesmium erythraeum (strain IMS101)
Taxonomic identifieri203124 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeOscillatorialesMicrocoleaceaeTrichodesmium
Proteomesi
  • UP000008878 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_10000087872 – 300Formamidopyrimidine-DNA glycosylaseAdd BLAST299

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi203124.Tery_1015

Structurei

3D structure databases

ProteinModelPortaliQ117D2
SMRiQ117D2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FPG family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri266 – 300FPG-typeUniRule annotationAdd BLAST35

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG4105ERD Bacteria
COG0266 LUCA
HOGENOMiHOG000020885
KOiK10563
OMAiGVHLRMT
OrthoDBiPOG091H01RH

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.

Q117D2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPELPEVEIV KQGLNQLTLN KRILGGEVLL ERTLAYPISV ADFLRGLEGK
60 70 80 90 100
AIAQWHRQGK YLLAQLYKWG KKNSKLQEYE NEDGWLGVHL RMTGQLLWVN
110 120 130 140 150
PEESLHKHTR VRLFFGHNSS GDKDSSNYEL RFVDQRTFGK MWGVPPGKEI
160 170 180 190 200
SKVITGLQQL GLEPFSPEFS PKYLNKKLYK RHRPIKTALL DQTTIAGLGN
210 220 230 240 250
IYADEALFLS GIRPTTICKD LTEKQIEQLH LAILKVLQTA INAGGTTFSN
260 270 280 290 300
FLNVKGVNGN YGGVAWVYSR AGQPCRICNT PLEKIKLAGR STHFCPQCQK
Length:300
Mass (Da):33,875
Last modified:August 22, 2006 - v1
Checksum:i627B960F42068282
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000393 Genomic DNA Translation: ABG50392.1
RefSeqiWP_011610779.1, NC_008312.1

Genome annotation databases

EnsemblBacteriaiABG50392; ABG50392; Tery_1015
KEGGiter:Tery_1015

Similar proteinsi

Entry informationi

Entry nameiFPG_TRIEI
AccessioniPrimary (citable) accession number: Q117D2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 22, 2006
Last modified: May 23, 2018
This is version 83 of the entry and version 1 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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