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Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901)
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 sitei59Proton donor; for beta-elimination activityUniRule annotation1
Binding sitei93DNAUniRule annotation1
Binding sitei111DNAUniRule annotation1
Active sitei253Proton donor; for delta-elimination activityUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri229 – 263FPG-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

BioCyciCHYD246194:G1G5B-1541-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:CHY_1649
OrganismiCarboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901)
Taxonomic identifieri246194 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeCarboxydothermus
Proteomesi
  • UP000002706 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002284252 – 263Formamidopyrimidine-DNA glycosylaseAdd BLAST262

Proteomic databases

PRIDEiQ3ABL4

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi246194.CHY_1649

Structurei

3D structure databases

ProteinModelPortaliQ3ABL4
SMRiQ3ABL4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FPG family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri229 – 263FPG-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.

Q3ABL4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPELPEVETI KRTLAPKILG KTIYRVEVYL PKIIKNVSVE EFTRRVVGKE
60 70 80 90 100
IVALKRRGKY LLIDLSGKET VTVHLRMTGK LLILPKGSPK DKHTHAIFDL
110 120 130 140 150
GDLELHFNDI RQFGGFSFEM PEIGPEPLED EFTPEYLKTK LKASQKNLKA
160 170 180 190 200
VLLDQKIIAG IGNIYADEIL FEAGLSPKRI AASLSEDEAE ELFKAIRKIL
210 220 230 240 250
ALGIEYRGTS IRDYVDAENQ QGSFQRLLKV YGKNGSLCVR CNNVLIRERH
260
AGRSTHYCPH CQK
Length:263
Mass (Da):29,817
Last modified:January 23, 2007 - v3
Checksum:iE68363E06BA4CAFB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000141 Genomic DNA Translation: ABB15292.1
RefSeqiWP_011344545.1, NC_007503.1

Genome annotation databases

EnsemblBacteriaiABB15292; ABB15292; CHY_1649
KEGGichy:CHY_1649

Similar proteinsi

Entry informationi

Entry nameiFPG_CARHZ
AccessioniPrimary (citable) accession number: Q3ABL4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 88 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health