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Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL 2338)
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 sitei61Proton donor; for beta-elimination activityUniRule annotation1
Binding sitei102DNAUniRule annotation1
Binding sitei122DNAUniRule annotation1
Binding sitei168DNAUniRule annotation1
Active sitei278Proton donor; for delta-elimination activityUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri254 – 288FPG-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

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:SACE_6099
OrganismiSaccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL 2338)
Taxonomic identifieri405948 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaPseudonocardialesPseudonocardiaceaeSaccharopolyspora
Proteomesi
  • UP000006728 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_10000087682 – 295Formamidopyrimidine-DNA glycosylaseAdd BLAST294

Proteomic databases

PRIDEiA4FMJ7

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi405948.SeryN2_010100021462

Structurei

3D structure databases

ProteinModelPortaliA4FMJ7
SMRiA4FMJ7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FPG family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri254 – 288FPG-typeUniRule annotationAdd BLAST35

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG4105ERD Bacteria
COG0266 LUCA
HOGENOMiHOG000020884
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
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
PS51066 ZF_FPG_2, 1 hit

Sequencei

Sequence statusi: Complete.

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

A4FMJ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPELPEVEVV RRGVAAHVVG RTVSEVEVLH PRSVRRHVPG PDDFATRLAG
60 70 80 90 100
RCLTAARRRG KYMWLELGGG PEEVDAGEAV LAHLGMSGQL LVQPDEAPDE
110 120 130 140 150
THLRVRFRFD DGGPQLRFVD QRTFGGLSLT ELVSVDGVAV PEPVAHIAPD
160 170 180 190 200
PLEPVFDLEA AVARMRKRRT GVKRALLDQT LVSGIGNIYA DEALWRAKLH
210 220 230 240 250
WARPTANLTR PQARTLLVAA VEVMQAALTA GGTSFDDLYV NVNGESGYFD
260 270 280 290
RSLAVYGQAG LPCPRCGTPV RRDAFMNRSS YSCPRCQPTP RNPHY
Length:295
Mass (Da):32,348
Last modified:April 17, 2007 - v1
Checksum:i92237F8778B13061
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM420293 Genomic DNA Translation: CAM05272.1
RefSeqiWP_009947561.1, NZ_PDBV01000001.1

Genome annotation databases

EnsemblBacteriaiCAM05272; CAM05272; SACE_6099
KEGGisen:SACE_6099

Similar proteinsi

Entry informationi

Entry nameiFPG_SACEN
AccessioniPrimary (citable) accession number: A4FMJ7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 17, 2007
Last modified: May 23, 2018
This is version 76 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

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