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Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Mycobacterium abscessus (strain ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC 1543)
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.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 sitei96DNAUniRule annotation1
Binding sitei115DNAUniRule annotation1
Binding sitei161DNAUniRule annotation1
Active sitei271Proton donor; for delta-elimination activityUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri247 – 281FPG-typeUniRule annotationAdd BLAST35

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, Glycosidase, Hydrolase, Lyase
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:MAB_3255c
OrganismiMycobacterium abscessus (strain ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC 1543)
Taxonomic identifieri561007 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium abscessus
Proteomesi
  • UP000007137 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_10000940562 – 286Formamidopyrimidine-DNA glycosylaseAdd BLAST285

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi561007.MAB_3255c.

Structurei

3D structure databases

ProteinModelPortaliB1MDL2.
SMRiB1MDL2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FPG family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri247 – 281FPG-typeUniRule annotationAdd BLAST35

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG4105ERD. Bacteria.
COG0266. LUCA.
HOGENOMiHOG000020884.
OMAiGVHLRMT.

Family and domain databases

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.
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.

B1MDL2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPELPEVEVV RRGLHHHLVG KTIASTLVYH ERAVRRQSGG AVELAGLLAG
60 70 80 90 100
QQISGTGRRG KYLWLTLEGS SGAQALVVHL GMSGQMLIGP ISRPQHLRIA
110 120 130 140 150
ATLDDGSVLS FVDQRTFGGW MVTDLVTVDG SELPEPVAHI ARDPLDELFE
160 170 180 190 200
IGAVVTRLRG KHTEIKRALL DQTVVSGVGN IYADEALWQA RVHGRRLTDG
210 220 230 240 250
MSRAKLTEVL DSAAAVMRLA LAQGGTSFDD LYVNVNGESG YFDRSLEAYG
260 270 280
REGEPCRRCG RAMRREAFMN RSSYFCPSCQ RLVEPR
Length:286
Mass (Da):31,350
Last modified:April 29, 2008 - v1
Checksum:i3EC469C1089D1C7D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU458896 Genomic DNA. Translation: CAM63331.1.

Genome annotation databases

EnsemblBacteriaiCAM63331; CAM63331; MAB_3255c.

Similar proteinsi

Entry informationi

Entry nameiFPG_MYCA9
AccessioniPrimary (citable) accession number: B1MDL2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: September 27, 2017
This is version 67 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, Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families