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Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei2Schiff-base intermediate with DNACurated1
Active sitei3Proton donorCurated1
Active sitei53Proton donor; for beta-elimination activityCurated1
Binding sitei82DNABy similarity1
Binding sitei100DNABy similarity1
Active sitei254Proton donor; for delta-elimination activityCurated1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri230 – 264FPG-typeAdd 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

BioCyciTTHE300852:G1GKC-1815-MONOMER

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:TTHA1806
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001708802 – 267Formamidopyrimidine-DNA glycosylaseAdd BLAST266

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi300852.TTHA1806

Structurei

Secondary structure

1267
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 18Combined sources15
Beta strandi22 – 27Combined sources6
Turni31 – 33Combined sources3
Beta strandi34 – 36Combined sources3
Helixi37 – 40Combined sources4
Beta strandi43 – 51Combined sources9
Beta strandi54 – 59Combined sources6
Turni60 – 62Combined sources3
Beta strandi63 – 68Combined sources6
Turni70 – 72Combined sources3
Beta strandi74 – 78Combined sources5
Beta strandi83 – 91Combined sources9
Beta strandi93 – 97Combined sources5
Beta strandi104 – 109Combined sources6
Helixi118 – 121Combined sources4
Helixi133 – 141Combined sources9
Helixi147 – 153Combined sources7
Beta strandi154 – 157Combined sources4
Helixi162 – 171Combined sources10
Beta strandi176 – 179Combined sources4
Helixi180 – 182Combined sources3
Helixi185 – 204Combined sources20
Helixi226 – 228Combined sources3
Turni240 – 242Combined sources3
Beta strandi247 – 253Combined sources7
Beta strandi255 – 258Combined sources4
Turni260 – 264Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EE8X-ray1.90A/B2-267[»]
ProteinModelPortaliO50606
SMRiO50606
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO50606

Family & Domainsi

Sequence similaritiesi

Belongs to the FPG family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri230 – 264FPG-typeAdd BLAST35

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG4105ERD Bacteria
COG0266 LUCA
HOGENOMiHOG000020884
KOiK10563
OMAiGVHLRMT
PhylomeDBiO50606

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.

O50606-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPELPEVETT RRRLRPLVLG QTLRQVVHRD PARYRNTALA EGRRILEVDR
60 70 80 90 100
RGKFLLFALE GGVELVAHLG MTGGFRLEPT PHTRAALVLE GRTLYFHDPR
110 120 130 140 150
RFGRLFGVRR GDYREIPLLL RLGPEPLSEA FAFPGFFRGL KESARPLKAL
160 170 180 190 200
LLDQRLAAGV GNIYADEALF RARLSPFRPA RSLTEEEARR LYRALREVLA
210 220 230 240 250
EAVELGGSTL SDQSYRQPDG LPGGFQTRHA VYGREGLPCP ACGRPVERRV
260
VAGRGTHFCP TCQGEGP
Length:267
Mass (Da):29,915
Last modified:January 23, 2007 - v3
Checksum:iCDEAEAB2BED893EA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB008520 Genomic DNA Translation: BAA24892.1
AP008226 Genomic DNA Translation: BAD71629.1
RefSeqiWP_011173830.1, NC_006461.1
YP_145072.1, NC_006461.1

Genome annotation databases

EnsemblBacteriaiBAD71629; BAD71629; BAD71629
GeneIDi3169771
KEGGittj:TTHA1806
PATRICifig|300852.9.peg.1777

Similar proteinsi

Entry informationi

Entry nameiFPG_THET8
AccessioniPrimary (citable) accession number: O50606
Secondary accession number(s): Q5SHC4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 136 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

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health