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Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase, Lyase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

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
Contains 1 FPG-type zinc finger.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.
OMAiKVHGARI.
PhylomeDBiO50606.

Family and domain databases

HAMAPiMF_00103. Fapy_DNA_glycosyl. 1 hit.
InterProiIPR015886. 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.
[Graphical view]
PfamiPF01149. Fapy_DNA_glyco. 1 hit.
PF06831. H2TH. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
SMARTiSM00898. Fapy_DNA_glyco. 1 hit.
SM01232. H2TH. 1 hit.
[Graphical view]
SUPFAMiSSF46946. SSF46946. 1 hit.
SSF81624. SSF81624. 1 hit.
TIGRFAMsiTIGR00577. fpg. 1 hit.
PROSITEiPS51068. FPG_CAT. 1 hit.
PS01242. ZF_FPG_1. 1 hit.
PS51066. ZF_FPG_2. 1 hit.
[Graphical view]

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.
PATRICi23958581. VBITheThe93045_1777.

Cross-referencesi

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.

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...

Protein-protein interaction databases

STRINGi300852.TTHA1806.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD71629; BAD71629; BAD71629.
GeneIDi3169771.
KEGGittj:TTHA1806.
PATRICi23958581. VBITheThe93045_1777.

Phylogenomic databases

eggNOGiENOG4105ERD. Bacteria.
COG0266. LUCA.
HOGENOMiHOG000020884.
KOiK10563.
OMAiKVHGARI.
PhylomeDBiO50606.

Miscellaneous databases

EvolutionaryTraceiO50606.

Family and domain databases

HAMAPiMF_00103. Fapy_DNA_glycosyl. 1 hit.
InterProiIPR015886. 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.
[Graphical view]
PfamiPF01149. Fapy_DNA_glyco. 1 hit.
PF06831. H2TH. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
SMARTiSM00898. Fapy_DNA_glyco. 1 hit.
SM01232. H2TH. 1 hit.
[Graphical view]
SUPFAMiSSF46946. SSF46946. 1 hit.
SSF81624. SSF81624. 1 hit.
TIGRFAMsiTIGR00577. fpg. 1 hit.
PROSITEiPS51068. FPG_CAT. 1 hit.
PS01242. ZF_FPG_1. 1 hit.
PS51066. ZF_FPG_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFPG_THET8
AccessioniPrimary (citable) accession number: O50606
Secondary accession number(s): Q5SHC4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.