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O50606

- FPG_THET8

UniProt

O50606 - FPG_THET8

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Protein

Formamidopyrimidine-DNA glycosylase

Gene
mutM, fpg, TTHA1806
Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - 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.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

Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21Schiff-base intermediate with DNA Inferred
Active sitei3 – 31Proton donor Inferred
Active sitei53 – 531Proton donor; for beta-elimination activity Inferred
Binding sitei82 – 821DNA By similarity
Binding sitei100 – 1001DNA By similarity
Active sitei254 – 2541Proton donor; for delta-elimination activity Inferred

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri230 – 26435FPG-typeUniRule annotationAdd
BLAST

GO - Molecular functioni

  1. damaged DNA binding Source: InterPro
  2. oxidized purine nucleobase lesion DNA N-glycosylase activity Source: UniProtKB-HAMAP
  3. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. base-excision repair Source: InterPro
  2. nucleotide-excision repair Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase, Lyase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1851-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
ProteomesiUP000000532: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedUniRule annotation
Chaini2 – 267266Formamidopyrimidine-DNA glycosylaseUniRule annotationPRO_0000170880Add
BLAST

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi300852.TTHA1806.

Structurei

Secondary structure

1
267
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1815
Beta strandi22 – 276
Turni31 – 333
Beta strandi34 – 363
Helixi37 – 404
Beta strandi43 – 519
Beta strandi54 – 596
Turni60 – 623
Beta strandi63 – 686
Turni70 – 723
Beta strandi74 – 785
Beta strandi83 – 919
Beta strandi93 – 975
Beta strandi104 – 1096
Helixi118 – 1214
Helixi133 – 1419
Helixi147 – 1537
Beta strandi154 – 1574
Helixi162 – 17110
Beta strandi176 – 1794
Helixi180 – 1823
Helixi185 – 20420
Helixi226 – 2283
Turni240 – 2423
Beta strandi247 – 2537
Beta strandi255 – 2584
Turni260 – 2645

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EE8X-ray1.90A/B2-267[»]
ProteinModelPortaliO50606.
SMRiO50606. Positions 2-267.

Miscellaneous databases

EvolutionaryTraceiO50606.

Family & Domainsi

Sequence similaritiesi

Belongs to the FPG family.

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri230 – 26435FPG-typeUniRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0266.
HOGENOMiHOG000020884.
KOiK10563.
OMAiIYCSESL.
OrthoDBiEOG6QP131.
PhylomeDBiO50606.

Family and domain databases

HAMAPiMF_00103. Fapy_DNA_glycosyl.
InterProiIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
IPR015887. DNA_glyclase_Znf_dom_DNA_BS.
IPR000191. DNA_glycosylase/AP_lyase.
IPR012319. DNA_glycosylase/AP_lyase_cat.
IPR020629. Formamido-pyr_DNA_Glyclase.
IPR010979. Ribosomal_S13-like_H2TH.
IPR000214. Znf_DNA_glyclase/AP_lyase.
IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
[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.
[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

MPELPEVETT RRRLRPLVLG QTLRQVVHRD PARYRNTALA EGRRILEVDR    50
RGKFLLFALE GGVELVAHLG MTGGFRLEPT PHTRAALVLE GRTLYFHDPR 100
RFGRLFGVRR GDYREIPLLL RLGPEPLSEA FAFPGFFRGL KESARPLKAL 150
LLDQRLAAGV GNIYADEALF RARLSPFRPA RSLTEEEARR LYRALREVLA 200
EAVELGGSTL SDQSYRQPDG LPGGFQTRHA VYGREGLPCP ACGRPVERRV 250
VAGRGTHFCP TCQGEGP 267
Length:267
Mass (Da):29,915
Last modified:January 23, 2007 - v3
Checksum:iCDEAEAB2BED893EA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AB008520 Genomic DNA. Translation: BAA24892.1 .
AP008226 Genomic DNA. Translation: BAD71629.1 .
RefSeqi WP_011173830.1. NC_006461.1.
YP_145072.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EE8 X-ray 1.90 A/B 2-267 [» ]
ProteinModelPortali O50606.
SMRi O50606. Positions 2-267.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 300852.TTHA1806.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD71629 ; BAD71629 ; BAD71629 .
GeneIDi 3169771.
KEGGi ttj:TTHA1806.
PATRICi 23958581. VBITheThe93045_1777.

Phylogenomic databases

eggNOGi COG0266.
HOGENOMi HOG000020884.
KOi K10563.
OMAi IYCSESL.
OrthoDBi EOG6QP131.
PhylomeDBi O50606.

Enzyme and pathway databases

BioCyci TTHE300852:GH8R-1851-MONOMER.

Miscellaneous databases

EvolutionaryTracei O50606.

Family and domain databases

HAMAPi MF_00103. Fapy_DNA_glycosyl.
InterProi IPR015886. DNA_glyclase/AP_lyase_DNA-bd.
IPR015887. DNA_glyclase_Znf_dom_DNA_BS.
IPR000191. DNA_glycosylase/AP_lyase.
IPR012319. DNA_glycosylase/AP_lyase_cat.
IPR020629. Formamido-pyr_DNA_Glyclase.
IPR010979. Ribosomal_S13-like_H2TH.
IPR000214. Znf_DNA_glyclase/AP_lyase.
IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
[Graphical view ]
Pfami PF01149. Fapy_DNA_glyco. 1 hit.
PF06831. H2TH. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view ]
SMARTi SM00898. Fapy_DNA_glyco. 1 hit.
[Graphical view ]
SUPFAMi SSF46946. SSF46946. 1 hit.
SSF81624. SSF81624. 1 hit.
TIGRFAMsi TIGR00577. fpg. 1 hit.
PROSITEi PS51068. FPG_CAT. 1 hit.
PS01242. ZF_FPG_1. 1 hit.
PS51066. ZF_FPG_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Thermostable repair enzyme for oxidative DNA damage from extremely thermophilic bacterium, Thermus thermophilus HB8."
    Mikawa T., Kato R., Sugahara M., Kuramitsu S.
    Nucleic Acids Res. 26:903-910(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
  2. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.
  3. "Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8."
    Sugahara M., Mikawa T., Kumasaka T., Yamamoto M., Kato R., Fukuyama K., Inoue Y., Kuramitsu S.
    EMBO J. 19:3857-3869(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

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: September 3, 2014
This is version 113 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

External Data

Dasty 3

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