SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q5WYY6

- FPG_LEGPL

UniProt

Q5WYY6 - FPG_LEGPL

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Formamidopyrimidine-DNA glycosylase

Gene
mutM, fpg, lpl0599
Organism
Legionella pneumophila (strain Lens)
Status
Reviewed - Annotation score: 4 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 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 By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21Schiff-base intermediate with DNA By similarity
Active sitei3 – 31Proton donor By similarity
Active sitei58 – 581Proton donor; for beta-elimination activity By similarity
Binding sitei91 – 911DNA By similarity
Binding sitei110 – 1101DNA By similarity
Binding sitei152 – 1521DNA By similarity
Active sitei261 – 2611Proton donor; for delta-elimination activity By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri237 – 27135FPG-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

BioCyciLPNE297245:GJD4-643-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:lpl0599
OrganismiLegionella pneumophila (strain Lens)
Taxonomic identifieri297245 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella
ProteomesiUP000002517: Chromosome

Organism-specific databases

LegioListilpl0599.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 274273Formamidopyrimidine-DNA glycosylaseUniRule annotationPRO_0000228443Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi297245.lpl0599.

Structurei

3D structure databases

ProteinModelPortaliQ5WYY6.

Family & Domainsi

Sequence similaritiesi

Belongs to the FPG family.

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri237 – 27135FPG-typeUniRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0266.
HOGENOMiHOG000020881.
KOiK10563.
OMAiCATPMRR.
OrthoDBiEOG6QP131.

Family and domain databases

HAMAPiMF_00103. Fapy_DNA_glycosyl.
InterProiIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
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.
PS51066. ZF_FPG_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q5WYY6-1 [UniParc]FASTAAdd to Basket

« Hide

MPELPEVETT KQGIKPHLEG CMITSVQVRN QKLRLPVPLN LNELCEGKHI    50
TAITRRGKYI LLHMDKGYLL IHLGMSGHLR IVSQTANPQK HDHVDLHINN 100
GLALRFRDPR RFGLFIYIDE NPYQHPLLAH LGPEPLSDDF NSEYLLRKAA 150
NKSQSIKSFI MDSQIVVGIG NIYAAESLFL AKIHPNTSAK KITTEEFNSL 200
TGHIKKILES AIEAGGTTLR DFYSSDGKPG YFRFALKVYG RKNLPCLVCE 250
NKIETVVIAG RHSAFCPHCQ PIIT 274
Length:274
Mass (Da):30,816
Last modified:January 23, 2007 - v3
Checksum:i99D832DDB4B68447
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR628337 Genomic DNA. Translation: CAH14832.1.
RefSeqiYP_125962.1. NC_006369.1.

Genome annotation databases

EnsemblBacteriaiCAH14832; CAH14832; lpl0599.
GeneIDi3113709.
KEGGilpf:lpl0599.
PATRICi22314723. VBILegPne33733_0700.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR628337 Genomic DNA. Translation: CAH14832.1 .
RefSeqi YP_125962.1. NC_006369.1.

3D structure databases

ProteinModelPortali Q5WYY6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 297245.lpl0599.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAH14832 ; CAH14832 ; lpl0599 .
GeneIDi 3113709.
KEGGi lpf:lpl0599.
PATRICi 22314723. VBILegPne33733_0700.

Organism-specific databases

LegioListi lpl0599.

Phylogenomic databases

eggNOGi COG0266.
HOGENOMi HOG000020881.
KOi K10563.
OMAi CATPMRR.
OrthoDBi EOG6QP131.

Enzyme and pathway databases

BioCyci LPNE297245:GJD4-643-MONOMER.

Family and domain databases

HAMAPi MF_00103. Fapy_DNA_glycosyl.
InterProi IPR015886. DNA_glyclase/AP_lyase_DNA-bd.
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.
PS51066. ZF_FPG_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
    Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
    Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Lens.

Entry informationi

Entry nameiFPG_LEGPL
AccessioniPrimary (citable) accession number: Q5WYY6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 75 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

Complete proteome, Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi