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Q5F8Z9

- FPG_NEIG1

UniProt

Q5F8Z9 - FPG_NEIG1

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Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Status
Reviewed - 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

Binds 1 zinc ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21Schiff-base intermediate with DNAUniRule annotation
Active sitei3 – 31Proton donorUniRule annotation
Active sitei58 – 581Proton donor; for beta-elimination activityUniRule annotation
Binding sitei95 – 951DNAUniRule annotation
Binding sitei114 – 1141DNAUniRule annotation
Active sitei265 – 2651Proton donor; for delta-elimination activityUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri241 – 27535FPG-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

BioCyciNGON242231:GI2G-578-MONOMER.

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:NGO0610
OrganismiNeisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Taxonomic identifieri242231 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
ProteomesiUP000000535: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 275274Formamidopyrimidine-DNA glycosylasePRO_0000228450Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi242231.NGO0610.

Structurei

3D structure databases

ProteinModelPortaliQ5F8Z9.
SMRiQ5F8Z9. Positions 2-275.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FPG family.UniRule annotation
Contains 1 FPG-type zinc finger.UniRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri241 – 27535FPG-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.
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.

Q5F8Z9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPELPEVETT LRGIAPHIEG KTVEAVILRQ LKLRWQINPD LGEILSGRQV
60 70 80 90 100
LSCGRRAKYL IVRFQTGILL IHLGMSGSLR IFTPSDGRIG RPDRHDHVDI
110 120 130 140 150
VFSDGTVMRY RDPRKFGAIL WYEGIEERHP LLEKLGPEPL SEAFCTDYLY
160 170 180 190 200
AGLKAQKRAV KLALMDNTVV VGVGNIYANE SLFRAGISPH RPANRLKKKE
210 220 230 240 250
CAVLVETVKA VLQRAIETGG STLRDFVDSD GKSGYFQQEY TVYGRHNQPC
260 270
LRCGGLVVKE TLGQRGTFYC TNCQK
Length:275
Mass (Da):30,856
Last modified:January 23, 2007 - v3
Checksum:i687127ACD3A9EEA9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE004969 Genomic DNA. Translation: AAW89338.1.
RefSeqiYP_207750.1. NC_002946.2.

Genome annotation databases

EnsemblBacteriaiAAW89338; AAW89338; NGO0610.
GeneIDi3281724.
KEGGingo:NGO0610.
PATRICi20334300. VBINeiGon24812_0722.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE004969 Genomic DNA. Translation: AAW89338.1 .
RefSeqi YP_207750.1. NC_002946.2.

3D structure databases

ProteinModelPortali Q5F8Z9.
SMRi Q5F8Z9. Positions 2-275.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 242231.NGO0610.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAW89338 ; AAW89338 ; NGO0610 .
GeneIDi 3281724.
KEGGi ngo:NGO0610.
PATRICi 20334300. VBINeiGon24812_0722.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci NGON242231:GI2G-578-MONOMER.

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

  1. "The complete genome sequence of Neisseria gonorrhoeae."
    Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H.
    , Qi S., Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.
    Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700825 / FA 1090.

Entry informationi

Entry nameiFPG_NEIG1
AccessioniPrimary (citable) accession number: Q5F8Z9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: January 23, 2007
Last modified: October 1, 2014
This is version 72 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3