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Q7VN67

- FPG_HAEDU

UniProt

Q7VN67 - FPG_HAEDU

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Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Haemophilus ducreyi (strain 35000HP / ATCC 700724)
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 sitei57 – 571Proton donor; for beta-elimination activityUniRule annotation
Binding sitei92 – 921DNAUniRule annotation
Binding sitei111 – 1111DNAUniRule annotation
Binding sitei152 – 1521DNAUniRule annotation
Active sitei261 – 2611Proton donor; for delta-elimination activityUniRule annotation

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

BioCyciHDUC233412:GH5F-649-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:HD_0710
OrganismiHaemophilus ducreyi (strain 35000HP / ATCC 700724)
Taxonomic identifieri233412 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
ProteomesiUP000001022: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 274273Formamidopyrimidine-DNA glycosylasePRO_0000170827Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi233412.HD0710.

Structurei

3D structure databases

ProteinModelPortaliQ7VN67.
SMRiQ7VN67. Positions 2-271.
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 fingeri237 – 27135FPG-typeUniRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0266.
KOiK10563.
OMAiDHVDLKL.
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.

Q7VN67-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPELPEVETC LRGIEPYLAG QTIQQIVIRT PKLRWPISAE LCAMSGAKIL
60 70 80 90 100
ALSRRAKYLI IHTERGDILV HLGMSGSLTL LNSSQPTKAS KHDHVDLITE
110 120 130 140 150
AGIILRYNDP RKFGAWLWAK QAENYPLITK LGPEPLSDTF TSDYLFKKSR
160 170 180 190 200
NKTVAVKNFI MNNDIVVGVG NIYASESLFM AGVHPELAAQ NLTEKQCVQL
210 220 230 240 250
RNVIQAVLTK AIIQGGTTLK DFTQPDGKPG YFAQVLQVYG RKGEECRECG
260 270
TLIQAKVIGQ RNSYFCPDCQ PLPK
Length:274
Mass (Da):30,443
Last modified:January 23, 2007 - v3
Checksum:i1E08BCA4B0D17F5E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017143 Genomic DNA. Translation: AAP95626.1.
RefSeqiNP_873237.1. NC_002940.2.

Genome annotation databases

EnsemblBacteriaiAAP95626; AAP95626; HD_0710.
GeneIDi1490671.
KEGGihdu:HD0710.
PATRICi20177859. VBIHaeDuc133973_0581.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017143 Genomic DNA. Translation: AAP95626.1 .
RefSeqi NP_873237.1. NC_002940.2.

3D structure databases

ProteinModelPortali Q7VN67.
SMRi Q7VN67. Positions 2-271.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 233412.HD0710.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAP95626 ; AAP95626 ; HD_0710 .
GeneIDi 1490671.
KEGGi hdu:HD0710.
PATRICi 20177859. VBIHaeDuc133973_0581.

Phylogenomic databases

eggNOGi COG0266.
KOi K10563.
OMAi DHVDLKL.
OrthoDBi EOG6QP131.

Enzyme and pathway databases

BioCyci HDUC233412:GH5F-649-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 Haemophilus ducreyi."
    Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L., Nguyen D., Wang J., Forst C., Hood L.
    Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 35000HP / ATCC 700724.

Entry informationi

Entry nameiFPG_HAEDU
AccessioniPrimary (citable) accession number: Q7VN67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 80 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