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C0RG65

- FPG_BRUMB

UniProt

C0RG65 - FPG_BRUMB

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Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Brucella melitensis biotype 2 (strain ATCC 23457)
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 sitei104 – 1041DNAUniRule annotation
Binding sitei127 – 1271DNAUniRule annotation
Binding sitei170 – 1701DNAUniRule annotation
Active sitei283 – 2831Proton donor; for delta-elimination activityUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri257 – 29337FPG-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

BioCyciBMEL546272:GJOX-2185-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:BMEA_A2244
OrganismiBrucella melitensis biotype 2 (strain ATCC 23457)
Taxonomic identifieri546272 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
ProteomesiUP000001748: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 293292Formamidopyrimidine-DNA glycosylasePRO_1000118881Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi546272.BMEA_A2244.

Structurei

3D structure databases

ProteinModelPortaliC0RG65.
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 fingeri257 – 29337FPG-typeUniRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0266.
HOGENOMiHOG000020881.
KOiK10563.
OMAiIYCSESL.
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.

C0RG65-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPELPEVETV RRGLQPFMEG ATVVRVEQNR PDLRFAFPEN FAERLSGRRI
60 70 80 90 100
EALGRRAKYL TVHLDDGLSI ISHLGMSGSF RIEAEDAQGL PGGFHHERSK
110 120 130 140 150
NSLHDHVVFH LMRPDGASAR IIYNDPRRFG FMLFAEKGAL EEHPLLKDLG
160 170 180 190 200
VEPTGNLLSG EVLAALFKGR RTPLKAALLD QRLIAGLGNI YVCEALWRPG
210 220 230 240 250
LSPMRAAGSV AGEMDVMERL AGAIRSVIAQ AIAAGGSSLK DYIQADGALG
260 270 280 290
YFQHSFSVYG REGKPCRNPA CGGTVERVVQ SGRSTFFCAS CQT
Length:293
Mass (Da):32,006
Last modified:May 5, 2009 - v1
Checksum:i2AF02788696CFB7B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001488 Genomic DNA. Translation: ACO01887.1.
RefSeqiYP_002733841.1. NC_012441.1.

Genome annotation databases

EnsemblBacteriaiACO01887; ACO01887; BMEA_A2244.
GeneIDi7676726.
KEGGibmi:BMEA_A2244.
PATRICi17840304. VBIBruMel14466_2263.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001488 Genomic DNA. Translation: ACO01887.1 .
RefSeqi YP_002733841.1. NC_012441.1.

3D structure databases

ProteinModelPortali C0RG65.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 546272.BMEA_A2244.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACO01887 ; ACO01887 ; BMEA_A2244 .
GeneIDi 7676726.
KEGGi bmi:BMEA_A2244.
PATRICi 17840304. VBIBruMel14466_2263.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci BMEL546272:GJOX-2185-MONOMER.

Miscellaneous databases

PROi C0RG65.

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. "Brucella melitensis ATCC 23457 whole genome shotgun sequencing project."
    Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., Lu J., Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Munk C.
    , Tapia R., Han C., Detter J.C., Bruce D., Brettin T.S.
    Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 23457.

Entry informationi

Entry nameiFPG_BRUMB
AccessioniPrimary (citable) accession number: C0RG65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 5, 2009
Last modified: October 1, 2014
This is version 39 of the entry and version 1 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