Skip Header

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

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Methylobacterium populi (strain ATCC BAA-705 / NCIMB 13946 / BJ001)
Status
Reviewed-Annotation score: 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

Zn2+UniRule annotationNote: 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 sitei106 – 1061DNAUniRule annotation
Binding sitei125 – 1251DNAUniRule annotation
Binding sitei168 – 1681DNAUniRule annotation
Active sitei285 – 2851Proton donor; for delta-elimination activityUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri259 – 29537FPG-typeUniRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

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

BioCyciMPOP441620:GHMI-4592-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:Mpop_4528
OrganismiMethylobacterium populi (strain ATCC BAA-705 / NCIMB 13946 / BJ001)
Taxonomic identifieri441620 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium
ProteomesiUP000007136 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 296295Formamidopyrimidine-DNA glycosylasePRO_1000094053Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi441620.Mpop_4528.

Structurei

3D structure databases

ProteinModelPortaliB1ZGU8.
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 fingeri259 – 29537FPG-typeUniRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0266.
HOGENOMiHOG000020881.
KOiK10563.
OMAiVCQPRPR.
OrthoDBiEOG6QP131.

Family and domain databases

HAMAPiMF_00103. Fapy_DNA_glycosyl.
InterProiIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
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.

B1ZGU8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPELPEVETV RRGLAPAMVG ARFARVTLRR PNLRFPFPER FAERLEGTTV
60 70 80 90 100
RELARRAKYL TAHLDSGESL ILHLGMSGRF DVRMPDGSNL SPGDFYLEGA
110 120 130 140 150
LGTPKHDHVV MAFANGATVT YNDARRFGFM DLVATRDLET CRHFAAMGVE
160 170 180 190 200
PLSDALDGAV LARLFARKIT PLKAALLDQR LIAGLGNIYV CEALHRSGLH
210 220 230 240 250
PALPAGALAK PDGAPTPKAK KLVKEIKAVL TEAVAAGGST LRDYARPDGE
260 270 280 290
RGAFQHGFRV YDRVGHACPT KGCTGRIGRI VQGGRSTFFC ETCQVR
Length:296
Mass (Da):32,192
Last modified:May 20, 2008 - v1
Checksum:i124AC7B5FD12961A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001029 Genomic DNA. Translation: ACB82626.1.
RefSeqiWP_012456228.1. NC_010725.1.
YP_001927161.1. NC_010725.1.

Genome annotation databases

EnsemblBacteriaiACB82626; ACB82626; Mpop_4528.
KEGGimpo:Mpop_4528.
PATRICi22566304. VBIMetPop124700_4548.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001029 Genomic DNA. Translation: ACB82626.1.
RefSeqiWP_012456228.1. NC_010725.1.
YP_001927161.1. NC_010725.1.

3D structure databases

ProteinModelPortaliB1ZGU8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi441620.Mpop_4528.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACB82626; ACB82626; Mpop_4528.
KEGGimpo:Mpop_4528.
PATRICi22566304. VBIMetPop124700_4548.

Phylogenomic databases

eggNOGiCOG0266.
HOGENOMiHOG000020881.
KOiK10563.
OMAiVCQPRPR.
OrthoDBiEOG6QP131.

Enzyme and pathway databases

BioCyciMPOP441620:GHMI-4592-MONOMER.

Family and domain databases

HAMAPiMF_00103. Fapy_DNA_glycosyl.
InterProiIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
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]
ProtoNetiSearch...

Publicationsi

  1. "Complete sequence of chromosome of Methylobacterium populi BJ001."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.
    , Kyrpides N., Mikhailova N., Marx C., Richardson P.
    Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-705 / NCIMB 13946 / BJ001.

Entry informationi

Entry nameiFPG_METPB
AccessioniPrimary (citable) accession number: B1ZGU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: May 27, 2015
This is version 52 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.