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.

Q65R59

- FPG_MANSM

UniProt

Q65R59 - FPG_MANSM

(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, MS1944
Organism
Mannheimia succiniciproducens (strain MBEL55E)
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 sitei57 – 571Proton donor; for beta-elimination activity By similarity
Binding sitei90 – 901DNA By similarity
Binding sitei109 – 1091DNA By similarity
Binding sitei150 – 1501DNA By similarity
Active sitei259 – 2591Proton donor; for delta-elimination activity By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri235 – 26935FPG-typeUniRule annotation
Add
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

BioCyciBMAN221988:GHGM-1999-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:MS1944
OrganismiMannheimia succiniciproducens (strain MBEL55E)
Taxonomic identifieri221988 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeBasfia
ProteomesiUP000000607: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 270269Formamidopyrimidine-DNA glycosylaseUniRule annotation
PRO_0000228446Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi221988.MS1944.

Structurei

3D structure databases

ProteinModelPortaliQ65R59.
SMRiQ65R59. Positions 2-269.

Family & Domainsi

Sequence similaritiesi

Belongs to the FPG family.

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0266.
HOGENOMiHOG000020881.
KOiK10563.
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.

Q65R59-1 [UniParc]FASTAAdd to Basket

« Hide

MPELPEVETA KNGITPYLEG YLIEKIIVRQ PKLRWEVSPQ LAQISQQKIT    50
ALSRRAKYLI IHTEQGYIIG HLGMSGSVRI VSARDPVDKH DHLDIVMNNG 100
KIMRYNDPRR FGTWLWSANL DEFHLFLKLG PEPLSDEFNA EYLFKKSRKK 150
QTPVKNFLMD NSVVVGVGNI YANETLFMCG LHPEKITAKL TKAQCALLVE 200
KIKQELKRAI EQGGTTLKDF LQPDGRPGYF AQELQIYGKK GAPCPNCGTK 250
IESLVVAQRN SYFCPKCQKK 270
Length:270
Mass (Da):30,693
Last modified:January 23, 2007 - v3
Checksum:i2FEECC1C9182CA75
GO

Sequence cautioni

The sequence AAU38551.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016827 Genomic DNA. Translation: AAU38551.1. Different initiation.
RefSeqiYP_089136.1. NC_006300.1.

Genome annotation databases

EnsemblBacteriaiAAU38551; AAU38551; MS1944.
GeneIDi3075401.
KEGGimsu:MS1944.
PATRICi22447141. VBIManSuc86752_1777.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016827 Genomic DNA. Translation: AAU38551.1 . Different initiation.
RefSeqi YP_089136.1. NC_006300.1.

3D structure databases

ProteinModelPortali Q65R59.
SMRi Q65R59. Positions 2-269.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 221988.MS1944.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAU38551 ; AAU38551 ; MS1944 .
GeneIDi 3075401.
KEGGi msu:MS1944.
PATRICi 22447141. VBIManSuc86752_1777.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci BMAN221988:GHGM-1999-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 genome sequence of the capnophilic rumen bacterium Mannheimia succiniciproducens."
    Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H., Jeong H., Hur C.G., Kim J.J.
    Nat. Biotechnol. 22:1275-1281(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MBEL55E.

Entry informationi

Entry nameiFPG_MANSM
AccessioniPrimary (citable) accession number: Q65R59
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