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P55044

- FPG_NEIMB

UniProt

P55044 - FPG_NEIMB

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Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Neisseria meningitidis serogroup B (strain MC58)
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 (By similarity).By similarity

Catalytic activityi

Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.
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.

Cofactori

Binds 1 zinc ion per subunit.By similarity

Sites

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

Regions

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

BioCyciNMEN122586:GHGG-1333-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:NMB1295
OrganismiNeisseria meningitidis serogroup B (strain MC58)
Taxonomic identifieri122586 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
ProteomesiUP000000425: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 275274Formamidopyrimidine-DNA glycosylasePRO_0000170843Add
BLAST

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi122586.NMB1295.

Structurei

3D structure databases

ProteinModelPortaliP55044.
SMRiP55044. Positions 2-275.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Zinc finger

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

P55044-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPELPEVETT LRGIAPHIEG KTVEAVVLRQ LKLRWQINPD LGEILSGRQV
60 70 80 90 100
LSCGRRAKYL LIRFQTGVLL IHLGMSGSLR IFTPSDGRIG RPDRHDHVDI
110 120 130 140 150
VFSDGTVMRY RDPRKFGAIL WYEGIEEHHP LLEKLGPEPL SEAFCADYLY
160 170 180 190 200
ARLKAQKRAV KLALMDNAVV VGVGNIYANE SLFRAGISPH RPANRLKKKE
210 220 230 240 250
CALLVETVKA VLQRAIETGG STLRDFVDSD GKSGYFQQEY TVYGRHNQPC
260 270
PRCGGLVVKE TLGQRGTFYC PNCQK
Length:275
Mass (Da):30,856
Last modified:January 23, 2007 - v4
Checksum:i29A38C945C5EC559
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 622LI → IV in AAB01505. (PubMed:8586265)Curated
Sequence conflicti66 – 683TGV → KGI in AAB01505. (PubMed:8586265)Curated
Sequence conflicti151 – 1511A → V in AAB01505. (PubMed:8586265)Curated
Sequence conflicti213 – 2131Q → R in AAB01505. (PubMed:8586265)Curated
Sequence conflicti252 – 2521R → Q in AAB01505. (PubMed:8586265)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U21808 Genomic DNA. Translation: AAB01505.1.
AE002098 Genomic DNA. Translation: AAF41671.1.
PIRiB81099.
RefSeqiNP_274315.1. NC_003112.2.

Genome annotation databases

EnsemblBacteriaiAAF41671; AAF41671; NMB1295.
GeneIDi903717.
KEGGinme:NMB1295.
PATRICi20358219. VBINeiMen85645_1621.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U21808 Genomic DNA. Translation: AAB01505.1 .
AE002098 Genomic DNA. Translation: AAF41671.1 .
PIRi B81099.
RefSeqi NP_274315.1. NC_003112.2.

3D structure databases

ProteinModelPortali P55044.
SMRi P55044. Positions 2-275.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 122586.NMB1295.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAF41671 ; AAF41671 ; NMB1295 .
GeneIDi 903717.
KEGGi nme:NMB1295.
PATRICi 20358219. VBINeiMen85645_1621.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci NMEN122586:GHGG-1333-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

« Hide 'large scale' publications
  1. "Co-transcription of a homologue of the formamidopyrimidine-DNA glycosylase (fpg) and lysophosphatidic acid acyltransferase (nlaA) in Neisseria meningitidis."
    Swartley J.S., Stephens D.S.
    FEMS Microbiol. Lett. 134:171-176(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MC58.

Entry informationi

Entry nameiFPG_NEIMB
AccessioniPrimary (citable) accession number: P55044
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: October 1, 2014
This is version 112 of the entry and version 4 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