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.

P42371

- FPG_LACLC

UniProt

P42371 - FPG_LACLC

(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
Organism
Lactococcus lactis subsp. cremoris (Streptococcus cremoris)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.1 Publication

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21Schiff-base intermediate with DNA Inferred
Active sitei3 – 31Proton donor Inferred
Active sitei58 – 581Proton donor; for beta-elimination activity Inferred
Binding sitei92 – 921DNA
Binding sitei110 – 1101DNA
Active sitei262 – 2621Proton donor; for delta-elimination activity Inferred

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri238 – 27235FPG-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

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
OrganismiLactococcus lactis subsp. cremoris (Streptococcus cremoris)
Taxonomic identifieri1359 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21P → G: Loss of activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 273272Formamidopyrimidine-DNA glycosylaseUniRule annotation
PRO_0000170830Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1815
Beta strandi25 – 295
Helixi31 – 333
Helixi38 – 458
Beta strandi49 – 568
Beta strandi59 – 646
Turni65 – 673
Beta strandi68 – 736
Turni75 – 773
Beta strandi79 – 835
Beta strandi93 – 986
Beta strandi103 – 1075
Beta strandi114 – 1196
Helixi120 – 1223
Helixi123 – 1297
Helixi144 – 1529
Helixi158 – 1636
Beta strandi165 – 1695
Helixi173 – 18210
Helixi191 – 1933
Helixi196 – 21520
Beta strandi221 – 2233
Turni227 – 2304
Helixi233 – 2364
Turni248 – 2503
Beta strandi255 – 2595
Beta strandi262 – 2665
Turni268 – 2703

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KFVX-ray2.55A/B2-273[»]
1NNJX-ray1.90A2-273[»]
1PJIX-ray1.90A2-273[»]
1PJJX-ray1.90A2-273[»]
1PM5X-ray1.95A2-273[»]
1TDZX-ray1.80A1-273[»]
1XC8X-ray1.95A2-273[»]
2XZFX-ray1.80A2-273[»]
2XZUX-ray1.82A2-273[»]
3C58X-ray1.90A2-273[»]
ProteinModelPortaliP42371.
SMRiP42371. Positions 2-273.

Miscellaneous databases

EvolutionaryTraceiP42371.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 7619DNA bindingUniRule annotation
Add
BLAST
Regioni162 – 17211DNA bindingUniRule annotation
Add
BLAST

Sequence similaritiesi

Belongs to the FPG family.

Keywords - Domaini

Zinc-finger

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.

P42371-1 [UniParc]FASTAAdd to Basket

« Hide

MPELPEVETV RRELEKRIVG QKIISIEATY PRMVLTGFEQ LKKELTGKTI    50
QGISRRGKYL IFEIGDDFRL ISHLRMEGKY RLATLDAPRE KHDHLTMKFA 100
DGQLIYADVR KFGTWELIST DQVLPYFLKK KIGPEPTYDE DFDEKLFREK 150
LRKSTKKIKP YLLEQTLVAG LGNIYVDEVL WLAKIHPEKE TNQLIESSIH 200
LLHDSIIEIL QKAIKLGGSS IRTYSALGST GKMQNELQVY GKTGEKCSRC 250
GAEIQKIKVA GRGTHFCPVC QQK 273
Length:273
Mass (Da):31,310
Last modified:January 23, 2007 - v3
Checksum:iEB16055C5E09840F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X74298 Genomic DNA. Translation: CAA52351.1.
M88106 Genomic DNA. No translation available.
PIRiS39200.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X74298 Genomic DNA. Translation: CAA52351.1 .
M88106 Genomic DNA. No translation available.
PIRi S39200.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KFV X-ray 2.55 A/B 2-273 [» ]
1NNJ X-ray 1.90 A 2-273 [» ]
1PJI X-ray 1.90 A 2-273 [» ]
1PJJ X-ray 1.90 A 2-273 [» ]
1PM5 X-ray 1.95 A 2-273 [» ]
1TDZ X-ray 1.80 A 1-273 [» ]
1XC8 X-ray 1.95 A 2-273 [» ]
2XZF X-ray 1.80 A 2-273 [» ]
2XZU X-ray 1.82 A 2-273 [» ]
3C58 X-ray 1.90 A 2-273 [» ]
ProteinModelPortali P42371.
SMRi P42371. Positions 2-273.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P42371.

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. "Repair of oxidative DNA damage in Gram-positive bacteria: the Lactococcus lactis Fpg protein."
    Duwat P., de Oliveira R., Ehrlich S.D., Boiteux S.
    Microbiology 141:411-417(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-22, FUNCTION.
    Strain: NCDO 763 / ML3.
  2. "Use of degenerate primers for polymerase chain reaction cloning and sequencing of the Lactococcus lactis subsp. lactis recA gene."
    Duwat P., Ehrlich S.D., Gruss A.
    Appl. Environ. Microbiol. 58:2674-2678(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 194-273.
    Strain: NCDO 763 / ML3.
  3. "Crystal structure of the Lactococcus lactis formamidopyrimidine-DNA glycosylase bound to an abasic site analogue-containing DNA."
    Serre L., Pereira de Jesus K., Boiteux S., Zelwer C., Castaing B.
    EMBO J. 21:2854-2865(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-273 OF MUTANT GLY-2 IN COMPLEX WITH SUBSTRATE ANALOG.

Entry informationi

Entry nameiFPG_LACLC
AccessioniPrimary (citable) accession number: P42371
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 106 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The zinc finger is important for DNA binding.

Keywords - Technical termi

3D-structure, Direct protein sequencing, Multifunctional enzyme

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi