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

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.
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

Zn2+Note: Binds 1 zinc ion per subunit.

Sites

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

Regions

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

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 glycosylasePRO_0000170830Add
BLAST

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
273
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1815Combined sources
Beta strandi25 – 295Combined sources
Helixi31 – 333Combined sources
Helixi38 – 458Combined sources
Beta strandi49 – 568Combined sources
Beta strandi59 – 646Combined sources
Turni65 – 673Combined sources
Beta strandi68 – 736Combined sources
Turni75 – 773Combined sources
Beta strandi79 – 835Combined sources
Beta strandi93 – 986Combined sources
Beta strandi103 – 1075Combined sources
Beta strandi114 – 1196Combined sources
Helixi120 – 1223Combined sources
Helixi123 – 1297Combined sources
Helixi144 – 1529Combined sources
Helixi158 – 1636Combined sources
Beta strandi165 – 1695Combined sources
Helixi173 – 18210Combined sources
Helixi191 – 1933Combined sources
Helixi196 – 21520Combined sources
Beta strandi221 – 2233Combined sources
Turni227 – 2304Combined sources
Helixi233 – 2364Combined sources
Turni248 – 2503Combined sources
Beta strandi255 – 2595Combined sources
Beta strandi262 – 2665Combined sources
Turni268 – 2703Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42371.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 7619DNA bindingAdd
BLAST
Regioni162 – 17211DNA bindingAdd
BLAST

Sequence similaritiesi

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

Zinc finger

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

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

        10         20         30         40         50
MPELPEVETV RRELEKRIVG QKIISIEATY PRMVLTGFEQ LKKELTGKTI
60 70 80 90 100
QGISRRGKYL IFEIGDDFRL ISHLRMEGKY RLATLDAPRE KHDHLTMKFA
110 120 130 140 150
DGQLIYADVR KFGTWELIST DQVLPYFLKK KIGPEPTYDE DFDEKLFREK
160 170 180 190 200
LRKSTKKIKP YLLEQTLVAG LGNIYVDEVL WLAKIHPEKE TNQLIESSIH
210 220 230 240 250
LLHDSIIEIL QKAIKLGGSS IRTYSALGST GKMQNELQVY GKTGEKCSRC
260 270
GAEIQKIKVA GRGTHFCPVC QQK
Length:273
Mass (Da):31,310
Last modified:January 23, 2007 - v3
Checksum:iEB16055C5E09840F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74298 Genomic DNA. Translation: CAA52351.1.
M88106 Genomic DNA. No translation available.
PIRiS39200.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74298 Genomic DNA. Translation: CAA52351.1 .
M88106 Genomic DNA. No translation available.
PIRi S39200.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 108 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