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Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Lactococcus lactis subsp. cremoris (Streptococcus cremoris)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei2Schiff-base intermediate with DNACurated1
Active sitei3Proton donorCurated1
Active sitei58Proton donor; for beta-elimination activityCurated1
Binding sitei92DNA1
Binding sitei110DNA1
Active sitei262Proton donor; for delta-elimination activityCurated1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri238 – 272FPG-typeAdd BLAST35

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

BRENDAi3.2.2.23. 2903.

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)DescriptionActionsGraphical viewLength
Mutagenesisi2P → G: Loss of activity. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001708302 – 273Formamidopyrimidine-DNA glycosylaseAdd BLAST272

Proteomic databases

PRIDEiP42371.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi416870.llmg_0373.

Structurei

Secondary structure

1273
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 18Combined sources15
Beta strandi25 – 29Combined sources5
Helixi31 – 33Combined sources3
Helixi38 – 45Combined sources8
Beta strandi49 – 56Combined sources8
Beta strandi59 – 64Combined sources6
Turni65 – 67Combined sources3
Beta strandi68 – 73Combined sources6
Turni75 – 77Combined sources3
Beta strandi79 – 83Combined sources5
Beta strandi93 – 98Combined sources6
Beta strandi103 – 107Combined sources5
Beta strandi114 – 119Combined sources6
Helixi120 – 122Combined sources3
Helixi123 – 129Combined sources7
Helixi144 – 153Combined sources10
Helixi158 – 163Combined sources6
Beta strandi165 – 169Combined sources5
Helixi173 – 182Combined sources10
Helixi191 – 193Combined sources3
Helixi196 – 215Combined sources20
Beta strandi221 – 223Combined sources3
Turni227 – 230Combined sources4
Helixi233 – 236Combined sources4
Turni248 – 250Combined sources3
Beta strandi255 – 259Combined sources5
Beta strandi262 – 266Combined sources5
Turni268 – 270Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4PCZX-ray1.70A2-273[»]
4PD2X-ray1.65A2-273[»]
4PDGX-ray2.40A2-273[»]
4PDIX-ray2.10A2-273[»]
ProteinModelPortaliP42371.
SMRiP42371.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42371.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni58 – 76DNA bindingAdd BLAST19
Regioni162 – 172DNA bindingAdd BLAST11

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri238 – 272FPG-typeAdd BLAST35

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG4105ERD. Bacteria.
COG0266. LUCA.

Family and domain databases

HAMAPiMF_00103. Fapy_DNA_glycosyl. 1 hit.
InterProiIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
IPR015887. DNA_glyclase_Znf_dom_DNA_BS.
IPR020629. Formamido-pyr_DNA_Glyclase.
IPR012319. FPG_cat.
IPR010979. Ribosomal_S13-like_H2TH.
IPR000214. Znf_DNA_glyclase/AP_lyase.
IPR010663. Znf_FPG/IleRS.
[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.
SM01232. H2TH. 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.
PIRiS39200.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4PCZX-ray1.70A2-273[»]
4PD2X-ray1.65A2-273[»]
4PDGX-ray2.40A2-273[»]
4PDIX-ray2.10A2-273[»]
ProteinModelPortaliP42371.
SMRiP42371.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi416870.llmg_0373.

Proteomic databases

PRIDEiP42371.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105ERD. Bacteria.
COG0266. LUCA.

Enzyme and pathway databases

BRENDAi3.2.2.23. 2903.

Miscellaneous databases

EvolutionaryTraceiP42371.

Family and domain databases

HAMAPiMF_00103. Fapy_DNA_glycosyl. 1 hit.
InterProiIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
IPR015887. DNA_glyclase_Znf_dom_DNA_BS.
IPR020629. Formamido-pyr_DNA_Glyclase.
IPR012319. FPG_cat.
IPR010979. Ribosomal_S13-like_H2TH.
IPR000214. Znf_DNA_glyclase/AP_lyase.
IPR010663. Znf_FPG/IleRS.
[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.
SM01232. H2TH. 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]
ProtoNetiSearch...

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 2, 2016
This is version 119 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

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 one 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.