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Protein

Adenine DNA glycosylase

Gene

mutY

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Base excision repair (BER) glycosylase that initiates repair of A:oxoG to C:G by removing the inappropriately paired adenine base from the DNA backbone, generating an abasic site product (PubMed:25995449) (PubMed:14961129). 8-oxoguanine (oxoG) is a genotoxic DNA lesion resulting from oxidation of guanine; this residue is misread by replicative DNA polymerases, that insert adenine instead of cytosine opposite the oxidized damaged base. Shows a powerful dicrimination of A versus C, since it does not cleave cytosine in oxoG:C pairs (PubMed:25995449). May also be able to remove adenine from A:G mispairs, although this activity may not be physiologically relevant (PubMed:14961129).1 Publication1 Publication

Cofactori

[4Fe-4S] cluster2 PublicationsNote: Binds 1 [4Fe-4S] cluster (PubMed:14961129, PubMed:25995449). The cluster has a structural role (PubMed:14961129).2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei43 – 431Proton donor/acceptor1 Publication
Binding sitei126 – 1261Interacts with mispaired A in DNA substrate1 Publication
Sitei144 – 1441Transition state stabilizer2 Publications
Binding sitei188 – 1881Interacts with mispaired A in DNA substrate1 Publication
Metal bindingi198 – 1981Iron-sulfur (4Fe-4S)Combined sources5 Publications
Metal bindingi205 – 2051Iron-sulfur (4Fe-4S)Combined sources5 Publications
Metal bindingi208 – 2081Iron-sulfur (4Fe-4S)Combined sources5 Publications
Metal bindingi214 – 2141Iron-sulfur (4Fe-4S)Combined sources5 Publications
Binding sitei308 – 3081Interacts with oxoG in DNA substrate2 Publications

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB
  • DNA binding Source: UniProtKB
  • DNA N-glycosylase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • base-excision repair Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Adenine DNA glycosylase2 Publications (EC:3.2.2.-2 Publications)
Alternative name(s):
oxoG:A-specific adenine glycosylase1 Publication
Gene namesi
Name:mutY1 Publication
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi43 – 431E → Q: Loss of catalytic activity. 1 Publication
Mutagenesisi144 – 1441D → N: Loss of catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 366366Adenine DNA glycosylasePRO_0000435340Add
BLAST

Structurei

Secondary structure

1
366
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2415Combined sources
Helixi29 – 313Combined sources
Helixi36 – 4510Combined sources
Turni46 – 483Combined sources
Helixi51 – 6414Combined sources
Helixi68 – 725Combined sources
Helixi76 – 838Combined sources
Helixi90 – 10617Combined sources
Helixi114 – 1174Combined sources
Helixi125 – 13612Combined sources
Helixi145 – 15410Combined sources
Helixi166 – 17712Combined sources
Beta strandi180 – 1823Combined sources
Helixi183 – 19614Combined sources
Beta strandi200 – 2023Combined sources
Helixi205 – 2073Combined sources
Helixi211 – 2133Combined sources
Helixi215 – 2184Combined sources
Helixi222 – 2243Combined sources
Beta strandi235 – 24612Combined sources
Beta strandi249 – 2557Combined sources
Beta strandi258 – 2603Combined sources
Turni261 – 2644Combined sources
Beta strandi270 – 2723Combined sources
Beta strandi274 – 2763Combined sources
Helixi281 – 2844Combined sources
Beta strandi289 – 2913Combined sources
Beta strandi294 – 2963Combined sources
Beta strandi301 – 3066Combined sources
Beta strandi308 – 32114Combined sources
Beta strandi331 – 3355Combined sources
Helixi336 – 3416Combined sources
Helixi346 – 35813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RRQX-ray2.22A1-366[»]
1RRSX-ray2.40A1-366[»]
1VRLX-ray2.50A1-366[»]
3FSPX-ray2.20A1-366[»]
3G0QX-ray2.20A9-360[»]
4YOQX-ray2.21A1-366[»]
4YPHX-ray2.32A1-366[»]
4YPRX-ray2.59A/B1-366[»]
5DPKX-ray2.20A1-366[»]
ProteinModelPortaliP83847.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP83847.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini105 – 13329HhHSequence analysisAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 312Interacts with mispaired A in DNA substrate1 Publication
Regioni48 – 492Interacts with oxoG in DNA substrate2 Publications
Regioni86 – 883Interacts with oxoG in DNA substrate2 Publications

Sequence similaritiesi

Belongs to the Nth/MutY family.Curated
Contains 1 HhH domain.Sequence analysis

Family and domain databases

CDDicd03431. DNA_Glycosylase_C. 1 hit.
cd00056. ENDO3c. 1 hit.
Gene3Di1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
3.90.79.10. 1 hit.
InterProiIPR005760. A/G_AdeGlyc_MutY.
IPR011257. DNA_glycosylase.
IPR003651. Endouclease3_FeS-loop_motif.
IPR003265. HhH-GPD_domain.
IPR000445. HhH_motif.
IPR023170. HTH_base_excis_C.
IPR029119. MutY_C.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamiPF00633. HHH. 1 hit.
PF00730. HhH-GPD. 1 hit.
PF14815. NUDIX_4. 1 hit.
[Graphical view]
SMARTiSM00478. ENDO3c. 1 hit.
SM00525. FES. 1 hit.
[Graphical view]
SUPFAMiSSF48150. SSF48150. 1 hit.
SSF55811. SSF55811. 1 hit.
TIGRFAMsiTIGR01084. mutY. 1 hit.

Sequencei

Sequence statusi: Complete.

P83847-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRETERFPA REFQRDLLDW FARERRDLPW RKDRDPYKVW VSEVMLQQTR
60 70 80 90 100
VETVIPYFEQ FIDRFPTLEA LADADEDEVL KAWEGLGYYS RVRNLHAAVK
110 120 130 140 150
EVKTRYGGKV PDDPDEFSRL KGVGPYTVGA VLSLAYGVPE PAVDGNVMRV
160 170 180 190 200
LSRLFLVTDD IAKPSTRKRF EQIVREIMAY ENPGAFNEAL IELGALVCTP
210 220 230 240 250
RRPSCLLCPV QAYCQAFAEG VAEELPVKMK KTAVKQVPLA VAVLADDEGR
260 270 280 290 300
VLIRKRDSTG LLANLWEFPS CETDGADGKE KLEQMVGEQY GLQVELTEPI
310 320 330 340 350
VSFEHAFSHL VWQLTVFPGR LVHGGPVEEP YRLAPEDELK AYAFPVSHQR
360
VWREYKEWAS GVRRPD
Length:366
Mass (Da):41,835
Last modified:January 20, 2016 - v2
Checksum:i0D37855DFCF30C6B
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RRQX-ray2.22A1-366[»]
1RRSX-ray2.40A1-366[»]
1VRLX-ray2.50A1-366[»]
3FSPX-ray2.20A1-366[»]
3G0QX-ray2.20A9-360[»]
4YOQX-ray2.21A1-366[»]
4YPHX-ray2.32A1-366[»]
4YPRX-ray2.59A/B1-366[»]
5DPKX-ray2.20A1-366[»]
ProteinModelPortaliP83847.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP83847.

Family and domain databases

CDDicd03431. DNA_Glycosylase_C. 1 hit.
cd00056. ENDO3c. 1 hit.
Gene3Di1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
3.90.79.10. 1 hit.
InterProiIPR005760. A/G_AdeGlyc_MutY.
IPR011257. DNA_glycosylase.
IPR003651. Endouclease3_FeS-loop_motif.
IPR003265. HhH-GPD_domain.
IPR000445. HhH_motif.
IPR023170. HTH_base_excis_C.
IPR029119. MutY_C.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamiPF00633. HHH. 1 hit.
PF00730. HhH-GPD. 1 hit.
PF14815. NUDIX_4. 1 hit.
[Graphical view]
SMARTiSM00478. ENDO3c. 1 hit.
SM00525. FES. 1 hit.
[Graphical view]
SUPFAMiSSF48150. SSF48150. 1 hit.
SSF55811. SSF55811. 1 hit.
TIGRFAMsiTIGR01084. mutY. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMUTY_GEOSE
AccessioniPrimary (citable) accession number: P83847
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2016
Last sequence update: January 20, 2016
Last modified: September 7, 2016
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

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.