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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)DescriptionActionsGraphical viewLength
Active sitei43Proton donor/acceptor1 Publication1
Binding sitei126Interaction with mispaired A in DNA substrate1 Publication1
Sitei144Transition state stabilizer2 Publications1
Binding sitei188Interaction with mispaired A in DNA substrate1 Publication1
Metal bindingi198Iron-sulfur (4Fe-4S)Combined sources5 Publications1
Metal bindingi205Iron-sulfur (4Fe-4S)Combined sources5 Publications1
Metal bindingi208Iron-sulfur (4Fe-4S)Combined sources5 Publications1
Metal bindingi214Iron-sulfur (4Fe-4S)Combined sources5 Publications1
Binding sitei308Interaction with oxoG in DNA substrate2 Publications1

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)DescriptionActionsGraphical viewLength
Mutagenesisi43E → Q: Loss of catalytic activity. 1 Publication1
Mutagenesisi144D → N: Loss of catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004353401 – 366Adenine DNA glycosylaseAdd BLAST366

Structurei

Secondary structure

1366
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 24Combined sources15
Helixi29 – 31Combined sources3
Helixi36 – 45Combined sources10
Turni46 – 48Combined sources3
Helixi51 – 64Combined sources14
Helixi68 – 72Combined sources5
Helixi76 – 83Combined sources8
Helixi90 – 106Combined sources17
Helixi114 – 117Combined sources4
Helixi125 – 136Combined sources12
Helixi145 – 154Combined sources10
Helixi166 – 177Combined sources12
Beta strandi180 – 182Combined sources3
Helixi183 – 196Combined sources14
Beta strandi200 – 202Combined sources3
Helixi205 – 207Combined sources3
Helixi211 – 213Combined sources3
Helixi215 – 218Combined sources4
Helixi222 – 224Combined sources3
Beta strandi235 – 246Combined sources12
Beta strandi249 – 255Combined sources7
Beta strandi258 – 260Combined sources3
Turni261 – 264Combined sources4
Beta strandi270 – 272Combined sources3
Beta strandi274 – 276Combined sources3
Helixi281 – 284Combined sources4
Beta strandi289 – 291Combined sources3
Beta strandi294 – 296Combined sources3
Beta strandi301 – 306Combined sources6
Beta strandi308 – 321Combined sources14
Beta strandi331 – 335Combined sources5
Helixi336 – 341Combined sources6
Helixi346 – 358Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RRQX-ray2.22A1-365[»]
1RRSX-ray2.40A1-365[»]
1VRLX-ray2.50A1-365[»]
3FSPX-ray2.20A1-365[»]
3G0QX-ray2.20A9-360[»]
4YOQX-ray2.21A1-365[»]
4YPHX-ray2.32A1-365[»]
4YPRX-ray2.59A/B1-365[»]
5DPKX-ray2.20A1-365[»]
ProteinModelPortaliP83847.
SMRiP83847.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP83847.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini105 – 133HhHSequence analysisAdd BLAST29

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni30 – 31Interaction with mispaired A in DNA substrate1 Publication2
Regioni48 – 49Interaction with oxoG in DNA substrate2 Publications2
Regioni86 – 88Interaction with oxoG in DNA substrate2 Publications3

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RRQX-ray2.22A1-365[»]
1RRSX-ray2.40A1-365[»]
1VRLX-ray2.50A1-365[»]
3FSPX-ray2.20A1-365[»]
3G0QX-ray2.20A9-360[»]
4YOQX-ray2.21A1-365[»]
4YPHX-ray2.32A1-365[»]
4YPRX-ray2.59A/B1-365[»]
5DPKX-ray2.20A1-365[»]
ProteinModelPortaliP83847.
SMRiP83847.
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: November 2, 2016
This is version 77 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.