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Q9R111 (GUAD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanine deaminase

Short name=Guanase
Short name=Guanine aminase
EC=3.5.4.3
Alternative name(s):
Guanine aminohydrolase
Short name=GAH
Gene names
Name:Gda
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length454 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.

Catalytic activity

Guanine + H2O = xanthine + NH3.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Pathway

Purine metabolism; guanine degradation; xanthine from guanine: step 1/1.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the ATZ/TRZ family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Dlg4Q621085EBI-2308876,EBI-300895

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 454454Guanine deaminase
PRO_0000122299

Sites

Metal binding821Zinc; via tele nitrogen By similarity
Metal binding841Zinc; via tele nitrogen By similarity
Metal binding2401Zinc; via tele nitrogen By similarity
Metal binding3301Zinc By similarity
Binding site871Substrate By similarity
Binding site2131Substrate By similarity
Binding site2431Substrate By similarity
Binding site2791Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9R111 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 7711573C8C93D64E

FASTA45451,013
        10         20         30         40         50         60 
MCAARTPPLA LVFRGTFVHS TWTCPMEVLR DHLLGVSDSG KIVFLEESSQ QEKLAKEWCF 

        70         80         90        100        110        120 
KPCEIRELSH HEFFMPGLVD THIHAPQYAF AGSNVDLPLL EWLNKYTFPT EQRFRSTDVA 

       130        140        150        160        170        180 
EEVYTRVVRR TLKNGTTTAC YFGTIHTDSS LILAEITDKF GQRAFVGKVC MDLNDTVPEY 

       190        200        210        220        230        240 
KETTEESVKE TERFVSEMLQ KNYPRVKPIV TPRFTLSCTE TLMSELGNIA KTHDLYIQSH 

       250        260        270        280        290        300 
ISENREEIEA VKSLYPSYKN YTDVYDKNNL LTNKTVMAHG CYLSEEELNI FSERGASIAH 

       310        320        330        340        350        360 
CPNSNLSLSS GLLNVLEVLK HKVKIGLGTD VAGGYSYSML DAIRRAVMVS NVLLINKVNE 

       370        380        390        400        410        420 
KNLTLKEVFR LATLGGSQAL GLDSEIGNFE VGKEFDALLI NPRASDSPID LFYGDFVGDI 

       430        440        450 
SEAVIQKFLY LGDDRNIEEV YVGGKQVVPF SSSV 

« Hide

References

[1]Paletzki R.F., Gerfen C.R.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6J.
[2]"Cloning and characterization of human guanine deaminase. Purification and partial amino acid sequence of the mouse protein."
Yuan G., Bin J.C., McKay D.J., Snyder F.F.
J. Biol. Chem. 274:8175-8180(1999) [PubMed: 10075721] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
Strain: C57BL/6J.
Tissue: Erythrocyte.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF174583 mRNA. Translation: AAD50297.1.
IPIIPI00469987.
RefSeqNP_034396.1. NM_010266.2.
UniGeneMm.45054.

3D structure databases

ProteinModelPortalQ9R111.
SMRQ9R111. Positions 8-451.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9R111. 1 interaction.
STRINGQ9R111.

Protein family/group databases

MEROPSM38.981.

PTM databases

PhosphoSiteQ9R111.

2D gel databases

REPRODUCTION-2DPAGEIPI00469987.
Q9R111.

Proteomic databases

PRIDEQ9R111.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000087600; ENSMUSP00000084882; ENSMUSG00000058624.
GeneID14544.
KEGGmmu:14544.

Organism-specific databases

CTD9615.
MGIMGI:95678. Gda.

Phylogenomic databases

GeneTreeENSGT00390000017130.
HOVERGENHBG005930.
InParanoidQ9R111.
OMACFKPCEI.
OrthoDBEOG4ZKJMM.
PhylomeDBQ9R111.

Gene expression databases

ArrayExpressQ9R111.
BgeeQ9R111.
CleanExMM_GDA.
GenevestigatorQ9R111.
GermOnlineENSMUSG00000058624. Mus musculus.

Family and domain databases

InterProIPR006680. Amidohydro_1.
IPR014311. Guanine_deaminase.
[Graphical view]
KOK01487.
PANTHERPTHR11271:SF6. Guanine_deaminase. 1 hit.
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR02967. Guan_deamin. 1 hit.
ProtoNetSearch...

Other

NextBio286216.
SOURCESearch...

Entry information

Entry nameGUAD_MOUSE
AccessionPrimary (citable) accession number: Q9R111
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: November 16, 2011
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families