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Q07729 (GUAD_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 90. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable 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:GUD1
Ordered Locus Names:YDL238C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length489 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia. Ref.5

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.

Subcellular location

Cytoplasm Ref.3.

Miscellaneous

Present with 279 molecules/cell in log phase SD medium. Ref.4

Sequence similarities

Belongs to the ATZ/TRZ family.

Biophysicochemical properties

Kinetic parameters:

KM=61.5 µM for guanine Ref.5

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from direct assay Ref.3. Source: SGD

   Molecular functionguanine deaminase activity

Inferred from direct assay Ref.5. Source: SGD

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 489489Probable guanine deaminase
PRO_0000122302

Sites

Metal binding1001Zinc; via tele nitrogen By similarity
Metal binding1021Zinc; via tele nitrogen By similarity
Metal binding2581Zinc; via tele nitrogen By similarity
Metal binding3481Zinc By similarity
Binding site1051Substrate By similarity
Binding site2311Substrate By similarity
Binding site2611Substrate By similarity
Binding site2971Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q07729 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 60D21F40CA23DF81

FASTA48955,204
        10         20         30         40         50         60 
MTKSDLLFDK FNDKHGKFLV FFGTFVDTPK LGELRIREKT SVGVLNGIIR FVNRNSLDPV 

        70         80         90        100        110        120 
KDCLDHDSSL SPEDVTVVDI IGKDKTRNNS FYFPGFVDTH NHVSQYPNVG VFGNSTLLDW 

       130        140        150        160        170        180 
LEKYTFPIEA ALANENIARE VYNKVISKTL SHGTTTVAYY NTIDLKSTKL LAQLSSLLGQ 

       190        200        210        220        230        240 
RVLVGKVCMD TNGPEYYIED TKTSFESTVK VVKYIRETIC DPLVNPIVTP RFAPSCSREL 

       250        260        270        280        290        300 
MQQLSKLVKD ENIHVQTHLS ENKEEIQWVQ DLFPECESYT DVYDKYGLLT EKTVLAHCIH 

       310        320        330        340        350        360 
LTDAEARVIK QRRCGISHCP ISNSSLTSGE CRVRWLLDQG IKVGLGTDVS AGHSCSILTT 

       370        380        390        400        410        420 
GRQAFAVSRH LAMRETDHAK LSVSECLFLA TMGGAQVLRM DETLGTFDVG KQFDAQMIDT 

       430        440        450        460        470        480 
NAPGSNVDMF HWQLKEKDQM QEQEQEQGQD PYKNPPLLTN EDIIAKWFFN GDDRNTTKVW 


VAGQQVYQI

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed: 9169867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]"GUD1 (YDL238c) encodes Saccharomyces cerevisiae guanine deaminase, an enzyme expressed during post-diauxic growth."
Saint-Marc C., Daignan-Fornier B.
Yeast 21:1359-1363(2004) [PubMed: 15565584] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z74286 Genomic DNA. Translation: CAA98818.1.
BK006938 Genomic DNA. Translation: DAA11628.1.
PIRS67802.
RefSeqNP_010043.1. NM_001180298.1.

3D structure databases

ProteinModelPortalQ07729.
SMRQ07729. Positions 19-487.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-5170N.
IntActQ07729. 1 interaction.
MINTMINT-543143.
STRINGQ07729.

Proteomic databases

PeptideAtlasQ07729.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL238C; YDL238C; YDL238C.
GeneID851360.
KEGGsce:YDL238C.
NMPDRfig|4932.3.peg.776.

Organism-specific databases

CYGDYDL238c.
SGDS000002397. GUD1.

Phylogenomic databases

eggNOGfuNOG06714.
GeneTreeEFGT00050000002135.
HOGENOMHBG417542.
OMAVDIFGWE.
OrthoDBEOG48PQTK.

Gene expression databases

ArrayExpressQ07729.
GenevestigatorQ07729.
GermOnlineYDL238C. Saccharomyces cerevisiae.

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

NextBio968462.

Entry information

Entry nameGUAD_YEAST
AccessionPrimary (citable) accession number: Q07729
Secondary accession number(s): D6VRB8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: December 14, 2011
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents