Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Probable guanine deaminase

Gene

GUD1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.1 Publication

Catalytic activityi

Guanine + H2O = xanthine + NH3.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Kineticsi

  1. KM=61.5 µM for guanine1 Publication

    Pathwayi: guanine degradation

    This protein is involved in step 1 of the subpathway that synthesizes xanthine from guanine.
    Proteins known to be involved in this subpathway in this organism are:
    1. Probable guanine deaminase (GUD1)
    This subpathway is part of the pathway guanine degradation, which is itself part of Purine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes xanthine from guanine, the pathway guanine degradation and in Purine metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi100 – 1001Zinc; via tele nitrogenBy similarity
    Metal bindingi102 – 1021Zinc; via tele nitrogenBy similarity
    Binding sitei105 – 1051SubstrateBy similarity
    Binding sitei231 – 2311SubstrateBy similarity
    Metal bindingi258 – 2581Zinc; via tele nitrogenBy similarity
    Binding sitei261 – 2611SubstrateBy similarity
    Binding sitei297 – 2971SubstrateBy similarity
    Metal bindingi348 – 3481ZincBy similarity

    GO - Molecular functioni

    • guanine deaminase activity Source: SGD
    • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides Source: SGD
    • zinc ion binding Source: InterPro

    GO - Biological processi

    • guanine catabolic process Source: UniProtKB-UniPathway
    • guanine metabolic process Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29615-MONOMER.
    YEAST:MONOMER3O-12.
    ReactomeiR-SCE-74259. Purine catabolism.
    UniPathwayiUPA00603; UER00660.

    Protein family/group databases

    MEROPSiM38.981.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable guanine deaminase (EC:3.5.4.3)
    Short name:
    Guanase
    Short name:
    Guanine aminase
    Alternative name(s):
    Guanine aminohydrolase
    Short name:
    GAH
    Gene namesi
    Name:GUD1
    Ordered Locus Names:YDL238C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome IV

    Organism-specific databases

    EuPathDBiFungiDB:YDL238C.
    SGDiS000002397. GUD1.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 489489Probable guanine deaminasePRO_0000122302Add
    BLAST

    Proteomic databases

    MaxQBiQ07729.
    PeptideAtlasiQ07729.

    Interactioni

    Protein-protein interaction databases

    BioGridi31873. 18 interactions.
    DIPiDIP-5170N.
    IntActiQ07729. 1 interaction.
    MINTiMINT-543143.

    Structurei

    3D structure databases

    ProteinModelPortaliQ07729.
    SMRiQ07729. Positions 88-486.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATZ/TRZ family.Curated

    Phylogenomic databases

    GeneTreeiENSGT00390000017130.
    HOGENOMiHOG000257692.
    InParanoidiQ07729.
    KOiK01487.
    OMAiLDYKATP.
    OrthoDBiEOG7C2R9V.

    Family and domain databases

    InterProiIPR006680. Amidohydro-rel.
    IPR014311. Guanine_deaminase.
    IPR032466. Metal_Hydrolase.
    [Graphical view]
    PANTHERiPTHR11271:SF6. PTHR11271:SF6. 2 hits.
    PfamiPF01979. Amidohydro_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF51556. SSF51556. 1 hit.
    TIGRFAMsiTIGR02967. guan_deamin. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q07729-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTKSDLLFDK FNDKHGKFLV FFGTFVDTPK LGELRIREKT SVGVLNGIIR
    60 70 80 90 100
    FVNRNSLDPV KDCLDHDSSL SPEDVTVVDI IGKDKTRNNS FYFPGFVDTH
    110 120 130 140 150
    NHVSQYPNVG VFGNSTLLDW LEKYTFPIEA ALANENIARE VYNKVISKTL
    160 170 180 190 200
    SHGTTTVAYY NTIDLKSTKL LAQLSSLLGQ RVLVGKVCMD TNGPEYYIED
    210 220 230 240 250
    TKTSFESTVK VVKYIRETIC DPLVNPIVTP RFAPSCSREL MQQLSKLVKD
    260 270 280 290 300
    ENIHVQTHLS ENKEEIQWVQ DLFPECESYT DVYDKYGLLT EKTVLAHCIH
    310 320 330 340 350
    LTDAEARVIK QRRCGISHCP ISNSSLTSGE CRVRWLLDQG IKVGLGTDVS
    360 370 380 390 400
    AGHSCSILTT GRQAFAVSRH LAMRETDHAK LSVSECLFLA TMGGAQVLRM
    410 420 430 440 450
    DETLGTFDVG KQFDAQMIDT NAPGSNVDMF HWQLKEKDQM QEQEQEQGQD
    460 470 480
    PYKNPPLLTN EDIIAKWFFN GDDRNTTKVW VAGQQVYQI
    Length:489
    Mass (Da):55,204
    Last modified:November 1, 1996 - v1
    Checksum:i60D21F40CA23DF81
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z74286 Genomic DNA. Translation: CAA98818.1.
    BK006938 Genomic DNA. Translation: DAA11628.1.
    PIRiS67802.
    RefSeqiNP_010043.1. NM_001180298.1.

    Genome annotation databases

    EnsemblFungiiYDL238C; YDL238C; YDL238C.
    GeneIDi851360.
    KEGGisce:YDL238C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z74286 Genomic DNA. Translation: CAA98818.1.
    BK006938 Genomic DNA. Translation: DAA11628.1.
    PIRiS67802.
    RefSeqiNP_010043.1. NM_001180298.1.

    3D structure databases

    ProteinModelPortaliQ07729.
    SMRiQ07729. Positions 88-486.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi31873. 18 interactions.
    DIPiDIP-5170N.
    IntActiQ07729. 1 interaction.
    MINTiMINT-543143.

    Protein family/group databases

    MEROPSiM38.981.

    Proteomic databases

    MaxQBiQ07729.
    PeptideAtlasiQ07729.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYDL238C; YDL238C; YDL238C.
    GeneIDi851360.
    KEGGisce:YDL238C.

    Organism-specific databases

    EuPathDBiFungiDB:YDL238C.
    SGDiS000002397. GUD1.

    Phylogenomic databases

    GeneTreeiENSGT00390000017130.
    HOGENOMiHOG000257692.
    InParanoidiQ07729.
    KOiK01487.
    OMAiLDYKATP.
    OrthoDBiEOG7C2R9V.

    Enzyme and pathway databases

    UniPathwayiUPA00603; UER00660.
    BioCyciYEAST:G3O-29615-MONOMER.
    YEAST:MONOMER3O-12.
    ReactomeiR-SCE-74259. Purine catabolism.

    Miscellaneous databases

    PROiQ07729.

    Family and domain databases

    InterProiIPR006680. Amidohydro-rel.
    IPR014311. Guanine_deaminase.
    IPR032466. Metal_Hydrolase.
    [Graphical view]
    PANTHERiPTHR11271:SF6. PTHR11271:SF6. 2 hits.
    PfamiPF01979. Amidohydro_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF51556. SSF51556. 1 hit.
    TIGRFAMsiTIGR02967. guan_deamin. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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.
      , 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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    4. 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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiGUAD_YEAST
    AccessioniPrimary (citable) accession number: Q07729
    Secondary accession number(s): D6VRB8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: June 8, 2016
    This is version 128 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 279 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    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.