(data stored in ACNUC8465 zone)

SWISSPROT: C5DD46_LACTC

ID   C5DD46_LACTC            Unreviewed;       474 AA.
AC   C5DD46;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 53.
DE   RecName: Full=Guanine deaminase {ECO:0000256|RuleBase:RU366009};
DE            Short=Guanase {ECO:0000256|RuleBase:RU366009};
DE            EC=3.5.4.3 {ECO:0000256|RuleBase:RU366009};
DE   AltName: Full=Guanine aminohydrolase {ECO:0000256|RuleBase:RU366009};
GN   OrderedLocusNames=KLTH0B08228g {ECO:0000313|EMBL:CAR21707.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21707.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21707.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P.,
RA   Jubin C., Poulain J., Barbe V., Segurens B., Artiguenave F.,
RA   Anthouard V., Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R.,
RA   Durrens P., Jean G., Marck C., Martin T., Nikolski M., Rolland T.,
RA   Seret M.-L., Casaregola S., Despons L., Fairhead C., Fischer G.,
RA   Lafontaine I., Leh V., Lemaire M., de Montigny J., Neuveglise C.,
RA   Thierry A., Blanc-Lenfle I., Bleykasten C., Diffels J., Fritsch E.,
RA   Frangeul L., Goeffon A., Jauniaux N., Kachouri-Lafond R., Payen C.,
RA   Potier S., Pribylova L., Ozanne C., Richard G.-F., Sacerdot C.,
RA   Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
CC   -!- FUNCTION: Catalyzes the hydrolytic deamination of guanine,
CC       producing xanthine and ammonia. {ECO:0000256|RuleBase:RU366009}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanine + H(+) + H2O = NH4(+) + xanthine;
CC         Xref=Rhea:RHEA:14665, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16235, ChEBI:CHEBI:17712, ChEBI:CHEBI:28938;
CC         EC=3.5.4.3; Evidence={ECO:0000256|RuleBase:RU366009};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU366009};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU366009};
CC   -!- PATHWAY: Purine metabolism; guanine degradation; xanthine from
CC       guanine: step 1/1. {ECO:0000256|RuleBase:RU366009}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. ATZ/TRZ family. {ECO:0000256|RuleBase:RU366009}.
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DR   EMBL; CU928166; CAR21707.1; -; Genomic_DNA.
DR   RefSeq; XP_002552145.1; XM_002552099.1.
DR   STRING; 381046.XP_002552145.1; -.
DR   EnsemblFungi; CAR21707; CAR21707; KLTH0B08228g.
DR   GeneID; 8290985; -.
DR   KEGG; lth:KLTH0B08228g; -.
DR   HOGENOM; HOG000257692; -.
DR   InParanoid; C5DD46; -.
DR   KO; K01487; -.
DR   OMA; ASYFATN; -.
DR   OrthoDB; 612054at2759; -.
DR   UniPathway; UPA00603; UER00660.
DR   Proteomes; UP000002036; Chromosome B.
DR   GO; GO:0008892; F:guanine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006147; P:guanine catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.30.40.10; -; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR014311; Guanine_deaminase.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR02967; guan_deamin; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5DD46.
DR   SWISS-2DPAGE; C5DD46.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002036};
KW   Hydrolase {ECO:0000256|RuleBase:RU366009};
KW   Metal-binding {ECO:0000256|RuleBase:RU366009};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036};
KW   Zinc {ECO:0000256|RuleBase:RU366009}.
FT   DOMAIN       77    466       Amidohydro-rel. {ECO:0000259|Pfam:
FT                                PF01979}.
SQ   SEQUENCE   474 AA;  52445 MW;  F37928049F921241 CRC64;
     MILKLTVYHG NFVDTPSLGD VRIRPQTTIG VGTDGKILFI KEKSQDPLRD ALDFDQTLQP
     SEVAVVKISG SQDGSFFFPG FVDTHVHASQ YPNAGIFGSS TLLDWLQTYT FPLEASLKDA
     DTARAVYNRV LDRTLANGTT TASYYTTIDA ASSNLMARIC AEKGQRAFIG KVCMDQNSPD
     YYVELFKECK HSTRQVVDYI KKELKDEKIQ PVLTPRFAPS CSRELMSWLG QLAHEEDLNV
     QTHLSENLAE LELVAELFPE CENYSQVYDN HHLLTKKTLL AHCVHLSDKE IELLKLRGCG
     VSHCPISNSS LASGECRVRL LLDNGINVGL GTDLSGGYSS SILAVARQAL LVSRHLAMKE
     TDAKKQEHVN LSVEDVLFLA SLGGAQALSL GSVVGSFEVN KQFDAQLINL DPVSSNVDVF
     EWQRTSWNDS PKEGENQKLA RNLLAKWLFT GDDRNTARVW VAGRLVHSYP ASAT
//

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