ID   GUAD_PONAB              Reviewed;         454 AA.
AC   Q5RAV9;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Guanine deaminase;
DE            Short=Guanase;
DE            Short=Guanine aminase;
DE            EC=3.5.4.3 {ECO:0000250|UniProtKB:Q9Y2T3};
DE   AltName: Full=Guanine aminohydrolase;
DE            Short=GAH;
GN   Name=GDA;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolytic deamination of guanine, producing
CC       xanthine and ammonia. {ECO:0000250|UniProtKB:Q9Y2T3}.
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; EC=3.5.4.3;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y2T3};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y2T3};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9Y2T3};
CC   -!- PATHWAY: Purine metabolism; guanine degradation; xanthine from guanine:
CC       step 1/1. {ECO:0000250|UniProtKB:Q9Y2T3}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9Y2T3}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       ATZ/TRZ family. {ECO:0000305}.
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DR   EMBL; CR858902; CAH91101.1; -; mRNA.
DR   RefSeq; NP_001127376.1; NM_001133904.1.
DR   RefSeq; XP_009242793.1; XM_009244518.1.
DR   AlphaFoldDB; Q5RAV9; -.
DR   SMR; Q5RAV9; -.
DR   STRING; 9601.ENSPPYP00000021605; -.
DR   MEROPS; M38.981; -.
DR   Ensembl; ENSPPYT00000022489; ENSPPYP00000021604; ENSPPYG00000019289.
DR   GeneID; 100174441; -.
DR   KEGG; pon:100174441; -.
DR   CTD; 9615; -.
DR   eggNOG; KOG3968; Eukaryota.
DR   GeneTree; ENSGT00390000017130; -.
DR   InParanoid; Q5RAV9; -.
DR   UniPathway; UPA00603; UER00660.
DR   Proteomes; UP000001595; Chromosome 9.
DR   GO; GO:0008892; F:guanine deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006147; P:guanine catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01303; GDEase; 1.
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   PANTHER; PTHR11271:SF6; PTHR11271:SF6; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR02967; guan_deamin; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Metal-binding; Phosphoprotein; Reference proteome; Zinc.
FT   CHAIN           1..454
FT                   /note="Guanine deaminase"
FT                   /id="PRO_0000284445"
FT   BINDING         82
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT   BINDING         84..87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT   BINDING         84
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT   BINDING         213..214
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT   BINDING         240..243
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT   BINDING         240
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT   BINDING         330
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT   BINDING         330
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT   MOD_RES         453
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WTT6"
SQ   SEQUENCE   454 AA;  51040 MW;  56911EBC82213830 CRC64;
     MCAAQMPPLA HIFRGTFVHS TWTCPMEVLR DHLLGVSDSG KIVFLEEASQ QEKLAKEWCF
     KPCEIRELSH HEFFMPGLVD THIHASQYSF AGSNIDLPLL EWLTKYTFPA EHRFQNTDFA
     EEVYTRVVRR TLKNGTTTAC YFATIHTDSS LLLADITDKF GQRAFVGKVC MNLNDTFPEY
     NETTEESIKE TERFVSEMLQ RKYSRVKPIV TPRFSLSCSE TLMGDLGNIA KTHDLHIQSH
     ISENRDEVEA VKNLYPSYKN YTDVYDKNNL LTNKTVMAHG CYLSAEELNV FHERGASIAH
     CPNSNLSLSS GFLNVLEVLK HEVKIGLGTD VAGGYSYSML DAIRRAVMVS NILLINKVNE
     KSLTLKEVFR LATLGGSQAL GLDGEIGNFE VGKEFDAILI NPKASDSPID LFYGDFFGDI
     SEAVIQKFLY LGDDRNIEEV YVGGKQVVPF SSSV