ID A0A364NGA3_9PLEO Unreviewed; 480 AA.
AC A0A364NGA3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Guanine deaminase {ECO:0000256|ARBA:ARBA00012781, ECO:0000256|RuleBase:RU366009};
DE Short=Guanase {ECO:0000256|RuleBase:RU366009};
DE EC=3.5.4.3 {ECO:0000256|ARBA:ARBA00012781, ECO:0000256|RuleBase:RU366009};
DE AltName: Full=Guanine aminohydrolase {ECO:0000256|RuleBase:RU366009};
GN ORFNames=DDE83_000428 {ECO:0000313|EMBL:RAR16300.1};
OS Stemphylium lycopersici.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Stemphylium.
OX NCBI_TaxID=183478 {ECO:0000313|EMBL:RAR16300.1, ECO:0000313|Proteomes:UP000249619};
RN [1] {ECO:0000313|Proteomes:UP000249619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIDEFI 213 {ECO:0000313|Proteomes:UP000249619};
RA Medina R., Franco M.E.E., Lucentini C.G., Saparrat M.C.N., Balatti P.A.;
RT "Draft genome sequence of Stemphylium lycopersici strain CIDEFI 213.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of guanine, producing
CC 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; EC=3.5.4.3;
CC 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. {ECO:0000256|RuleBase:RU366009};
CC -!- PATHWAY: Purine metabolism; guanine degradation; xanthine from guanine:
CC step 1/1. {ECO:0000256|ARBA:ARBA00004984,
CC ECO:0000256|RuleBase:RU366009}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC ATZ/TRZ family. {ECO:0000256|ARBA:ARBA00006745,
CC ECO:0000256|RuleBase:RU366009}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RAR16300.1}.
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DR EMBL; QGDH01000004; RAR16300.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364NGA3; -.
DR STRING; 183478.A0A364NGA3; -.
DR OrthoDB; 65153at2759; -.
DR UniPathway; UPA00603; UER00660.
DR Proteomes; UP000249619; Unassembled WGS sequence.
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 CDD; cd01303; GDEase; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR014311; Guanine_deaminase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR02967; guan_deamin; 1.
DR PANTHER; PTHR11271; GUANINE DEAMINASE; 1.
DR PANTHER; PTHR11271:SF50; GUANINE DEAMINASE-RELATED; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366009, ECO:0000313|EMBL:RAR16300.1};
KW Metal-binding {ECO:0000256|RuleBase:RU366009};
KW Reference proteome {ECO:0000313|Proteomes:UP000249619};
KW Zinc {ECO:0000256|RuleBase:RU366009}.
FT DOMAIN 82..465
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 480 AA; 52482 MW; 58540BA70824C44A CRC64;
MAASTPIPRT IYLGPFVHST SLTTLEIAPE GAIGVDEDGI ICFVEQNVSS LDNLITSLPS
SQVEGWTDAK IVSIDGSSGF FFPGFIDTHV HAPQHPNTGL FGKTTLLDWL QKYTFPTESS
FSDLQRAHRV YQNFVSRTLS HGTTTAAYYA TIHVPATNAL ADICLERGQR ALVGRVCMNS
DLSPEYYRDE STESSYEDSK ASIDYIRSID PKGEIVKPII TPRFAPSCTE SCLTAMGKLA
KETDAHIQTH ISENKGEIEL VNSLFPDSKN YADVYDSHGL MNEKTILAHC VHLEPEERKL
ILERKSKISH CPASNTAITS GCAPIRDLLD EGHTIGLGTD ISGGFSPSIL ENVRQAIWVS
RHLCIQTSVE TAKLSTEEAL YLATRGGAAV VGMEDKVGGF EVGKEWDAQM INLGSVSEGG
CEDGIFEQGP VDVFGWESWP DKVEKWVYSG DDRNTVAVWV KGRIVHMKSG YPGEKRAATP
//
