ID A0A317VQG5_9EURO Unreviewed; 501 AA.
AC A0A317VQG5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=BO70DRAFT_372742 {ECO:0000313|EMBL:PWY75531.1};
OS Aspergillus heteromorphus CBS 117.55.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY75531.1, ECO:0000313|Proteomes:UP000247233};
RN [1] {ECO:0000313|EMBL:PWY75531.1, ECO:0000313|Proteomes:UP000247233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY75531.1,
RC ECO:0000313|Proteomes:UP000247233};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) 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:PWY75531.1}.
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DR EMBL; MSFL01000021; PWY75531.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317VQG5; -.
DR STRING; 1448321.A0A317VQG5; -.
DR VEuPathDB; FungiDB:BO70DRAFT_372742; -.
DR OrthoDB; 65153at2759; -.
DR UniPathway; UPA00603; UER00660.
DR Proteomes; UP000247233; 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 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; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366009, ECO:0000313|EMBL:PWY75531.1};
KW Metal-binding {ECO:0000256|RuleBase:RU366009};
KW Reference proteome {ECO:0000313|Proteomes:UP000247233};
KW Zinc {ECO:0000256|RuleBase:RU366009}.
FT DOMAIN 94..494
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 501 AA; 54750 MW; C288012EAAED0687 CRC64;
MYTLYIGTFI HLPRLPADAD LDADHKLSIN HGALWVSEDG IIEGFDWSVK SPKDVKAFLR
KKGWVAEGEK GKGKGQATQV KVVVAREDRN EFFFPGFVDT HIHAPQYPNT GLFSTSGLLT
WLQTYTFPME SSFASPSSLP TVPPPQAYRV YNQVISRTLS HGTTTASYFA TIHLPATNLL
ATLCHARGQR ALIGRVCMDN PATCPDYLLD EPDSVVPITE ASIAHIRRLD PEGQLINPVI
TPRFAPSCTH ASLASLSELA ASATPPLHIQ THLAENLDEL ALVHDLFPRA RDYTSVYDHF
GLLTPKTILA HAVHLSDAER EMIRDRKAKI SHCPASNSAL GSGICPVRRT LRAGIPVGLG
TDVSGGYAVS MLEAVRQACL VSRLLPHASP TTTTEEKQKN QDIIDVNQAL YLSTRGSAAV
LNMAGQIGGF DAGMSWDAQL IRLGAYRSVV SGKGVAESNV DVFGMESWEE KVQKWVWSGD
DRNVRAVWVG GRLVHETRDG R
//
