ID A0A0Q9YY57_9COXI Unreviewed; 443 AA.
AC A0A0Q9YY57;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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 Name=guaD_1 {ECO:0000313|EMBL:KRG21886.1};
GN ORFNames=HT99x_01080 {ECO:0000313|EMBL:KRG21886.1};
OS Candidatus Berkiella aquae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Berkiella.
OX NCBI_TaxID=295108 {ECO:0000313|EMBL:KRG21886.1, ECO:0000313|Proteomes:UP000051497};
RN [1] {ECO:0000313|EMBL:KRG21886.1, ECO:0000313|Proteomes:UP000051497}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HT99 {ECO:0000313|EMBL:KRG21886.1,
RC ECO:0000313|Proteomes:UP000051497};
RA Mehari Y.T., Arivett B.A., Farone A.L., Gunderson J.H., Farone M.B.;
RT "Draft Genome Sequences of Two Novel Amoeba-resistant Intranuclear
RT Bacteria, Candidatus Berkiella cookevillensis and Candidatus Berkiella
RT aquae.";
RL Submitted (SEP-2015) 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:KRG21886.1}.
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DR EMBL; LKAJ01000003; KRG21886.1; -; Genomic_DNA.
DR RefSeq; WP_075065705.1; NZ_LKAJ02000001.1.
DR AlphaFoldDB; A0A0Q9YY57; -.
DR STRING; 295108.HT99x_01080; -.
DR PATRIC; fig|1590043.3.peg.1092; -.
DR OrthoDB; 9787621at2; -.
DR UniPathway; UPA00603; UER00660.
DR Proteomes; UP000051497; 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:SF6; GUANINE DEAMINASE; 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:KRG21886.1};
KW Metal-binding {ECO:0000256|RuleBase:RU366009};
KW Reference proteome {ECO:0000313|Proteomes:UP000051497};
KW Zinc {ECO:0000256|RuleBase:RU366009}.
FT DOMAIN 75..436
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 443 AA; 49385 MW; BB4F18206D7E1511 CRC64;
MTIKLSGPSH AIRGPVLTFK GDAFKDGLEK TMIYEPDAIV AFANGYITHF GPADKIKSQL
PQDITIKNYG SDSLISAGFL DSHVHFPQIP MIAAFGAQLL DWLNNYTYPI ERKYADKAFA
SAVAKVFLNE CLKNGITTSC VYCTVFPQSV DALFEEAERL GMRIAAGKVL MNRNAPDYLL
DTTQTGYDDS KALINQWHGR NRLMYAITPR FAPTSTAEQL ESAAALWSEY PDCYLQTHVS
ENKNEVAWVK ALFPERKNYL DVYDYHKLCR PRAVFGHGIY LNDDEMQCMH RSGSAISHCP
TSNFFLGSGF FNIHRAMQND RPVRVGLGTD LGGGTTFSIL QTLSEAYKAA QFNSNQLTAG
HAFYLATRGT ARAMYLEDKV GSIAPGMEAD VVVLNMKSTP IIQYRMQFAE DIQEALFIQM
MMGDDRAVQA TYVAGELRYS KEA
//
