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Database: UniProt
Entry: A0A0F0FRF7_9BURK
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ID   A0A0F0FRF7_9BURK        Unreviewed;       443 AA.
AC   A0A0F0FRF7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=UB46_17745 {ECO:0000313|EMBL:KJK23025.1};
OS   Burkholderiaceae bacterium 16.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae.
OX   NCBI_TaxID=1619952 {ECO:0000313|EMBL:KJK23025.1, ECO:0000313|Proteomes:UP000033515};
RN   [1] {ECO:0000313|EMBL:KJK23025.1, ECO:0000313|Proteomes:UP000033515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16 {ECO:0000313|EMBL:KJK23025.1,
RC   ECO:0000313|Proteomes:UP000033515};
RA   Roco C.A., Bergaust L., Bakken L., Yavitt J., Shapleigh J.P.;
RT   "The modularity of denitrifying soil bacteria: using gas kinetics and
RT   genome sequencing to connect denitrifier phenotype to genotype.";
RL   Submitted (FEB-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:KJK23025.1}.
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DR   EMBL; JYOD01000047; KJK23025.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0FRF7; -.
DR   STRING; 1619952.UB46_17745; -.
DR   PATRIC; fig|1619952.3.peg.5423; -.
DR   UniPathway; UPA00603; UER00660.
DR   Proteomes; UP000033515; 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: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};
KW   Metal-binding {ECO:0000256|RuleBase:RU366009};
KW   Zinc {ECO:0000256|RuleBase:RU366009}.
FT   DOMAIN          74..433
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   443 AA;  48711 MW;  E95234E45A24B284 CRC64;
     MTTTPPTPSI TRAIRGRVLH FLRDPQFHDD ACQYWEDGVL VVTAGHVAAV GDYAELAAQI
     PAGAEVIDRR GKLIVPGFID THVHYPQTDI IASPSPGLLH WLETYTFPEE RRFAEPEYAA
     AVAGFFADEL LRNGTTSAVA WSTVHTASAD ALFAEADRRN LRLVTGKVLM DRNCPEFLRD
     TAESGARDSA DLISRWHGKN RLSYAITPRF APTSSEAQLA ACGELAKAYP DAYIQTHVAE
     NRDEVKWVAE LFPQARSYLD IYDHYGLLRP GAFYGHAIYL DQDDRKRLAD SGAAVAHCPT
     SNLFLGSGFY DFHQSDAYRL NVTLATDVGG GTSFSMLRTM NAAHKVARMG GYHLTALRMF
     YLATRAAADA LGWSERVGSF TPGCEADFIV LDPQATPLIA RRSERSETLE EQLFAFAMLG
     DDRVIDEVYV MGEPASAPAS VAH
//
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