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
//