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Database: UniProt
Entry: A0A066UKA5_9VIBR
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ID   A0A066UKA5_9VIBR        Unreviewed;       444 AA.
AC   A0A066UKA5;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=VFDL14_10380 {ECO:0000313|EMBL:KDN26292.1};
OS   Vibrio fortis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=212667 {ECO:0000313|EMBL:KDN26292.1, ECO:0000313|Proteomes:UP000027219};
RN   [1] {ECO:0000313|EMBL:KDN26292.1, ECO:0000313|Proteomes:UP000027219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dalian14 {ECO:0000313|EMBL:KDN26292.1,
RC   ECO:0000313|Proteomes:UP000027219};
RA   Wang Y., Song L., Liu G., Ding J.;
RT   "Vibrio fortis Dalian14 Genome Sequencing.";
RL   Submitted (FEB-2014) 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:KDN26292.1}.
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DR   EMBL; JFFR01000033; KDN26292.1; -; Genomic_DNA.
DR   RefSeq; WP_032553517.1; NZ_JFFR01000033.1.
DR   AlphaFoldDB; A0A066UKA5; -.
DR   STRING; 212667.VFDL14_10380; -.
DR   OrthoDB; 9787621at2; -.
DR   UniPathway; UPA00603; UER00660.
DR   Proteomes; UP000027219; 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          70..429
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   444 AA;  50502 MW;  0E13FEA5F573B0D8 CRC64;
     MTTQRKAYRA SILHSVADPK DVGLEESYEY FEDGILVVEN GHVVDLGNAD DVLARQPKTL
     DVKEYKDKLI TSGFIDTHIH YPQTGMIASY GEQLLDWLEN YTFPEEKRFK NPVYAHKVAK
     LFLDELASNG TTTALVFGTV HKESVNVFFE EAERRNLRMI AGKVLMDRNA PDYLTDTPES
     GYVDSKELID KWHNRGRLLY AVTPRFAPTS TPEQLATVGK LLEEYPDVYM HTHLSENEKE
     IEWVKALFPE RDSYLDVYDH YGLLHKRSVF AHGIHLSDCE CKRLADTESA IAFCPTSNLF
     LGSGLFRLPE MEEHGIRVGM GTDVGAGTSF SILQTMSEAY KIMQLQHKKL HPAKSLFLAT
     LGGARSLHLE DKIGNLEVGK EADFVVLDMH ATQLMRFRME QATKLEEKLF VLMSLGDDRT
     VSETYIYGEK AYDANFKEYK KLVS
//
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