ID   GUAD_DEIRA              Reviewed;         439 AA.
AC   Q9RYX4;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Probable guanine deaminase;
DE            Short=Guanase;
DE            Short=Guanine aminase;
DE            EC=3.5.4.3;
DE   AltName: Full=Guanine aminohydrolase;
DE            Short=GAH;
GN   Name=guaD; OrderedLocusNames=DR_A0180;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
CC   -!- FUNCTION: Catalyzes the hydrolytic deamination of guanine, producing
CC       xanthine and ammonia. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Purine metabolism; guanine degradation; xanthine from guanine:
CC       step 1/1.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       ATZ/TRZ family. {ECO:0000305}.
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DR   EMBL; AE001825; AAF12192.1; -; Genomic_DNA.
DR   PIR; F75614; F75614.
DR   RefSeq; NP_285504.1; NC_001264.1.
DR   RefSeq; WP_010889440.1; NZ_CP015082.1.
DR   AlphaFoldDB; Q9RYX4; -.
DR   SMR; Q9RYX4; -.
DR   STRING; 243230.DR_A0180; -.
DR   EnsemblBacteria; AAF12192; AAF12192; DR_A0180.
DR   KEGG; dra:DR_A0180; -.
DR   PATRIC; fig|243230.17.peg.3069; -.
DR   eggNOG; COG0402; Bacteria.
DR   HOGENOM; CLU_012358_0_2_0; -.
DR   InParanoid; Q9RYX4; -.
DR   OMA; HGVHLCD; -.
DR   OrthoDB; 785930at2; -.
DR   UniPathway; UPA00603; UER00660.
DR   Proteomes; UP000002524; Chromosome II.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0019239; F:deaminase activity; IBA:GO_Central.
DR   GO; GO:0008892; F:guanine deaminase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0006147; P:guanine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046098; P:guanine metabolic process; IBA:GO_Central.
DR   Gene3D; 2.30.40.10; -; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR014311; Guanine_deaminase.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR11271:SF6; PTHR11271:SF6; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR02967; guan_deamin; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..439
FT                   /note="Probable guanine deaminase"
FT                   /id="PRO_0000122296"
FT   BINDING         76
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT   BINDING         78..81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT   BINDING         78
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT   BINDING         203..204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT   BINDING         231..234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT   BINDING         231
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT   BINDING         321
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT   BINDING         321
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
SQ   SEQUENCE   439 AA;  46688 MW;  F8AC177B09FB0F92 CRC64;
     MKIYRSTLLH TPASPFAVPD ALQTFSDGAL AVGDTGTIAH LGTFTEVLAE VRAACPDAEV
     HDLRGGVLLP GFIDTHVHYP QVRVLGGLGM ALLEWLDRNT LPEEARLADA AYARTIAGEF
     LHGLASHGTT TALVFGSHFA GAMDEFFAEA AARGLRVVAG QVVSDRLLRP ELHTTPERAY
     AEGKALIERW HGQGRSLYAV TPRFSLSASE GILDACAALL TEFPDVRFTS HINENNQEIE
     VVRGLFPGAR DYLDTYERAG LVTPRSVFAH NVHPNERELG VLAAQRCSVA HCPCSNSALG
     SGLFPLRRHL AAGVHVALGT DVGGGTGFSL LKEGLQAYFM QQLLGEEGAA LSPAHLLYLA
     TLAGAQALGL DGQVGDFTPG KQFDAVWLRP RAGSTLATVL AHAESEERTL AALFALGTGD
     DVERVWVGGG VVFAREAEA