GUAD_DICDI
ID GUAD_DICDI Reviewed; 450 AA.
AC Q86AW9; Q54Z75;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=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; ORFNames=DDB_G0277743;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP PROTEIN SEQUENCE OF 207-218 AND 391-398, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RA Bienvenut W.V., Veltman D.M., Insall R.H.;
RL Submitted (JAN-2010) to UniProtKB.
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; AAFI02000022; EAL68545.1; -; Genomic_DNA.
DR RefSeq; XP_642478.1; XM_637386.1.
DR AlphaFoldDB; Q86AW9; -.
DR SMR; Q86AW9; -.
DR STRING; 44689.DDB0230211; -.
DR MEROPS; M38.981; -.
DR PaxDb; Q86AW9; -.
DR EnsemblProtists; EAL68545; EAL68545; DDB_G0277743.
DR GeneID; 8621189; -.
DR KEGG; ddi:DDB_G0277743; -.
DR dictyBase; DDB_G0277743; guaD.
DR eggNOG; KOG3968; Eukaryota.
DR HOGENOM; CLU_012358_0_1_1; -.
DR InParanoid; Q86AW9; -.
DR OMA; ALIGKVC; -.
DR PhylomeDB; Q86AW9; -.
DR Reactome; R-DDI-74259; Purine catabolism.
DR UniPathway; UPA00603; UER00660.
DR PRO; PR:Q86AW9; -.
DR Proteomes; UP000002195; Chromosome 2.
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 CDD; cd01303; GDEase; 1.
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; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR02967; guan_deamin; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Metal-binding; Reference proteome;
KW Zinc.
FT CHAIN 1..450
FT /note="Guanine deaminase"
FT /id="PRO_0000327713"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 90..93
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 218..219
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 245..248
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 335
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
SQ SEQUENCE 450 AA; 50730 MW; 99ECF5D6972C1A99 CRC64;
MMKANKIIKL FKGTVIHSIE IGKVEILPNS LIGIDEDGVI QHMKSNYEDL KQLEKDVTMI
CTDNGINEQE SVIDMGNKFL IPGFIDTHAH APQYHNAGTG TDLPLLKWLE KYTFPVESKF
KDLIFAENVY GKVVDRMLRH GTTTCCYYAT IHLEASELLA EIVSKRGQRA FIGKVCMDRH
SPDHYVETTE QSISNTKEFV DRILAKGNPL VQPIVTPRFA PSCTDELMVA LGNLSHEKQT
LIQSHLSENK DEIEWVKSLY PGIESYTHVY KHFNLLNERT IMAHCVHLSD EEIKLISTQQ
TAISHCPISN FTLSSGNLDV RKVLEANIKL GLGSDISGGY HPSILQVIRD SIKCSNSHFF
NNGNHTPLTF EEAFYLATVG GSKVVNLDHR IGNFIVGKDF DAQIIDPFVQ NSPFDCFDGE
TLKDIFQKFI YLGDDRNLSS LYIKGNKIKF
