GUAD_SCHPO
ID GUAD_SCHPO Reviewed; 527 AA.
AC O14057;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
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 ORFNames=SPCC1672.03c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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; CU329672; CAA20441.1; -; Genomic_DNA.
DR PIR; T41047; T41047.
DR RefSeq; NP_587874.1; NM_001022866.2.
DR AlphaFoldDB; O14057; -.
DR SMR; O14057; -.
DR BioGRID; 275801; 5.
DR STRING; 4896.SPCC1672.03c.1; -.
DR iPTMnet; O14057; -.
DR MaxQB; O14057; -.
DR PaxDb; O14057; -.
DR PRIDE; O14057; -.
DR EnsemblFungi; SPCC1672.03c.1; SPCC1672.03c.1:pep; SPCC1672.03c.
DR GeneID; 2539231; -.
DR KEGG; spo:SPCC1672.03c; -.
DR PomBase; SPCC1672.03c; -.
DR VEuPathDB; FungiDB:SPCC1672.03c; -.
DR eggNOG; KOG3968; Eukaryota.
DR HOGENOM; CLU_012358_0_1_1; -.
DR InParanoid; O14057; -.
DR OMA; FGNETWQ; -.
DR PhylomeDB; O14057; -.
DR Reactome; R-SPO-74259; Purine catabolism.
DR UniPathway; UPA00603; UER00660.
DR PRO; PR:O14057; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0019239; F:deaminase activity; IBA:GO_Central.
DR GO; GO:0008892; F:guanine deaminase activity; ISS:PomBase.
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 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..527
FT /note="Probable guanine deaminase"
FT /id="PRO_0000122301"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 81..84
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 212..213
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 239..242
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 329
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
SQ SEQUENCE 527 AA; 58047 MW; 23D9A3F1117601C1 CRC64;
MDGHTCDVFV GKLIHTPSLG ELEITDATVG VYNGKIVFLE KSMTPKTLEE AKSHHLLKEA
TIHKLKPLQF MFPGLIDTHI HAPQYPNSGI GIDVPLLQWL EKYTFPLESS LADLEEARQV
YKRVVERTLS NGTTFASYFS TLHTPTSALL AEICYSYGQR AYIGKCNMNN LSPDHYCEKS
AESSLEATRQ LISYMSILDP KREMVTPIIT PRFAPSCTED LLSGCGELAE KHNLPIQTHI
SENTSEIELV KELFPERKSY ADVYDYYKLL TPQTILAHAI HLEDEEIELL TKRSSGISHC
PTSNSILASG LANVRKLLDS GINVGLGTDV SGGYAPSILI ALRHAAMTSR SLSYVLGDPK
VMLDLSELLY LATQGGAEVV SRGDQVGSFA VGKYWDALIV DLSAETHSCV DIFERDTWPV
MLSKWVFTSD DRNLAQVWVN GRLVSGFEMK ANLKNSTPLT NGVTSSGHQV FKELTQAHLL
PRTQCVDTPP SCCGGHCCKE ESCRTENCKG AYPANATVTV EEDSGMS
