GUAD_RAT
ID GUAD_RAT Reviewed; 454 AA.
AC Q9WTT6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Guanine deaminase;
DE Short=Guanase;
DE Short=Guanine aminase;
DE EC=3.5.4.3 {ECO:0000250|UniProtKB:Q9Y2T3};
DE AltName: Full=Guanine aminohydrolase;
DE Short=GAH;
GN Name=Gda;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Seong Y.S., Kimm S.W., Park J.B.;
RT "Molecular cloning and expression of rat guanine aminohydrolase.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 114-126; 325-344 AND 385-403, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of guanine, producing
CC xanthine and ammonia. {ECO:0000250|UniProtKB:Q9Y2T3}.
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:0000250|UniProtKB:Q9Y2T3};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2T3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9Y2T3};
CC -!- PATHWAY: Purine metabolism; guanine degradation; xanthine from guanine:
CC step 1/1. {ECO:0000250|UniProtKB:Q9Y2T3}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9Y2T3}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC ATZ/TRZ family. {ECO:0000305}.
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DR EMBL; AF026472; AAD15629.2; -; mRNA.
DR AlphaFoldDB; Q9WTT6; -.
DR SMR; Q9WTT6; -.
DR ELM; Q9WTT6; -.
DR IntAct; Q9WTT6; 1.
DR MINT; Q9WTT6; -.
DR STRING; 10116.ENSRNOP00000024775; -.
DR ChEMBL; CHEMBL3308947; -.
DR MEROPS; M38.981; -.
DR iPTMnet; Q9WTT6; -.
DR PhosphoSitePlus; Q9WTT6; -.
DR SwissPalm; Q9WTT6; -.
DR World-2DPAGE; 0004:Q9WTT6; -.
DR PaxDb; Q9WTT6; -.
DR PRIDE; Q9WTT6; -.
DR UCSC; RGD:621617; rat.
DR RGD; 621617; Gda.
DR eggNOG; KOG3968; Eukaryota.
DR InParanoid; Q9WTT6; -.
DR PhylomeDB; Q9WTT6; -.
DR Reactome; R-RNO-74259; Purine catabolism.
DR UniPathway; UPA00603; UER00660.
DR PRO; PR:Q9WTT6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0019239; F:deaminase activity; IBA:GO_Central.
DR GO; GO:0008892; F:guanine deaminase activity; IDA:RGD.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0000255; P:allantoin metabolic process; ISO:RGD.
DR GO; GO:0006161; P:deoxyguanosine catabolic process; ISO:RGD.
DR GO; GO:0046055; P:dGMP catabolic process; ISO:RGD.
DR GO; GO:0046038; P:GMP catabolic process; ISO:RGD.
DR GO; GO:0006147; P:guanine catabolic process; ISO:RGD.
DR GO; GO:0046098; P:guanine metabolic process; IBA:GO_Central.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IDA:CACAO.
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; SSF51338; SSF51338; 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; Phosphoprotein;
KW Reference proteome; Zinc.
FT CHAIN 1..454
FT /note="Guanine deaminase"
FT /id="PRO_0000122300"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 84..87
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 213..214
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 240..243
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2T3"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 454 AA; 51016 MW; 518B487A74F99F81 CRC64;
MCAARRRELA LIFRGTFVHS TWTCPMEVLR DHLLGVSDSG KIVFLEESSQ QEKLAKEWCF
KPCEIRELSH HEFFMPGLVD THIHAPQYAF AGSNVDLPLL DWLNKYTFPT EKRFQSTDVA
EEVYTRVVRR TLKNGTTTAC YFGTIHTDSS LILAEITDKF GQRAFVGKVC MDLNNTVPEY
KETTEESVKE TERFVSEMLQ KNYSRVKPIV TPRFSLSCTE TLMSELGNIA KTHDLYIQSH
ISENREEIEA VKSLYPGYKN YTDVYDKNNL LTNKTVMAHG CYLSEEELNV FSERGASIAH
CPNSNLSLSS GLLNVLDVLK HKVKIGLGTD VAGGYSYSML DAIRRAVMVS NVLLINKVNE
KSLTLKEVFR LATLGGSQAL GLDREIGNFE VGKDFDALLI NPRASDSPID LFCGDFVGDI
SEAVIQKFLY LGDDRNIEEV YVGGKQVVPF SSSV
