OXODE_PSEAE
ID OXODE_PSEAE Reviewed; 449 AA.
AC Q9I6Z0;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=8-oxoguanine deaminase;
DE EC=3.5.4.32;
GN OrderedLocusNames=PA0142;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20088583; DOI=10.1021/ja909817d;
RA Hall R.S., Fedorov A.A., Marti-Arbona R., Fedorov E.V., Kolb P.,
RA Sauder J.M., Burley S.K., Shoichet B.K., Almo S.C., Raushel F.M.;
RT "The hunt for 8-oxoguanine deaminase.";
RL J. Am. Chem. Soc. 132:1762-1763(2010).
CC -!- FUNCTION: Specifically deaminates 8-Oxoguanine (8-oxoG) to uric acid.
CC 8-oxoG is formed via the oxidation of guanine within DNA by reactive
CC oxygen species and leads, if uncorrected, to the incorporation of 8-
CC oxoG:A mismatches and eventually to G:C to T:A transversions.
CC {ECO:0000269|PubMed:20088583}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8-oxoguanine + H(+) + H2O = NH4(+) + urate;
CC Xref=Rhea:RHEA:32067, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17775, ChEBI:CHEBI:28938, ChEBI:CHEBI:52617; EC=3.5.4.32;
CC Evidence={ECO:0000269|PubMed:20088583};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.6 mM for guanine {ECO:0000269|PubMed:20088583};
CC KM=1.8 mM for isocytosine {ECO:0000269|PubMed:20088583};
CC Note=kcat is 3.3 sec(-1) with guanine as substrate. kcat is 3.9 sec(-
CC 1) with isocytosine as substrate.;
CC -!- PATHWAY: Purine metabolism.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC ATZ/TRZ family. {ECO:0000305}.
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DR EMBL; AE004091; AAG03532.1; -; Genomic_DNA.
DR PIR; F83627; F83627.
DR RefSeq; NP_248832.1; NC_002516.2.
DR RefSeq; WP_003112635.1; NZ_QZGE01000015.1.
DR AlphaFoldDB; Q9I6Z0; -.
DR SMR; Q9I6Z0; -.
DR STRING; 287.DR97_3099; -.
DR PaxDb; Q9I6Z0; -.
DR PRIDE; Q9I6Z0; -.
DR EnsemblBacteria; AAG03532; AAG03532; PA0142.
DR GeneID; 879447; -.
DR KEGG; pae:PA0142; -.
DR PATRIC; fig|208964.12.peg.148; -.
DR PseudoCAP; PA0142; -.
DR HOGENOM; CLU_012358_2_3_6; -.
DR InParanoid; Q9I6Z0; -.
DR OMA; TWLAHGI; -.
DR PhylomeDB; Q9I6Z0; -.
DR BioCyc; MetaCyc:MON-15640; -.
DR BioCyc; PAER208964:G1FZ6-144-MON; -.
DR BRENDA; 3.5.4.32; 5087.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0102127; F:8-oxoguanine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0019239; F:deaminase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
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.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..449
FT /note="8-oxoguanine deaminase"
FT /id="PRO_0000418757"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 449 AA; 48303 MW; FA1F0E63FB811307 CRC64;
MSRTWIRNPL AIFTANGLDA AGGLVVEDGR IVELLGAGQQ PAQPCASQFD ASRHVVLPGL
VNTHHHFYQT LTRAWAPVVN QPLFPWLKTL YPVWARLTPE KLELATKVAL AELLLSGCTT
AADHHYLFPG GLEQAIDVQA GVVEELGMRA MLTRGSMSLG EKDGGLPPQQ TVQEAETILA
DSERLIARYH QRGDGARVQI ALAPCSPFSV TPEIMRASAE VAARHDVRLH THLAETLDEE
DFCLQRFGLR TVDYLDSVGW LGPRTWLAHG IHFNAEEIRR LGEAGTGICH CPSSNMRLAS
GICPTVELEA AGAPIGLGVD GSASNDASNM ILEARQALYL QRLRYGAERI TPELALGWAT
RGSARLLGRS DIGELAPGKQ ADLALFKLDE LRFSGSHDPL SALLLCAADR ADRVMVGGAW
RVVDGAVEGL DLAALIARHR AAASALIAG
