ID   UREA_ORYSJ              Reviewed;         843 AA.
AC   B9GCH9;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2013, sequence version 2.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Urease;
DE            EC=3.5.1.5;
DE   AltName: Full=Urea amidohydrolase;
GN   OrderedLocusNames=Os12g0234800, LOC_Os12g13270; ORFNames=OsJ_35660;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
CC   -!- FUNCTION: Urea hydrolase involved in nitrogen recycling from ureide,
CC       purine, and arginine catabolism. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+); Xref=Rhea:RHEA:20557,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.5;
CC   -!- COFACTOR:
CC       Name=Ni cation; Xref=ChEBI:CHEBI:25516; Evidence={ECO:0000250};
CC       Note=Binds 2 nickel ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC       urea (urease route): step 1/1.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- PTM: Carboxylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000250}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the metallo-dependent
CC       hydrolases superfamily. Urease alpha subunit family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EEE52986.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP008218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP014968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CM000149; EEE52986.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_015620844.1; XM_015765358.1.
DR   AlphaFoldDB; B9GCH9; -.
DR   SMR; B9GCH9; -.
DR   STRING; 39947.B9GCH9; -.
DR   PRIDE; B9GCH9; -.
DR   GeneID; 107279825; -.
DR   KEGG; osa:107279825; -.
DR   HOGENOM; CLU_110878_0_0_1; -.
DR   OrthoDB; 183108at2759; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000000763; Chromosome 12.
DR   Proteomes; UP000007752; Chromosome 12.
DR   Proteomes; UP000059680; Chromosome 12.
DR   GO; GO:0035550; C:urease complex; IEA:InterPro.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   GO; GO:0009039; F:urease activity; IEA:UniProtKB-EC.
DR   GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00375; Urease_alpha; 1.
DR   CDD; cd00407; Urease_beta; 1.
DR   CDD; cd00390; Urease_gamma; 1.
DR   Gene3D; 2.10.150.10; -; 1.
DR   Gene3D; 2.30.40.10; -; 1.
DR   Gene3D; 3.30.280.10; -; 1.
DR   HAMAP; MF_01953; Urease_alpha; 1.
DR   HAMAP; MF_01954; Urease_beta; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR008221; Urease.
DR   InterPro; IPR011612; Urease_alpha_N_dom.
DR   InterPro; IPR017950; Urease_AS.
DR   InterPro; IPR005848; Urease_asu.
DR   InterPro; IPR017951; Urease_asu_c.
DR   InterPro; IPR002019; Urease_beta.
DR   InterPro; IPR036461; Urease_betasu_sf.
DR   InterPro; IPR002026; Urease_gamma/gamma-beta_su.
DR   InterPro; IPR036463; Urease_gamma_sf.
DR   InterPro; IPR040881; Urease_linker.
DR   InterPro; IPR029754; Urease_Ni-bd.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF00449; Urease_alpha; 1.
DR   Pfam; PF00699; Urease_beta; 1.
DR   Pfam; PF00547; Urease_gamma; 1.
DR   Pfam; PF18473; Urease_linker; 1.
DR   PIRSF; PIRSF001222; Urease; 1.
DR   PRINTS; PR01752; UREASE.
DR   SUPFAM; SSF51278; SSF51278; 1.
DR   SUPFAM; SSF51338; SSF51338; 2.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   SUPFAM; SSF54111; SSF54111; 1.
DR   TIGRFAMs; TIGR01792; urease_alph; 1.
DR   TIGRFAMs; TIGR00192; urease_beta; 1.
DR   TIGRFAMs; TIGR00193; urease_gam; 1.
DR   PROSITE; PS01120; UREASE_1; 1.
DR   PROSITE; PS00145; UREASE_2; 1.
DR   PROSITE; PS51368; UREASE_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Nickel; Reference proteome.
FT   CHAIN           1..843
FT                   /note="Urease"
FT                   /id="PRO_0000424248"
FT   DOMAIN          400..843
FT                   /note="Urease"
FT   ACT_SITE        591
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         405
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         407
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         488
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000250"
FT   BINDING         488
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000250"
FT   BINDING         490
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         517
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         543
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         631
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         488
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   843 AA;  90480 MW;  3FF2F2ABBEDEA8A2 CRC64;
     MKLVQREAEK LALHNAGFLA QKRLARGLRL NYTEAVALIA AQILEFVRDG DRTVTDLMDL
     GKQLLGRRQV LPAVPHLLET VQVEGTFMDG TKLITVHDPI SSDDGNLELA LHGSFLPVPS
     LEKFSSVGVD DFPGEVRFCS GHIVLNLHRR ALTLKVVNKA DRPIQIGSHY HFIEANPYLV
     FDRQRAYGMR LNIPAGTAVR FEPGDAKTVT LVSIGGRKVI RGGNGIADGA VNRSQLNEVM
     EKVIANGFGH EDYPDSSEGI IGDGTHDYSV DHEKYASMYG PTTGDKIRLG DTDLFAEIEK
     DYAIYGDECI FGGGKVLRDG MGQSAGYPAS DCLDTVVTNA VVIDYTGIYK ADIGINGGLI
     VAIGKAGNPD VMDMDGVNEE MIVGVNTEVI AAEGMIVTAG GIDCHVHFIC PQLAEEAIAS
     GITTLVGGGT GPAHGTCATT CTPSPSHMKL MLQSTDELPI NMGFTGKGNT TKPDGLAEII
     KAGAMGLKLH EDWGSTPAAI DNCLSVAEAF DIQVNIHTDT LNESGCVEHT IAAFKDRTIH
     TYHSEGAGGG HAPDIIKVCG VKNVLPSSTN PTRPFTLNTV DEHLDMLMVC HHLDRNIPED
     VAFAESRIRA ETIAAEDILH DMGAISIISS DSQAMGRIGE VITRTWQTAN KMKRQRGRLP
     ISSSPDAAED NDNFRIRRYI AKYTINPAIV NGFSDFVGSV EVGKLADLVI WKPSFFGAKP
     EMVIKGGAIA CANMGDPNAS IPTPEPVMMR PMFGAFGGAG SANSIAFVSK AAKEAGVAVQ
     YKLGKRVEAV GRVRGLTKLN MKLNDALPKI DVDPETYTVT ADGEVLRCQP TPTVPLSRNY
     FLF