UREA_ORYSI
ID UREA_ORYSI Reviewed; 843 AA.
AC E0ZS48;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Urease {ECO:0000303|PubMed:20631318};
DE EC=3.5.1.5 {ECO:0000269|PubMed:20631318};
DE AltName: Full=Urea amidohydrolase {ECO:0000305};
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Hunan Late 2;
RX PubMed=20631318; DOI=10.1104/pp.110.160929;
RA Cao F.Q., Werner A.K., Dahncke K., Romeis T., Liu L.H., Witte C.P.;
RT "Identification and characterization of proteins involved in rice urea and
RT arginine catabolism.";
RL Plant Physiol. 154:98-108(2010).
CC -!- FUNCTION: Urea hydrolase involved in nitrogen recycling from ureide,
CC purine, and arginine catabolism. {ECO:0000269|PubMed:20631318}.
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 Evidence={ECO:0000269|PubMed:20631318};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20558;
CC Evidence={ECO:0000269|PubMed:20631318};
CC -!- COFACTOR:
CC Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC Evidence={ECO:0000250|UniProtKB:P07374};
CC Note=Binds 2 nickel ions per subunit. {ECO:0000250|UniProtKB:P18314};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.53 mM for urea {ECO:0000269|PubMed:20631318};
CC -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC urea (urease route): step 1/1. {ECO:0000305}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:P07374}.
CC -!- PTM: Carboxylation allows a single lysine to coordinate two nickel
CC ions. {ECO:0000250|UniProtKB:P07374}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the metallo-dependent
CC hydrolases superfamily. Urease alpha subunit family. {ECO:0000305}.
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DR EMBL; HM369060; ADK73999.1; -; mRNA.
DR AlphaFoldDB; E0ZS48; -.
DR SMR; E0ZS48; -.
DR SABIO-RK; E0ZS48; -.
DR UniPathway; UPA00258; UER00370.
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; IDA:UniProtKB.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Nickel.
FT CHAIN 1..843
FT /note="Urease"
FT /id="PRO_0000424247"
FT DOMAIN 400..843
FT /note="Urease"
FT ACT_SITE 591
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P18314"
FT BINDING 405
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07374"
FT BINDING 407
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07374"
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|UniProtKB:P07374"
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|UniProtKB:P07374"
FT BINDING 490
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P18314"
FT BINDING 517
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07374"
FT BINDING 543
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P07374"
FT BINDING 631
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P07374"
FT MOD_RES 488
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250|UniProtKB:P07374"
SQ SEQUENCE 843 AA; 90520 MW; 9876B16DB28A8210 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
EKVIAKGFGH EDYPDSSEGI IGDGTHDYIV 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
