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Database: UniProt
Entry: A0A067JSC9_JATCU
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Original site: A0A067JSC9_JATCU 
ID   A0A067JSC9_JATCU        Unreviewed;       837 AA.
AC   A0A067JSC9;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   13-SEP-2023, entry version 48.
DE   RecName: Full=Urease {ECO:0000256|ARBA:ARBA00013883, ECO:0000256|PIRNR:PIRNR001222};
DE            EC=3.5.1.5 {ECO:0000256|ARBA:ARBA00012934, ECO:0000256|PIRNR:PIRNR001222};
DE   AltName: Full=Urea amidohydrolase {ECO:0000256|PIRNR:PIRNR001222};
GN   ORFNames=JCGZ_17930 {ECO:0000313|EMBL:KDP26772.1};
OS   Jatropha curcas (Barbados nut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Jatropheae;
OC   Jatropha.
OX   NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP26772.1, ECO:0000313|Proteomes:UP000027138};
RN   [1] {ECO:0000313|EMBL:KDP26772.1, ECO:0000313|Proteomes:UP000027138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. GZQX0401 {ECO:0000313|Proteomes:UP000027138};
RC   TISSUE=Young leaves {ECO:0000313|EMBL:KDP26772.1};
RX   PubMed=24837971; DOI=10.1371/journal.pone.0097878;
RA   Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.;
RT   "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha curcas
RT   L.) Seedlings Exposed to Salt Stress.";
RL   PLoS ONE 9:E97878-E97878(2014).
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:0000256|PIRNR:PIRNR001222};
CC   -!- COFACTOR:
CC       Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001222-51};
CC       Note=Binds 2 nickel ions per subunit. {ECO:0000256|PIRSR:PIRSR001222-
CC       51};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC       urea (urease route): step 1/1. {ECO:0000256|ARBA:ARBA00004897,
CC       ECO:0000256|PIRNR:PIRNR001222}.
CC   -!- PTM: Carbamylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000256|PIRSR:PIRSR001222-50}.
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DR   EMBL; KK914893; KDP26772.1; -; Genomic_DNA.
DR   RefSeq; XP_012085638.1; XM_012230248.1.
DR   AlphaFoldDB; A0A067JSC9; -.
DR   STRING; 180498.A0A067JSC9; -.
DR   MEROPS; M38.982; -.
DR   GeneID; 105644779; -.
DR   KEGG; jcu:105644779; -.
DR   OrthoDB; 1408002at2759; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000027138; Unassembled WGS sequence.
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; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.10.150.10; Urease, beta subunit; 1.
DR   Gene3D; 3.30.280.10; Urease, gamma-like subunit; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 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-like.
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   NCBIfam; TIGR01792; urease_alph; 1.
DR   NCBIfam; TIGR00192; urease_beta; 1.
DR   NCBIfam; TIGR00193; urease_gam; 1.
DR   PANTHER; PTHR33569; UREASE; 1.
DR   PANTHER; PTHR33569:SF1; UREASE; 1.
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; SSF51338; Composite domain of metallo-dependent hydrolases; 2.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51278; Urease, beta-subunit; 1.
DR   SUPFAM; SSF54111; Urease, gamma-subunit; 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 {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001222};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR001222};
KW   Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|PIRNR:PIRNR001222};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027138}.
FT   DOMAIN          399..837
FT                   /note="Urease"
FT                   /evidence="ECO:0000259|PROSITE:PS51368"
FT   ACT_SITE        590
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-52,
FT                   ECO:0000256|PROSITE-ProRule:PRU00700"
FT   BINDING         404
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   BINDING         406
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   BINDING         487
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   BINDING         487
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   BINDING         489
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00700"
FT   BINDING         516
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   BINDING         542
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   BINDING         630
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   MOD_RES         487
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-50"
SQ   SEQUENCE   837 AA;  89398 MW;  629ACD7B85E1F83A CRC64;
     MKLTPREVDK LGLHNAGFLA QKRLARGLTL NYTEAVALIA TQILEFVRDG NKTVAELMDL
     GKQLLGRRQV LPAVPHLLHT VQVEGTFPDG TKLVTVHDPI ASENGNLELA LHGSFLPVPS
     LDKFPGVDDD EIPGVIIFGD GNITLNPGRK AVILRVVNRG DRPIQVGSHY HFIETNPSLY
     FDRMKAYGMR LNILAGTATR FEPGESKSVI LVSIGGGKVI RGGNGIVDGP VDDANYEAVA
     KAITEGGFGN QEETNASEGV TGEGSTFSTI VSHEAYANMY GPTTGDKIRL GDTNLYAEIE
     RDFASYGDEC IFGGGKVIRD GMGQSCGDQP VDYLDTVITN AVIIDYSGIY KADIGIRGGI
     IAAIGKAGNP DTMNDVNDDM IIGVNTEVIA GEGMIITAGA IDCHVHFICP QLAYEAISSG
     ITTLVGGGTG PADGTRATTC TPAPFQMKLM LQSTDDLPLN FGFTGKGNGS KPAELREIIE
     AGAMGLKLHE DWGTTPAAID SCLTVAEEYD IQVNIHTDTL NESGFVEHTI AAFNGRTIHT
     YHSEGAGGGH APDIIKVCGV KNVLPSSTNP TRPYTRNTID EHLDMLMVCH HLDKDIPEDV
     AFAESRIRAE TIAAEDILHD MGAISIISSD SQAMGRIGEV ISRTWQTADK MKSQRGAIGP
     GGSDNDNFRI KRYIAKYTIN PAVANGFADL IGSVEVGKFA DLVLWKPSFF GAKPELVLKG
     GVIAWADMGD PNASIPTPEP VISRPMFGAY GKAGSANSIA FVSKAAVNNG IKAMYRLNKM
     VKAVGDVRRL TKLDMKLNDA LPSITVDPET YIVTADNEVL TCAAATTVPL SRNYFLF
//
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