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Database: UniProt
Entry: A0A2G3DBT8_CAPCH
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Original site: A0A2G3DBT8_CAPCH 
ID   A0A2G3DBT8_CAPCH        Unreviewed;       834 AA.
AC   A0A2G3DBT8;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   31-JUL-2019, entry version 14.
DE   RecName: Full=Urease {ECO:0000256|PIRNR:PIRNR001222};
DE            EC=3.5.1.5 {ECO:0000256|PIRNR:PIRNR001222};
DE   AltName: Full=Urea amidohydrolase {ECO:0000256|PIRNR:PIRNR001222};
GN   ORFNames=BC332_00549 {ECO:0000313|EMBL:PHU28456.1};
OS   Capsicum chinense (Scotch bonnet) (Bonnet pepper).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae;
OC   Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Solanoideae;
OC   Capsiceae; Capsicum.
OX   NCBI_TaxID=80379 {ECO:0000313|EMBL:PHU28456.1, ECO:0000313|Proteomes:UP000224522};
RN   [1] {ECO:0000313|EMBL:PHU28456.1, ECO:0000313|Proteomes:UP000224522}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. PI159236 {ECO:0000313|Proteomes:UP000224522};
RC   TISSUE=Leaf {ECO:0000313|EMBL:PHU28456.1};
RX   PubMed=29089032; DOI=10.1186/s13059-017-1341-9;
RA   Kim S., Park J., Yeom S.I., Kim Y.M., Seo E., Kim K.T., Kim M.S.,
RA   Lee J.M., Cheong K., Shin H.S., Kim S.B., Han K., Lee J., Park M.,
RA   Lee H.A., Lee H.Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E.,
RA   Lee S.E., Jeon J., Kim H., Choi G., Song H., Lee J., Lee S.C.,
RA   Kwon J.K., Lee H.Y., Koo N., Hong Y., Kim R.W., Kang W.H., Huh J.H.,
RA   Kang B.C., Yang T.J., Lee Y.H., Bennetzen J.L., Choi D.;
RT   "New reference genome sequences of hot pepper reveal the massive
RT   evolution of plant disease-resistance genes by retroduplication.";
RL   Genome Biol. 18:R210.1-R210.11(2017).
RN   [2] {ECO:0000313|EMBL:PHU28456.1, ECO:0000313|Proteomes:UP000224522}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. PI159236 {ECO:0000313|Proteomes:UP000224522};
RC   TISSUE=Leaf {ECO:0000313|EMBL:PHU28456.1};
RA   Kim S., Park J., Yeom S.-I., Kim Y.-M., Seo E., Kim K.-T., Kim M.-S.,
RA   Lee J.M., Cheong K., Shin H.-S., Kim S.-B., Han K., Lee J., Park M.,
RA   Lee H.-A., Lee H.-Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E.,
RA   Lee S.E., Jeon J., Kim H., Choi G., Song H., Lee J., Lee S.-C.,
RA   Kwon J.-K., Lee H.-Y., Koo N., Hong Y., Kim R.W., Kang W.-H.,
RA   Huh J.H., Kang B.-C., Yang T.-J., Lee Y.-H., Bennetzen J.L., Choi D.;
RT   "Multiple reference genome sequences of hot pepper reveal the massive
RT   evolution of plant disease resistance genes by retroduplication.";
RL   J. Anim. Genet. bioRxivorg:115410-115410(2017).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+);
CC         Xref=Rhea:RHEA:20557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16199, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938;
CC         EC=3.5.1.5; Evidence={ECO:0000256|PIRNR:PIRNR001222};
CC   -!- COFACTOR:
CC       Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC         Evidence={ECO:0000256|PIRNR:PIRNR001222,
CC         ECO:0000256|PIRSR:PIRSR001222-51};
CC       Note=Binds 2 nickel ions per subunit.
CC       {ECO:0000256|PIRNR:PIRNR001222, ECO:0000256|PIRSR:PIRSR001222-51};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3)
CC       from urea (urease route): step 1/1.
CC       {ECO:0000256|PIRNR:PIRNR001222}.
CC   -!- PTM: Carbamylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000256|PIRSR:PIRSR001222-50}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the metallo-
CC       dependent hydrolases superfamily. Urease alpha subunit family.
CC       {ECO:0000256|PIRNR:PIRNR001222}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:PHU28456.1}.
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DR   EMBL; MCIT02000001; PHU28456.1; -; Genomic_DNA.
DR   OrthoDB; 183108at2759; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000224522; Chromosome 1.
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   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   Complete proteome {ECO:0000313|Proteomes:UP000224522};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001222, ECO:0000256|PROSITE-
KW   ProRule:PRU00700};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR001222,
KW   ECO:0000256|PIRSR:PIRSR001222-51};
KW   Nickel {ECO:0000256|PIRNR:PIRNR001222, ECO:0000256|PIRSR:PIRSR001222-
KW   51}; Reference proteome {ECO:0000313|Proteomes:UP000224522}.
FT   DOMAIN      396    834       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    587    587       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR611612-52, ECO:0000256|PROSITE-
FT                                ProRule:PRU00700}.
FT   METAL       401    401       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       403    403       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       484    484       Nickel 1; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       484    484       Nickel 2; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       513    513       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       539    539       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       627    627       Nickel 1. {ECO:0000256|PIRSR:PIRSR001222-
FT                                51}.
FT   BINDING     486    486       Substrate. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     484    484       N6-carboxylysine. {ECO:0000256|PIRSR:
FT                                PIRSR001222-50}.
SQ   SEQUENCE   834 AA;  90127 MW;  C394D698BE4515F2 CRC64;
     MNLVPREIEK LMLHNAGYLA QKRLARAQPL NYTEAVALIA AQVLEFVRDG DKSVAELMDM
     GRQLLGRRQV LPMVPHMLDT VQVEGTFPDG TKLITIHDPI SCENGNLDLA LHGSFLPVPP
     QDKFPVLEDS KIPGEMCFRD GLIVLNPQRK AVILKVTNTG DRPIQVGSHY HFIEVNPSLI
     FDRMRAHGMR LNIPAGTVTR FEPGETRSVV LVTISGKQVI RGGNAVADCP VDDAKVMKLM
     GALSEGGFGN LEEPNAREGV VGEESGFSFS MSHEAYANMY GPTTGDRIRL GDTDLFAEIE
     KDFGIYGDEC VFGGGKVLRD GMGQACGYPS VACLDTVITN AVVIDYTGIF KCDIGIKDGR
     IVSLCKAGNP DVMNVDTIIA VNTEVIAGEG MIVTAGAIDC HVHFICPQQA YEAISSGITT
     MIGGGTGPAH GTRATTCTPG HVHMELMLQS TDEIPLNFGF TGKGNSSKAD GLHEIIKAGA
     MGLKLHEDWG TTPAAIDMCL IVADQYDIQV NIHTDTLNES GFVERTIAAF KGRTIHTYHS
     EGAGGGHAPD IIKVCGVKNV IPSSTNPTRP FTLNTVDEHL DMLMVCHHLN KDIREDVAFA
     ESRIRAETIA AEDILHDMGA ISIISSDSQA MGRIGEVICR TWQTAHKMKS FRGPLDIDGP
     YNDNFRIKRY IAKYTINPAI ANGISQYVGS VEVGKLADLV VWKPSFFGAK PEMVIKGGVI
     AWSNMGDPNA SIPTPEPVLM RPMFGAFSKA ASTNSIAFVS KASLDAGIKD SYGLNKRVEA
     VTNVRNISKL DMKHNDALPD IKVDPETYTV TADGTVLTCP PAATVPLSRN YFLF
//
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