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Database: UniProt
Entry: A0A2G3AEY0_CAPAN
LinkDB: A0A2G3AEY0_CAPAN
Original site: A0A2G3AEY0_CAPAN 
ID   A0A2G3AEY0_CAPAN        Unreviewed;       651 AA.
AC   A0A2G3AEY0;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   13-SEP-2023, entry version 25.
DE   RecName: Full=urease {ECO:0000256|ARBA:ARBA00012934};
DE            EC=3.5.1.5 {ECO:0000256|ARBA:ARBA00012934};
GN   ORFNames=T459_00666 {ECO:0000313|EMBL:PHT92784.1};
OS   Capsicum annuum (Capsicum pepper).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX   NCBI_TaxID=4072 {ECO:0000313|EMBL:PHT92784.1, ECO:0000313|Proteomes:UP000222542};
RN   [1] {ECO:0000313|EMBL:PHT92784.1, ECO:0000313|Proteomes:UP000222542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. CM334 {ECO:0000313|Proteomes:UP000222542};
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., Lee J.M.,
RA   Cheong K., Shin H.S., Kim S.B., Han K., Lee J., Park M., Lee H.A.,
RA   Lee H.Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E., Jeon J.,
RA   Kim H., Choi G., Song H., Lee J., Lee S.C., Kwon J.K., Lee H.Y., Koo N.,
RA   Hong Y., Kim R.W., Kang W.H., Huh J.H., Kang B.C., Yang T.J., Lee Y.H.,
RA   Bennetzen J.L., Choi D.;
RT   "New reference genome sequences of hot pepper reveal the massive evolution
RT   of plant disease-resistance genes by retroduplication.";
RL   Genome Biol. 18:R210.1-R210.11(2017).
CC   -!- COFACTOR:
CC       Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC         Evidence={ECO:0000256|PIRSR:PIRSR611612-51};
CC       Note=Binds 2 nickel ions per subunit. {ECO:0000256|PIRSR:PIRSR611612-
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   -!- PTM: Carbamylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000256|PIRSR:PIRSR611612-50}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PHT92784.1}.
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DR   EMBL; AYRZ02000001; PHT92784.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G3AEY0; -.
DR   STRING; 4072.A0A2G3AEY0; -.
DR   EnsemblPlants; PHT92784; PHT92784; T459_00666.
DR   Gramene; PHT92784; PHT92784; T459_00666.
DR   OMA; DTMDGVH; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000222542; Chromosome 1.
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   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.10.150.10; Urease, beta subunit; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 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; 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; IPR040881; Urease_linker.
DR   InterPro; IPR029754; Urease_Ni-bd.
DR   NCBIfam; TIGR01792; urease_alph; 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; PF18473; Urease_linker; 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   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|PROSITE-
KW   ProRule:PRU00700};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR611612-51};
KW   Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|PIRSR:PIRSR611612-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000222542}.
FT   DOMAIN          213..651
FT                   /note="Urease"
FT                   /evidence="ECO:0000259|PROSITE:PS51368"
FT   ACT_SITE        404
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-52,
FT                   ECO:0000256|PROSITE-ProRule:PRU00700"
FT   BINDING         218
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT   BINDING         220
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT   BINDING         301
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT   BINDING         301
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT   BINDING         303
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00700"
FT   BINDING         330
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT   BINDING         356
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT   BINDING         444
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT   MOD_RES         301
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-50"
SQ   SEQUENCE   651 AA;  69621 MW;  9815C357451F4BF6 CRC64;
     MRAHGMRLNI PAGTATRFEP GETRSVVLVT ISGKQVIRGG NAVADCPVDD AKVMKLMGAL
     SEGGFGNLEE PNAREGVVGE ESGFSFSMSH EAYANMYGPT TGDRIRLGDT DLFAEIEKDF
     GIYGDECVFG GGKVLRDGMG QACGYSSVAC LDTVITNAVV IDYTGIFKCD IGIKDGRIVS
     LCKAGNPDVM NVDTIIGVNT EVIAGEGMIV TAGAIDCHVH FICPQLAYEA ISSGITTMIG
     GGTGPAHGTR ATTCTPGHVH MELMLQSTDE IPLNFGFTGK GNSSKADGLH EIIKAGAMGL
     KLHEDWGTTP AAIDMCLIVA DQYDIQVNIH TDTLNESGFV ERTIAAFKGR TIHTYHSEGA
     GGGHAPDIIK VCGVKNVIPS STNPTRPFTL NTVDEHLDML MVCHHLNKDI REDVAFAESR
     IRAETIAAED ILHDMGAISI ISSDSQAMGR IGEVICRTWQ TAHKMKSFRG PLDIDGPYND
     NFRIKRYIAK YTINPAIANG ISQYVGSVEV GKLADLVVWK PSFFGAKPEM VIKGGVIAWS
     NMGDPNASIP TPEPVLMRPM FGAFSKAAST NSIAFVSKAS LDAGIKDSYG LNKRVEAVTN
     VRNISKLDMK HNDALPDIKV DPETYTVTAD GTVLTCPPAA TVPLSRNYFL F
//
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