ID A0A381GDR7_CITFR Unreviewed; 486 AA. AC A0A381GDR7; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 25-MAY-2022, entry version 12. DE RecName: Full=Urease subunit alpha {ECO:0000256|HAMAP-Rule:MF_01953}; DE EC=3.5.1.5 {ECO:0000256|HAMAP-Rule:MF_01953}; DE AltName: Full=Urea amidohydrolase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01953}; GN Name=ureC_1 {ECO:0000313|EMBL:SUX69438.1}; GN Synonyms=ureC {ECO:0000256|HAMAP-Rule:MF_01953}; GN ORFNames=NCTC6267_00814 {ECO:0000313|EMBL:SUX69438.1}; OS Citrobacter freundii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex. OX NCBI_TaxID=546 {ECO:0000313|EMBL:SUX69438.1, ECO:0000313|Proteomes:UP000255366}; RN [1] {ECO:0000313|EMBL:SUX69438.1, ECO:0000313|Proteomes:UP000255366} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC6267 {ECO:0000313|EMBL:SUX69438.1, RC ECO:0000313|Proteomes:UP000255366}; RG Pathogen Informatics; RA Doyle S.; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. 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|HAMAP-Rule:MF_01953, CC ECO:0000256|RuleBase:RU000510}; CC -!- COFACTOR: CC Name=Ni cation; Xref=ChEBI:CHEBI:25516; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01953, CC ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|RuleBase:RU000510}; CC Note=Binds 2 nickel ions per subunit. {ECO:0000256|HAMAP-Rule:MF_01953, CC ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|RuleBase:RU000510}; 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|HAMAP-Rule:MF_01953}. CC -!- SUBUNIT: Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) CC subunits. Three heterotrimers associate to form the active enzyme. CC {ECO:0000256|HAMAP-Rule:MF_01953}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01953, CC ECO:0000256|PROSITE-ProRule:PRU00700}. CC -!- PTM: Carbamylation allows a single lysine to coordinate two nickel CC ions. {ECO:0000256|PIRSR:PIRSR611612-50}. CC -!- PTM: Carboxylation allows a single lysine to coordinate two nickel CC ions. {ECO:0000256|HAMAP-Rule:MF_01953}. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC Urease alpha subunit family. {ECO:0000256|HAMAP-Rule:MF_01953, CC ECO:0000256|RuleBase:RU004158}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; UFWO01000001; SUX69438.1; -; Genomic_DNA. DR EnsemblBacteria; SUX69438; SUX69438; NCTC6267_00814. DR UniPathway; UPA00258; UER00370. DR Proteomes; UP000255366; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule. DR GO; GO:0009039; F:urease activity; IEA:UniProtKB-UniRule. DR GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway. DR CDD; cd00375; Urease_alpha; 1. DR Gene3D; 2.30.40.10; -; 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; IPR011612; Urease_alpha_N_dom. DR InterPro; IPR017950; Urease_AS. DR InterPro; IPR005848; Urease_asu. DR InterPro; IPR017951; Urease_asu_c. DR InterPro; IPR029754; Urease_Ni-bd. DR Pfam; PF01979; Amidohydro_1; 1. DR Pfam; PF00449; Urease_alpha; 1. DR PRINTS; PR01752; UREASE. DR SUPFAM; SSF51338; SSF51338; 1. DR SUPFAM; SSF51556; SSF51556; 1. DR TIGRFAMs; TIGR01792; urease_alph; 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01953, ECO:0000256|PROSITE- KW ProRule:PRU00700}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01953}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01953}; KW Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|HAMAP-Rule:MF_01953}. FT DOMAIN 48..486 FT /note="Urease" FT /evidence="ECO:0000259|PROSITE:PS51368" FT ACT_SITE 239 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953, FT ECO:0000256|PIRSR:PIRSR611612-52" FT METAL 53 FT /note="Nickel 1; via tele nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953, FT ECO:0000256|PIRSR:PIRSR611612-51" FT METAL 55 FT /note="Nickel 1; via tele nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953, FT ECO:0000256|PIRSR:PIRSR611612-51" FT METAL 136 FT /note="Nickel 1; via carbamate group" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953, FT ECO:0000256|PIRSR:PIRSR611612-51" FT METAL 136 FT /note="Nickel 2; via carbamate group" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953, FT ECO:0000256|PIRSR:PIRSR611612-51" FT METAL 165 FT /note="Nickel 2; via pros nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953, FT ECO:0000256|PIRSR:PIRSR611612-51" FT METAL 191 FT /note="Nickel 2; via tele nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953, FT ECO:0000256|PIRSR:PIRSR611612-51" FT METAL 279 FT /note="Nickel 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953, FT ECO:0000256|PIRSR:PIRSR611612-51" FT BINDING 138 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953, FT ECO:0000256|PROSITE-ProRule:PRU00700" FT MOD_RES 136 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953, FT ECO:0000256|PIRSR:PIRSR611612-50" SQ SEQUENCE 486 AA; 51800 MW; 07C521074E9DD8A3 CRC64; MKADIGIKDA RIFAIGKAGN PDIQPDVTIP IGVGTEVIAG EGKIVTAGGV DTHIHWICPQ QAQEALISGV TTMIGGGTGP AAGTHATTCT PGPWYIARML QAADALPVNI GLLGKGNGSN PDALREQITA GAIGLKIHED WGATPATINC SLEVAEEMDI QVALHSDTLN ESGFVEDTLA AIGDRTIHTF HTEGAGGGHA PDIITACAHP NILPSSTNPT LPYTVNTIDE HLDMLMVCHH LDPDIAEDVA FAESRIRRET IAAEDVLHDI GAFSLTSSDS QAMGRVGEVI LRTWQVAHRM KVQRGPLAEE TGDNDNQRVK RYVAKYTINP ALTHGIAHEV GSVEPGKLAD LVLWSPAFFG VKPATIVKGG MIACAPMGDI NASIPTPQPV HYRMMFGALG AARHRTRLTF ISQAAHAQNI PQQLNLQSAI AVVKGCRTVK KADMIHNDLQ PNITVDAQTY EVRIDGELIT SEPADVLPMA QRYFLF //