ID URE1_CITK8 Reviewed; 567 AA. AC A8APV0; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 02-SEP-2026, entry version 95. DE RecName: Full=Urease subunit alpha {ECO:0000255|HAMAP-Rule:MF_01953}; DE EC=3.5.1.5 {ECO:0000255|HAMAP-Rule:MF_01953}; DE AltName: Full=Urea amidohydrolase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01953}; GN Name=ureC {ECO:0000255|HAMAP-Rule:MF_01953}; GN OrderedLocusNames=CKO_04457; OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Citrobacter. OX NCBI_TaxID=290338; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696; RG The Citrobacter koseri Genome Sequencing Project; RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W., RA Johnson M., Thiruvilangam P., Wilson R.; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=urea + 2 H2O + H(+) = hydrogencarbonate + 2 NH4(+); CC Xref=Rhea:RHEA:20557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16199, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938; EC=3.5.1.5; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01953}; CC -!- COFACTOR: CC Name=Ni cation; Xref=ChEBI:CHEBI:25516; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01953}; CC Note=Binds 2 nickel ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01953}; CC -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from CC urea (urease route): step 1/1. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01953}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01953}. CC -!- PTM: Carboxylation allows a single lysine to coordinate two nickel CC ions. {ECO:0000255|HAMAP-Rule:MF_01953}. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC Urease alpha subunit family. {ECO:0000255|HAMAP-Rule:MF_01953}. 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; CP000822; ABV15513.1; -; Genomic_DNA. DR RefSeq; WP_012135196.1; NC_009792.1. DR AlphaFoldDB; A8APV0; -. DR SMR; A8APV0; -. DR STRING; 290338.CKO_04457; -. DR MEROPS; M38.982; -. DR GeneID; 45138026; -. DR KEGG; cko:CKO_04457; -. DR HOGENOM; CLU_000980_0_0_6; -. DR OrthoDB; 9802793at2; -. DR UniPathway; UPA00258; UER00370. DR Proteomes; UP000008148; Chromosome. 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-UniRule. DR CDD; cd00375; Urease_alpha; 1. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 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; IPR029754; Urease_Ni-bd. DR NCBIfam; NF009685; PRK13206.1; 1. DR NCBIfam; NF009686; PRK13207.1; 1. DR NCBIfam; TIGR01792; urease_alph; 1. DR PANTHER; PTHR43440; UREASE; 1. DR PANTHER; PTHR43440:SF1; UREASE; 1. DR Pfam; PF01979; Amidohydro_1; 1. DR Pfam; PF00449; Urease_alpha; 1. DR PRINTS; PR01752; UREASE. DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 2. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 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; Hydrolase; Metal-binding; Nickel; Reference proteome. FT CHAIN 1..567 FT /note="Urease subunit alpha" FT /id="PRO_1000070654" FT DOMAIN 129..567 FT /note="Urease" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953" FT ACT_SITE 320 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953" FT BINDING 134 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953" FT BINDING 136 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953" FT BINDING 217 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="1" FT /note="via carbamate group" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953" FT BINDING 217 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="2" FT /note="via carbamate group" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953" FT BINDING 219 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953" FT BINDING 246 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953" FT BINDING 272 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953" FT BINDING 360 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953" FT MOD_RES 217 FT /note="N6-carboxylysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953" SQ SEQUENCE 567 AA; 60475 MW; B9CAE08BFA390FE5 CRC64; MTEISRQAYA DMFGPTTGDR VRLADTELWI EVENDLTAYG EEVKFGGGKV IRDGMGQGQM RARACVDLVI TNALIVDHWG IVKADIGIKD GRIFAIGKAG NPDIQPNVTI PIGVGTEAIA GEGKIVTAGG VDTHIHWICP QQAEEALVSG VTTMIGGGTG PAAGTNATTC TPGPWYIARM LQAADSLPVN IGFLGKGNGS NPDALREQIA AGAIGLKIHE DWGATPAAID CALTVAEEMD IQVALHSDTL NESGFVEDTL AAIGDRTIHT FHTEGAGGGH APDIITACAH PHILPSSTNP TLPYTVNTID EHLDMLMVCH HLDPDIAEDV AFAESRIRRE TIAAEDVLHD LGAFSLTSSD SQAMGRVGEV ILRTWQVAHR MKVQRGPLAE ETGDNDNQRV KRYIAKYTIN PALTHGIAHE VGSVEAGKLA DLVLWSPAFF GVKPATLIKG GMIVCAPMGD INASIPTPQP VHYRPMFGAL GAARHHCRLT FLSQAAVENG IAQQLNLRSA TAVVKGCRTV KKADMIHNSL QPNITVDAQT YEVRIDGEPI TSEPADVLPM AQRYFLF //