ID A0A381GDR7_CITFR Unreviewed; 486 AA. AC A0A381GDR7; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 05-DEC-2018, entry version 2. 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(+); 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|HAMAP-Rule:MF_01953, CC ECO:0000256|RuleBase:RU000510, ECO:0000256|SAAS:SAAS00354639}; CC -!- COFACTOR: CC Name=Ni cation; Xref=ChEBI:CHEBI:25516; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01953, CC ECO:0000256|RuleBase:RU000510}; CC Note=Binds 2 nickel ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01953, ECO:0000256|RuleBase:RU000510}; CC -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) CC from urea (urease route): step 1/1. {ECO:0000256|HAMAP- CC Rule:MF_01953, ECO:0000256|SAAS:SAAS00354661}. CC -!- SUBUNIT: Heterotrimer of UreA (gamma), UreB (beta) and UreC CC (alpha) subunits. Three heterotrimers associate to form the active CC enzyme. {ECO:0000256|HAMAP-Rule:MF_01953}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01953, CC ECO:0000256|PROSITE-ProRule:PRU00700, CC ECO:0000256|SAAS:SAAS00548017}. CC -!- PTM: Carbamylation allows a single lysine to coordinate two nickel CC ions. {ECO:0000256|HAMAP-Rule:MF_01953}. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases CC superfamily. Urease alpha subunit family. {ECO:0000256|HAMAP- CC Rule:MF_01953, ECO:0000256|RuleBase:RU004158, CC ECO:0000256|SAAS:SAAS00849550}. 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 UniPathway; UPA00258; UER00370. DR Proteomes; UP000255366; Unassembled WGS sequence. DR GO; GO:0009039; F:urease activity; IEA:UniProtKB-EC. 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 PANTHER; PTHR43440; PTHR43440; 1. 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 Complete proteome {ECO:0000313|Proteomes:UP000255366}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01953, ECO:0000256|PROSITE- KW ProRule:PRU00700, ECO:0000256|SAAS:SAAS00432677}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01953, ECO:0000256|PROSITE- KW ProRule:PRU00700, ECO:0000256|RuleBase:RU000510, KW ECO:0000256|SAAS:SAAS00444540}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01953, KW ECO:0000256|RuleBase:RU000510, ECO:0000256|SAAS:SAAS00444531}; KW Nickel {ECO:0000256|HAMAP-Rule:MF_01953, KW ECO:0000256|RuleBase:RU000510, ECO:0000256|SAAS:SAAS00432700}. FT DOMAIN 48 486 Urease. {ECO:0000259|PROSITE:PS51368}. FT ACT_SITE 239 239 Proton donor. {ECO:0000256|HAMAP-Rule: FT MF_01953, ECO:0000256|PROSITE-ProRule: FT PRU00700}. FT METAL 53 53 Nickel 1; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01953}. FT METAL 55 55 Nickel 1; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01953}. FT METAL 136 136 Nickel 1; via carbamate group. FT {ECO:0000256|HAMAP-Rule:MF_01953}. FT METAL 136 136 Nickel 2; via carbamate group. FT {ECO:0000256|HAMAP-Rule:MF_01953}. FT METAL 165 165 Nickel 2; via pros nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01953}. FT METAL 191 191 Nickel 2; via tele nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01953}. FT METAL 279 279 Nickel 1. {ECO:0000256|HAMAP-Rule: FT MF_01953}. FT BINDING 138 138 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01953, ECO:0000256|PROSITE-ProRule: FT PRU00700}. FT MOD_RES 136 136 N6-carboxylysine. {ECO:0000256|HAMAP- FT Rule:MF_01953}. 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 //