ID URE1_ACIAD Reviewed; 566 AA. AC Q6FD83; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 02-SEP-2026, entry version 133. 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=ACIAD1091; OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Moraxellales; Moraxellaceae; Acinetobacter. OX NCBI_TaxID=62977; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33305 / BD413 / ADP1; RX PubMed=15514110; DOI=10.1093/nar/gkh910; RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.; RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, RT a versatile and naturally transformation competent bacterium."; RL Nucleic Acids Res. 32:5766-5779(2004). 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; CR543861; CAG67976.1; -; Genomic_DNA. DR RefSeq; WP_004921563.1; NC_005966.1. DR AlphaFoldDB; Q6FD83; -. DR SMR; Q6FD83; -. DR STRING; 202950.GCA_001485005_01276; -. DR MEROPS; M38.982; -. DR GeneID; 45233527; -. DR KEGG; aci:ACIAD1091; -. DR eggNOG; COG0804; Bacteria. DR HOGENOM; CLU_000980_0_0_6; -. DR OrthoDB; 9802793at2; -. DR BioCyc; ASP62977:ACIAD_RS05015-MONOMER; -. DR UniPathway; UPA00258; UER00370. DR Proteomes; UP000000430; 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..566 FT /note="Urease subunit alpha" FT /id="PRO_0000234129" FT DOMAIN 128..566 FT /note="Urease" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953" FT ACT_SITE 319 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953" FT BINDING 133 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953" FT BINDING 135 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953" FT BINDING 216 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 216 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 218 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953" FT BINDING 245 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953" FT BINDING 271 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953" FT BINDING 359 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 216 FT /note="N6-carboxylysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953" SQ SEQUENCE 566 AA; 61192 MW; 75691EE2513D67CA CRC64; MKMSRRAYAE MFGPTVGDRV RLADTELFIE VEQDLTTYGE EVKFGGGKVI RDGMGQSQLL ADEVADTVIT NALIVDWWGI VKADVGLKNG RIWKIGKAGN PDIQPDITIP LGAATEVIAG EGQILTAGGI DTHIHWICPQ QVETALMSGV TTMVGGGTGP AAGTSATTVT PGPWHIGTML QAIDDLPMNI GLLGKGNLSL PDPIREQIKA GVVGLKLHED WGSTPAAIDN CLSVADEFDV QVAIHTDTLN ESGFLEETLA AFKNRTIHTY HTEGAGGGHA PDILKAIGQA NVLPSSTNPT RPYTINTIDE HLDMLMVCHH LDPAIAEDVA FAESRIRRET IAAEDILQDL GAIAMMSSDS QAMGRVGEVI IRTWQTAHKM KVQRGALQGD ETSHDNSRVK RYIAKYTINP AITHGLSHEI GSVEEGKLAD LVLWKPAFFG VKPSMIIKGG MIAAAPMGDI NASIPTPQPV HYRPMFGAYP RGVHNTCITF LSQAAIDDGV AEKLKLKKLI SPCKNTRQIT KADMKHNTYC PVMDVHPETY EVRADGELLT CEPADVLPMA QRYFLF //