ID URE11_BRUAB Reviewed; 570 AA. AC Q93T81; Q57F85; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 123. DE RecName: Full=Urease subunit alpha 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01953}; GN Name=ureC1 {ECO:0000255|HAMAP-Rule:MF_01953}; GN OrderedLocusNames=BruAb1_0296; OS Brucella abortus biovar 1 (strain 9-941). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=262698; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=9-941; RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005; RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.; RT "Completion of the genome sequence of Brucella abortus and comparison to RT the highly similar genomes of Brucella melitensis and Brucella suis."; RL J. Bacteriol. 187:2715-2726(2005). 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: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; AE017223; AAX73699.1; -; Genomic_DNA. DR RefSeq; WP_002963434.1; NC_006932.1. DR AlphaFoldDB; Q93T81; -. DR SMR; Q93T81; -. DR EnsemblBacteria; AAX73699; AAX73699; BruAb1_0296. DR GeneID; 3789048; -. DR KEGG; bmb:BruAb1_0296; -. DR HOGENOM; CLU_000980_0_0_5; -. DR UniPathway; UPA00258; UER00370. DR Proteomes; UP000000540; Chromosome I. 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; 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; 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. FT CHAIN 1..570 FT /note="Urease subunit alpha 1" FT /id="PRO_0000234139" FT DOMAIN 131..570 FT /note="Urease" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953" FT ACT_SITE 322 FT /note="Proton donor" 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 138 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953" FT BINDING 219 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 219 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 221 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953" FT BINDING 248 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953" FT BINDING 274 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953" FT BINDING 362 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 219 FT /note="N6-carboxylysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953" SQ SEQUENCE 570 AA; 61011 MW; 648464AD7EDBB7EC CRC64; MPARISRATY AQMFGPTVGD KVRLADTDLI IEVERDLTTY GEEVKFGGGK VIRDGMGQSQ LSRAEGAMDT VITNALILDH SGIYKADIGL LDGRIALIGK AGNPDTQPGI SIIIGPGTEI IAGEGKIVTA GGIDTHVHFI SPQQVDEALN AGITCMVGGG TGPAHGTLAT TCTPGPWHIA RLIQSFDGLP MNIGVFGKGN ASLPGALEEM VRAGACGLKL HEDWGCTPAA IDNCLSVADH FDVQVAIHTD TLNEGGFVED TLNAFKGRTI HSFHTEGAGG GHAPDIIRVC QYPNVLPAST NPTRPYTVNT IAEHLDMLMV CHHLSPAIPE DIAFAESRIR KETIAAEDIL HDMGAFSIIS SDSQAMGRVG EMIIRCWQTA DKMKKQRGSL PDDRPGNDNY RARRYIAKYT INPAIAHGMA HEIGSVEVGK RADLVLWNPA FFGVKPDMVL LGGWIATAPM GDANGSIPTP QPMHTRPMFG SFGKALTNTS ITFVSQAAMD EGLREKIGVD KQLVAVVNTR GGIGKHSMIL NNAMPQMEVD PETYEVRADG ELLTCEPVDV VPMAQRYFLF //