URE12_BRUAB
ID URE12_BRUAB Reviewed; 573 AA.
AC Q57CE8;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Urease subunit alpha 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01953};
GN Name=ureC2 {ECO:0000255|HAMAP-Rule:MF_01953};
GN OrderedLocusNames=BruAb1_1355;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Proteobacteria; 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;
CC Evidence={ECO:0000255|HAMAP-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}.
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DR EMBL; AE017223; AAX74686.1; -; Genomic_DNA.
DR RefSeq; WP_002966881.1; NC_006932.1.
DR AlphaFoldDB; Q57CE8; -.
DR SMR; Q57CE8; -.
DR EnsemblBacteria; AAX74686; AAX74686; BruAb1_1355.
DR GeneID; 3787947; -.
DR KEGG; bmb:BruAb1_1355; -.
DR HOGENOM; CLU_000980_0_0_5; -.
DR OMA; CHHLSHD; -.
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; 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; IPR001763; Rhodanese-like_dom.
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; 2.
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; Hydrolase; Metal-binding; Nickel.
FT CHAIN 1..573
FT /note="Urease subunit alpha 2"
FT /id="PRO_0000234140"
FT DOMAIN 135..573
FT /note="Urease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT ACT_SITE 326
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 140
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 142
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 223
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 223
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 225
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 252
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 278
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 366
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 223
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
SQ SEQUENCE 573 AA; 60738 MW; C9A71703FF500BF6 CRC64;
MTQISRQQYA DLYGPTIGDK IRLGDSDLYV EIEKDLRATY GDELQYGGGK TLRDGMGSEN
FLTQEAGCLD LVITNVTVID AIQGVVKADV GIRNGRIVGL GKAGNPSTKD GVTRGLVTGA
STDAISGEHL ILTAGGMDTH VHYIAPQQVE AALSNGITTL WGGGIGPVDG TNGVTTTNGP
WNLEMMLRSI EGLPINFGIQ GKGNSTGIAP LIEQLEAGAA GFKVHEDYGA TPATIRACLS
VADEYDVSVA VHTDTLNESG YVEDTIAAFD GRSVHTYHSE GAGGGHAPDL LKVVGQNNIL
PSSTNPTLPC GKNSVAELFD MIMVCHNLNP KIPSDVAFAE SRVRAETIVA ESVLHDMGAI
SMIGSDSQAM GRLGETFLRA IQTADAMKKA RGPLPEDAPG NDNFRVLRYI AKVTINPALT
AGVGDVIGSI ESGKFADLVL WEPAFFGVKP KLVLKGGLVA WANMGDPNAS LPTPQPMYYR
PMFAAYGSAL QKTSITFVSR AAYDKGVADR FGLQRLVMPV SGTRVIGKAH MVRNSYLPNI
EVDPQTFAVK VDGVHATVKP PQSISLNQLY FFS
