URE11_BRUA2
ID URE11_BRUA2 Reviewed; 570 AA.
AC Q2YPD5;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
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}; OrderedLocusNames=BAB1_0300;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, AND
RP CHARACTERIZATION OF ROLE IN VIRULENCE.
RX PubMed=17101645; DOI=10.1128/iai.01244-06;
RA Sangari F.J., Seoane A., Rodriguez M.C., Aguero J., Garcia Lobo J.M.;
RT "Characterization of the urease operon of Brucella abortus and assessment
RT of its role in virulence of the bacterium.";
RL Infect. Immun. 75:774-780(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
CC -!- FUNCTION: May protect brucellae during their passage through the
CC stomach. The major route of infection in human brucellosis is oral.
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 -!- DISRUPTION PHENOTYPE: Disruption of the ure1 gene cluster via a large
CC in-frame deletion in this gene abrogates urease activity.
CC {ECO:0000269|PubMed:17101645}.
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; AF361941; AAK51069.1; -; Genomic_DNA.
DR EMBL; AM040264; CAJ10256.1; -; Genomic_DNA.
DR RefSeq; WP_002963434.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YPD5; -.
DR SMR; Q2YPD5; -.
DR STRING; 359391.BAB1_0300; -.
DR MEROPS; M38.982; -.
DR EnsemblBacteria; CAJ10256; CAJ10256; BAB1_0300.
DR GeneID; 3789048; -.
DR KEGG; bmf:BAB1_0300; -.
DR PATRIC; fig|359391.11.peg.2348; -.
DR HOGENOM; CLU_000980_0_0_5; -.
DR OMA; GFDSHIH; -.
DR PhylomeDB; Q2YPD5; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000002719; 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; 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 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Metal-binding; Nickel; Reference proteome; Virulence.
FT CHAIN 1..570
FT /note="Urease subunit alpha 1"
FT /id="PRO_0000234141"
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
