URE1_BEII9
ID URE1_BEII9 Reviewed; 570 AA.
AC B2IIJ1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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}; OrderedLocusNames=Bind_1041;
OS Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIMB
OS 8712).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Beijerinckiaceae; Beijerinckia.
OX NCBI_TaxID=395963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Dunfield P.F., Dedysh S.N.,
RA Liesack W., Saw J.H., Alam M., Chen Y., Murrell J.C., Richardson P.;
RT "Complete sequence of chromosome of Beijerinckia indica subsp. indica ATCC
RT 9039.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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; CP001016; ACB94684.1; -; Genomic_DNA.
DR RefSeq; WP_012384041.1; NC_010581.1.
DR AlphaFoldDB; B2IIJ1; -.
DR SMR; B2IIJ1; -.
DR STRING; 395963.Bind_1041; -.
DR MEROPS; M38.982; -.
DR EnsemblBacteria; ACB94684; ACB94684; Bind_1041.
DR KEGG; bid:Bind_1041; -.
DR eggNOG; COG0804; Bacteria.
DR HOGENOM; CLU_000980_0_0_5; -.
DR OMA; GFDSHIH; -.
DR OrthoDB; 157757at2; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000001695; 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-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 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Metal-binding; Nickel; Reference proteome.
FT CHAIN 1..570
FT /note="Urease subunit alpha"
FT /id="PRO_1000188863"
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; 60983 MW; 2B05AB1503EC7424 CRC64;
MAVTLPRPAY AGMFGPTTGD KVRLADTELF IEIERDFTLY GEEVKFGGGK VIRDGMGQGQ
ASKAEGAADT IITNAVIIDH WGIVKADVGL RDGRIIGIGK AGNPDVQPGI DLIIGPGTEI
IAGEGRILTA GGFDSHIHFI CPQQIEEALA SGMTTMLGGG TGPATGTFAT TCTPGPWHIA
RMIEASDGFA MNLGFAGKGN ASRSEGLVEQ IEAGACALKL HEDWGTTPAA IDCCLSVADD
HDIQVMIHTD TLNESGFVED TIRAFKGRTI HAFHTEGAGG GHAPDIMKVA GLPNVLPSST
NPTRPFTVNT LDEHLDMLMV CHHLDPSIAE DLAFAESRIR KETIAAEDIL HDLGALSMMS
SDSQAMGRIG EVITRTWQTA DKMKRQRGPL PEDKSNNDNF RVRRYIAKYT INPAITHGVS
RHIGSIEPGK LADLVLWTPA FFGVKPDLVI KGGMIAYAMM GDPNASIPTP QPVHGRPMFG
SFGGARTGTS LTFTSKTALA HGLAQKLKIS RKLVPVENTR GNLRKTSLIL NGAMPHIEID
PETYVVKADG MVLTCEPARS LPMAQRYFLF
