ID   URE1_PHODD              Reviewed;         154 AA.
AC   P50046;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Urease subunit alpha;
DE            EC=3.5.1.5;
DE   AltName: Full=Urea amidohydrolase subunit alpha;
DE   Flags: Fragment;
GN   Name=ureC;
OS   Photobacterium damselae subsp. damselae (Listonella damsela).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=85581;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=501;
RA   Bruett L., Knight I.T.;
RL   Submitted (NOV-1995) 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|PROSITE-ProRule:PRU00700};
CC   -!- COFACTOR:
CC       Name=Ni cation; Xref=ChEBI:CHEBI:25516; Evidence={ECO:0000250};
CC       Note=Binds 2 nickel ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC       urea (urease route): step 1/1.
CC   -!- SUBUNIT: Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha)
CC       subunits. Three heterotrimers associate to form the active enzyme (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00700}.
CC   -!- PTM: Carboxylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Urease alpha subunit family.
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DR   EMBL; U40071; AAA82721.1; -; Genomic_DNA.
DR   AlphaFoldDB; P50046; -.
DR   SMR; P50046; -.
DR   STRING; 85581.CAY62_17985; -.
DR   MEROPS; M38.982; -.
DR   UniPathway; UPA00258; UER00370.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   GO; GO:0009039; F:urease activity; IEA:UniProtKB-EC.
DR   GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.30.40.10; -; 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; IPR017951; Urease_asu_c.
DR   InterPro; IPR029754; Urease_Ni-bd.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF00449; Urease_alpha; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   PROSITE; PS01120; UREASE_1; 1.
DR   PROSITE; PS51368; UREASE_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Metal-binding; Nickel.
FT   CHAIN           <1..>154
FT                   /note="Urease subunit alpha"
FT                   /id="PRO_0000067545"
FT   DOMAIN          38..>154
FT                   /note="Urease"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00700"
FT   BINDING         43
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00700"
FT   BINDING         45
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00700"
FT   BINDING         126
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00700"
FT   BINDING         126
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00700"
FT   BINDING         128
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00700"
FT   MOD_RES         126
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         154
SQ   SEQUENCE   154 AA;  15731 MW;  94A62F454A774F14 CRC64;
     RISGIGKAGN PDVQPNVDIV IGPGTEVVAG EGKIVTAGGI DTHIHFICPQ QAEEGLCSGL
     TTFIGGGTGP VAGSNATTVT PGVWNMSRML EAVDDLPINV GLFGKGCVSK PEALREQIEA
     GAVGLKLHED WGATPAAINN CMNVADEMDI QVAI