ID A0A196P6Z6_9RHOB Unreviewed; 569 AA.
AC A0A196P6Z6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Urease subunit alpha {ECO:0000256|HAMAP-Rule:MF_01953};
DE EC=3.5.1.5 {ECO:0000256|HAMAP-Rule:MF_01953};
DE AltName: Full=Urea amidohydrolase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01953};
GN Name=ureC {ECO:0000256|HAMAP-Rule:MF_01953};
GN ORFNames=A8B82_16340 {ECO:0000313|EMBL:OAN75380.1};
OS Sulfitobacter sp. EhC04.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=1849168 {ECO:0000313|EMBL:OAN75380.1, ECO:0000313|Proteomes:UP000078479};
RN [1] {ECO:0000313|EMBL:OAN75380.1, ECO:0000313|Proteomes:UP000078479}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EhC04 {ECO:0000313|EMBL:OAN75380.1,
RC ECO:0000313|Proteomes:UP000078479};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) 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:0000256|HAMAP-Rule:MF_01953,
CC ECO:0000256|RuleBase:RU000510};
CC -!- COFACTOR:
CC Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01953,
CC ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|RuleBase:RU000510};
CC Note=Binds 2 nickel ions per subunit. {ECO:0000256|HAMAP-Rule:MF_01953,
CC ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|RuleBase:RU000510};
CC -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC urea (urease route): step 1/1. {ECO:0000256|ARBA:ARBA00004897,
CC ECO:0000256|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:0000256|HAMAP-Rule:MF_01953}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01953,
CC ECO:0000256|PROSITE-ProRule:PRU00700}.
CC -!- PTM: Carbamylation allows a single lysine to coordinate two nickel
CC ions. {ECO:0000256|PIRSR:PIRSR611612-50}.
CC -!- PTM: Carboxylation allows a single lysine to coordinate two nickel
CC ions. {ECO:0000256|HAMAP-Rule:MF_01953}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Urease alpha subunit family. {ECO:0000256|HAMAP-Rule:MF_01953,
CC ECO:0000256|RuleBase:RU004158}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAN75380.1}.
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DR EMBL; LXYI01000024; OAN75380.1; -; Genomic_DNA.
DR RefSeq; WP_067292570.1; NZ_LXYI01000024.1.
DR AlphaFoldDB; A0A196P6Z6; -.
DR STRING; 1849168.A8B82_16340; -.
DR OrthoDB; 9802793at2; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000078479; Unassembled WGS sequence.
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 {ECO:0000256|HAMAP-Rule:MF_01953, ECO:0000256|PROSITE-
KW ProRule:PRU00700};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01953};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01953};
KW Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|HAMAP-Rule:MF_01953}.
FT DOMAIN 131..569
FT /note="Urease"
FT /evidence="ECO:0000259|PROSITE:PS51368"
FT ACT_SITE 322
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-52"
FT BINDING 136
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-51"
FT BINDING 138
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-51"
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:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-51"
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:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-51"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PROSITE-ProRule:PRU00700"
FT BINDING 248
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-51"
FT BINDING 274
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-51"
FT BINDING 362
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-51"
FT MOD_RES 219
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-50"
SQ SEQUENCE 569 AA; 60603 MW; CD3B712EF84DDCD0 CRC64;
MPTSIPRAQY AAMYGPTTGD RVRLADTDLV IEVERDLTTY GEEVKFGGGK VIRDGMGQSQ
VTRAGGAVDT VITNALIIDH AGIFKADVAL KDGLIHAIGK AGNPDTQPGV DIIIGPGTEI
IAGEGRILTA GGVDSHIHFI CPQQMEDSLH SGVTTCFGGG TGPAHGTLAT TCTPGPWHIG
RMLQAFDGIA MNVGLSGKGN ASQPEALVEM VKGGASALKL HEDWGTTPAA IDCCLSVADD
MDVQVMIHTD TLNESGFVEH TVGAMKGRTI HAFHTEGAGG GHAPDIIKIC GESFVLPSST
NPTRPFTVNT LEEHLDMLMV CHHLDKSIPE DIAFAESRIR RETIAAEDIL HDMGAFSIIA
SDSQAMGRVG EVLIRTWQTA DKMKKQRGRL AEETGENDNF RVRRYIAKYT INPAIAQGVS
HVVGSIEVGK RADLVLWSPA FFGVKPEMVL MGGTIVVAQM GDPNASIPTP QPVYTRPMFG
AYGRSLEHSS ITFVSGAAQA DGIRGKLGLA KQTVAVANTR NIGKKDLLLN DATPKVEVDP
ETYEVRADGE LLTCAPAEVL PMAQRYFMF
//
