ID A0A1Q8Q6Q8_9BACI Unreviewed; 569 AA.
AC A0A1Q8Q6Q8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=BTO30_06525 {ECO:0000313|EMBL:OLN23028.1};
OS Domibacillus antri.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX NCBI_TaxID=1714264 {ECO:0000313|EMBL:OLN23028.1, ECO:0000313|Proteomes:UP000185568};
RN [1] {ECO:0000313|EMBL:OLN23028.1, ECO:0000313|Proteomes:UP000185568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XD80 {ECO:0000313|EMBL:OLN23028.1,
RC ECO:0000313|Proteomes:UP000185568};
RA Verma A., Krishnamurthi S.;
RT "Domibacillus antri genome sequencing.";
RL Submitted (DEC-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:OLN23028.1}.
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DR EMBL; MSDU01000010; OLN23028.1; -; Genomic_DNA.
DR RefSeq; WP_075397916.1; NZ_MSDU01000010.1.
DR AlphaFoldDB; A0A1Q8Q6Q8; -.
DR STRING; 1714264.BTO30_06525; -.
DR OrthoDB; 9802793at2; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000185568; 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; 61610 MW; 0BB6C1299E9E508F CRC64;
MSFHMSRRQY ADMFGPTTGD CIRLADTELF IEIEKDYTVY GDEVKFGGGK VIRDGMGQHP
HAKRDEAVDL VLTNAIVLDY TGIYKADIGV KDGEIWAIGK AGNPLLMDGV DIVIGASTEV
IAAEGKIVTA GGIDSHIHFI CPQQIETALA SGVTTMIGGG TGPATGTNAT TCTPGEWNIF
RMLEAAEAFP MNIGFLGKGN ASGLEPLVEQ IEAGAIGLKL HEDWGTTAAA IDASLKTADK
YDVQIAIHSD TLNEGGFVED TIVAIDGRVI HTYHTEGAGG GHAPDIIKAA GFPNVLPSST
NPTRPYTINT LDEHLDMLMV CHHLDPSVPE DIAFADSRIR KETIAAEDIL HDLGVFSMIS
SDSQAMGRIG EVILRTWQTA DKMKKQRGKM EEEMGEGDNF RAKRYIAKYT INPALTHGIS
DYVGSVETGK LADLAVWEPA FFGVKPELVL KGGLIAHSVM GDPNASIPTP QPALYRPMFA
SFGKALYQTS MTFLSKAAID RGVPEKLGLE KMIRPVQNIR TLQKSDMKYN GETPDIEVDP
QTYEVKVDGE LVTCEPAEIV PMAQRYFLF
//
