ID A0A151BSH9_9MICO Unreviewed; 574 AA.
AC A0A151BSH9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
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 ECO:0000313|EMBL:KYH42899.1};
GN ORFNames=AZH51_00540 {ECO:0000313|EMBL:KYH42899.1};
OS Branchiibius sp. NY16-3462-2.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC Branchiibius.
OX NCBI_TaxID=1807500 {ECO:0000313|EMBL:KYH42899.1, ECO:0000313|Proteomes:UP000075667};
RN [1] {ECO:0000313|EMBL:KYH42899.1, ECO:0000313|Proteomes:UP000075667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NY16-3462-2 {ECO:0000313|EMBL:KYH42899.1};
RA Lapierre P., Halse T.A., Shea J., Musser K.A., Escuyer V.E.;
RT "Draft genome assembly of Branchiibius sp. 15-3462-2 from a clinical sputum
RT sample.";
RL Submitted (MAR-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:KYH42899.1}.
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DR EMBL; LVCF01000049; KYH42899.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151BSH9; -.
DR STRING; 1807500.AZH51_00540; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000075667; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000075667}.
FT DOMAIN 136..574
FT /note="Urease"
FT /evidence="ECO:0000259|PROSITE:PS51368"
FT ACT_SITE 327
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-52"
FT BINDING 141
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 143
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 224
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 224
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 226
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PROSITE-ProRule:PRU00700"
FT BINDING 253
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 279
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 367
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 224
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-50"
SQ SEQUENCE 574 AA; 60945 MW; 8F3BA73596286484 CRC64;
MAILSRKEYT DLFGPTRGDK VQLADTNLVI EIEKDFAEGH YGDEVVYGGG KSARDGMAQD
PRASQSKGAL DLLITNVIVM DPILGIIKAD IGIKDGLIAG VGKSGNPQLQ DGVDPKLLVG
PGTEIIAGEH MIATAGAMDA HVHYISPQQA HDALSNGITT LFGGGTGPTD GTNGTTCTPG
AWNIHRMLQS VEAMPVNMGI MGKGNGSLAE ALAEQIEAGA AGLKVHEDWG TTPAALSKAL
DVADEYDVQI AVHTDSLNEA GFVEDTINAI NGRAIHTYHT EGAGGGHAPD IMKIASSANV
LPSSTNPTLP YTVNSVDELL DMVMVCHHLS HEIPEDVAFA DSRVRAETIS AETVLHDQGV
LSIFSSDSQA MGRIGESVTR AFQTAHHCKD KRGKLPEDAA GNDNFRVLRY LAKVTINPAI
AQGISDYVGS LETGKMADIV LWPIDSFAAK PKMVIKGGMV SWAQMGDPNA SLPTPQPVYY
RPMFGAIGKT LQKTRATFMS QAAIDNGVPE QLGLESQVFP VRRTRTVGKK DMVRNSATPV
IEVDPETYVV TLDGVPAHIE PAQSLPLTQL FYLV
//
