URE1_RHILW
ID URE1_RHILW Reviewed; 570 AA.
AC B5ZMP0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=Rleg2_3051;
OS Rhizobium leguminosarum bv. trifolii (strain WSM2304).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=395492;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM2304;
RX PubMed=21304679; DOI=10.4056/sigs.44642;
RA Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA Yates R., Howieson J.;
RT "Complete genome sequence of Rhizobium leguminosarum bv trifolii strain
RT WSM2304, an effective microsymbiont of the South American clover Trifolium
RT polymorphum.";
RL Stand. Genomic Sci. 2:66-76(2010).
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}.
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DR EMBL; CP001191; ACI56318.1; -; Genomic_DNA.
DR RefSeq; WP_012558726.1; NC_011369.1.
DR AlphaFoldDB; B5ZMP0; -.
DR SMR; B5ZMP0; -.
DR STRING; 395492.Rleg2_3051; -.
DR EnsemblBacteria; ACI56318; ACI56318; Rleg2_3051.
DR KEGG; rlt:Rleg2_3051; -.
DR eggNOG; COG0804; Bacteria.
DR HOGENOM; CLU_000980_0_0_5; -.
DR OMA; GFDSHIH; -.
DR OrthoDB; 157757at2; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000008330; 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.
FT CHAIN 1..570
FT /note="Urease subunit alpha"
FT /id="PRO_1000188890"
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; 60688 MW; A73D55623A5D25A1 CRC64;
MPYKISRAAY AGMFGPTTGD KVRLADTELF IEIEKDFTTY GEEVKFGGGK VIRDGMGQSQ
VTRADGAVDT VITNAVIVDH SGVYKADIGL KDGRIVAIGK AGNPDMQPGV NIIVGPGTEA
IAAEGKIVTA GGMDSHIHFI APQQIEEALM SGMTCMLGGG TGPAHGTLAT TCTPGPWHLA
RMIEAADAFP MNLAFAGKGN ASLPGALTEM VLAGATSLKL HEDWGTTPGA IDCCLSVADE
YDVQVMIHTD TLNESGFVED TIGAIKGRTI HAFHTEGAGG GHAPDIIKIC GQPNVIPSST
NPTRPYTVNT IAEHLDMLMV CHHLSPSIPE DIAFAESRIR KETIAAEDIL HDIGAFSIIS
SDSQAMGRVG EVAIRTWQTA DKMKRQRGRL KQENGDNDNF RVRRYIAKYT INPAIAHGLS
HEIGSVEVGK RADLVLWNPA FFGVKPDMVL LGGSIAAAPM GDPNASIPTP QPVHYRPMFA
SYGRSLTNSS VTFVSQASLD AGLKGRLGVA KQLVAVKNTR GGISKASMIH NDLTPEIEVD
PETYEVRANG ELLTCEPATV LPMAQRYFLF
