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URE12_BRUME
ID   URE12_BRUME             Reviewed;         573 AA.
AC   Q8YHZ8;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Urease subunit alpha 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01953};
GN   Name=ureC2 {ECO:0000255|HAMAP-Rule:MF_01953}; OrderedLocusNames=BMEI0647;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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; AE008917; AAL51828.1; -; Genomic_DNA.
DR   PIR; AI3332; AI3332.
DR   RefSeq; WP_004683985.1; NZ_GG703780.1.
DR   AlphaFoldDB; Q8YHZ8; -.
DR   SMR; Q8YHZ8; -.
DR   STRING; 224914.BMEI0647; -.
DR   MEROPS; M38.982; -.
DR   EnsemblBacteria; AAL51828; AAL51828; BMEI0647.
DR   GeneID; 29593437; -.
DR   KEGG; bme:BMEI0647; -.
DR   PATRIC; fig|224914.52.peg.817; -.
DR   eggNOG; COG0804; Bacteria.
DR   OMA; CHHLSHD; -.
DR   PhylomeDB; Q8YHZ8; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000000419; Chromosome I.
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; IPR001763; Rhodanese-like_dom.
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..573
FT                   /note="Urease subunit alpha 2"
FT                   /id="PRO_0000234144"
FT   DOMAIN          135..573
FT                   /note="Urease"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   ACT_SITE        326
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         140
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         142
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         223
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         223
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         225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         252
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         278
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         366
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         223
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
SQ   SEQUENCE   573 AA;  60785 MW;  A297E706F15A490B CRC64;
     MTQISRQQYA DLYGPTIGDK IRLGDSDLYV EIEKDLRATY GDELQYGGGK TLRDGMGSEN
     FLTQEAGCLD LVITNVTVID AIQGVVKADV GIRNGRIVGL GKAGNPSTMD GVTRGLVTGA
     STDAISGEHL ILTAGGMDTH VHYIAPQQVE AALSNGITTL WGGGIGPVDG TNGVTTTNGP
     WNLEMMLRSI EGLPINFGIQ GKGNSTGIAP LIEQLEAGAA GFKVHEDYGA TPATIRACLS
     VADEYDVSVA VHTDTLNESG YVEDTIAAFD GRSVHTYHSE GAGGGHAPDL LKVVGQNNIL
     PSSTNPTLPC GKNSVAELFD MIMVCHNLNP RIPSDVAFAE SRVRAETIVA ESVLHDMGAI
     SMIGSDSQAM GRIGETYLRA IQTADAMKKA RGPLPEDAPG NDNFRVLRYI AKVTINPALT
     AGVGDVIGSI ESGKFADLVL WEPAFFGVKP KLVLKGGLVA WANMGDPNAS LPTPQPMYYR
     PMFAAYGSAL QKTSITFVSR AAYDKGVADR FGLQRLVMPV SGTRVIGKAH MVRNSYLPNI
     EVDPQTFAVK VDGVHATVKP PQSISLNQLY FFS
 
 
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