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Database: UniProt
Entry: A0A108D3V6_9BURK
LinkDB: A0A108D3V6_9BURK
Original site: A0A108D3V6_9BURK 
ID   A0A108D3V6_9BURK        Unreviewed;       568 AA.
AC   A0A108D3V6;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   11-DEC-2019, entry version 28.
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:KWK85898.1};
GN   ORFNames=WJ35_07560 {ECO:0000313|EMBL:AOJ74934.1}, WM16_29690
GN   {ECO:0000313|EMBL:KWK85898.1};
OS   Burkholderia ubonensis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=101571 {ECO:0000313|EMBL:KWK85898.1, ECO:0000313|Proteomes:UP000065504};
RN   [1] {ECO:0000313|EMBL:KWK85898.1, ECO:0000313|Proteomes:UP000065504}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSMB782WGS {ECO:0000313|EMBL:KWK85898.1,
RC   ECO:0000313|Proteomes:UP000065504};
RA   Sahl J., Keim P., Wagner D.;
RT   "Expanding the genomic diversity of Burkholderia species for the
RT   development of highly accurate diagnostics.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AOJ74934.1, ECO:0000313|Proteomes:UP000243680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSMB0783 {ECO:0000313|EMBL:AOJ74934.1,
RC   ECO:0000313|Proteomes:UP000243680};
RA   Sahl J., Wagner D., Keim P.;
RT   "Diversity of Burkholderia near neighbor genomes.";
RL   Submitted (DEC-2015) 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, ECO:0000256|SAAS:SAAS01119912};
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|HAMAP-Rule:MF_01953,
CC       ECO:0000256|SAAS:SAAS00317636}.
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, ECO:0000256|SAAS:SAAS00548017}.
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, ECO:0000256|SAAS:SAAS00849550}.
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DR   EMBL; CP013420; AOJ74934.1; -; Genomic_DNA.
DR   EMBL; LPLU01000008; KWK85898.1; -; Genomic_DNA.
DR   RefSeq; WP_060231496.1; NZ_LPLU01000008.1.
DR   EnsemblBacteria; KWK85898; KWK85898; WM16_29690.
DR   OrthoDB; 157757at2; -.
DR   BioCyc; GCF_001718695:G1F4P-1581-MONOMER; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000065504; Unassembled WGS sequence.
DR   Proteomes; UP000243680; Chromosome 1.
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 {ECO:0000256|HAMAP-Rule:MF_01953, ECO:0000256|PROSITE-
KW   ProRule:PRU00700, ECO:0000256|SAAS:SAAS00317631};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01953, ECO:0000256|PROSITE-
KW   ProRule:PRU00700, ECO:0000256|RuleBase:RU000510,
KW   ECO:0000256|SAAS:SAAS00321417};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01953,
KW   ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|RuleBase:RU000510,
KW   ECO:0000256|SAAS:SAAS00321440};
KW   Nickel {ECO:0000256|HAMAP-Rule:MF_01953, ECO:0000256|PIRSR:PIRSR611612-51,
KW   ECO:0000256|RuleBase:RU000510, ECO:0000256|SAAS:SAAS00317628}.
FT   DOMAIN          130..568
FT                   /note="Urease"
FT                   /evidence="ECO:0000259|PROSITE:PS51368"
FT   ACT_SITE        321
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-52, ECO:0000256|PROSITE-
FT                   ProRule:PRU00700"
FT   METAL           135
FT                   /note="Nickel 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           137
FT                   /note="Nickel 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           218
FT                   /note="Nickel 1; via carbamate group"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           218
FT                   /note="Nickel 2; via carbamate group"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           247
FT                   /note="Nickel 2; via pros nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           273
FT                   /note="Nickel 2; via tele nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           361
FT                   /note="Nickel 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   BINDING         220
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PROSITE-ProRule:PRU00700"
FT   MOD_RES         218
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-50"
SQ   SEQUENCE   568 AA;  60870 MW;  4CFB3DFE6FF1999F CRC64;
     MTLRLSRRAY AEMFGPTTGD RIRLADTELL IEIERDFTIY GEEVKFGGGK VIRDGMGQSQ
     RVAADVPDTV ITNAVILDHW GIVKADIAIK HGRIAAIGKA GNPDIQPGVT IAIGAATEVI
     AGEGLIVTAG GIDTHIHFIS PQQIDEALAS GVTTMLGGGT GPATGTNATT CTPGPWHMER
     MLQAADGWPI NLGFLGKGNA SLPQPLVEQI AAGAIGLKLH EDWGTTPAAI DNCLSVADDT
     DTQVAIHTDT LNEAGFVEST VAAFKGRTIH TYHTEGAGGG HAPDILKVCG EANVLPSSTN
     PTRPYTINTL DEHLDMLMVC HHLDPSIAED LAFAESRIRR ETIAAEDILH DLGALSMLSS
     DSQAMGRVGE VIIRTWQTAH KMKVQRGALP EDSARHDNFR AKRYVAKYTI NPALTHGIAH
     EVGSIEPGKW ADLVLWEPAF FGIKPAMILK GGMIAVAQMG DPNASIPTPQ PVHYREMFAT
     RGGALARTSL TFVSQMAADA GIAERYGLAK RIVPVRNCRN VTKADMIHNA WRPAISVDPE
     TYDVIADGQL LTCEPAAVLP MAQRYFLF
//
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