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Database: UniProt
Entry: I1AT33_9RHOB
LinkDB: I1AT33_9RHOB
Original site: I1AT33_9RHOB 
ID   I1AT33_9RHOB            Unreviewed;       570 AA.
AC   I1AT33;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   08-MAY-2019, entry version 50.
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:EIE49654.1};
GN   ORFNames=C357_17790 {ECO:0000313|EMBL:EIE49654.1};
OS   Citreicella sp. 357.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Citreicella.
OX   NCBI_TaxID=766499 {ECO:0000313|EMBL:EIE49654.1, ECO:0000313|Proteomes:UP000003110};
RN   [1] {ECO:0000313|EMBL:EIE49654.1, ECO:0000313|Proteomes:UP000003110}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=357 {ECO:0000313|EMBL:EIE49654.1,
RC   ECO:0000313|Proteomes:UP000003110};
RX   PubMed=22965089; DOI=10.1128/JB.01261-12;
RA   Suarez-Suarez L.Y., Brunet-Galmes I., Pina-Villalonga J.M.,
RA   Christie-Oleza J.A., Pena A., Bennasar A., Armengaud J., Nogales B.,
RA   Bosch R.;
RT   "Draft Genome Sequence of Citreicella aestuarii Strain 357, a Member
RT   of the Roseobacter Clade Isolated without Xenobiotic Pressure from a
RT   Petroleum-Polluted Beach.";
RL   J. Bacteriol. 194:5464-5465(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+);
CC         Xref=Rhea:RHEA:20557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16199, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938;
CC         EC=3.5.1.5; 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,
CC         ECO:0000256|RuleBase:RU000510};
CC       Note=Binds 2 nickel ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01953, ECO:0000256|PIRSR:PIRSR611612-51,
CC       ECO:0000256|RuleBase:RU000510};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3)
CC       from urea (urease route): step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01953, ECO:0000256|SAAS:SAAS00317636}.
CC   -!- SUBUNIT: Heterotrimer of UreA (gamma), UreB (beta) and UreC
CC       (alpha) subunits. Three heterotrimers associate to form the active
CC       enzyme. {ECO:0000256|HAMAP-Rule:MF_01953}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01953,
CC       ECO:0000256|PROSITE-ProRule:PRU00700,
CC       ECO:0000256|SAAS:SAAS00548017}.
CC   -!- PTM: Carbamylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000256|HAMAP-Rule:MF_01953,
CC       ECO:0000256|PIRSR:PIRSR611612-50}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. Urease alpha subunit family. {ECO:0000256|HAMAP-
CC       Rule:MF_01953, ECO:0000256|RuleBase:RU004158,
CC       ECO:0000256|SAAS:SAAS00849550}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EIE49654.1}.
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DR   EMBL; AJKJ01000133; EIE49654.1; -; Genomic_DNA.
DR   RefSeq; WP_009506073.1; NZ_AJKJ01000133.1.
DR   STRING; 766499.C357_17790; -.
DR   EnsemblBacteria; EIE49654; EIE49654; C357_17790.
DR   PATRIC; fig|766499.3.peg.3471; -.
DR   OrthoDB; 157757at2; -.
DR   BioCyc; CSP766499:G1H4Q-3390-MONOMER; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000003110; 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; 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   Complete proteome {ECO:0000313|Proteomes:UP000003110};
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,
KW   ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|RuleBase:RU000510,
KW   ECO:0000256|SAAS:SAAS00317628};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003110}.
FT   DOMAIN      134    570       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    322    322       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                52, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   METAL       139    139       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       141    141       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       219    219       Nickel 1; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       219    219       Nickel 2; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       248    248       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       274    274       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       362    362       Nickel 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                51}.
FT   BINDING     221    221       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     219    219       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01953, ECO:0000256|PIRSR:
FT                                PIRSR611612-50}.
SQ   SEQUENCE   570 AA;  60603 MW;  91C7D9731E65F7A4 CRC64;
     MVTMTRAEYA AMFGPTTGDL MRLGDTQLWA EIEHDYTSYG DECLHGGGKT LRDGLGLAVG
     VTSAQGALDM LICNVVVIDA VAGIVKGDIG IKDGKIVAIG KAGNPDVMNG VDPRLIVGAG
     TTVRDAEGMI ATAGAIDVHV HFDSAQLVEH AMSSGITTML GGSLGPITVG IDSGGPFNTG
     KMLQAAEHWP MNFGFLGRGN AHRPDAMHEQ IRTGCLGLKI HEDWGAMPAA IDACLSAADE
     LDFQVQLHTD TLNESGFVED TLAAIGGRAI HMYHTEGAGG GHAPDIIRVA GVANCLPSST
     NPTNPFTVNT FDEHLDMTMV CHHLSPSIPE DVAFAESRIR AQTIAAEDVL HDIGAISMLG
     SDSQGMGRIH EVISRTWQLA SKMREQRGRL PDETSAKGDN LRIKRFIAKY TINAARCFGI
     EKHVGSIEPG KLADIVLWRP GYFGVKPELV VKGGFIAWGA MGDSAASLMT CEPLIMRPQW
     GAFGKAAPAL GACFVNPLAI EDGLDADLGL TKPLLPAVGT RHLRKSDMHL NDACPDIRVD
     PATFEVFVDG ELATCEPATE LPLAQRYMLR
//
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