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Database: UniProt
Entry: K0BGB1_9ARCH
LinkDB: K0BGB1_9ARCH
Original site: K0BGB1_9ARCH 
ID   K0BGB1_9ARCH            Unreviewed;       570 AA.
AC   K0BGB1;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   08-MAY-2019, entry version 42.
DE   RecName: Full=Urease {ECO:0000256|RuleBase:RU000510};
DE            EC=3.5.1.5 {ECO:0000256|RuleBase:RU000510};
GN   Name=ureC {ECO:0000313|EMBL:AFS83321.1};
GN   ORFNames=NSED_07645 {ECO:0000313|EMBL:AFS83321.1};
OS   Candidatus Nitrosopumilus sediminis.
OC   Archaea; Thaumarchaeota; Nitrosopumilales; Nitrosopumilaceae;
OC   Nitrosopumilus.
OX   NCBI_TaxID=1229909 {ECO:0000313|EMBL:AFS83321.1, ECO:0000313|Proteomes:UP000006100};
RN   [1] {ECO:0000313|EMBL:AFS83321.1, ECO:0000313|Proteomes:UP000006100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AR2 {ECO:0000313|EMBL:AFS83321.1,
RC   ECO:0000313|Proteomes:UP000006100};
RX   PubMed=23209211; DOI=10.1128/JB.01869-12;
RA   Park S.J., Kim J.G., Jung M.Y., Kim S.J., Cha I.T., Ghai R.,
RA   Martin-Cuadrado A.B., Rodriguez-Valera F., Rhee S.K.;
RT   "Draft Genome Sequence of an Ammonia-Oxidizing Archaeon, "Candidatus
RT   Nitrosopumilus sediminis" AR2, from Svalbard in the Arctic Circle.";
RL   J. Bacteriol. 194:6948-6949(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|RuleBase:RU000510};
CC   -!- COFACTOR:
CC       Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC         Evidence={ECO:0000256|PIRSR:PIRSR611612-51,
CC         ECO:0000256|RuleBase:RU000510};
CC       Note=Binds 2 nickel ions per subunit.
CC       {ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|RuleBase:RU000510};
CC   -!- PTM: Carbamylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000256|PIRSR:PIRSR611612-50}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. Urease alpha subunit family.
CC       {ECO:0000256|RuleBase:RU004158}.
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DR   EMBL; CP003843; AFS83321.1; -; Genomic_DNA.
DR   RefSeq; WP_014965691.1; NC_018656.1.
DR   STRING; 1229909.NSED_07645; -.
DR   EnsemblBacteria; AFS83321; AFS83321; NSED_07645.
DR   GeneID; 13698285; -.
DR   KEGG; nir:NSED_07645; -.
DR   PATRIC; fig|1229909.8.peg.1677; -.
DR   KO; K01428; -.
DR   BioCyc; CNIT1229909:G1HAJ-1546-MONOMER; -.
DR   Proteomes; UP000006100; Chromosome.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   GO; GO:0009039; F:urease activity; IEA:UniProtKB-EC.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
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   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; PS00145; UREASE_2; 1.
DR   PROSITE; PS51368; UREASE_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006100};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00700,
KW   ECO:0000256|RuleBase:RU000510, ECO:0000313|EMBL:AFS83321.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR611612-51,
KW   ECO:0000256|RuleBase:RU000510};
KW   Nickel {ECO:0000256|PIRSR:PIRSR611612-51,
KW   ECO:0000256|RuleBase:RU000510}.
FT   DOMAIN      132    570       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    323    323       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR611612-52, ECO:0000256|PROSITE-
FT                                ProRule:PRU00700}.
FT   METAL       137    137       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       139    139       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       220    220       Nickel 1; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       220    220       Nickel 2; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       249    249       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       275    275       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       363    363       Nickel 1. {ECO:0000256|PIRSR:PIRSR611612-
FT                                51}.
FT   BINDING     222    222       Substrate. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     220    220       N6-carboxylysine. {ECO:0000256|PIRSR:
FT                                PIRSR611612-50}.
SQ   SEQUENCE   570 AA;  61364 MW;  66CDB67ACC7BFB02 CRC64;
     MTLNIPRKNY VDLFGPTVGD RVRLADTDLI IEIEKDLITY GDEAVFGGGK SVRDGLGQAS
     GVSRTESVDL VITNAIVMDP LLGIIKADIG IKDGKIVGVG NAGNPNIMDD VDMIISSNTE
     IIAGEHTICT PGTIDSHIHF ISPQQAIHAI CNGTTTMIGG GTGPADGTNA TTCTPGKWNI
     HRMIESVDEL PLNFGFLAKG NDSLETALLE QIEAGACGLK LHEDWGSTPA AIDSALSVAD
     KTDTQVAIHT DTLNECGFVD DTIEAIAGRT IHTYHTEGAG GGHAPDIMKV AGEENILPSS
     TNPTRPFTVN TLAEHLDMMM VCHHLNPSVP EDVSFAESRI RGETIAAEDV LHDIGVLSMI
     SSDSQAMGRV GEVTTRNWQT ADKMKKMTGK LPEDNVRNDN FRVKRYLAKI TINPAITHGI
     SDYVGSMQPG RLADIVIWSP QFFGVKPKMI IKGGFIAYSI MGDPNASIPT TEPVLYRPMF
     GALGKTIQST SVTFTSQLAL DKGIESEINS EKKLVPVKNC RSIGKKDMLY NDLTPEIEVN
     PETYEVKVDG KLATVDPADK VSMSRLYNLF
//
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