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Database: UniProt
Entry: A0RUS3_CENSY
LinkDB: A0RUS3_CENSY
Original site: A0RUS3_CENSY 
ID   A0RUS3_CENSY            Unreviewed;       569 AA.
AC   A0RUS3;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 83.
DE   RecName: Full=Urease {ECO:0000256|RuleBase:RU000510};
DE            EC=3.5.1.5 {ECO:0000256|RuleBase:RU000510};
GN   OrderedLocusNames=CENSYa_0456 {ECO:0000313|EMBL:ABK77090.1};
OS   Cenarchaeum symbiosum (strain A).
OC   Archaea; Thaumarchaeota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX   NCBI_TaxID=414004 {ECO:0000313|EMBL:ABK77090.1, ECO:0000313|Proteomes:UP000000758};
RN   [1] {ECO:0000313|EMBL:ABK77090.1, ECO:0000313|Proteomes:UP000000758}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A {ECO:0000313|Proteomes:UP000000758};
RX   PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA   Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA   Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT   "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT   symbiosum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006).
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; DP000238; ABK77090.1; -; Genomic_DNA.
DR   MEROPS; M38.982; -.
DR   EnsemblBacteria; ABK77090; ABK77090; CENSYa_0456.
DR   KEGG; csy:CENSYa_0456; -.
DR   PATRIC; fig|414004.10.peg.415; -.
DR   HOGENOM; HOG000075064; -.
DR   KO; K01428; -.
DR   OMA; GFDSHIH; -.
DR   BioCyc; CSYM414004:G132A-453-MONOMER; -.
DR   Proteomes; UP000000758; 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:UP000000758};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00700,
KW   ECO:0000256|RuleBase:RU000510, ECO:0000313|EMBL:ABK77090.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000758}.
FT   DOMAIN      132    569       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   569 AA;  60442 MW;  C29ACEA84255FC16 CRC64;
     MTLEIPRSTY VDLFGPTTGD RIRLGDTDLI IEVERDLIRH GDEAVFGGGK SIRDGLCQAA
     GTGRDGSLDL VITNAIIADP ILGIVKADIG VKGGLIAGVG NAGNPGIMDG VDMVISSSTE
     VVAGEHYICT PGTVDSHVHY ISPQQAVHAI CNGTTTMIGG GTGPADGTNA TTCTPGRWNI
     ARMMESIRDM PLNFGFLAKG NDSIEGALMD QLKAGACGLK LHEDWGTTPA TIDSALKVAE
     RTDTQVAIHT DTLNECGFVD DTIRAIAGRT IHTYHTEGAG GGHAPDIMKI AGEPNVLPSS
     TNPTRPFTVN TLAEHLDMMM VCHHLNPHVP EDVSFAESRI RGETIAAEDV LHDMGVLSMM
     SSDSQAMGRV GEVTTRNWQT ADKMKKMAGP LPGDTAHNDN LRVKRYLAKI TINPAITHGI
     SEYVGSIRPG RLADMVLWSP KFFGAKPRLI IKGGMIAYSL MGDPGASIPT TEPVLYRPMF
     GAHGAAAAST SLTFTSQIAL DSGLGPEVAG RRLAPVRGCR HIGKKDMVHN DLTPDIQINP
     ETYEVRVDGA LATTEPARSV SLARLYNLF
//
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