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Database: UniProt
Entry: A0A2G2JS93_9FLAO
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ID   A0A2G2JS93_9FLAO        Unreviewed;       536 AA.
AC   A0A2G2JS93;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   11-DEC-2019, entry version 13.
DE   RecName: Full=Urease {ECO:0000256|RuleBase:RU000510, ECO:0000256|SAAS:SAAS00325551};
DE            EC=3.5.1.5 {ECO:0000256|RuleBase:RU000510, ECO:0000256|SAAS:SAAS00325551};
DE   Flags: Fragment;
GN   Name=ureC {ECO:0000313|EMBL:PHS01155.1};
GN   ORFNames=COA80_02370 {ECO:0000313|EMBL:PHS01155.1};
OS   Leeuwenhoekiella sp.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Leeuwenhoekiella.
OX   NCBI_TaxID=1977054 {ECO:0000313|EMBL:PHS01155.1, ECO:0000313|Proteomes:UP000226343};
RN   [1] {ECO:0000313|Proteomes:UP000226343}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT   "A dynamic microbial community with high functional redundancy inhabits the
RT   cold, oxic subseafloor aquifer.";
RL   Submitted (AUG-2017) 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|RuleBase:RU000510,
CC         ECO:0000256|SAAS:SAAS01119912};
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. {ECO:0000256|PIRSR:PIRSR611612-
CC       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|SAAS:SAAS00317636}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PROSITE-ProRule:PRU00700}.
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 superfamily.
CC       Urease alpha subunit family. {ECO:0000256|RuleBase:RU004158}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PHS01155.1}.
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DR   EMBL; NVVZ01000019; PHS01155.1; -; Genomic_DNA.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000226343; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   GO; GO:0009039; F:urease activity; IEA:UniProtKB-EC.
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; 1.
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|PROSITE-ProRule:PRU00700};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00700,
KW   ECO:0000256|RuleBase:RU000510, ECO:0000256|SAAS:SAAS00321417};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR611612-51,
KW   ECO:0000256|RuleBase:RU000510, ECO:0000256|SAAS:SAAS00321440};
KW   Nickel {ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|RuleBase:RU000510,
KW   ECO:0000256|SAAS:SAAS00317628}.
FT   DOMAIN          97..536
FT                   /note="Urease"
FT                   /evidence="ECO:0000259|PROSITE:PS51368"
FT   ACT_SITE        288
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-52,
FT                   ECO:0000256|PROSITE-ProRule:PRU00700"
FT   METAL           102
FT                   /note="Nickel 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           104
FT                   /note="Nickel 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           185
FT                   /note="Nickel 1; via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           185
FT                   /note="Nickel 2; via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           214
FT                   /note="Nickel 2; via pros nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           240
FT                   /note="Nickel 2; via tele nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           328
FT                   /note="Nickel 1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT   BINDING         187
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00700"
FT   MOD_RES         185
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-50"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:PHS01155.1"
SQ   SEQUENCE   536 AA;  56999 MW;  EC14464DB34461F6 CRC64;
     ESDATHYGDE VKFGGGKVIR DGMGQSQRAD EAVMDTVITN ALILDWWGIV KADIGLQNGR
     IAAIGKAGNP DTQPDVTIVI GPGTEIIAGE GKILTAGGID AHIHFICPQQ IEEALMSGVT
     TMLGGGTGPA TGSNATTCTP GPWHIGKMLQ AVDDMPMNIG FLGKGNASLP ESLELQIKAG
     AMGLKLHEDW GTTPASIDNC LTVADKFDVQ IAIHTDTLNE SGFVEDTLAA FKGRCIHTYH
     TEGAGGGHAP DIITACSKDY VLPSSTNPTR PYTVNTIDEH LDMLMVCHHL DPNIPEDVAF
     ADSRIRRETI AAEDILQDMG VISMIASDSQ AMGRVGEVVC RTWQTAHKMK VQRGLLPDDE
     XLGADNLRAK RYIAKYTINP AITHGIAHEV GSVEVGKLAD LVLWDPAFFG VKPALIVKGG
     MIAAAPMGDP NASIPTPQPV HYRMMFGALG RAASATRLSF VSQAALDAGI GKELGLNSTL
     AACKNVRNVR KGDLKLNDAC PHLTVDPQTY EVHADGELLT CEPATELPLA QLYHLF
//
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