GenomeNet

Database: UniProt
Entry: A0A095EN78_CRYGR
LinkDB: A0A095EN78_CRYGR
Original site: A0A095EN78_CRYGR 
ID   A0A095EN78_CRYGR        Unreviewed;       833 AA.
AC   A0A095EN78;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   11-DEC-2019, entry version 31.
DE   RecName: Full=Urease {ECO:0000256|PIRNR:PIRNR001222};
DE            EC=3.5.1.5 {ECO:0000256|PIRNR:PIRNR001222};
DE   AltName: Full=Urea amidohydrolase {ECO:0000256|PIRNR:PIRNR001222};
GN   ORFNames=CNBG_4331 {ECO:0000313|EMBL:KGB78493.1};
OS   Cryptococcus gattii serotype B (strain R265) (Filobasidiella gattii)
OS   (Cryptococcus bacillisporus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus gattii species complex.
OX   NCBI_TaxID=294750 {ECO:0000313|EMBL:KGB78493.1, ECO:0000313|Proteomes:UP000029445};
RN   [1] {ECO:0000313|EMBL:KGB78493.1, ECO:0000313|Proteomes:UP000029445}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R265 {ECO:0000313|EMBL:KGB78493.1,
RC   ECO:0000313|Proteomes:UP000029445};
RX   PubMed=21304167; DOI=10.1128/mBio.00342-10;
RA   D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA   Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T., Sawkins J.,
RA   McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q., Bartlett K., Li W.,
RA   Wang X., Heitman J., Stajich J.E., Fraser J.A., Meyer W., Carter D.,
RA   Schein J., Krzywinski M., Kwon-Chung K.J., Varma A., Wang J., Brunham R.,
RA   Fyfe M., Ouellette B.F., Siddiqui A., Marra M., Jones S., Holt R.,
RA   Birren B.W., Galagan J.E., Cuomo C.A.;
RT   "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT   immunocompetent hosts.";
RL   MBio 2:E342-E342(2011).
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|PIRNR:PIRNR001222};
CC   -!- COFACTOR:
CC       Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC         Evidence={ECO:0000256|PIRNR:PIRNR001222,
CC         ECO:0000256|PIRSR:PIRSR001222-51};
CC       Note=Binds 2 nickel ions per subunit. {ECO:0000256|PIRNR:PIRNR001222,
CC       ECO:0000256|PIRSR:PIRSR001222-51};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC       urea (urease route): step 1/1. {ECO:0000256|PIRNR:PIRNR001222}.
CC   -!- PTM: Carbamylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000256|PIRSR:PIRSR001222-50}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the metallo-dependent
CC       hydrolases superfamily. Urease alpha subunit family.
CC       {ECO:0000256|PIRNR:PIRNR001222}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KQ410567; KGB78493.1; -; Genomic_DNA.
DR   EnsemblFungi; KGB78493; KGB78493; CNBG_4331.
DR   OMA; GFDSHIH; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000029445; Unassembled WGS sequence.
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   CDD; cd00407; Urease_beta; 1.
DR   CDD; cd00390; Urease_gamma; 1.
DR   Gene3D; 2.10.150.10; -; 1.
DR   Gene3D; 2.30.40.10; -; 1.
DR   Gene3D; 3.30.280.10; -; 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; IPR008221; Urease.
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; IPR002019; Urease_beta.
DR   InterPro; IPR036461; Urease_betasu_sf.
DR   InterPro; IPR002026; Urease_gamma/gamma-beta_su.
DR   InterPro; IPR036463; Urease_gamma_sf.
DR   InterPro; IPR029754; Urease_Ni-bd.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF00449; Urease_alpha; 1.
DR   Pfam; PF00699; Urease_beta; 1.
DR   Pfam; PF00547; Urease_gamma; 1.
DR   PIRSF; PIRSF001222; Urease; 1.
DR   PRINTS; PR01752; UREASE.
DR   SUPFAM; SSF51278; SSF51278; 1.
DR   SUPFAM; SSF51338; SSF51338; 2.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   SUPFAM; SSF54111; SSF54111; 1.
DR   TIGRFAMs; TIGR01792; urease_alph; 1.
DR   TIGRFAMs; TIGR00192; urease_beta; 1.
DR   TIGRFAMs; TIGR00193; urease_gam; 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   Hydrolase {ECO:0000256|PIRNR:PIRNR001222, ECO:0000256|PROSITE-
KW   ProRule:PRU00700};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR001222,
KW   ECO:0000256|PIRSR:PIRSR001222-51};
KW   Nickel {ECO:0000256|PIRNR:PIRNR001222, ECO:0000256|PIRSR:PIRSR001222-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029445}.
FT   DOMAIN          395..833
FT                   /note="Urease"
FT                   /evidence="ECO:0000259|PROSITE:PS51368"
FT   ACT_SITE        586
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-52,
FT                   ECO:0000256|PROSITE-ProRule:PRU00700"
FT   METAL           400
FT                   /note="Nickel 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   METAL           402
FT                   /note="Nickel 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   METAL           483
FT                   /note="Nickel 1; via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   METAL           483
FT                   /note="Nickel 2; via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   METAL           512
FT                   /note="Nickel 2; via pros nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   METAL           538
FT                   /note="Nickel 2; via tele nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   METAL           626
FT                   /note="Nickel 1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   BINDING         485
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00700"
FT   MOD_RES         483
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-50"
SQ   SEQUENCE   833 AA;  90559 MW;  10EA9F100FCFE544 CRC64;
     MHLLPRETDK LILTTLGTLA QRRLARGLIL NRAETIALIS SQLQEFIRDG RHSVAELMDM
     GKKMLGRRHV RKGVPESIHS IQVEGTFPDG VFLVTVDDPI SSDDGDLNNA FYGSFLPIPS
     ADVFPAAPEP KDTLLGALIC REEPIKINVS RRRFRLEVKN AGDRPIQVGS HYHFLETNPA
     LVFDRLLSYG YHLDIPAGTA VRFEPGEKKT VTMVEFGGKK IFHGGSGLGS GPFNENLRET
     TIKAMVEKGG FSHKEQEKVE EGPVTEMNRE VYASMFGPTT GDKIKLADMD LWIEIEKDYT
     VYGEECKFGG GKVLRDGGGQ ASGRYDHEVL DLVITNALIV DWNGIYKADI GVKNGIIVGI
     GKAGNPDMMD GVTDGMIVGS NSEVIAGEKL IVTAGALDVH VHYICPQLMT EALASGITTV
     VGGGTGPADG SNATTCTSSP FYMQNMIKAT DTMPLNFGFT GKGNDSGTNS LRDIIEAGAC
     GLKVHEDWGA TPEVIDRALT IADEYDVQVN LHSDTLNESG YVESTLAAIK GRTIHSYHTE
     GAGGGHAPDI IVVCEHENVL PSSTNPTRPY AVNTLDEHLD MLMVCHHLDK SIPEDIAFAD
     SRIRSETVAA EDVLQDTGAI SMISSDSQAM GRIGEVITRT WRTAAKMKQY RGPLEGDEPT
     RDNNRVKRYV AKYTINPAIT HGMSHLIGHV AVGCLADLVF WTAESFGARP EMVLKGGVIA
     WAAIGEANAA IPTVQPVIGR PMWGAQPAAA ALNSIVWVSQ ASLDKDLVKR FDIKKRAEAV
     KNCRAIGKKD MKWNDTMPKM TVDPETYDVR ADGVLCDVPP ADKLPLTKRY FVY
//
DBGET integrated database retrieval system