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Database: UniProt
Entry: D0MRB0_PHYIT
LinkDB: D0MRB0_PHYIT
Original site: D0MRB0_PHYIT 
ID   D0MRB0_PHYIT            Unreviewed;       842 AA.
AC   D0MRB0;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   03-JUL-2019, entry version 64.
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=PITG_00636 {ECO:0000313|EMBL:EEY58029.1};
OS   Phytophthora infestans (strain T30-4) (Potato late blight fungus).
OC   Eukaryota; Stramenopiles; Oomycetes; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=403677 {ECO:0000313|Proteomes:UP000006643};
RN   [1] {ECO:0000313|Proteomes:UP000006643}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T30-4 {ECO:0000313|Proteomes:UP000006643};
RX   PubMed=19741609; DOI=10.1038/nature08358;
RG   The Broad Institute Genome Sequencing Platform;
RA   Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E.,
RA   Cano L.M., Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T.,
RA   Bozkurt T.O., Ah-Fong A.M., Alvarado L., Anderson V.L.,
RA   Armstrong M.R., Avrova A., Baxter L., Beynon J., Boevink P.C.,
RA   Bollmann S.R., Bos J.I., Bulone V., Cai G., Cakir C., Carrington J.C.,
RA   Chawner M., Conti L., Costanzo S., Ewan R., Fahlgren N.,
RA   Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S., Green P.J.,
RA   Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA   Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA   Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA   Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA   Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA   Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA   Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA   Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J.,
RA   Studholme D.J., Sykes S., Thines M., van de Vondervoort P.J.,
RA   Phuntumart V., Wawra S., Weide R., Win J., Young C., Zhou S., Fry W.,
RA   Meyers B.C., van West P., Ristaino J., Govers F., Birch P.R.,
RA   Whisson S.C., Judelson H.S., Nusbaum C.;
RT   "Genome sequence and analysis of the Irish potato famine pathogen
RT   Phytophthora infestans.";
RL   Nature 461:393-398(2009).
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|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.
CC       {ECO:0000256|PIRNR:PIRNR001222, ECO:0000256|PIRSR:PIRSR001222-51};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3)
CC       from urea (urease route): step 1/1.
CC       {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-
CC       dependent hydrolases superfamily. Urease alpha subunit family.
CC       {ECO:0000256|PIRNR:PIRNR001222}.
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DR   EMBL; DS028118; EEY58029.1; -; Genomic_DNA.
DR   RefSeq; XP_002909215.1; XM_002909169.1.
DR   STRING; 4787.PITG_00636T0; -.
DR   PRIDE; D0MRB0; -.
DR   EnsemblProtists; PITG_00636T0; PITG_00636T0; PITG_00636.
DR   GeneID; 9479573; -.
DR   KEGG; pif:PITG_00636; -.
DR   EuPathDB; FungiDB:PITG_00636; -.
DR   HOGENOM; HOG000075064; -.
DR   InParanoid; D0MRB0; -.
DR   KO; K01427; -.
DR   OMA; GFDSHIH; -.
DR   OrthoDB; 183108at2759; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000006643; Partially assembled 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   Complete proteome {ECO:0000313|Proteomes:UP000006643};
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-
KW   51}; Reference proteome {ECO:0000313|Proteomes:UP000006643}.
FT   DOMAIN      401    842       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    592    592       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR611612-52, ECO:0000256|PROSITE-
FT                                ProRule:PRU00700}.
FT   METAL       406    406       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       408    408       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       489    489       Nickel 1; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       489    489       Nickel 2; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       518    518       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       544    544       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       632    632       Nickel 1. {ECO:0000256|PIRSR:PIRSR001222-
FT                                51}.
FT   BINDING     491    491       Substrate. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     489    489       N6-carboxylysine. {ECO:0000256|PIRSR:
FT                                PIRSR001222-50}.
SQ   SEQUENCE   842 AA;  90125 MW;  5CF247D58A7B03DD CRC64;
     MRLSPREEEH LMLHTAGALA QKRLARGLRL NYSESVALLA TQVLELIRDG KTVAELMTLG
     AQMLGRRQVM EGVASILDEV QVEGTFPDGT KLVTIHNPIS NLDGDLSLAL YGSFLPVPKL
     EVFGAAATVT AIAPGALITQ DTDIVLNEGR KARVLQITNL SDRPIQVGSH YHLIEANPYL
     EMDRKLAYGH RLNIAAGTAV RFEPGDQKTV SIVPIAGNKV ITGGNNLATG VVDESKVDAI
     VAKAVAEGFH HRELELSTLP RHVTKPEFGV CKMPRSVYAQ TYGPTTGDVV RLGDMELYVA
     VEKDMTVYGD ECKFGGGKVL REGMGQASGR NSAQVVDTII TNALIVDYTG IYKADVGIKD
     GLIAGIGKGG NPDVMEGVLP DLIVGVNTEV IAGEGLILTA GGFDAHVHFI CPQLCTEALS
     SGLTTLVGGG TGPATGTNAT TCTPGPNHIK MMLQATDSTP MNIGLTSKGN TSLPEGLQDT
     IDAGAVGMKL HEDWGTTPAA IDNCLNVAEK NDVQVTIHTD TLNESSCVEH TIKAFKGRTI
     HTYHSEGAGG GHAPDIVTVC GELNVLPSST NPTRPYTRNT IDEHVDMLMV CHHLDKNIAE
     DVAFAESRIR GETIAAEDLL HDMGAISIIS SDSQAMGRIG EVVTRTWQTA DKMKKELGLL
     PEDAASEHKR DNFRVRRYVA KYTINPAIAH GMAHLIGSVE VNKLADLCLW KPCFFGSKPE
     LVIKGGAIAY AQMGDPNASI PTPQPVKMRP MFGALGAAVG MGSIAFVSKS CVDKKIAQSY
     GLKKRVEAVR NCRGVTKKDM KLNDALPKIQ VDPETYKVHA DEKLLTCGPA TSLPLTQRFF
     LF
//
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