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Database: UniProt
Entry: M4BA19_HYAAE
LinkDB: M4BA19_HYAAE
Original site: M4BA19_HYAAE 
ID   M4BA19_HYAAE            Unreviewed;       798 AA.
AC   M4BA19;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   03-JUL-2019, entry version 36.
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};
OS   Hyaloperonospora arabidopsidis (strain Emoy2) (Downy mildew agent)
OS   (Peronospora arabidopsidis).
OC   Eukaryota; Stramenopiles; Oomycetes; Peronosporales; Peronosporaceae;
OC   Hyaloperonospora.
OX   NCBI_TaxID=559515 {ECO:0000313|EnsemblProtists:HpaP803129, ECO:0000313|Proteomes:UP000011713};
RN   [1] {ECO:0000313|EnsemblProtists:HpaP803129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Emoy2 {ECO:0000313|EnsemblProtists:HpaP803129};
RX   PubMed=21148394; DOI=10.1126/science.1195203;
RA   Baxter L., Tripathy S., Ishaque N., Boot N., Cabral A., Kemen E.,
RA   Thines M., Ah-Fong A., Anderson R., Badejoko W., Bittner-Eddy P.,
RA   Boore J.L., Chibucos M.C., Coates M., Dehal P., Delehaunty K.,
RA   Dong S., Downton P., Dumas B., Fabro G., Fronick C.,
RA   Fuerstenberg S.I., Fulton L., Gaulin E., Govers F., Hughes L.,
RA   Humphray S., Jiang R.H., Judelson H., Kamoun S., Kyung K., Meijer H.,
RA   Minx P., Morris P., Nelson J., Phuntumart V., Qutob D., Rehmany A.,
RA   Rougon-Cardoso A., Ryden P., Torto-Alalibo T., Studholme D., Wang Y.,
RA   Win J., Wood J., Clifton S.W., Rogers J., Van den Ackerveken G.,
RA   Jones J.D., McDowell J.M., Beynon J., Tyler B.M.;
RT   "Signatures of adaptation to obligate biotrophy in the
RT   Hyaloperonospora arabidopsidis genome.";
RL   Science 330:1549-1551(2010).
RN   [2] {ECO:0000313|EnsemblProtists:HpaP803129}
RP   IDENTIFICATION.
RC   STRAIN=Emoy2 {ECO:0000313|EnsemblProtists:HpaP803129};
RG   EnsemblProtists;
RL   Submitted (JUN-2015) to UniProtKB.
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; JH598048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 272952.HpaP803129; -.
DR   EnsemblProtists; HpaT803129; HpaP803129; HpaG803129.
DR   InParanoid; M4BA19; -.
DR   OMA; GFDSHIH; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000011713; 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   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   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:UP000011713};
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:UP000011713}.
FT   DOMAIN      357    798       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    548    548       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR611612-52, ECO:0000256|PROSITE-
FT                                ProRule:PRU00700}.
FT   METAL       362    362       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       364    364       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       445    445       Nickel 1; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       445    445       Nickel 2; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       474    474       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       500    500       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       588    588       Nickel 1. {ECO:0000256|PIRSR:PIRSR001222-
FT                                51}.
FT   BINDING     447    447       Substrate. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     445    445       N6-carboxylysine. {ECO:0000256|PIRSR:
FT                                PIRSR001222-50}.
SQ   SEQUENCE   798 AA;  85102 MW;  3F0AE7267F8301C6 CRC64;
     MTGLPRICKN LSYLYNFLLC SRRQVMDGVA SILDEVQVEG TFPDGTKLVT IHNPIANSDG
     DLALALYGSF LPVPELKVFG AAVSKPTVAP GAITTQDADI VLNAGRQVRV LQITNLSDRP
     IQVGSHYHLI EANPFLEMDR KRAYGHRLNI ASGTAVRFEP GDQKTVAVVP IAGNKVITGG
     NNLATGVVDE SRVNTIVANA LAKGFHHKSL DLSKLPASAA EPDYGICRIP KSVYAHTYGP
     TTGDMVRLGD MELYIVVEKD MTVYGDECKF GGGKAIREGM GQASGKTSDQ VVDTIITNAL
     IVDCTGIYKA DVGIKNDLIV SIGKGGNPDV LAGVTPDLIV GVNTEVIAGE GLILTAGGFD
     AHVHFICPQL CTEALASGLT TLVGGGTGPA TGTKATTCTP GPNHVKLMLQ ATDVIPMNIG
     LTCKGNTALP QGLQDAIDAG AVGMKLHEDW GTTPAAIDNC LRAAEENDVQ VTIHTDTLNE
     SCCVEHTIAA FKGRTIHTYH SEGAGGGHAP DIITVCGEPN VLPSSTNPTR PYTRNTIDEH
     VDMLMVCHHL NKNIAEDVAF AESRIRGETI AAEDLLHDMG AISIISSDSQ AMGRIGEVIT
     RTWQTADKMK RERGTLPEDA ASEHKGDNFR VRRYIAKYTI NPAITHGMSH LIGSVEVNKL
     ADLCLWKPCF FGSKPELVIK GGAIAFAQIG DPNASIPTPQ PVKMRPMFGT LGAAVGSSSI
     VFVSKSCADK KIAQSYGLKK RIEPVRGCRS VTKKELKLND AMPKIEVDPE TYKVHADGKL
     LTCESASLLP LAQRFFLF
//
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