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Database: UniProt
Entry: R7S2H5_PUNST
LinkDB: R7S2H5_PUNST
Original site: R7S2H5_PUNST 
ID   R7S2H5_PUNST            Unreviewed;       838 AA.
AC   R7S2H5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   03-JUL-2019, entry version 40.
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=PUNSTDRAFT_108919 {ECO:0000313|EMBL:EIN04054.1};
OS   Punctularia strigosozonata (strain HHB-11173) (White-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Corticiales; Punctulariaceae; Punctularia.
OX   NCBI_TaxID=741275 {ECO:0000313|EMBL:EIN04054.1};
RN   [1] {ECO:0000313|EMBL:EIN04054.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HHB-11173 SS5 {ECO:0000313|EMBL:EIN04054.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A.,
RA   Henrissat B., Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S.,
RA   Aerts A., Benoit I., Boyd A., Carlson A., Copeland A., Coutinho P.M.,
RA   de Vries R.P., Ferreira P., Findley K., Foster B., Gaskell J.,
RA   Glotzer D., Gorecki P., Heitman J., Hesse C., Hori C., Igarashi K.,
RA   Jurgens J.A., Kallen N., Kersten P., Kohler A., Kues U., Kumar T.K.,
RA   Kuo A., LaButti K., Larrondo L.F., Lindquist E., Ling A., Lombard V.,
RA   Lucas S., Lundell T., Martin R., McLaughlin D.J., Morgenstern I.,
RA   Morin E., Murat C., Nagy L.G., Nolan M., Ohm R.A., Patyshakuliyeva A.,
RA   Rokas A., Ruiz-Duenas F.J., Sabat G., Salamov A., Samejima M.,
RA   Schmutz J., Slot J.C., St Johnn, F, Stenlid J., Sun H., Sun S.,
RA   Syed K., Tsang A., Wiebenga A., Young D., Pisabarro A., Eastwood D.C.,
RA   Martin F., Cullen D., Grigoriev I.V., Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic mechanisms for decay of lignin
RT   reconstructed using 31 fungal genomes.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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; JH687557; EIN04054.1; -; Genomic_DNA.
DR   RefSeq; XP_007388843.1; XM_007388781.1.
DR   STRING; 202698.XP_007388843.1; -.
DR   EnsemblFungi; EIN04054; EIN04054; PUNSTDRAFT_108919.
DR   GeneID; 18876200; -.
DR   KEGG; psq:PUNSTDRAFT_108919; -.
DR   KO; K01427; -.
DR   OMA; GFDSHIH; -.
DR   OrthoDB; 183108at2759; -.
DR   UniPathway; UPA00258; UER00370.
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-
KW   51}.
FT   DOMAIN      398    838       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    589    589       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR611612-52, ECO:0000256|PROSITE-
FT                                ProRule:PRU00700}.
FT   METAL       403    403       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       405    405       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       486    486       Nickel 1; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       486    486       Nickel 2; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       515    515       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       541    541       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       629    629       Nickel 1. {ECO:0000256|PIRSR:PIRSR001222-
FT                                51}.
FT   BINDING     488    488       Substrate. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     486    486       N6-carboxylysine. {ECO:0000256|PIRSR:
FT                                PIRSR001222-50}.
SQ   SEQUENCE   838 AA;  89601 MW;  855E688002EC02A0 CRC64;
     MHILPRDEAK LLLHQAGFLA QKRLARGLKL NQTEATALIA SVLQERIRDA RHSVAELMQH
     GKTLLGRRHV LPDVVSLLHE IQVEGTFPDG VFLVTVHDPV CTESGDIAAA LYGSFLPVPP
     EDAFPSTDPA DFAREKVAGA IIARKESIVI NKGRERIRLR VTNNGDRPIQ IGSHYHFVET
     NKALSFDRGK AYGKRLDIAA GTAVRFEPGD VKTVTLCTIA GAKIISGGNN LASGVFDLAR
     TDDIIRGLVQ KGFGYAPEPG ALEVSEDTSI GRDAYIAMFG PTVGDRVRLG DTALWIEVER
     DETVYGDEVK FGGGKSIREG MGQATNRSSS ETLDLVITNA LIVDWSGIYK ADVGVKNGYI
     AGIGKAGNPD VMAGVHPSLV IGSSTEVIAG EKMILTAGAI DAHVHYICPQ QVNEALAAGT
     TTMIGGGTGP SAGTNATTCT PSPFYMRHML AATDGLPMNF GFTGKGNDAG TTAVEEIVKA
     GACGLKLHED WGTTPAVIVK ALDVGDKYDV QVNIHTDTLN ESGFVESTIA AFGGRTIHTY
     HTEGAGGGHA PDIIVVCGQN NVLPSSTNPT RPFTKNTLDE HLDMLMVCHH LDKSIPEDLA
     FAESRIRAET VAAEDVLHDT GAISMISSDS QAMGRVGEVV SRTWRTASKM REFRGPLSAL
     GDSEGVDNGR VKRYISKYTI NPAITHGMSH LVGQVATGTL ADLVLWKPEN FGSKPSMVLK
     SGVIAWSQMG DANASIPTVQ PFYSKPMWGS YPASAALNSI SFVSEISISS GTVASYKLSK
     RFEPVTGCRA VTKKDMKWND ATPEMKVDPE NYEVHADGVL ADIEPAERLP LGKAYNLF
//
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