(data stored in ACNUC7421 zone)

SWISSPROT: A2Q896_ASPNC

ID   A2Q896_ASPNC            Unreviewed;       831 AA.
AC   A2Q896;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 91.
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=An01g03550 {ECO:0000313|EMBL:CAK36893.1};
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011 {ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK36893.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 {ECO:0000313|Proteomes:UP000006706};
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA   Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA   van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA   Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA   Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA   Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA   van Ooyen A.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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}.
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DR   EMBL; AM269958; CAK36893.1; -; Genomic_DNA.
DR   SMR; A2Q896; -.
DR   PaxDb; A2Q896; -.
DR   EnsemblFungi; CAK36893; CAK36893; An01g03550.
DR   HOGENOM; HOG000075064; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000006706; Chromosome 2R.
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; 1.
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;
DR   PRODOM; A2Q896.
DR   SWISS-2DPAGE; A2Q896.
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001222, ECO:0000256|PROSITE-
KW   ProRule:PRU00700, ECO:0000313|EMBL:CAK36893.1};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR001222,
KW   ECO:0000256|PIRSR:PIRSR001222-51};
KW   Nickel {ECO:0000256|PIRNR:PIRNR001222, ECO:0000256|PIRSR:PIRSR001222-51}.
FT   DOMAIN          392..831
FT                   /note="Urease"
FT                   /evidence="ECO:0000259|PROSITE:PS51368"
FT   ACT_SITE        583
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-52,
FT                   ECO:0000256|PROSITE-ProRule:PRU00700"
FT   METAL           397
FT                   /note="Nickel 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   METAL           399
FT                   /note="Nickel 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   METAL           480
FT                   /note="Nickel 1; via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   METAL           480
FT                   /note="Nickel 2; via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   METAL           509
FT                   /note="Nickel 2; via pros nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   METAL           535
FT                   /note="Nickel 2; via tele nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   METAL           623
FT                   /note="Nickel 1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   BINDING         482
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00700"
FT   MOD_RES         480
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-50"
SQ   SEQUENCE   831 AA;  89993 MW;  24C499622E751F6F CRC64;
     MHLCPKELDK LVISQLGFLA QRRLARGIRL NHAEAALIRD GQYSVADLMS IGKSMLGRRH
     VLPSVVSTLY ELQVEGTFTT GTYLVTVHNP ISSDDGDLEK ALYGSFLPIP PADAFPDPDP
     EDYEPEKTPG AILPVKNERI ILNEGRKRIK LKVMSRGDRP IQVGSHYHFI ETNPQLHFDR
     LRSYGYRLDI PAGTSVRFEP GDTKVVTLVE IGGHRVIRGG NCIASGKVDL ARAEEIMARL
     QVQNFAHVPE PTADSALVPT PFSMDREAYA RMFGPTTGDL VRLGLTNLWV RVEKDYTSYG
     DECTFGGGKT IRDGMGQSSE KSTQHALDTV ITNALIIDWT GIFKADIGIK DGLIVGIGKA
     GNPDIMDGVT PGMTVGSSTD VIAGENKIVT AGGFDTHIHF ICPQQVDEAL ASGITTFLGG
     GTGPSTGSNA TTCTPGPVHM RQMLQACDRL PINVGITGKG NDCGGVSIEE QIYAGAAGLK
     LHEDWGSTPA AIDSCLDLCD KFDVQCMIHT DTLNESGFVE QTIEAFKNRT IHTYHTEGAG
     GGHAPDIISV VEHPNVLPSS TNPTRPFTLN TLDEHLDMLM VCHHLSKNIA EDVAFAESRI
     RAETIAAEDV LHDLGAISMM SSDSQAMGRC GEVILRTWNT AHKNKEQRGP LPEDEGTGAD
     NFRVKRYVSK YTINPAIAQG MSHMIGSIEV GKIADLVLWT PSAFGVKPTQ VVKSGMIAVS
     VMGDPNASIP TVQPVIMRPQ FGNTQALVPS TSITFVSQAS LDAGIVQSYN LQKRVEAVKN
     CRNIGKADMK FNDIMPKMHV DPESYRVEAD GMLCDAEPAG SLPLTQDYFV Y
//

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