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Database: UniProt
Entry: A0A1L9P550_ASPVE
LinkDB: A0A1L9P550_ASPVE
Original site: A0A1L9P550_ASPVE 
ID   A0A1L9P550_ASPVE        Unreviewed;       836 AA.
AC   A0A1L9P550;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   03-JUL-2019, entry version 17.
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=ASPVEDRAFT_122059 {ECO:0000313|EMBL:OJI96543.1};
OS   Aspergillus versicolor CBS 583.65.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1036611 {ECO:0000313|EMBL:OJI96543.1, ECO:0000313|Proteomes:UP000184073};
RN   [1] {ECO:0000313|Proteomes:UP000184073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 583.65 {ECO:0000313|Proteomes:UP000184073};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K.,
RA   Battaglia E., Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C.,
RA   Canovas D., Cerqueira G.C., Chen F., Chen W., Choi C., Clum A.,
RA   Dos Santos R.A., Damasio A.R., Diallinas G., Emri T., Fekete E.,
RA   Flipphi M., Freyberg S., Gallo A., Gournas C., Habgood R., Hainaut M.,
RA   Harispe M.L., Henrissat B., Hilden K.S., Hope R., Hossain A.,
RA   Karabika E., Karaffa L., Karanyi Z., Krasevec N., Kuo A., Kusch H.,
RA   LaButti K., Lagendijk E.L., Lapidus A., Levasseur A., Lindquist E.,
RA   Lipzen A., Logrieco A.F., MacCabe A., Maekelae M.R., Malavazi I.,
RA   Melin P., Meyer V., Mielnichuk N., Miskei M., Molnar A.P., Mule G.,
RA   Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P., Overkamp K.M.,
RA   Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F., Ramon A.,
RA   Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E.,
RA   Sanguinetti M., Schuetze T., Sepcic K., Shelest E., Sherlock G.,
RA   Sophianopoulou V., Squina F.M., Sun H., Susca A., Todd R.B., Tsang A.,
RA   Unkles S.E., van de Wiele N., van Rossen-Uffink D., Oliveira J.V.,
RA   Vesth T.C., Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B.,
RA   Baker S.E., Benoit I., Brakhage A.A., Braus G.H., Fischer R.,
RA   Frisvad J.C., Goldman G.H., Houbraken J., Oakley B., Pocsi I.,
RA   Scazzocchio C., Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S.,
RA   Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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; KV878125; OJI96543.1; -; Genomic_DNA.
DR   EnsemblFungi; OJI96543; OJI96543; ASPVEDRAFT_122059.
DR   OrthoDB; 183108at2759; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000184073; 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   HAMAP; MF_01954; Urease_beta; 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   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:UP000184073};
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:UP000184073}.
FT   DOMAIN      400    836       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    591    591       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR611612-52, ECO:0000256|PROSITE-
FT                                ProRule:PRU00700}.
FT   METAL       405    405       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       407    407       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       488    488       Nickel 1; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       488    488       Nickel 2; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       517    517       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       543    543       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       631    631       Nickel 1. {ECO:0000256|PIRSR:PIRSR001222-
FT                                51}.
FT   BINDING     490    490       Substrate. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     488    488       N6-carboxylysine. {ECO:0000256|PIRSR:
FT                                PIRSR001222-50}.
SQ   SEQUENCE   836 AA;  90729 MW;  F02DE46019DC5D9B CRC64;
     MHLIPKELDK LAISQLGFLA QRRLARGVRL NHAEAAALIS SNLHELIRDG PYSVADLMSI
     GKTMLGRRHV LPSVPSTLVE LQVEGTFRTG TYLVTVHHPI SSDDGDLERA LYGSFLPIPP
     GDTFPDPNPD DYLPEKVPGA VIPVKDARIT LNEGRKRIKL KVMSKGDRPI QVGSHYHFIE
     VNPQLHFDRI RAYGFRLDIP AGTSVRFEPG DTKTVTLVEI GGHKVIKGGN FLASGAIDLG
     RADEIIQRLQ TAGFAHVPEP GADSALVAPF TLEREAYARL FGPTTGDMIR LGTTNLWVKV
     EKDYTYYGDE CSFGGGKSIR EGMGQAAGKS TKECLDTVIT NAIIIDWSGI YKADIGIRDG
     IIVGIGKSGN PDVMDGVHPN MVIGSSTDVI AGENKIITAG GLDTHIHFIC PQQAQEALAT
     GITTFLGGGT GPSTGTNATT CTPGPTHMRQ MIQACDQIPI NVGITGKGND SGGVSIEEQI
     IAGAAGLKLH EDWGSTPAAI DTCLDVCDKY DVQCMIHTDT LNESGFVEQT IEAFKNRTIH
     TYHTEGAGGG HAPDIISVVE HPNVLPSSTN PTRPFTMNTL DEHLDMLMVC HHLSKNIPED
     VAFAESRIRA ETIAAEDVLH DLGAISMMSS DSQAMGRCGE VILRTWNTAH KNKEQRGPLP
     EDEGTDADNF RVKRYISKYT INPAIAQGMS HLIGSVEVGK LADLVIWSPN YFGTKPTQIL
     KSGMIVASMM GDPNGSIPTI QPVIMRPQFG AYLPSTSVMF VSQASVDTNT VQKYGLKKRI
     EAVKHCRNIG KNDMKFNDTM PKMKVDPESY RVEADGELCT AEPAEWLPLT QDYFVY
//
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