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Database: UniProt
Entry: A0A178DUP0_9PLEO
LinkDB: A0A178DUP0_9PLEO
Original site: A0A178DUP0_9PLEO 
ID   A0A178DUP0_9PLEO        Unreviewed;       839 AA.
AC   A0A178DUP0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   03-JUL-2019, entry version 19.
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=IQ07DRAFT_590179 {ECO:0000313|EMBL:OAL47324.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae;
OC   Cucurbitariaceae; Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL47324.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL47324.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL47324.1,
RC   ECO:0000313|Proteomes:UP000077535};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L.,
RA   Chaput D.L., Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) 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; KV441652; OAL47324.1; -; Genomic_DNA.
DR   EnsemblFungi; OAL47324; OAL47324; IQ07DRAFT_590179.
DR   OrthoDB; 183108at2759; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000077535; 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   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:UP000077535};
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:UP000077535}.
FT   DOMAIN      403    839       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    594    594       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR611612-52, ECO:0000256|PROSITE-
FT                                ProRule:PRU00700}.
FT   METAL       408    408       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       410    410       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       491    491       Nickel 1; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       491    491       Nickel 2; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       520    520       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       546    546       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       634    634       Nickel 1. {ECO:0000256|PIRSR:PIRSR001222-
FT                                51}.
FT   BINDING     493    493       Substrate. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     491    491       N6-carboxylysine. {ECO:0000256|PIRSR:
FT                                PIRSR001222-50}.
SQ   SEQUENCE   839 AA;  90748 MW;  6CFF68EA38D02319 CRC64;
     MQLCPKELDK LVISQLGLLA QRRLARGVKL NHAEAAALIA NNLQELIRDG NHTVADLMSI
     GKTMLGRRHV LPSVVSSLAE LMVEGTFRTG TYLVTVHHPV SSDDGDLEKA LYGSFLPIPS
     NDMFPLPEAS VYEDHKQSGA IIAVKGEAGR ITLNEGRKRI KLKVKSMGDR PIQVGSHYHF
     IETNPQLHFD RVRAHGFRLD IPAGTSVRFE PGDTKTVTLV QIAGNQIIRG GNRLASGFIG
     DLSVAEGIAD RMKAGGFLHE PEPLGDAVHI DFCTMEREAY ISMFGPTTGD LVRLGATDLW
     IKVEKDMTKY GDECAFGGGK TLREGMGQAG GVSDKGSLDT VITNALIIDW TGIYKADIGI
     KDGIIVGIGK AGNPDVMDGV HPDLIVGSCT DVIAGEHNIV TAGGFDTHIH FICPQQAQEA
     IASGITTMLG GGTGPSTGTN ATTCTPGKTH IRQMLQAIDE LPVNYGITGK GNDSDLRPLQ
     QQAEAGVCGL KLHEDWGTTP AAIDACLTVC DEYDIQTLIH TDTLNESGFV EQTIAAFKNR
     TIHTYHTEGA GGGHAPDIIS VVEHDNVLPS STNPTRPYTR NTLDEHLDML MVCHHLSRNI
     PEDVAFAESR IRAETIAAED VLHDLGAISM MSSDSQAMGR CGEVILRTWN TAHKNKVQRG
     TLKEDEGTGA DNFRVKRYIS KYTINPAIAQ GMGHLIGSIE VGKVADLVVW TPRNFGVKPK
     LIVKSGFCAY ALMGDPNASI PTVEPIIMRP MFAPLVPSSS ITFVSQASIS SGVVKSYGLR
     KRVEAVKNCR NIGKKDMKFN DTRPKMKVDP ERYTVEADGM VCTAEPAEVL PLTQEYFVY
//
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