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Database: UniProt
Entry: A0A0D2C8F8_9EURO
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ID   A0A0D2C8F8_9EURO        Unreviewed;       836 AA.
AC   A0A0D2C8F8;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   03-JUL-2019, entry version 28.
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=PV05_01389 {ECO:0000313|EMBL:KIW61241.1};
OS   Exophiala xenobiotica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Exophiala.
OX   NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW61241.1, ECO:0000313|Proteomes:UP000054342};
RN   [1] {ECO:0000313|EMBL:KIW61241.1, ECO:0000313|Proteomes:UP000054342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW61241.1,
RC   ECO:0000313|Proteomes:UP000054342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL   Submitted (JAN-2015) 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; KN847317; KIW61241.1; -; Genomic_DNA.
DR   RefSeq; XP_013321828.1; XM_013466374.1.
DR   EnsemblFungi; KIW61241; KIW61241; PV05_01389.
DR   GeneID; 25323297; -.
DR   OrthoDB; 183108at2759; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000054342; 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:UP000054342};
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:UP000054342}.
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;  89732 MW;  3ECED8BD921C3FA5 CRC64;
     MQLVPKELDK LVTAQLGFLA QRRLARGVRL NHAEACALIA SVLHELVRDG NHTCADLMAM
     GKQLLGRRHV LPAVVSTLHT VQIEGTFKTG TYLVTVDHPI SSDDGDLEKA LYGSFLPVPS
     KDAFPLADAS EYEDKKMPGA VIPVKQGKIV LSEGRKRIKL KVTSKGDRPI QIGSHYHFIE
     TNPALEFDRA RAYGYHLDVA AGTSVRFEPG DTKTVTLVEI AGNKVIHGGN NLATGPVDLS
     RVDEIISKLQ AGGFAHKPEP VRDMGFIDAA SLTRADYIGM FGPTTGDMVR LGSTDLWIKV
     ERDMTVYGDE CKFGGGKTLR EGMGQASGRH DVEVLDTVIT NALIVDWTGI YKADIGIKNG
     VIAGIGKAGN PDVMDGVHKD MVVGNGTDVV AGEGLIVTAG GIDSHIHLIC PQQVYEAISA
     GITTFLGGGT GPSAGTSATT CTPGKTLMKQ MLQAVDSLPI NYGITGKGND SDPVALRESC
     EAGACGLKLH EDWGTTPAAI DTCLSVCDEY DVQCLIHTDT LNESGFVESS IAAFKGRTIH
     TYHTEGAGGG HAPDIIKVVE HENVLPSSTN PTRPYTRDTL DEHLDMLMVC HHLSKNIPED
     VAFAESRIRA ETIAAEDVLH DLGAISMMSS DSQAMGRCGE VIMRTWNTAH KNKQQRGFLP
     EDEGTGVDNF RVKRYVSKYT VNAAIAQGMG HLIGSVEVGK VADLCLWKPA MFGTKPQLVI
     KSGFIAQAMM GDPNASIPTV EPIVSRPMFA AMVPKTSITF VSAKSIESGV IDGYGLNKRV
     EAVKGCRSVG KKDMKFNDVM PKMKVDPERY TVEADGQICK AEPATEVGLG QAYYVF
//
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