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Entry: A0A1B8EN60_9PEZI
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ID   A0A1B8EN60_9PEZI        Unreviewed;       835 AA.
AC   A0A1B8EN60;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   11-DEC-2019, entry version 20.
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=VF21_08330 {ECO:0000313|EMBL:OBT72810.1};
OS   Pseudogymnoascus sp. 05NY08.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus;
OC   unclassified Pseudogymnoascus.
OX   NCBI_TaxID=1622149 {ECO:0000313|EMBL:OBT72810.1, ECO:0000313|Proteomes:UP000092096};
RN   [1] {ECO:0000313|EMBL:OBT72810.1, ECO:0000313|Proteomes:UP000092096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05NY08 {ECO:0000313|EMBL:OBT72810.1,
RC   ECO:0000313|Proteomes:UP000092096};
RA   Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT   "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT   white-nose syndrome of bats.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000092096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05NY08 {ECO:0000313|Proteomes:UP000092096};
RX   PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA   Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT   "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT   white-nose syndrome of bats.";
RL   Nat. Commun. 9:35-35(2018).
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; KV458877; OBT72810.1; -; Genomic_DNA.
DR   EnsemblFungi; OBT72810; OBT72810; VF21_08330.
DR   OrthoDB; 183108at2759; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000092096; 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   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:PIRSR001222-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092096}.
FT   DOMAIN          399..835
FT                   /note="Urease"
FT                   /evidence="ECO:0000259|PROSITE:PS51368"
FT   ACT_SITE        590
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-52,
FT                   ECO:0000256|PROSITE-ProRule:PRU00700"
FT   METAL           404
FT                   /note="Nickel 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   METAL           406
FT                   /note="Nickel 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   METAL           487
FT                   /note="Nickel 1; via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   METAL           487
FT                   /note="Nickel 2; via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   METAL           516
FT                   /note="Nickel 2; via pros nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   METAL           542
FT                   /note="Nickel 2; via tele nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   METAL           630
FT                   /note="Nickel 1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   BINDING         489
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00700"
FT   MOD_RES         487
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-50"
SQ   SEQUENCE   835 AA;  90521 MW;  6C13D04123A35C8B CRC64;
     MHLIPREIDK LVISQLGLLA QRRLARGVRL NHSEACALIA NNLQELIRDG NHNVADLMSI
     GTTMLGRRHV LPAVVSTLKQ IQVEGTFPQG TYLVTVQTPI SSDDGDLNKA LYGSFLPIPD
     ADLFKVPDDE ECTAEKMPGA VIAVKGKITI NKGRKRIQLK VTNHGDRPVQ VGSHFHFIET
     NPHLEFDRVR SYGYRLDIAA GTSIRFEAGD EKTVTLVEIA GRKIVRGGNN IASGVFDLSR
     TDEILKNIEA GNFRNILEPA GDAAHIKPFE LDRSVYASMF GPTVGDKIRL GDTDLWIKVE
     KDLTSYGDEC KFGGGKTLRD GMGQATGESD EDSLDLVIIN ALIVDWSGIY KADIGIKNGF
     ISGIGKAGSP DVMDGVTEGM IVGSCTDVMA GEGMIVTAGG IDTHIHYICP QQASECMATG
     VTTLLGGGTG PTAATTATTC TPGKNNMRDM LQALDTMPLN YGITGKGNDS DPKALREQVE
     AGACGLKLHE DWGCTPAAID SCLTVCDEYD VQCLIHTDTL NESGFVESTI AAFKDRAIHT
     YHTEGAGGGH APDIISVVEY DNVLPSSTNP TRPFTRNTLD EHLDMVMVCH HLSKNIPEDI
     AFAESRIRAE TIAAEDVLHD MGAISMMSSD SQAMGRCGEV VLRTWNTAHK NKVQRGFLKE
     DEGTDADNFR VKRYVSKYTI NPALAQGMSH LLGSVEVGKL ADLVIWDPAW FGTKPTMVVK
     SGLISYSMMG DPNASISTVQ PIIGRPMFAP HVPSTSVLFV SQASIDCGNI ESYGLKKRIE
     AVKGCRTVRK TDMKHNFEMP KIHVDPENYR VEADGVHCTA EPSTELPLTQ SVFVF
//
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