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Database: UniProt
Entry: A0A1Y1UFQ9_9TREE
LinkDB: A0A1Y1UFQ9_9TREE
Original site: A0A1Y1UFQ9_9TREE 
ID   A0A1Y1UFQ9_9TREE        Unreviewed;       837 AA.
AC   A0A1Y1UFQ9;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   03-JUL-2019, entry version 11.
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=BD324DRAFT_489307 {ECO:0000313|EMBL:ORX36344.1};
OS   Kockovaella imperatae.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Tremellomycetes; Tremellales; Cuniculitremaceae; Kockovaella.
OX   NCBI_TaxID=4999 {ECO:0000313|EMBL:ORX36344.1, ECO:0000313|Proteomes:UP000193218};
RN   [1] {ECO:0000313|EMBL:ORX36344.1, ECO:0000313|Proteomes:UP000193218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-17943 {ECO:0000313|EMBL:ORX36344.1,
RC   ECO:0000313|Proteomes:UP000193218};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Louie K.B., Bewick A.J.,
RA   Labutti K., Haridas S., Kuo A., Salamov A., Ahrendt S.R., Lau R.,
RA   Bowen B.P., Lipzen A., Sullivan W., Andreopoulos W.B., Clum A.,
RA   Lindquist E., Daum C., Northen T.R., Ramamoorthy G., Schmitz R.J.,
RA   Gryganskyi A., Culley D., Magnuson J., James T.Y., O'Malley M.A.,
RA   Stajich J.E., Spatafora J.W., Visel A., Grigoriev I.V.;
RT   "Widespread Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (MAR-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ORX36344.1}.
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DR   EMBL; NBSH01000008; ORX36344.1; -; Genomic_DNA.
DR   OrthoDB; 183108at2759; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000193218; 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:UP000193218};
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:UP000193218}.
FT   DOMAIN      395    837       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    590    590       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR611612-52, ECO:0000256|PROSITE-
FT                                ProRule:PRU00700}.
FT   METAL       400    400       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       402    402       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       483    483       Nickel 1; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       483    483       Nickel 2; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       516    516       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       542    542       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       630    630       Nickel 1. {ECO:0000256|PIRSR:PIRSR001222-
FT                                51}.
FT   BINDING     485    485       Substrate. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     483    483       N6-carboxylysine. {ECO:0000256|PIRSR:
FT                                PIRSR001222-50}.
SQ   SEQUENCE   837 AA;  91216 MW;  A1D3E10D40386D31 CRC64;
     MHLLPRERDK LLLYTLGSLA QRRLARGLQL NRSETIALIA FQLHEYIRDG RHSVAQLMDL
     GKQMLGRRHV MEGVPESIHD IQVEGTFPDG TFLVTVHDPI CSDSGNLAHA LYGSFLPLPS
     EDLFPIPLPS LAPLPGQVIC VKEKIKLNEG RKRWLIQVKN EGDRPIQVGS HYPFLETNPS
     LVFDRLLSYG LHLDIAAGTA VRFEPGERKT VSMVEFGGTK FISGGNGIGS GRFDESRRHT
     DIAKYVERGG FGHRMQETVE EGVVPEMDRE VYASMFGPTT GDRLRLADTD LWIEVEKDYT
     VYGDECKFGG GKVLRDGAGQ ASNRSDQEVL DLVITNALII DWSGIYKADI GVKNGVIAGI
     GKAGNPDIME GVTDGMIVGS CTEVVAGEKL IVTAGAIDVH VHFITADMWQ EALSTGITTL
     VGGGTGPAEG TKATTCTSSK WYMQTMLAAT DEIPLNFGFT GKGNDSGVRG MRDVIEAGAC
     GLKVHEDWGA TPEVIDRSLA MGDEYDVQLT VQVNIHTDTL NESGFVEQTV AAFKGRTIHT
     YHTEGAGGGH APDIIRVCEY ENVLPSSTNP TRPFAVNTLD EHLDMLMVCH HLDKSIPEDI
     AFADSRIRAE TVAAEDVLQD TGAISMISSD ALAMGRIGEV VARTWRTAAK MREMRGPLDG
     DIDGRDNERV KRYIAKYTIN PAITHGMSHL VGHIAKGCLA DLVLWKPEFF GTRAETVIKG
     GVIAWAQVGE SNGSIPTVQP SYGRPQWGAN AGSVAMNSIA WVSQAAVDKD IKSQYGLKKR
     VEAVKNCRNI GKKDMKLNDA TPKMEVDPET YIVKADGILC DVPPATSLPL TKKHWIF
//
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