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Database: UniProt
Entry: A0A229Z3R7_9EURO
LinkDB: A0A229Z3R7_9EURO
Original site: A0A229Z3R7_9EURO 
ID   A0A229Z3R7_9EURO        Unreviewed;       836 AA.
AC   A0A229Z3R7;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   13-SEP-2023, entry version 27.
DE   RecName: Full=Urease {ECO:0000256|ARBA:ARBA00013883, ECO:0000256|PIRNR:PIRNR001222};
DE            EC=3.5.1.5 {ECO:0000256|ARBA:ARBA00012934, ECO:0000256|PIRNR:PIRNR001222};
DE   AltName: Full=Urea amidohydrolase {ECO:0000256|ARBA:ARBA00030395, ECO:0000256|PIRNR:PIRNR001222};
GN   Name=URE1 {ECO:0000313|EMBL:RHZ64885.1};
GN   ORFNames=CDV55_106565 {ECO:0000313|EMBL:RHZ64885.1}, CFD26_105683
GN   {ECO:0000313|EMBL:RLL99711.1};
OS   Aspergillus turcosus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1245748 {ECO:0000313|EMBL:RHZ64885.1, ECO:0000313|Proteomes:UP000215394};
RN   [1] {ECO:0000313|Proteomes:UP000215289, ECO:0000313|Proteomes:UP000215394}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLL99711.1}, and HMR AF 23
RC   {ECO:0000313|EMBL:RHZ64885.1};
RA   Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA   Perkins V., De Repentigny L., Dufresne S.F.;
RT   "Draft genome sequences of two Aspergillus turcosus clinical strains
RT   isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT   other azole-resistant.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000242,
CC         ECO:0000256|PIRNR:PIRNR001222};
CC   -!- COFACTOR:
CC       Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001222-51};
CC       Note=Binds 2 nickel ions per subunit. {ECO:0000256|PIRSR:PIRSR001222-
CC       51};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC       urea (urease route): step 1/1. {ECO:0000256|ARBA:ARBA00004897,
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-dependent
CC       hydrolases superfamily. Urease alpha subunit family.
CC       {ECO:0000256|ARBA:ARBA00007966}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RHZ64885.1}.
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DR   EMBL; NKHV02000071; RHZ64885.1; -; Genomic_DNA.
DR   EMBL; NIDN02000026; RLL99711.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A229Z3R7; -.
DR   STRING; 1245748.A0A229Z3R7; -.
DR   OrthoDB; 1408002at2759; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000215289; Unassembled WGS sequence.
DR   Proteomes; UP000215394; Unassembled WGS sequence.
DR   GO; GO:0035550; C:urease complex; IEA:InterPro.
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; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.10.150.10; Urease, beta subunit; 1.
DR   Gene3D; 3.30.280.10; Urease, gamma-like subunit; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 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-like.
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   NCBIfam; TIGR01792; urease_alph; 1.
DR   NCBIfam; TIGR00192; urease_beta; 1.
DR   NCBIfam; TIGR00193; urease_gam; 1.
DR   PANTHER; PTHR33569; UREASE; 1.
DR   PANTHER; PTHR33569:SF1; UREASE; 1.
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; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51278; Urease, beta-subunit; 1.
DR   SUPFAM; SSF54111; Urease, gamma-subunit; 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|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001222};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR001222};
KW   Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|PIRNR:PIRNR001222};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215289}.
FT   DOMAIN          400..836
FT                   /note="Urease"
FT                   /evidence="ECO:0000259|PROSITE:PS51368"
FT   ACT_SITE        591
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-52,
FT                   ECO:0000256|PROSITE-ProRule:PRU00700"
FT   BINDING         405
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   BINDING         407
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   BINDING         488
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   BINDING         488
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   BINDING         490
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00700"
FT   BINDING         517
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   BINDING         543
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   BINDING         631
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   MOD_RES         488
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-50"
SQ   SEQUENCE   836 AA;  91013 MW;  30B9FCB7DD8F0095 CRC64;
     MHLIPKELDK LVISQLGFLA QRRLARGVRL NHAEAAALIS SNLQELIRDG HYSVADLMSI
     GKTMLGRRHV LPSVVHTLVE LQVEGTFPTG TYLVTVHHPI SSDDGDLEKA LYGSFLPIPP
     ADTFPDPNPD DYLPEKMPGA VLPVKNERIT LNDGRKRIRL KVMSKGDRPI QVGSHYHFIE
     TNPQLHFDRL RAYGYRLDIP AGTSVRFEPG DTKTVTLVEI AGNRIIKGGN FLASGKVDIS
     RAEEIMQRLQ AEGFAHVPEP TADSALITPF TMDREAYARM FGPTTGDLVR LGLTNLWVRV
     EKDCTVYGDE CTFGGGKTLR EGMGQSSERS EAECLDTVIT NALIIDWSGI YKADIGIKNG
     LISAIGKAGN PDMMDGVHPD MIVGSSTDVI AGENKIVTAG GFDTHIHFIC PQQVDEALAS
     GITTFLGGGT GPSTGTNATT CTPGPTHMRQ MIQACDSLPI NVGITGKGND CGGKSIEEQI
     RAGAAGLKLH EDWGSTPAAI DTCLDMCDKF DVQCMIHTDT LNESGFVEQT VKSFKNRTIH
     TYHTEGAGGG HAPDIISVVE HPNVLPSSTN PTRPFTMNTL DEHLDMLMVC HHLSKNIPED
     VAFAESRIRA ETIAAEDVLH DLGAISMMSS DSQAMGRCGE VILRTWNTAH KNKAQRGPLQ
     EDEGTGADNF RVKRYISKYT INPAIAQGMS HLIGSVEVGK LADLVIWHPS SFGTKPAQIL
     KSGMIVASQM GDPNGSIPTI EPVIMRPMFG SFVPSTSIMW VSQASIDDGI VQSYGLKKRI
     EPVRNCRNVG KKDMKFNDTM PKMRVDPESY RVEADGVLCE AEPADSLPLT QDYFVY
//
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