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Database: UniProt
Entry: F0Y0Q2_AURAN
LinkDB: F0Y0Q2_AURAN
Original site: F0Y0Q2_AURAN 
ID   F0Y0Q2_AURAN            Unreviewed;       833 AA.
AC   F0Y0Q2;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 66.
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|PIRNR:PIRNR001222};
GN   Name=URE1 {ECO:0000313|EMBL:EGB11704.1};
GN   ORFNames=AURANDRAFT_77851 {ECO:0000313|EMBL:EGB11704.1};
OS   Aureococcus anophagefferens (Harmful bloom alga).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Pelagophyceae; Pelagomonadales;
OC   Aureococcus.
OX   NCBI_TaxID=44056 {ECO:0000313|Proteomes:UP000002729};
RN   [1] {ECO:0000313|EMBL:EGB11704.1, ECO:0000313|Proteomes:UP000002729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP 1984 {ECO:0000313|Proteomes:UP000002729};
RX   PubMed=21368207; DOI=10.1073/pnas.1016106108;
RA   Gobler C.J., Berry D.L., Dyhrman S.T., Wilhelm S.W., Salamov A.,
RA   Lobanov A.V., Zhang Y., Collier J.L., Wurch L.L., Kustka A.B., Dill B.D.,
RA   Shah M., VerBerkmoes N.C., Kuo A., Terry A., Pangilinan J., Lindquist E.A.,
RA   Lucas S., Paulsen I.T., Hattenrath-Lehmann T.K., Talmage S.C., Walker E.A.,
RA   Koch F., Burson A.M., Marcoval M.A., Tang Y.Z., Lecleir G.R., Coyne K.J.,
RA   Berg G.M., Bertrand E.M., Saito M.A., Gladyshev V.N., Grigoriev I.V.;
RT   "Niche of harmful alga Aureococcus anophagefferens revealed through
RT   ecogenomics.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:4352-4357(2011).
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|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}.
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DR   EMBL; GL833122; EGB11704.1; -; Genomic_DNA.
DR   RefSeq; XP_009034045.1; XM_009035797.1.
DR   AlphaFoldDB; F0Y0Q2; -.
DR   MEROPS; M38.982; -.
DR   EnsemblProtists; EGB11704; EGB11704; AURANDRAFT_77851.
DR   GeneID; 20229053; -.
DR   KEGG; aaf:AURANDRAFT_77851; -.
DR   eggNOG; ENOG502QPKB; Eukaryota.
DR   InParanoid; F0Y0Q2; -.
DR   OrthoDB; 1408002at2759; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000002729; 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   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; 2.
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:UP000002729}.
FT   DOMAIN          394..833
FT                   /note="Urease"
FT                   /evidence="ECO:0000259|PROSITE:PS51368"
FT   ACT_SITE        585
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-52,
FT                   ECO:0000256|PROSITE-ProRule:PRU00700"
FT   BINDING         399
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   BINDING         401
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   BINDING         482
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         482
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         484
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00700"
FT   BINDING         511
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   BINDING         537
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   BINDING         625
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT   MOD_RES         482
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-50"
SQ   SEQUENCE   833 AA;  87170 MW;  CD7CC35C9F784B67 CRC64;
     MKLTPREVDH LQLHQCGALA QKRLARGLKL NEPEAIALIA AVCMELVRDG LSVFELMEKG
     KTLLGARQVQ PGVRELVGEV QIEATFPDGT KLLTIHDPIA SADGDLALAL HGSFLPVPDL
     AAFGDAPPAA RPPGATTPRD GSVTLCEGRD RVELVVRNGG DRPIQVGSHY PFLETNRALT
     FDRRAALGMR LDVPSGSSVR FEPGDEKTVT LVAYGGARVV RSGNLLTDGA ASADRADEVM
     AKVAAGGFGH APLPGPPPPG APFSMARAEY AATFGPTLGD VVRLGDTDLV VRVEKDFTVY
     GDECKFGGGK TLREGMGQQT GCAASDALDV VITNALVVDA VLGVVKCDIG LKGNRIVGIG
     KAGNPDVMDG VTPGMIVGVT TEAVAGEKLI ATAGGIDAHI HFICPQQCDD AIASGLTTMY
     GGGTGPATGT CATTCTPAPS EVEMMLKATD GIPLNFGFSG KGNTSDPKGL REVVAAGASG
     LKLHEDWGTT PAAIDACLSF ADEYDVAVTI HTDTLNESGF VDDSLGAIKG RTIHTYHSEG
     AGGGHAPDII KVCGEPNVLP SSTNPTRPFT VNTVDEHLDM LMVCHHLDKS IPEDVAFAES
     RIRGETIAAE DILHDMGAIS MISSDSQAMG RIGEVITRTW QTADKMKRQR GPLPEDATSG
     DDNARVKRYV AKYTINPAIA HGMADHIGSL EVGKLADIVL WKPSHFGAKP EMVIKGGTIA
     WAQMGDPNAS IPTPQPVKMR PMFGAFGKAV GGTSLAFVSK LAVETNIQNR LGLGKLAVAV
     ANTRALSKKD MVNNAALPAI AVDPETFEVT ADGVQLTCAP AKTVPLARTY FLF
//
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