ID A0A0D2XB04_FUSOF Unreviewed; 779 AA. AC A0A0D2XB04; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 08-NOV-2023, entry version 47. DE RecName: Full=Urease {ECO:0000256|ARBA:ARBA00013883}; DE EC=3.5.1.5 {ECO:0000256|ARBA:ARBA00012934}; DE AltName: Full=Urea amidohydrolase {ECO:0000256|ARBA:ARBA00030395}; GN Name=28943345 {ECO:0000313|EnsemblFungi:FOXG_01071P0}; OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium; OC Fusarium oxysporum species complex. OX NCBI_TaxID=660025 {ECO:0000313|EnsemblFungi:FOXG_01071P0, ECO:0000313|Proteomes:UP000002489}; RN [1] {ECO:0000313|Proteomes:UP000002489} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fo5176 {ECO:0000313|Proteomes:UP000002489}; RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212; RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.; RT "A highly conserved effector in Fusarium oxysporum is required for full RT virulence on Arabidopsis."; RL Mol. Plant Microbe Interact. 25:180-190(2012). RN [2] {ECO:0000313|EnsemblFungi:FOXG_01071P0} RP IDENTIFICATION. RC STRAIN=4287 / CBS 123668 / FGSC 9935 / NRRL 34936 RC {ECO:0000313|EnsemblFungi:FOXG_01071P0}; RG EnsemblFungi; RL Submitted (JUL-2023) to UniProtKB. 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 -!- COFACTOR: CC Name=Ni cation; Xref=ChEBI:CHEBI:25516; CC Evidence={ECO:0000256|PIRSR:PIRSR611612-51}; CC Note=Binds 2 nickel ions per subunit. {ECO:0000256|PIRSR:PIRSR611612- 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 -!- PTM: Carbamylation allows a single lysine to coordinate two nickel CC ions. {ECO:0000256|PIRSR:PIRSR611612-50}. 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; A0A0D2XB04; -. DR STRING; 426428.A0A0D2XB04; -. DR MEROPS; M38.982; -. DR EnsemblFungi; FOXG_01071T0; FOXG_01071P0; FOXG_01071. DR VEuPathDB; FungiDB:FOXG_01071; -. DR OMA; DTMDGVH; -. DR OrthoDB; 1408002at2759; -. DR UniPathway; UPA00258; UER00370. DR Proteomes; UP000002489; 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 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; 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 PANTHER; PTHR43440; UREASE; 1. DR PANTHER; PTHR43440: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 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}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR611612-51}; KW Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|PIRSR:PIRSR611612-51}; KW Reference proteome {ECO:0000313|Proteomes:UP000002489}. FT ACT_SITE 534 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR611612-52" FT BINDING 348 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51" FT BINDING 350 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51" FT BINDING 431 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="1" FT /note="via carbamate group" FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51" FT BINDING 431 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="2" FT /note="via carbamate group" FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51" FT BINDING 460 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51" FT BINDING 486 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51" FT BINDING 574 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51" FT MOD_RES 431 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|PIRSR:PIRSR611612-50" SQ SEQUENCE 779 AA; 83745 MW; C0930F6874728716 CRC64; MALGATMLGR RHVLPSVCTT LHEIQVEGTF PSGTYLVTVH NPISSDDGDL RRALYGSFLP VPDNSIFPMA ATEDYQLDKQ PGAVVPVKTK KITLNEGRKR IRLQVTSTGD RPIQVGSHYH FIETNPQLEF DRIRAYGYRL DIPAGTSVRF EPGDTKTVTL VEIGGNRVIR GGNNLASGVV DLSRADEILA RLQEAGYAHK PDPAGDMAHI DVFQMDHASY ATMFGPTTGD LVRLGSTDLW IKVERDETVY GDECKFGGGK TLREGMGQAT GRHDADTLDL VVTNALIVDW TGIYKADIGV KEGMIVGIGK AGNPDVMDGV TEGMVVGSCT DVVAGEGKIV TAGAIDTHIH FICPQQVPEA LASGVTTMLG GGTGPSAGTN ATTCTPGAHY MRQMLQACDQ LPINIGITGK GNDSSPEGLR DQVNAGACGL KLHEDWGCTP AAIDACLSVC DEFDIQCLIH TDTLNESGFV ESTIAAFKNR TIHTYHTEGA GGGHAPDIIS VVEHQNVLPS STNPTRPFTR NTLDEHLDML MVCHHLSKNI PEDVAFAESR IRAETIAAED VLHDKGAISM MSSDSQAMGR CGEVVLRTWN TAHKNKVQRG WLPEDEGTGA DNARVKRYVS KYTINPAIAQ GFGHVIGSIE VGKFADLVLW DPAWFGTKPS HVLKGGHIAY AQMGDPNASI PTVQPIIARP MFSPHCASTS ILFVSSASIE TGAIASYGLR SRVEAVKGCR NIGKSDMRHN DLKPKMRVDP ESYTVEADGE VCVAAPAETL PLTQQFYVY //