ID A0A7H8QHG6_9EURO Unreviewed; 1142 AA. AC A0A7H8QHG6; DT 10-FEB-2021, integrated into UniProtKB/TrEMBL. DT 10-FEB-2021, sequence version 1. DT 13-SEP-2023, entry version 10. 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 ORFNames=TRUGW13939_00493 {ECO:0000313|EMBL:QKX53414.1}; OS Talaromyces rugulosus. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces; OC Talaromyces sect. Islandici. OX NCBI_TaxID=121627 {ECO:0000313|EMBL:QKX53414.1, ECO:0000313|Proteomes:UP000509510}; RN [1] {ECO:0000313|Proteomes:UP000509510} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=W13939 {ECO:0000313|Proteomes:UP000509510}; RA Wang B., Guo L., Ye K., Wang L.; RT "A chromosome-scale genome assembly of Talaromyces rugulosus W13939."; RL Submitted (JUN-2020) 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 -!- 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 EMBL; CP055898; QKX53414.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7H8QHG6; -. DR OrthoDB; 1408002at2759; -. DR UniPathway; UPA00258; UER00370. DR Proteomes; UP000509510; Chromosome i. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-UniRule. DR GO; GO:0035550; C:urease complex; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. 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; 1.10.30.10; High mobility group box domain; 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; IPR009071; HMG_box_dom. DR InterPro; IPR036910; HMG_box_dom_sf. 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 NCBIfam; TIGR00193; urease_gam; 1. DR PANTHER; PTHR43440; UREASE; 1. DR PANTHER; PTHR43440:SF1; UREASE; 1. DR Pfam; PF01979; Amidohydro_1; 1. DR Pfam; PF00505; HMG_box; 1. DR Pfam; PF00449; Urease_alpha; 1. DR Pfam; PF00699; Urease_beta; 1. DR Pfam; PF00547; Urease_gamma; 1. DR PRINTS; PR01752; UREASE. DR SMART; SM00398; HMG; 1. DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1. DR SUPFAM; SSF47095; HMG-box; 1. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1. DR SUPFAM; SSF51278; Urease, beta-subunit; 1. DR SUPFAM; SSF54111; Urease, gamma-subunit; 1. DR PROSITE; PS50118; HMG_BOX_2; 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 DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE- KW ProRule:PRU00700}; 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 Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267}; KW Reference proteome {ECO:0000313|Proteomes:UP000509510}. FT DOMAIN 117..186 FT /note="HMG box" FT /evidence="ECO:0000259|PROSITE:PS50118" FT DOMAIN 706..1142 FT /note="Urease" FT /evidence="ECO:0000259|PROSITE:PS51368" FT DNA_BIND 117..186 FT /note="HMG box" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267" FT REGION 84..120 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 136..156 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 195..311 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 96..114 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 212..226 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 228..242 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 264..291 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 897 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR611612-52, FT ECO:0000256|PROSITE-ProRule:PRU00700" FT BINDING 711 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51" FT BINDING 713 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51" FT BINDING 794 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 794 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 796 FT /ligand="substrate" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00700" FT BINDING 823 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51" FT BINDING 849 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51" FT BINDING 937 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51" FT MOD_RES 794 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|PIRSR:PIRSR611612-50" SQ SEQUENCE 1142 AA; 123037 MW; 128E9861ACAB1FCF CRC64; MSRKDDSKAK DAIVTVNIDD FTRTRDNVIV SLATLQSAVS DLSRAYINHA NTVLNRGPIT VESSLSSGLA GGLATTLLEN GLLGAGLPRH SSPPEATKPE VGDKKKRKRA PPDPNAPKRA LTPYFLYMQH NRSQIASELG PQAKPKEVSD EGTKRWAEMP EEDKAVWKKL YADNLAVYKA KMTAYKAGLP LPDDDNAKAD NQLQQSVAAA EAEAAEDDDS SSSSNEDESS EEPAKEPTPP PSGKRRRVGA KAANNVSTPV SAKKASPEKK KTPAPKKTET KEVKEAKEPA STRKSLGTSA DGKPSKKKRK SDIDKLVISQ LGFLAQRRLA RGVRLNHAEA TALISSNLQE LIRDGNHTVA DLMSIGKTML GRRHVLPSVV SSLVEMQVEG TFPTGTYLVT IHHPISSEDG DLEKALYGSF LPIPPQTAFP DPDPQDYKAE NQPGAVIVVK NTRIALNGGR KRIRLKVMSK GDRPVQVGSH YHFIETNPQL HFDRVKAYGY RLDIAAGTSV RFEPGDTKTV TLVEIGGNKI INGGNSLASG KVDTSRVDEI LLRLQQAGFA HTPEPAGGDL GPINPGSMDR EAYARMFGPT TGDIVRLGAT NLWIKVEKDW TTYGDECTFG GGKVLREGMG QASGRSSKDC LDTVITNALI VDWSGIYKAD IGIKDGIIAG IGKAGNPDVM DGVHPDLLVG SSTDVIAAEN KIVTAGGFDT HIHFICPQQV NEAISSGITT MLGGGTGPST GSNATTCTPG PNHMRQMMQA CDALPVNIGI TGKGNDSGKQ SLREQCLAGA AGLKLHEDWG STPAAIDSCL EVCDEFDVQC LIHTDTLNES GFVEQTIGAF KNRTIHTYHT EGAGGGHAPD IISVVEHSNV LPSSTNPTRP FTLNTLDEHL DMLMVCHHLS KNIPEDVAFA ESRIRAETIA AEDVLHDLGA ISMMSSDSQA MGRCGEVILR TWNTAHKNKL QRGTLSEDEG TGADNFRVKR YISKYTINPA IAQGMSHLIG SVETGKIADL VLWTPDNFGT KPKMVLKSGM IAVAQMGDPN ASIPTVEPII MRPQFGVLVP STSIMFVSEA SISQGIVQTY NLRKRIEPIK NCRNIGKGDM KYNDIMPRMK VDPERYTVEA DGQLCTAEPA TSLPLTQQYF VY //