ID URE3_SPOPA Reviewed; 100 AA. AC P41022; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 27-MAR-2024, entry version 123. DE RecName: Full=Urease subunit gamma {ECO:0000255|HAMAP-Rule:MF_00739}; DE EC=3.5.1.5 {ECO:0000255|HAMAP-Rule:MF_00739}; DE AltName: Full=Urea amidohydrolase subunit gamma {ECO:0000255|HAMAP-Rule:MF_00739}; GN Name=ureA {ECO:0000255|HAMAP-Rule:MF_00739}; OS Sporosarcina pasteurii (Bacillus pasteurii). OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina. OX NCBI_TaxID=1474; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822; RA Moersdorf G., Weinmann P., Kaltwasser H.; RT "Nucleotide sequence of three genes on a urease encoding DNA-fragment from RT Bacillus pasteurii."; RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases. RN [2] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH UREB; UREC AND RP BETA-MERCAPTOETHANOL. RX PubMed=9761912; DOI=10.1107/s0907444997013085; RA Benini S., Ciurli S., Rypniewski W.R., Wilson K.S., Mangani S.; RT "Crystallization and preliminary high-resolution X-ray diffraction analysis RT of native and beta-mercaptoethanol-inhibited urease from Bacillus RT pasteurii."; RL Acta Crystallogr. D 54:409-412(1998). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH UREB; UREC AND RP DIAMIDOPHOSPHATE. RX PubMed=10368287; DOI=10.1016/s0969-2126(99)80026-4; RA Benini S., Rypniewski W.R., Wilson K.S., Miletti S., Ciurli S., Mangani S.; RT "A new proposal for urease mechanism based on the crystal structures of the RT native and inhibited enzyme from Bacillus pasteurii: why urea hydrolysis RT costs two nickels."; RL Structure 7:205-216(1999). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH UREB; UREC AND RP ACETOHYDROXAMIC ACID. RX PubMed=10766443; DOI=10.1007/s007750050014; RA Benini S., Rypniewski W.R., Wilson K.S., Miletti S., Ciurli S., Mangani S.; RT "The complex of Bacillus pasteurii urease with acetohydroxamate anion from RT X-ray data at 1.55 A resolution."; RL J. Biol. Inorg. Chem. 5:110-118(2000). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH UREB; UREC AND RP PHOSPHATE. RX PubMed=11713685; DOI=10.1007/s007750100254; RA Benini S., Rypniewski W.R., Wilson K.S., Ciurli S., Mangani S.; RT "Structure-based rationalization of urease inhibition by phosphate: novel RT insights into the enzyme mechanism."; RL J. Biol. Inorg. Chem. 6:778-790(2001). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH UREB; UREC AND BORATE RP IONS. RX PubMed=15038715; DOI=10.1021/ja049618p; RA Benini S., Rypniewski W.R., Wilson K.S., Mangani S., Ciurli S.; RT "Molecular details of urease inhibition by boric acid: insights into the RT catalytic mechanism."; RL J. Am. Chem. Soc. 126:3714-3715(2004). 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:0000255|HAMAP-Rule:MF_00739}; CC -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from CC urea (urease route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00739}. CC -!- SUBUNIT: Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) CC subunits. Three heterotrimers associate to form the active enzyme. CC {ECO:0000255|HAMAP-Rule:MF_00739, ECO:0000269|PubMed:10368287, CC ECO:0000269|PubMed:10766443, ECO:0000269|PubMed:11713685, CC ECO:0000269|PubMed:15038715, ECO:0000269|PubMed:9761912}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00739}. CC -!- PTM: Although not discussed in the published references, Met-1 is CC represented in the submitted PDB entries as being modified by either a CC formyl, a carboxyl, or an acetyl group. The N-terminal is probably N- CC (dihydroxymethyl)methionine, the hydrated form of N-formylmethionine. CC -!- SIMILARITY: Belongs to the urease gamma subunit family. CC {ECO:0000255|HAMAP-Rule:MF_00739}. 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; X78411; CAA55173.1; -; Genomic_DNA. DR PIR; S47102; S47102. DR PDB; 1IE7; X-ray; 1.85 A; A=1-100. DR PDB; 1S3T; X-ray; 2.10 A; A=1-100. DR PDB; 1UBP; X-ray; 1.65 A; A=1-100. DR PDB; 2UBP; X-ray; 2.00 A; A=1-100. DR PDB; 3UBP; X-ray; 2.00 A; A=1-100. DR PDB; 4AC7; X-ray; 1.50 A; A=1-100. DR PDB; 4CEU; X-ray; 1.58 A; A=1-100. DR PDB; 4CEX; X-ray; 1.59 A; A=1-100. DR PDB; 4UBP; X-ray; 1.55 A; A=1-100. DR PDB; 5A6T; X-ray; 1.65 A; A=1-100. DR PDB; 5FSD; X-ray; 1.75 A; A=1-100. DR PDB; 5FSE; X-ray; 2.07 A; A=1-100. DR PDB; 5G4H; X-ray; 1.50 A; A=1-100. DR PDB; 5OL4; X-ray; 1.28 A; A=1-100. DR PDB; 6H8J; X-ray; 1.45 A; A=1-100. DR PDB; 6QDY; X-ray; 1.42 A; A=1-100. DR PDB; 6RKG; X-ray; 1.32 A; A=1-100. DR PDB; 6RP1; X-ray; 1.49 A; A=1-100. DR PDB; 7B58; X-ray; 1.72 A; AAA=1-100. DR PDB; 7B59; X-ray; 1.63 A; AAA=1-100. DR PDB; 7B5A; X-ray; 1.97 A; AAA=1-100. DR PDB; 7P7N; X-ray; 1.80 A; AAA=1-100. DR PDB; 7P7O; X-ray; 1.87 A; AAA=1-100. DR PDB; 7ZCY; X-ray; 1.54 A; A=1-100. DR PDB; 8A18; X-ray; 1.63 A; AAA=1-100. DR PDB; 8Q2E; X-ray; 1.68 A; A=1-100. DR PDBsum; 1IE7; -. DR PDBsum; 1S3T; -. DR PDBsum; 1UBP; -. DR PDBsum; 2UBP; -. DR PDBsum; 3UBP; -. DR PDBsum; 4AC7; -. DR PDBsum; 4CEU; -. DR PDBsum; 4CEX; -. DR PDBsum; 4UBP; -. DR PDBsum; 5A6T; -. DR PDBsum; 5FSD; -. DR PDBsum; 5FSE; -. DR PDBsum; 5G4H; -. DR PDBsum; 5OL4; -. DR PDBsum; 6H8J; -. DR PDBsum; 6QDY; -. DR PDBsum; 6RKG; -. DR PDBsum; 6RP1; -. DR PDBsum; 7B58; -. DR PDBsum; 7B59; -. DR PDBsum; 7B5A; -. DR PDBsum; 7P7N; -. DR PDBsum; 7P7O; -. DR PDBsum; 7ZCY; -. DR PDBsum; 8A18; -. DR PDBsum; 8Q2E; -. DR AlphaFoldDB; P41022; -. DR SMR; P41022; -. DR BindingDB; P41022; -. DR DrugBank; DB02899; N-Carboxymethionine. DR BRENDA; 3.5.1.5; 682. DR UniPathway; UPA00258; UER00370. DR EvolutionaryTrace; P41022; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro. DR GO; GO:0009039; F:urease activity; IEA:UniProtKB-UniRule. DR GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway. DR CDD; cd00390; Urease_gamma; 1. DR Gene3D; 3.30.280.10; Urease, gamma-like subunit; 1. DR HAMAP; MF_00739; Urease_gamma; 1. DR InterPro; IPR012010; Urease_gamma. DR InterPro; IPR002026; Urease_gamma/gamma-beta_su. DR InterPro; IPR036463; Urease_gamma_sf. DR NCBIfam; TIGR00193; urease_gam; 1. DR PANTHER; PTHR33569; UREASE; 1. DR PANTHER; PTHR33569:SF1; UREASE; 1. DR Pfam; PF00547; Urease_gamma; 1. DR PIRSF; PIRSF001223; Urease_gamma; 1. DR SUPFAM; SSF54111; Urease, gamma-subunit; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Formylation; Hydrolase. FT CHAIN 1..100 FT /note="Urease subunit gamma" FT /id="PRO_0000097991" FT HELIX 5..25 FT /evidence="ECO:0007829|PDB:5OL4" FT HELIX 32..48 FT /evidence="ECO:0007829|PDB:5OL4" FT HELIX 53..59 FT /evidence="ECO:0007829|PDB:5OL4" FT HELIX 60..62 FT /evidence="ECO:0007829|PDB:5OL4" FT HELIX 66..68 FT /evidence="ECO:0007829|PDB:5OL4" FT HELIX 73..76 FT /evidence="ECO:0007829|PDB:5OL4" FT STRAND 78..86 FT /evidence="ECO:0007829|PDB:5OL4" FT STRAND 89..97 FT /evidence="ECO:0007829|PDB:5OL4" SQ SEQUENCE 100 AA; 11146 MW; 773EC3587BF6CA36 CRC64; MHLNPAEKEK LQIFLASELL LRRKARGLKL NYPEAVAIIT SFIMEGARDG KTVAMLMEEG KHVLTRDDVM EGVPEMIDDI QAEATFPDGT KLVTVHNPIS //