URE3_KLEAE
ID URE3_KLEAE Reviewed; 100 AA.
AC P18316;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 25-MAY-2022, entry version 131.
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 Klebsiella aerogenes (Enterobacter aerogenes).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=548;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC STRAIN=CG253;
RX PubMed=2211515; DOI=10.1128/jb.172.10.5837-5843.1990;
RA Mulrooney S.B., Hausinger R.P.;
RT "Sequence of the Klebsiella aerogenes urease genes and evidence for
RT accessory proteins facilitating nickel incorporation.";
RL J. Bacteriol. 172:5837-5843(1990).
RN [2]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=1400317; DOI=10.1016/s0021-9258(19)88659-3;
RA Martin P.R., Hausinger R.P.;
RT "Site-directed mutagenesis of the active site cysteine in Klebsiella
RT aerogenes urease.";
RL J. Biol. Chem. 267:20024-20027(1992).
RN [3]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8318888; DOI=10.1002/pro.5560020616;
RA Park I.-S., Hausinger R.P.;
RT "Site-directed mutagenesis of Klebsiella aerogenes urease: identification
RT of histidine residues that appear to function in nickel ligation, substrate
RT binding, and catalysis.";
RL Protein Sci. 2:1034-1041(1993).
RN [4]
RP CATALYTIC ACTIVITY, AND INTERACTION WITH UREB; UREC AND URED.
RX PubMed=7909161; DOI=10.1073/pnas.91.8.3233;
RA Park I.-S., Carr M.B., Hausinger R.P.;
RT "In vitro activation of urease apoprotein and role of UreD as a chaperone
RT required for nickel metallocenter assembly.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:3233-3237(1994).
RN [5]
RP CATALYTIC ACTIVITY, AND INTERACTION WITH UREB; UREC; URED; UREF AND UREG.
RX PubMed=7721685; DOI=10.1128/jb.177.8.1947-1951.1995;
RA Park I.-S., Hausinger R.P.;
RT "Evidence for the presence of urease apoprotein complexes containing UreD,
RT UreF, and UreG in cells that are competent for in vivo enzyme activation.";
RL J. Bacteriol. 177:1947-1951(1995).
RN [6]
RP CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=7855593; DOI=10.1126/science.7855593;
RA Park I.-S., Hausinger R.P.;
RT "Requirement of carbon dioxide for in vitro assembly of the urease nickel
RT metallocenter.";
RL Science 267:1156-1158(1995).
RN [7]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND INTERACTION WITH UREB; UREC;
RP URED AND UREF.
RX PubMed=8808930; DOI=10.1128/jb.178.18.5417-5421.1996;
RA Moncrief M.B.C., Hausinger R.P.;
RT "Purification and activation properties of UreD-UreF-urease apoprotein
RT complexes.";
RL J. Bacteriol. 178:5417-5421(1996).
RN [8]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND INTERACTION WITH UREB; UREC;
RP URED; UREF AND UREG.
RX PubMed=10500143; DOI=10.1073/pnas.96.20.11140;
RA Soriano A., Hausinger R.P.;
RT "GTP-dependent activation of urease apoprotein in complex with the UreD,
RT UreF, and UreG accessory proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:11140-11144(1999).
RN [9]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND ACTIVATION OF THE APOPROTEIN
RP BY UREE.
RX PubMed=11015224; DOI=10.1021/bi001296o;
RA Soriano A., Colpas G.J., Hausinger R.P.;
RT "UreE stimulation of GTP-dependent urease activation in the UreD-UreF-UreG-
RT urease apoprotein complex.";
RL Biochemistry 39:12435-12440(2000).
RN [10]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11594743; DOI=10.1006/abbi.2001.2536;
RA Mulrooney S.B., Zakharian T., Schaller R.A., Hausinger R.P.;
RT "Dual effects of ionic strength on Klebsiella aerogenes urease: pH-
RT dependent activation and inhibition.";
RL Arch. Biochem. Biophys. 394:280-282(2001).
RN [11]
RP INTERACTION WITH UREB; UREC; URED AND UREF, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=14749331; DOI=10.1074/jbc.m312979200;
RA Chang Z., Kuchar J., Hausinger R.P.;
RT "Chemical cross-linking and mass spectrometric identification of sites of
RT interaction for UreD, UreF, and urease.";
RL J. Biol. Chem. 279:15305-15313(2004).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH UREB AND UREC.
RX PubMed=7754395; DOI=10.1126/science.7754395;
RA Jabri E., Carr M.B., Hausinger R.P., Karplus P.A.;
RT "The crystal structure of urease from Klebsiella aerogenes.";
RL Science 268:998-1004(1995).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH UREB AND UREC.
RX PubMed=8718850; DOI=10.1021/bi960424z;
RA Jabri E., Karplus P.A.;
RT "Structures of the Klebsiella aerogenes urease apoenzyme and two active-
RT site mutants.";
RL Biochemistry 35:10616-10626(1996).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH UREB AND UREC.
RX PubMed=8702515; DOI=10.1074/jbc.271.31.18632;
RA Park I.-S., Michel L.O., Pearson M.A., Jabri E., Karplus P.A., Wang S.,
RA Dong J., Scott R.A., Koehler B.P., Johnson M.K., Hausinger R.P.;
RT "Characterization of the mononickel metallocenter in H134A mutant urease.";
RL J. Biol. Chem. 271:18632-18637(1996).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH UREB; UREC AND
RP ACETOHYDROXAMIC ACID.
RX PubMed=9201965; DOI=10.1021/bi970514j;
RA Pearson M.A., Michel L.O., Hausinger R.P., Karplus P.A.;
RT "Structures of Cys319 variants and acetohydroxamate-inhibited Klebsiella
RT aerogenes urease.";
RL Biochemistry 36:8164-8172(1997).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH UREB; UREC AND
RP FORMATE.
RX PubMed=9558361; DOI=10.1021/bi980021u;
RA Pearson M.A., Schaller R.A., Michel L.O., Karplus P.A., Hausinger R.P.;
RT "Chemical rescue of Klebsiella aerogenes urease variants lacking the
RT carbamylated-lysine nickel ligand.";
RL Biochemistry 37:6214-6220(1998).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH UREB AND UREC.
RX PubMed=10555581; DOI=10.1007/s007750050333;
RA Yamaguchi K., Cosper N.J., Staalhandske C., Scott R.A., Pearson M.A.,
RA Karplus P.A., Hausinger R.P.;
RT "Characterization of metal-substituted Klebsiella aerogenes urease.";
RL J. Biol. Inorg. Chem. 4:468-477(1999).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH UREB AND UREC, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10913264; DOI=10.1021/bi000613o;
RA Pearson M.A., Park I.-S., Schaller R.A., Michel L.O., Karplus P.A.,
RA Hausinger R.P.;
RT "Kinetic and structural characterization of urease active site variants.";
RL Biochemistry 39:8575-8584(2000).
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 ECO:0000269|PubMed:10500143, ECO:0000269|PubMed:11015224,
CC ECO:0000269|PubMed:1400317, ECO:0000269|PubMed:2211515,
CC ECO:0000269|PubMed:7721685, ECO:0000269|PubMed:7855593,
CC ECO:0000269|PubMed:7909161, ECO:0000269|PubMed:8318888,
CC ECO:0000269|PubMed:8808930};
CC -!- ACTIVITY REGULATION: The apoenzyme can be activated in vitro in the
CC presence of nickel ions and carbon dioxide, which promotes
CC carbamylation of 'Lys-217' of the UreC (alpha) subunit.
CC {ECO:0000269|PubMed:10500143, ECO:0000269|PubMed:11015224,
CC ECO:0000269|PubMed:7855593, ECO:0000269|PubMed:8808930}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.3 mM for urea {ECO:0000269|PubMed:10913264,
CC ECO:0000269|PubMed:11594743, ECO:0000269|PubMed:1400317,
CC ECO:0000269|PubMed:8318888};
CC Vmax=1.9 mmol/min/mg enzyme {ECO:0000269|PubMed:10913264,
CC ECO:0000269|PubMed:11594743, ECO:0000269|PubMed:1400317,
CC ECO:0000269|PubMed:8318888};
CC pH dependence:
CC Optimum pH is 7.75. {ECO:0000269|PubMed:10913264,
CC ECO:0000269|PubMed:11594743, ECO:0000269|PubMed:1400317,
CC ECO:0000269|PubMed:8318888};
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. The
CC apoenzyme interacts with an accessory complex composed of UreD, UreF
CC and UreG, which is required for the assembly of the nickel containing
CC metallocenter of UreC. The UreE protein may also play a direct role as
CC a metallochaperone in nickel transfer to the urease apoprotein.
CC {ECO:0000255|HAMAP-Rule:MF_00739, ECO:0000269|PubMed:10500143,
CC ECO:0000269|PubMed:10555581, ECO:0000269|PubMed:10913264,
CC ECO:0000269|PubMed:14749331, ECO:0000269|PubMed:7721685,
CC ECO:0000269|PubMed:7754395, ECO:0000269|PubMed:7909161,
CC ECO:0000269|PubMed:8702515, ECO:0000269|PubMed:8718850,
CC ECO:0000269|PubMed:8808930, ECO:0000269|PubMed:9201965,
CC ECO:0000269|PubMed:9558361}.
CC -!- INTERACTION:
CC P18316; P18314: ureC; NbExp=11; IntAct=EBI-1028581, EBI-1028571;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00739}.
CC -!- SIMILARITY: Belongs to the urease gamma subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_00739}.
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DR EMBL; M36068; AAA25149.1; -; Genomic_DNA.
DR PIR; A36138; A36138.
DR RefSeq; WP_002916871.1; NZ_LR134254.1.
DR PDB; 1A5K; X-ray; 2.20 A; A=1-100.
DR PDB; 1A5L; X-ray; 2.20 A; A=1-100.
DR PDB; 1A5M; X-ray; 2.00 A; A=1-100.
DR PDB; 1A5N; X-ray; 2.40 A; A=1-100.
DR PDB; 1A5O; X-ray; 2.50 A; A=1-100.
DR PDB; 1EF2; X-ray; 2.50 A; C=1-100.
DR PDB; 1EJR; X-ray; 2.00 A; A=1-100.
DR PDB; 1EJS; X-ray; 2.00 A; A=1-100.
DR PDB; 1EJT; X-ray; 2.00 A; A=1-100.
DR PDB; 1EJU; X-ray; 2.00 A; A=1-100.
DR PDB; 1EJV; X-ray; 2.40 A; A=1-100.
DR PDB; 1EJW; X-ray; 1.90 A; A=1-100.
DR PDB; 1EJX; X-ray; 1.60 A; A=1-100.
DR PDB; 1FWA; X-ray; 2.00 A; A=1-100.
DR PDB; 1FWB; X-ray; 2.00 A; A=1-100.
DR PDB; 1FWC; X-ray; 2.00 A; A=1-100.
DR PDB; 1FWD; X-ray; 2.00 A; A=1-100.
DR PDB; 1FWE; X-ray; 2.00 A; A=1-100.
DR PDB; 1FWF; X-ray; 2.00 A; A=1-100.
DR PDB; 1FWG; X-ray; 2.00 A; A=1-100.
DR PDB; 1FWH; X-ray; 2.00 A; A=1-100.
DR PDB; 1FWI; X-ray; 2.00 A; A=1-100.
DR PDB; 1FWJ; X-ray; 2.20 A; A=1-100.
DR PDB; 1KRA; X-ray; 2.30 A; A=1-100.
DR PDB; 1KRB; X-ray; 2.50 A; A=1-100.
DR PDB; 1KRC; X-ray; 2.50 A; A=1-100.
DR PDB; 2KAU; X-ray; 2.00 A; A=1-100.
DR PDB; 4EP8; X-ray; 1.55 A; A=1-100.
DR PDB; 4EPB; X-ray; 1.75 A; A=1-100.
DR PDB; 4EPD; X-ray; 1.70 A; A=1-100.
DR PDB; 4EPE; X-ray; 2.05 A; A=1-100.
DR PDBsum; 1A5K; -.
DR PDBsum; 1A5L; -.
DR PDBsum; 1A5M; -.
DR PDBsum; 1A5N; -.
DR PDBsum; 1A5O; -.
DR PDBsum; 1EF2; -.
DR PDBsum; 1EJR; -.
DR PDBsum; 1EJS; -.
DR PDBsum; 1EJT; -.
DR PDBsum; 1EJU; -.
DR PDBsum; 1EJV; -.
DR PDBsum; 1EJW; -.
DR PDBsum; 1EJX; -.
DR PDBsum; 1FWA; -.
DR PDBsum; 1FWB; -.
DR PDBsum; 1FWC; -.
DR PDBsum; 1FWD; -.
DR PDBsum; 1FWE; -.
DR PDBsum; 1FWF; -.
DR PDBsum; 1FWG; -.
DR PDBsum; 1FWH; -.
DR PDBsum; 1FWI; -.
DR PDBsum; 1FWJ; -.
DR PDBsum; 1KRA; -.
DR PDBsum; 1KRB; -.
DR PDBsum; 1KRC; -.
DR PDBsum; 2KAU; -.
DR PDBsum; 4EP8; -.
DR PDBsum; 4EPB; -.
DR PDBsum; 4EPD; -.
DR PDBsum; 4EPE; -.
DR AlphaFoldDB; P18316; -.
DR SMR; P18316; -.
DR IntAct; P18316; 2.
DR GeneID; 61334821; -.
DR GeneID; 64293496; -.
DR BRENDA; 3.5.1.5; 152.
DR SABIO-RK; P18316; -.
DR UniPathway; UPA00258; UER00370.
DR EvolutionaryTrace; P18316; -.
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; -; 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 Pfam; PF00547; Urease_gamma; 1.
DR PIRSF; PIRSF001223; Urease_gamma; 1.
DR SUPFAM; SSF54111; SSF54111; 1.
DR TIGRFAMs; TIGR00193; urease_gam; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase.
FT CHAIN 1..100
FT /note="Urease subunit gamma"
FT /id="PRO_0000098015"
FT HELIX 5..25
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 32..49
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 53..59
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 78..86
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 89..97
FT /evidence="ECO:0007829|PDB:4EP8"
SQ SEQUENCE 100 AA; 11087 MW; C5B9E7FAF615C04D CRC64;
MELTPREKDK LLLFTAALVA ERRLARGLKL NYPESVALIS AFIMEGARDG KSVASLMEEG
RHVLTREQVM EGVPEMIPDI QVEATFPDGS KLVTVHNPII
