URE1_KLEAE
ID URE1_KLEAE Reviewed; 567 AA.
AC P18314;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Urease subunit alpha {ECO:0000255|HAMAP-Rule:MF_01953};
DE EC=3.5.1.5 {ECO:0000255|HAMAP-Rule:MF_01953};
DE AltName: Full=Urea amidohydrolase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01953};
GN Name=ureC {ECO:0000255|HAMAP-Rule:MF_01953};
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 COFACTOR.
RX PubMed=1624427; DOI=10.1128/jb.174.13.4324-4330.1992;
RA Lee M.H., Mulrooney S.B., Renner M.J., Markowicz Y., Hausinger R.P.;
RT "Klebsiella aerogenes urease gene cluster: sequence of ureD and
RT demonstration that four accessory genes (ureD, ureE, ureF, and ureG) are
RT involved in nickel metallocenter biosynthesis.";
RL J. Bacteriol. 174:4324-4330(1992).
RN [3]
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF CYS-319.
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 [4]
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF HIS-134; HIS-136; HIS-219; HIS-246; HIS-320 AND HIS-320.
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 [5]
RP CATALYTIC ACTIVITY, AND INTERACTION WITH UREA; UREB 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 [6]
RP CATALYTIC ACTIVITY, AND INTERACTION WITH UREA; UREB; 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 [7]
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 [8]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND INTERACTION WITH UREA; UREB;
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 [9]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND INTERACTION WITH UREA; UREB;
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 [10]
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 [11]
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 [12]
RP INTERACTION WITH UREA; UREB; 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 [13]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH UREA; UREB AND NICKEL
RP IONS, AND CARBOXYLATION AT LYS-217.
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 [14]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF WILD-TYPE AND MUTANTS ALA-219 AND
RP ALA-320 IN COMPLEX WITH UREA; UREB AND NICKEL IONS, AND CARBOXYLATION AT
RP LYS-217.
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 [15]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT ALA-134 IN COMPLEX WITH
RP UREA; UREB AND NICKEL IONS, MAGNETIC CIRCULAR DICHROISM, ABSORPTION
RP SPECTROSCOPY, AND CARBOXYLATION AT LYS-217.
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 [16]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS ALA/ASP/SER/TYR-319 IN
RP COMPLEX WITH UREA; UREB; NICKEL IONS AND 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 [17]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS ALA/CYS/GLU-217 IN COMPLEX
RP WITH UREA; UREB AND FORMATE, AND MUTAGENESIS OF LYS-217.
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 [18]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH UREA; UREB AND
RP MANGANESE IONS, ABSORPTION SPECTROSCOPY, AND MUTAGENESIS OF CYS-319.
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 [19]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF WILD-TYPE AND MUTANTS ASN/GLN-219;
RP ALA-221 AND ASN/GLN-320 IN COMPLEX WITH UREA; UREB AND NICKEL IONS,
RP CARBOXYLATION AT LYS-217, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP HIS-219; ASP-221; HIS-320 AND ARG-336.
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_01953,
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 -!- COFACTOR:
CC Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01953,
CC ECO:0000269|PubMed:1400317, ECO:0000269|PubMed:1624427,
CC ECO:0000269|PubMed:8318888};
CC Note=Binds 2 nickel ions per subunit. {ECO:0000255|HAMAP-Rule:MF_01953,
CC ECO:0000269|PubMed:1400317, ECO:0000269|PubMed:1624427,
CC ECO:0000269|PubMed:8318888};
CC -!- ACTIVITY REGULATION: The apoenzyme can be activated in vitro in the
CC presence of nickel ions and carbon dioxide, which promotes
CC carboxylation of Lys-217. {ECO:0000269|PubMed:10500143,
CC ECO:0000269|PubMed:11015224, ECO:0000269|PubMed:7855593,
CC 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_01953}.
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_01953, 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 P18314; P18316: ureA; NbExp=11; IntAct=EBI-1028571, EBI-1028581;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01953}.
CC -!- PTM: Carboxylation allows a single lysine to coordinate two nickel
CC ions. {ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10913264,
CC ECO:0000269|PubMed:7754395, ECO:0000269|PubMed:8702515,
CC ECO:0000269|PubMed:8718850}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Urease alpha subunit family. {ECO:0000255|HAMAP-Rule:MF_01953}.
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DR EMBL; M36068; AAA25151.1; -; Genomic_DNA.
DR PDB; 1A5K; X-ray; 2.20 A; C=2-567.
DR PDB; 1A5L; X-ray; 2.20 A; C=2-567.
DR PDB; 1A5M; X-ray; 2.00 A; C=2-567.
DR PDB; 1A5N; X-ray; 2.40 A; C=2-567.
DR PDB; 1A5O; X-ray; 2.50 A; C=2-567.
DR PDB; 1EF2; X-ray; 2.50 A; A=2-567.
DR PDB; 1EJR; X-ray; 2.00 A; C=1-567.
DR PDB; 1EJS; X-ray; 2.00 A; C=1-567.
DR PDB; 1EJT; X-ray; 2.00 A; C=1-567.
DR PDB; 1EJU; X-ray; 2.00 A; C=1-567.
DR PDB; 1EJV; X-ray; 2.40 A; C=1-567.
DR PDB; 1EJW; X-ray; 1.90 A; C=1-567.
DR PDB; 1EJX; X-ray; 1.60 A; C=1-567.
DR PDB; 1FWA; X-ray; 2.00 A; C=1-567.
DR PDB; 1FWB; X-ray; 2.00 A; C=1-567.
DR PDB; 1FWC; X-ray; 2.00 A; C=1-567.
DR PDB; 1FWD; X-ray; 2.00 A; C=1-567.
DR PDB; 1FWE; X-ray; 2.00 A; C=1-567.
DR PDB; 1FWF; X-ray; 2.00 A; C=1-567.
DR PDB; 1FWG; X-ray; 2.00 A; C=1-567.
DR PDB; 1FWH; X-ray; 2.00 A; C=1-567.
DR PDB; 1FWI; X-ray; 2.00 A; C=1-567.
DR PDB; 1FWJ; X-ray; 2.20 A; C=1-567.
DR PDB; 1KRA; X-ray; 2.30 A; C=1-567.
DR PDB; 1KRB; X-ray; 2.50 A; C=1-567.
DR PDB; 1KRC; X-ray; 2.50 A; C=1-567.
DR PDB; 2KAU; X-ray; 2.00 A; C=1-567.
DR PDB; 4EP8; X-ray; 1.55 A; C=2-567.
DR PDB; 4EPB; X-ray; 1.75 A; C=2-567.
DR PDB; 4EPD; X-ray; 1.70 A; C=2-567.
DR PDB; 4EPE; X-ray; 2.05 A; C=2-567.
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; P18314; -.
DR SMR; P18314; -.
DR IntAct; P18314; 3.
DR DrugBank; DB00551; Acetohydroxamic acid.
DR DrugBank; DB05265; Ecabet.
DR MEROPS; M38.982; -.
DR BRENDA; 3.5.1.5; 152.
DR SABIO-RK; P18314; -.
DR UniPathway; UPA00258; UER00370.
DR EvolutionaryTrace; P18314; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009039; F:urease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00375; Urease_alpha; 1.
DR Gene3D; 2.30.40.10; -; 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; IPR011612; Urease_alpha_N_dom.
DR InterPro; IPR017950; Urease_AS.
DR InterPro; IPR005848; Urease_asu.
DR InterPro; IPR017951; Urease_asu_c.
DR InterPro; IPR029754; Urease_Ni-bd.
DR Pfam; PF01979; Amidohydro_1; 1.
DR Pfam; PF00449; Urease_alpha; 1.
DR PRINTS; PR01752; UREASE.
DR SUPFAM; SSF51338; SSF51338; 2.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01792; urease_alph; 1.
DR PROSITE; PS01120; UREASE_1; 1.
DR PROSITE; PS00145; UREASE_2; 1.
DR PROSITE; PS51368; UREASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Metal-binding; Nickel.
FT CHAIN 1..567
FT /note="Urease subunit alpha"
FT /id="PRO_0000067543"
FT DOMAIN 129..567
FT /note="Urease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT ACT_SITE 320
FT /note="Proton donor"
FT BINDING 134
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT BINDING 136
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT BINDING 217
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /note="via carbamate group"
FT BINDING 217
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /note="via carbamate group"
FT BINDING 219
FT /ligand="substrate"
FT BINDING 246
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT BINDING 272
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT BINDING 360
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT MOD_RES 217
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953,
FT ECO:0000269|PubMed:10913264, ECO:0000269|PubMed:7754395,
FT ECO:0000269|PubMed:8702515, ECO:0000269|PubMed:8718850"
FT MUTAGEN 134
FT /note="H->A: Abrogates activity and reduces binding to
FT nickel ions."
FT /evidence="ECO:0000269|PubMed:8318888"
FT MUTAGEN 136
FT /note="H->A: Abrogates activity and reduces binding to
FT nickel ions."
FT /evidence="ECO:0000269|PubMed:8318888"
FT MUTAGEN 217
FT /note="K->A,C,E: Reduces activity 8000-fold and abrogates
FT binding to nickel ions."
FT /evidence="ECO:0000269|PubMed:9558361"
FT MUTAGEN 219
FT /note="H->A: Reduces activity 500-fold and increases KM
FT 1000-fold. Resistant to inactivation by
FT diethylpyrocarbonate and iodoacetamide."
FT /evidence="ECO:0000269|PubMed:10913264,
FT ECO:0000269|PubMed:8318888"
FT MUTAGEN 219
FT /note="H->N,Q: Increases KM 100-fold; optimum pH is 6."
FT /evidence="ECO:0000269|PubMed:10913264,
FT ECO:0000269|PubMed:8318888"
FT MUTAGEN 221
FT /note="D->A: Reduces activity 1000-fold and increases KM
FT 10-fold."
FT /evidence="ECO:0000269|PubMed:10913264"
FT MUTAGEN 221
FT /note="D->N: Reduces activity 50-fold."
FT /evidence="ECO:0000269|PubMed:10913264"
FT MUTAGEN 246
FT /note="H->A: Abrogates activity and reduces binding to
FT nickel ions."
FT /evidence="ECO:0000269|PubMed:8318888"
FT MUTAGEN 312
FT /note="H->A: Enhances thermal stability above 50 degrees
FT Celsius."
FT MUTAGEN 319
FT /note="C->A: Reduces activity 2-fold, but increases KM only
FT 1.7-fold; optimum pH is 6.7. Reduces binding of nickel
FT ions. Resistant to inactivation by iodoacetamide."
FT /evidence="ECO:0000269|PubMed:10555581,
FT ECO:0000269|PubMed:1400317"
FT MUTAGEN 319
FT /note="C->D: Reduces activity 20-fold, but increases KM
FT only 1.9-fold; optimum pH is 5.2. Reduces binding of nickel
FT ions. Resistant to inactivation by iodoacetamide."
FT /evidence="ECO:0000269|PubMed:10555581,
FT ECO:0000269|PubMed:1400317"
FT MUTAGEN 319
FT /note="C->S: Reduces activity 3000-fold, but increases KM
FT only 3.9-fold; optimum pH is 5.2. Reduces binding of nickel
FT ions. Resistant to inactivation by iodoacetamide."
FT /evidence="ECO:0000269|PubMed:10555581,
FT ECO:0000269|PubMed:1400317"
FT MUTAGEN 319
FT /note="C->Y: Abrogates activity."
FT /evidence="ECO:0000269|PubMed:10555581,
FT ECO:0000269|PubMed:1400317"
FT MUTAGEN 320
FT /note="H->A: Reduces activity 100000-fold, but increases KM
FT only 3-fold; optimum pH is 6.75. Resistant to inactivation
FT by diethylpyrocarbonate and iodoacetamide."
FT /evidence="ECO:0000269|PubMed:10913264,
FT ECO:0000269|PubMed:8318888"
FT MUTAGEN 320
FT /note="H->N,Q: Reduces activity 100000-fold, but increases
FT KM only 3-fold."
FT /evidence="ECO:0000269|PubMed:10913264,
FT ECO:0000269|PubMed:8318888"
FT MUTAGEN 336
FT /note="R->Q: Reduces activity 10000-fold, but has no effect
FT on KM."
FT /evidence="ECO:0000269|PubMed:10913264"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 6..13
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:4EP8"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 67..77
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 80..89
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:4EP8"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:4EPD"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:4EPB"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 142..149
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 173..184
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 187..196
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 202..211
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 226..239
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 256..263
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:4EP8"
FT TURN 271..274
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:4EP8"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 284..289
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 293..297
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:4EPB"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:1KRA"
FT HELIX 308..320
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:1EJW"
FT HELIX 327..336
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 339..350
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:1EJX"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 370..385
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 397..404
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 409..414
FT /evidence="ECO:0007829|PDB:4EP8"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 432..435
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 437..439
FT /evidence="ECO:0007829|PDB:4EP8"
FT TURN 440..442
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 445..449
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 452..458
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 463..466
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 472..475
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 481..487
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 489..492
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 494..498
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 501..504
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 509..513
FT /evidence="ECO:0007829|PDB:4EP8"
FT TURN 517..519
FT /evidence="ECO:0007829|PDB:4EP8"
FT HELIX 522..524
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:4EP8"
FT TURN 538..540
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 548..550
FT /evidence="ECO:0007829|PDB:1FWI"
FT STRAND 555..557
FT /evidence="ECO:0007829|PDB:4EP8"
FT STRAND 559..561
FT /evidence="ECO:0007829|PDB:4EP8"
FT TURN 562..564
FT /evidence="ECO:0007829|PDB:4EP8"
SQ SEQUENCE 567 AA; 60305 MW; 2ECF3C4268A2E2C7 CRC64;
MSNISRQAYA DMFGPTVGDK VRLADTELWI EVEDDLTTYG EEVKFGGGKV IRDGMGQGQM
LAADCVDLVL TNALIVDHWG IVKADIGVKD GRIFAIGKAG NPDIQPNVTI PIGAATEVIA
AEGKIVTAGG IDTHIHWICP QQAEEALVSG VTTMVGGGTG PAAGTHATTC TPGPWYISRM
LQAADSLPVN IGLLGKGNVS QPDALREQVA AGVIGLKIHE DWGATPAAID CALTVADEMD
IQVALHSDTL NESGFVEDTL AAIGGRTIHT FHTEGAGGGH APDIITACAH PNILPSSTNP
TLPYTLNTID EHLDMLMVCH HLDPDIAEDV AFAESRIRRE TIAAEDVLHD LGAFSLTSSD
SQAMGRVGEV ILRTWQVAHR MKVQRGALAE ETGDNDNFRV KRYIAKYTIN PALTHGIAHE
VGSIEVGKLA DLVVWSPAFF GVKPATVIKG GMIAIAPMGD INASIPTPQP VHYRPMFGAL
GSARHHCRLT FLSQAAAANG VAERLNLRSA IAVVKGCRTV QKADMVHNSL QPNITVDAQT
YEVRVDGELI TSEPADVLPM AQRYFLF
