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 02-SEP-2026, entry version 167. 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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; 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=urea + 2 H2O + H(+) = hydrogencarbonate + 2 NH4(+); CC Xref=Rhea:RHEA:20557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16199, ChEBI:CHEBI:17544, 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01953, ECO:0000269|PubMed:1400317, CC ECO:0000269|PubMed:1624427, 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}. 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; 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 AlphaFoldDB; P18314; -. DR MDRepo; 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-UniRule. DR CDD; cd00375; Urease_alpha; 1. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 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; 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 NCBIfam; NF009685; PRK13206.1; 1. DR NCBIfam; NF009686; PRK13207.1; 1. DR NCBIfam; TIGR01792; urease_alph; 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 PRINTS; PR01752; UREASE. DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 2. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1. DR PROSITE; PS01120; UREASE_1; 1. DR PROSITE; PS00145; UREASE_2; 1. DR PROSITE; PS51368; UREASE_3; 1. 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; -. 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..351 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 //