ARSC_STAAU
ID ARSC_STAAU Reviewed; 131 AA.
AC P0A006; P30330; Q6Y0M0; Q6Y0M4; Q6Y0N2; Q8GQH3;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Arsenate reductase {ECO:0000255|HAMAP-Rule:MF_01624, ECO:0000303|PubMed:1409657};
DE EC=1.20.4.4 {ECO:0000269|PubMed:10606519, ECO:0000269|PubMed:11862551, ECO:0000269|PubMed:12072565, ECO:0000269|PubMed:12682056, ECO:0000269|PubMed:1409657, ECO:0000269|PubMed:16797027, ECO:0000269|PubMed:8003493};
DE AltName: Full=Arsenical pump modifier;
DE AltName: Full=Protein ArsC;
GN Name=arsC {ECO:0000255|HAMAP-Rule:MF_01624, ECO:0000303|PubMed:1534328};
OS Staphylococcus aureus.
OG Plasmid pI258.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND DISRUPTION PHENOTYPE.
RC PLASMID=pI258;
RX PubMed=1534328; DOI=10.1128/jb.174.11.3684-3694.1992;
RA Ji G., Silver S.;
RT "Regulation and expression of the arsenic resistance operon from
RT Staphylococcus aureus plasmid pI258.";
RL J. Bacteriol. 174:3684-3694(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SW1, SW18, SW24, and SW4;
RA Tibor L., Cramton S.E., Goetz F., Hunt T.K.;
RT "Characterization of a collection of clinical Staphylococcus aureus wound
RT isolates.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC PLASMID=pI258;
RX PubMed=1409657; DOI=10.1073/pnas.89.20.9474;
RA Ji G., Silver S.;
RT "Reduction of arsenate to arsenite by the ArsC protein of the arsenic
RT resistance operon of Staphylococcus aureus plasmid pI258.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:9474-9478(1992).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MASS
RP SPECTROMETRY.
RC PLASMID=pI258;
RX PubMed=8003493; DOI=10.1021/bi00189a034;
RA Ji G., Garber E.A.E., Armes L.G., Chen C.-M., Fuchs J.A., Silver S.;
RT "Arsenate reductase of Staphylococcus aureus plasmid pI258.";
RL Biochemistry 33:7294-7299(1994).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MASS
RP SPECTROMETRY, MUTAGENESIS OF CYS-10; CYS-15; CYS-82 AND CYS-89, AND
RP REACTION MECHANISM.
RC PLASMID=pI258;
RX PubMed=10606519; DOI=10.1021/bi9911841;
RA Messens J., Hayburn G., Desmyter A., Laus G., Wyns L.;
RT "The essential catalytic redox couple in arsenate reductase from
RT Staphylococcus aureus.";
RL Biochemistry 38:16857-16865(1999).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND STRUCTURE BY NMR.
RC PLASMID=pI258;
RX PubMed=11862551; DOI=10.1007/s007750100282;
RA Messens J., Martins J.C., Brosens E., Van Belle K., Jacobs D.M., Willem R.,
RA Wyns L.;
RT "Kinetics and active site dynamics of Staphylococcus aureus arsenate
RT reductase.";
RL J. Biol. Inorg. Chem. 7:146-156(2002).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, METAL-BINDING, AND MUTAGENESIS OF ASN-13; GLU-21; SER-36 AND
RP ASP-65.
RX PubMed=12682056; DOI=10.1074/jbc.m303194200;
RA Lah N., Lah J., Zegers I., Wyns L., Messens J.;
RT "Specific potassium binding stabilizes pI258 arsenate reductase from
RT Staphylococcus aureus.";
RL J. Biol. Chem. 278:24673-24679(2003).
RN [8] {ECO:0007744|PDB:1JF8, ECO:0007744|PDB:1JFV}
RP X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS) OF REDUCED AND OXIDIZED FORM OF
RP DOUBLE MUTANT SER-10/ALA-15 IN COMPLEX WITH POTASSIUM, FUNCTION AS A
RP PHOSPHATASE, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-10; CYS-15
RP AND CYS-89, ACTIVE SITE, AND REACTION MECHANISM.
RC PLASMID=pI258;
RX PubMed=11573087; DOI=10.1038/nsb1001-843;
RA Zegers I., Martins J.C., Willem R., Wyns L., Messens J.;
RT "Arsenate reductase from S. aureus plasmid pI258 is a phosphatase drafted
RT for redox duty.";
RL Nat. Struct. Biol. 8:843-847(2001).
RN [9] {ECO:0007744|PDB:1LJL, ECO:0007744|PDB:1LJU, ECO:0007744|PDB:1LK0}
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF WILD-TYPE AND OF MUTANTS ALA-15
RP AND LEU-89 IN COMPLEXES WITH POTASSIUM, FUNCTION, CATALYTIC ACTIVITY,
RP MUTAGENESIS OF ARG-16; SER-17; CYS-89 AND ASP-105, STRUCTURE BY NMR OF
RP MUTANTS CYS-82 AND CYS-89, ACTIVE SITE, AND REACTION MECHANISM.
RC PLASMID=pI258;
RX PubMed=12072565; DOI=10.1073/pnas.132142799;
RA Messens J., Martins J.C., Van Belle K., Brosens E., Desmyter A.,
RA De Gieter M., Wieruszeski J.-M., Willem R., Wyns L., Zegers I.;
RT "All intermediates of the arsenate reductase mechanism, including an
RT intramolecular dynamic disulfide cascade.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:8506-8511(2002).
RN [10] {ECO:0007744|PDB:1RXE, ECO:0007744|PDB:1RXI}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF TRIPLE MUTANT
RP SER-10/ALA-15/SER-82 IN COMPLEX WITH 5-THIO-2-NITROBENZOIC ACID AND
RP POTASSIUM.
RX PubMed=15159594; DOI=10.1107/s0907444904007334;
RA Messens J., Van Molle I., Vanhaesebrouck P., Van Belle K., Wahni K.,
RA Martins J.C., Wyns L., Loris R.;
RT "The structure of a triple mutant of pI258 arsenate reductase from
RT Staphylococcus aureus and its 5-thio-2-nitrobenzoic acid adduct.";
RL Acta Crystallogr. D 60:1180-1184(2004).
RN [11] {ECO:0007744|PDB:2CD7, ECO:0007744|PDB:2FXI}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF MUTANT GLN-62 IN COMPLEX WITH
RP SODIUM AND OF DOUBLE MUTANT SER-10/ALA-15 IN COMPLEX WITH POTASSIUM,
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF HIS-62.
RX PubMed=16797027; DOI=10.1016/j.jmb.2006.05.054;
RA Roos G., Buts L., Van Belle K., Brosens E., Geerlings P., Loris R.,
RA Wyns L., Messens J.;
RT "Interplay between ion binding and catalysis in the thioredoxin-coupled
RT arsenate reductase family.";
RL J. Mol. Biol. 360:826-838(2006).
CC -!- FUNCTION: Catalyzes the reduction of arsenate [As(V)] to arsenite
CC [As(III)] (PubMed:1409657, PubMed:8003493, PubMed:10606519,
CC PubMed:11862551, PubMed:12072565, PubMed:12682056, PubMed:16797027). In
CC vitro, has also low phosphatase activity with para-nitrophenyl
CC phosphate (pNPP) as substrate (PubMed:11573087).
CC {ECO:0000269|PubMed:10606519, ECO:0000269|PubMed:11573087,
CC ECO:0000269|PubMed:11862551, ECO:0000269|PubMed:12072565,
CC ECO:0000269|PubMed:12682056, ECO:0000269|PubMed:1409657,
CC ECO:0000269|PubMed:16797027, ECO:0000269|PubMed:8003493}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + arsenate + H(+) = [thioredoxin]-
CC disulfide + arsenite + H2O; Xref=Rhea:RHEA:43848, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29242, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:48597, ChEBI:CHEBI:50058; EC=1.20.4.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01624,
CC ECO:0000269|PubMed:10606519, ECO:0000269|PubMed:11862551,
CC ECO:0000269|PubMed:12072565, ECO:0000269|PubMed:12682056,
CC ECO:0000269|PubMed:1409657, ECO:0000269|PubMed:16797027,
CC ECO:0000269|PubMed:8003493};
CC -!- ACTIVITY REGULATION: Potassium binding stabilizes the enzyme and
CC increases its specific activity (PubMed:12682056, PubMed:16797027).
CC Activity is also stimulated by sulfate (PubMed:16797027). Inhibited by
CC arsenite (mixed inhibitor) (PubMed:11862551).
CC {ECO:0000269|PubMed:11862551, ECO:0000269|PubMed:12682056,
CC ECO:0000269|PubMed:16797027}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.8 uM for arsenate (below 1 mM arsenate)
CC {ECO:0000269|PubMed:8003493};
CC KM=2 mM for arsenate (above 1 mM arsenate)
CC {ECO:0000269|PubMed:8003493};
CC KM=0.066 uM for arsenate {ECO:0000269|PubMed:10606519};
CC KM=68 uM for arsenate {ECO:0000269|PubMed:11862551};
CC KM=9 uM for arsenate (in the presence of KCl)
CC {ECO:0000269|PubMed:12682056, ECO:0000269|PubMed:16797027};
CC KM=22 uM for arsenate (in the presence of NaCl)
CC {ECO:0000269|PubMed:12682056, ECO:0000269|PubMed:16797027};
CC KM=61 uM for arsenate (in the presence of Na(2)SO(4))
CC {ECO:0000269|PubMed:16797027};
CC KM=81 uM for arsenate (in the presence of K(2)SO(4))
CC {ECO:0000269|PubMed:16797027};
CC KM=146 mM for para-nitrophenyl phosphate (reduced form only)
CC {ECO:0000269|PubMed:11573087};
CC Vmax=200 nmol/min/mg enzyme (below 1 mM arsenate)
CC {ECO:0000269|PubMed:8003493};
CC Vmax=450 nmol/min/mg enzyme (above 1 mM arsenate)
CC {ECO:0000269|PubMed:8003493};
CC Note=kcat is 4.5 min(-1) with arsenate as substrate (at 2 uM
CC arsenate) and kcat is 9.9 min(-1) with arsenate as substrate (at 10
CC mM arsenate) (PubMed:10606519). kcat is 54 min(-1) in the presence of
CC KCl (PubMed:12682056, PubMed:16797027). kcat is 35 min(-1) in the
CC presence of NaCl (PubMed:12682056, PubMed:16797027). kcat is 172
CC min(-1) in the presence of Na(2)SO(4) (PubMed:16797027). kcat is 219
CC min(-1) in the presence of K(2)SO(4) (PubMed:16797027). kcat is 0.53
CC min(-1) for the phosphatase activity with para-nitrophenyl phosphate
CC as substrate (PubMed:11573087). {ECO:0000269|PubMed:10606519,
CC ECO:0000269|PubMed:11573087, ECO:0000269|PubMed:12682056,
CC ECO:0000269|PubMed:16797027};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:11862551};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01624,
CC ECO:0000269|PubMed:1409657}.
CC -!- INDUCTION: Induced by arsenate [As(V)], arsenite [As(III)], and
CC antimonite [Sb(III)]. {ECO:0000269|PubMed:1534328}.
CC -!- PTM: Cys-89 performs a nucleophilic attack on a Cys-10-Cys-82
CC intermediate, forming another disulfide intermediate with Cys-82.
CC {ECO:0000305|PubMed:11573087, ECO:0000305|PubMed:12072565}.
CC -!- MASS SPECTROMETRY: Mass=14810.5; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8003493};
CC -!- MASS SPECTROMETRY: Mass=14812; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10606519};
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene leads to a complete loss of
CC arsenate resistance, but does not affect arsenite or antimony
CC resistance. {ECO:0000269|PubMed:1534328}.
CC -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein
CC phosphatase family. Thioredoxin-coupled ArsC subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01624, ECO:0000305}.
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DR EMBL; M86824; AAA25638.1; -; Genomic_DNA.
DR EMBL; AY194061; AAP32334.1; -; Genomic_DNA.
DR EMBL; AY194062; AAP32338.1; -; Genomic_DNA.
DR EMBL; AY194064; AAP32346.1; -; Genomic_DNA.
DR EMBL; AY194065; AAP32350.1; -; Genomic_DNA.
DR PIR; A53641; A53641.
DR PIR; D41903; D41903.
DR RefSeq; WP_000163242.1; NZ_WKIT01000072.1.
DR RefSeq; WP_000358995.1; NZ_WWCF01000102.1.
DR RefSeq; YP_001573918.1; NC_010077.1.
DR RefSeq; YP_001715971.1; NC_010419.1.
DR RefSeq; YP_006937217.1; NC_013292.1.
DR RefSeq; YP_006937607.1; NC_013319.1.
DR RefSeq; YP_006937727.1; NC_013322.1.
DR RefSeq; YP_006937753.1; NC_013323.1.
DR RefSeq; YP_006938161.1; NC_013333.1.
DR RefSeq; YP_006938435.1; NC_013340.1.
DR RefSeq; YP_006938641.1; NC_013347.1.
DR RefSeq; YP_006938712.1; NC_013349.1.
DR RefSeq; YP_006938775.1; NC_013352.1.
DR RefSeq; YP_006939395.1; NC_018965.1.
DR RefSeq; YP_006940871.1; NC_019009.1.
DR RefSeq; YP_536862.1; NC_007931.1.
DR PDB; 1JF8; X-ray; 1.12 A; A=1-131.
DR PDB; 1JFV; X-ray; 2.00 A; A=1-131.
DR PDB; 1LJL; X-ray; 2.01 A; A=1-131.
DR PDB; 1LJU; X-ray; 1.40 A; A=1-131.
DR PDB; 1LK0; X-ray; 1.60 A; A/B=1-131.
DR PDB; 1RXE; X-ray; 1.70 A; A=1-131.
DR PDB; 1RXI; X-ray; 1.50 A; A=1-131.
DR PDB; 2CD7; X-ray; 1.50 A; A=1-131.
DR PDB; 2FXI; X-ray; 1.80 A; A=1-131.
DR PDBsum; 1JF8; -.
DR PDBsum; 1JFV; -.
DR PDBsum; 1LJL; -.
DR PDBsum; 1LJU; -.
DR PDBsum; 1LK0; -.
DR PDBsum; 1RXE; -.
DR PDBsum; 1RXI; -.
DR PDBsum; 2CD7; -.
DR PDBsum; 2FXI; -.
DR AlphaFoldDB; P0A006; -.
DR BMRB; P0A006; -.
DR SMR; P0A006; -.
DR ChEMBL; CHEMBL4523173; -.
DR DrugBank; DB02763; 5-Mercapto-2-Nitro-Benzoic Acid.
DR DrugBank; DB03138; Perchlorate.
DR DrugBank; DB03352; S-Arsonocysteine.
DR BioCyc; MetaCyc:MON-10862; -.
DR BRENDA; 1.20.4.1; 3352.
DR BRENDA; 1.20.4.4; 3352.
DR SABIO-RK; P0A006; -.
DR EvolutionaryTrace; P0A006; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030612; F:arsenate reductase (thioredoxin) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR GO; GO:0046685; P:response to arsenic-containing substance; IEA:UniProtKB-KW.
DR HAMAP; MF_01624; Arsenate_reduct; 1.
DR InterPro; IPR014064; Arsenate_reductase_ArsC.
DR InterPro; IPR023485; Ptyr_pPase.
DR InterPro; IPR036196; Ptyr_pPase_sf.
DR Pfam; PF01451; LMWPc; 1.
DR SMART; SM00226; LMWPc; 1.
DR SUPFAM; SSF52788; SSF52788; 1.
DR TIGRFAMs; TIGR02691; arsC_pI258_fam; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Arsenical resistance; Cytoplasm; Disulfide bond;
KW Metal-binding; Oxidoreductase; Plasmid; Potassium; Redox-active center.
FT CHAIN 1..131
FT /note="Arsenate reductase"
FT /id="PRO_0000162523"
FT ACT_SITE 10
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01624,
FT ECO:0000305|PubMed:11573087, ECO:0000305|PubMed:12072565"
FT ACT_SITE 82
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01624,
FT ECO:0000305|PubMed:11573087, ECO:0000305|PubMed:12072565"
FT ACT_SITE 89
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01624,
FT ECO:0000305|PubMed:11573087, ECO:0000305|PubMed:12072565"
FT BINDING 13
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:11573087,
FT ECO:0000269|PubMed:12072565, ECO:0000269|PubMed:12682056,
FT ECO:0000269|PubMed:15159594, ECO:0000269|PubMed:16797027"
FT BINDING 36
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:11573087,
FT ECO:0000269|PubMed:12072565, ECO:0000269|PubMed:12682056,
FT ECO:0000269|PubMed:15159594, ECO:0000269|PubMed:16797027"
FT BINDING 63
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:11573087,
FT ECO:0000269|PubMed:12072565, ECO:0000269|PubMed:12682056,
FT ECO:0000269|PubMed:15159594, ECO:0000269|PubMed:16797027"
FT BINDING 65
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:11573087,
FT ECO:0000269|PubMed:12072565, ECO:0000269|PubMed:12682056,
FT ECO:0000269|PubMed:15159594, ECO:0000269|PubMed:16797027"
FT DISULFID 10..82
FT /note="Redox-active; alternate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01624,
FT ECO:0000305|PubMed:11573087, ECO:0000305|PubMed:12072565,
FT ECO:0007744|PDB:1LK0"
FT DISULFID 82..89
FT /note="Redox-active; alternate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01624,
FT ECO:0000305|PubMed:10606519, ECO:0000305|PubMed:11573087,
FT ECO:0000305|PubMed:12072565, ECO:0007744|PDB:1JFV,
FT ECO:0007744|PDB:1LJU"
FT VARIANT 2
FT /note="D -> T (in strain: SW18, SW4, SW24 and SW1)"
FT VARIANT 24..33
FT /note="GKEILGEGWN -> AKQILAKDWD (in strain: SW18)"
FT VARIANT 24..31
FT /note="GKEILGEG -> AKQILADD (in strain: SW24 and SW1)"
FT VARIANT 24..31
FT /note="GKEILGEG -> AKQILAED (in strain: SW4)"
FT VARIANT 56
FT /note="D -> G (in strain: SW18, SW4, SW24 and SW1)"
FT VARIANT 65
FT /note="D -> N (in strain: SW24 and SW1)"
FT VARIANT 70..76
FT /note="DILKQSD -> NIIKNSN (in strain: SW18, SW4, SW24 and
FT SW1)"
FT VARIANT 87
FT /note="N -> V (in strain: SW18, SW4, SW24 and SW1)"
FT VARIANT 91
FT /note="I -> S (in strain: SW4, SW24 and SW1)"
FT VARIANT 91
FT /note="I -> T (in strain: SW18)"
FT VARIANT 94
FT /note="P -> T (in strain: SW18, SW4, SW24 and SW1)"
FT VARIANT 110
FT /note="E -> P (in strain: SW18, SW4, SW24 and SW1)"
FT VARIANT 123
FT /note="L -> I (in strain: SW4, SW24 and SW1)"
FT VARIANT 123
FT /note="L -> V (in strain: SW18)"
FT VARIANT 127
FT /note="K -> N (in strain: SW18, SW4, SW24 and SW1)"
FT VARIANT 130
FT /note="L -> S (in strain: SW18, SW4, SW24 and SW1)"
FT MUTAGEN 10
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10606519"
FT MUTAGEN 10
FT /note="C->S: Loss of activity; when associated with A-15."
FT /evidence="ECO:0000269|PubMed:10606519,
FT ECO:0000269|PubMed:11573087"
FT MUTAGEN 13
FT /note="N->A: Loss of K(+) stabilization over Na(+)."
FT /evidence="ECO:0000269|PubMed:12682056"
FT MUTAGEN 15
FT /note="C->A: 2-fold decrease in affinity for arsenate. Does
FT not affect affinity for pNPP. Loss of activity; when
FT associated with S-10."
FT /evidence="ECO:0000269|PubMed:10606519,
FT ECO:0000269|PubMed:11573087"
FT MUTAGEN 16
FT /note="R->K: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12072565"
FT MUTAGEN 17
FT /note="S->A: 5-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:12072565"
FT MUTAGEN 21
FT /note="E->A: Decreases the thermal stabilization effect of
FT K(+)."
FT /evidence="ECO:0000269|PubMed:12682056"
FT MUTAGEN 36
FT /note="S->A: Strong impact on thermal stabilization."
FT /evidence="ECO:0000269|PubMed:12682056"
FT MUTAGEN 62
FT /note="H->Q: Uncouples the sulfate effect from the
FT potassium effect on the kinetics."
FT /evidence="ECO:0000269|PubMed:16797027"
FT MUTAGEN 65
FT /note="D->A: Loss of K(+) stabilization over Na(+)."
FT /evidence="ECO:0000269|PubMed:12682056"
FT MUTAGEN 82
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10606519"
FT MUTAGEN 89
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10606519"
FT MUTAGEN 89
FT /note="C->L: Leads to a reductase locked in the C-10/C-82
FT intermediate form. Decrease in affinity for pNPP."
FT /evidence="ECO:0000269|PubMed:11573087,
FT ECO:0000269|PubMed:12072565"
FT MUTAGEN 105
FT /note="D->A: 4-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:12072565"
FT STRAND 4..15
FT /evidence="ECO:0007829|PDB:1JF8"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:1JF8"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:1JF8"
FT STRAND 32..40
FT /evidence="ECO:0007829|PDB:1JF8"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:1JF8"
FT HELIX 69..74
FT /evidence="ECO:0007829|PDB:1JF8"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:1JF8"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:1JF8"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:1JF8"
FT HELIX 111..129
FT /evidence="ECO:0007829|PDB:1JF8"
SQ SEQUENCE 131 AA; 14813 MW; 03871148DC433A18 CRC64;
MDKKTIYFIC TGNSCRSQMA EGWGKEILGE GWNVYSAGIE THGVNPKAIE AMKEVDIDIS
NHTSDLIDND ILKQSDLVVT LCSDADNNCP ILPPNVKKEH WGFDDPAGKE WSEFQRVRDE
IKLAIEKFKL R
