SODC_ECOLI
ID SODC_ECOLI Reviewed; 173 AA.
AC P0AGD1; P53635; P96756; Q2MB67;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Superoxide dismutase [Cu-Zn];
DE EC=1.15.1.1;
DE AltName: Full=Bacteriocuprein;
DE Flags: Precursor;
GN Name=sodC; OrderedLocusNames=b1646, JW1638;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 20-36, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8626323; DOI=10.1128/jb.178.9.2564-2571.1996;
RA Imlay K.R.C., Imlay J.A.;
RT "Cloning and analysis of sodC, encoding the copper-zinc superoxide
RT dismutase of Escherichia coli.";
RL J. Bacteriol. 178:2564-2571(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-173.
RC STRAIN=QC871;
RX PubMed=9003353; DOI=10.1042/bj3200713;
RA Battistoni A., Folcarelli S., Gabbianelli R., Capo C., Rotilio G.;
RT "The Cu,Zn superoxide dismutase from Escherichia coli retains monomeric
RT structure at high protein concentration. Evidence for altered subunit
RT interaction in all the bacteriocupreins.";
RL Biochem. J. 320:713-716(1996).
RN [5]
RP ACTIVITY REGULATION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=7929223; DOI=10.1016/s0021-9258(18)47248-1;
RA Benov L.T., Fridovich I.;
RT "Escherichia coli expresses a copper- and zinc-containing superoxide
RT dismutase.";
RL J. Biol. Chem. 269:25310-25314(1994).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=7786035; DOI=10.1006/abbi.1995.1324;
RA Benov L.T., Chang L.Y., Day B., Fridovich I.;
RT "Copper, zinc superoxide dismutase in Escherichia coli: periplasmic
RT localization.";
RL Arch. Biochem. Biophys. 319:508-511(1995).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=7589534; DOI=10.1016/0014-5793(95)01106-o;
RA Battistoni A., Rotilio G.;
RT "Isolation of an active and heat-stable monomeric form of Cu,Zn superoxide
RT dismutase from the periplasmic space of Escherichia coli.";
RL FEBS Lett. 374:199-202(1995).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 20-173, AND DISULFIDE BOND.
RX PubMed=9405149; DOI=10.1006/jmbi.1997.1400;
RA Pesce A., Capasso C., Battistoni A., Folcarelli S., Rotilio G.,
RA Desideri A., Bolognesi M.;
RT "Unique structural features of the monomeric Cu,Zn superoxide dismutase
RT from Escherichia coli, revealed by X-ray crystallography.";
RL J. Mol. Biol. 274:408-420(1997).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:18421; EC=1.15.1.1; Evidence={ECO:0000269|PubMed:7929223,
CC ECO:0000269|PubMed:8626323};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Note=Binds 1 copper ion per subunit.;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- ACTIVITY REGULATION: Inactivated by diethyldithiocarbamate
CC (PubMed:7929223). Inhibited by cyanide (PubMed:7929223).
CC {ECO:0000269|PubMed:7929223}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.8. {ECO:0000269|PubMed:7929223};
CC Temperature dependence:
CC Highly thermostable.;
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:7589534,
CC ECO:0000269|PubMed:7786035}.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; U51242; AAB03729.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74718.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76489.1; -; Genomic_DNA.
DR EMBL; X97766; CAA66363.1; -; Genomic_DNA.
DR PIR; JC6004; JC6004.
DR RefSeq; NP_416163.1; NC_000913.3.
DR RefSeq; WP_001296937.1; NZ_STEB01000003.1.
DR PDB; 1ESO; X-ray; 2.00 A; A=20-173.
DR PDBsum; 1ESO; -.
DR AlphaFoldDB; P0AGD1; -.
DR SMR; P0AGD1; -.
DR BioGRID; 4259604; 26.
DR STRING; 511145.b1646; -.
DR jPOST; P0AGD1; -.
DR PaxDb; P0AGD1; -.
DR PRIDE; P0AGD1; -.
DR EnsemblBacteria; AAC74718; AAC74718; b1646.
DR EnsemblBacteria; BAE76489; BAE76489; BAE76489.
DR GeneID; 66674462; -.
DR GeneID; 945343; -.
DR KEGG; ecj:JW1638; -.
DR KEGG; eco:b1646; -.
DR PATRIC; fig|1411691.4.peg.613; -.
DR EchoBASE; EB3195; -.
DR eggNOG; COG2032; Bacteria.
DR HOGENOM; CLU_056632_7_1_6; -.
DR InParanoid; P0AGD1; -.
DR OMA; EHGFNNP; -.
DR PhylomeDB; P0AGD1; -.
DR BioCyc; EcoCyc:G6886-MON; -.
DR BioCyc; MetaCyc:G6886-MON; -.
DR EvolutionaryTrace; P0AGD1; -.
DR PRO; PR:P0AGD1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0042597; C:periplasmic space; IDA:EcoliWiki.
DR GO; GO:0005507; F:copper ion binding; IDA:EcoliWiki.
DR GO; GO:0004784; F:superoxide dismutase activity; IDA:EcoliWiki.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
DR GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
DR GO; GO:0006801; P:superoxide metabolic process; IDA:EcoliWiki.
DR CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR Gene3D; 2.60.40.200; -; 1.
DR InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR InterPro; IPR018152; SOD_Cu/Zn_BS.
DR InterPro; IPR001424; SOD_Cu_Zn_dom.
DR PANTHER; PTHR10003; PTHR10003; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR SUPFAM; SSF49329; SSF49329; 1.
DR PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antioxidant; Copper; Direct protein sequencing;
KW Disulfide bond; Metal-binding; Oxidoreductase; Periplasm;
KW Reference proteome; Signal; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:8626323"
FT CHAIN 20..173
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000032824"
FT REGION 72..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 67
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:9405149"
FT BINDING 69
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:9405149"
FT BINDING 92
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:9405149"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:9405149"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:9405149"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:9405149"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:9405149"
FT BINDING 147
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:9405149"
FT DISULFID 74..169
FT /evidence="ECO:0000269|PubMed:9405149"
FT STRAND 21..30
FT /evidence="ECO:0007829|PDB:1ESO"
FT STRAND 33..46
FT /evidence="ECO:0007829|PDB:1ESO"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:1ESO"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:1ESO"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:1ESO"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1ESO"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:1ESO"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1ESO"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1ESO"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1ESO"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:1ESO"
FT STRAND 142..149
FT /evidence="ECO:0007829|PDB:1ESO"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:1ESO"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:1ESO"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:1ESO"
SQ SEQUENCE 173 AA; 17681 MW; 9A0CB65F03AAB197 CRC64;
MKRFSLAILA LVVATGAQAA SEKVEMNLVT SQGVGQSIGS VTITETDKGL EFSPDLKALP
PGEHGFHIHA KGSCQPATKD GKASAAESAG GHLDPQNTGK HEGPEGAGHL GDLPALVVNN
DGKATDAVIA PRLKSLDEIK DKALMVHVGG DNMSDQPKPL GGGGERYACG VIK
