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Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (Bacteriocuprein)

 SODC_ECOLI              Reviewed;         173 AA.
P0AGD1; P53635; P96756; Q2MB67;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
20-DEC-2005, sequence version 1.
13-FEB-2019, entry version 110.
RecName: Full=Superoxide dismutase [Cu-Zn];
EC=1.15.1.1;
AltName: Full=Bacteriocuprein;
Flags: Precursor;
Name=sodC; OrderedLocusNames=b1646, JW1638;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 20-36.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8626323; DOI=10.1128/jb.178.9.2564-2571.1996;
Imlay K.R.C., Imlay J.A.;
"Cloning and analysis of sodC, encoding the copper-zinc superoxide
dismutase of Escherichia coli.";
J. Bacteriol. 178:2564-2571(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-173.
STRAIN=QC871;
PubMed=9003353; DOI=10.1042/bj3200713;
Battistoni A., Folcarelli S., Gabbianelli R., Capo C., Rotilio G.;
"The Cu,Zn superoxide dismutase from Escherichia coli retains
monomeric structure at high protein concentration. Evidence for
altered subunit interaction in all the bacteriocupreins.";
Biochem. J. 320:713-716(1996).
[5]
CHARACTERIZATION.
PubMed=7929223;
Benov L.T., Fridovich I.;
"Escherichia coli expresses a copper- and zinc-containing superoxide
dismutase.";
J. Biol. Chem. 269:25310-25314(1994).
[6]
CHARACTERIZATION.
PubMed=7786035; DOI=10.1006/abbi.1995.1324;
Benov L.T., Chang L.Y., Day B., Fridovich I.;
"Copper, zinc superoxide dismutase in Escherichia coli: periplasmic
localization.";
Arch. Biochem. Biophys. 319:508-511(1995).
[7]
CHARACTERIZATION.
PubMed=7589534; DOI=10.1016/0014-5793(95)01106-O;
Battistoni A., Rotilio G.;
"Isolation of an active and heat-stable monomeric form of Cu,Zn
superoxide dismutase from the periplasmic space of Escherichia coli.";
FEBS Lett. 374:199-202(1995).
[8]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 20-173, AND DISULFIDE BOND.
PubMed=9405149; DOI=10.1006/jmbi.1997.1400;
Pesce A., Capasso C., Battistoni A., Folcarelli S., Rotilio G.,
Desideri A., Bolognesi M.;
"Unique structural features of the monomeric Cu,Zn superoxide
dismutase from Escherichia coli, revealed by X-ray crystallography.";
J. Mol. Biol. 274:408-420(1997).
-!- FUNCTION: Destroys radicals which are normally produced within the
cells and which are toxic to biological systems.
-!- CATALYTIC ACTIVITY:
Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
ChEBI:CHEBI:18421; EC=1.15.1.1;
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378;
Note=Binds 1 copper ion per subunit.;
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 1 zinc ion per subunit.;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Temperature dependence:
Highly thermostable.;
-!- SUBUNIT: Monomer.
-!- SUBCELLULAR LOCATION: Periplasm.
-!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U51242; AAB03729.1; -; Genomic_DNA.
EMBL; U00096; AAC74718.1; -; Genomic_DNA.
EMBL; AP009048; BAE76489.1; -; Genomic_DNA.
EMBL; X97766; CAA66363.1; -; Genomic_DNA.
PIR; JC6004; JC6004.
RefSeq; NP_416163.1; NC_000913.3.
RefSeq; WP_001296937.1; NZ_LN832404.1.
PDB; 1ESO; X-ray; 2.00 A; A=20-173.
PDBsum; 1ESO; -.
ProteinModelPortal; P0AGD1; -.
SMR; P0AGD1; -.
BioGrid; 4259604; 26.
STRING; 316385.ECDH10B_1780; -.
EPD; P0AGD1; -.
jPOST; P0AGD1; -.
PaxDb; P0AGD1; -.
PRIDE; P0AGD1; -.
EnsemblBacteria; AAC74718; AAC74718; b1646.
EnsemblBacteria; BAE76489; BAE76489; BAE76489.
GeneID; 945343; -.
KEGG; ecj:JW1638; -.
KEGG; eco:b1646; -.
PATRIC; fig|1411691.4.peg.613; -.
EchoBASE; EB3195; -.
EcoGene; EG13419; sodC.
eggNOG; ENOG4108Z7T; Bacteria.
eggNOG; COG2032; LUCA.
HOGENOM; HOG000263449; -.
InParanoid; P0AGD1; -.
KO; K04565; -.
PhylomeDB; P0AGD1; -.
BioCyc; EcoCyc:G6886-MONOMER; -.
BioCyc; ECOL316407:JW1638-MONOMER; -.
BioCyc; MetaCyc:G6886-MONOMER; -.
EvolutionaryTrace; P0AGD1; -.
PRO; PR:P0AGD1; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
GO; GO:0042597; C:periplasmic space; IDA:EcoliWiki.
GO; GO:0005507; F:copper ion binding; IDA:EcoliWiki.
GO; GO:0004784; F:superoxide dismutase activity; IDA:EcoliWiki.
GO; GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
GO; GO:0006801; P:superoxide metabolic process; IDA:EcoliWiki.
CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
Gene3D; 2.60.40.200; -; 1.
InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
InterPro; IPR018152; SOD_Cu/Zn_BS.
InterPro; IPR001424; SOD_Cu_Zn_dom.
PANTHER; PTHR10003; PTHR10003; 1.
Pfam; PF00080; Sod_Cu; 1.
SUPFAM; SSF49329; SSF49329; 1.
PROSITE; PS00332; SOD_CU_ZN_2; 1.
1: Evidence at protein level;
3D-structure; Antioxidant; Complete proteome; Copper;
Direct protein sequencing; Disulfide bond; Metal-binding;
Oxidoreductase; Periplasm; Reference proteome; Signal; Zinc.
SIGNAL 1 19 {ECO:0000269|PubMed:8626323}.
CHAIN 20 173 Superoxide dismutase [Cu-Zn].
/FTId=PRO_0000032824.
METAL 67 67 Copper; catalytic.
METAL 69 69 Copper; catalytic.
METAL 92 92 Copper; catalytic.
METAL 92 92 Zinc; structural.
METAL 101 101 Zinc; structural.
METAL 109 109 Zinc; structural.
METAL 112 112 Zinc; structural.
METAL 147 147 Copper; catalytic.
DISULFID 74 169 {ECO:0000269|PubMed:9405149}.
STRAND 21 30 {ECO:0000244|PDB:1ESO}.
STRAND 33 46 {ECO:0000244|PDB:1ESO}.
STRAND 49 56 {ECO:0000244|PDB:1ESO}.
STRAND 61 64 {ECO:0000244|PDB:1ESO}.
STRAND 66 72 {ECO:0000244|PDB:1ESO}.
STRAND 80 82 {ECO:0000244|PDB:1ESO}.
HELIX 87 89 {ECO:0000244|PDB:1ESO}.
STRAND 106 108 {ECO:0000244|PDB:1ESO}.
STRAND 116 118 {ECO:0000244|PDB:1ESO}.
STRAND 128 130 {ECO:0000244|PDB:1ESO}.
HELIX 136 139 {ECO:0000244|PDB:1ESO}.
STRAND 142 149 {ECO:0000244|PDB:1ESO}.
STRAND 153 158 {ECO:0000244|PDB:1ESO}.
HELIX 159 162 {ECO:0000244|PDB:1ESO}.
STRAND 165 172 {ECO:0000244|PDB:1ESO}.
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


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[mbnA MettrDRAFT_4473] Methanobactin mb-OB3b (Copper-binding compound) (CBC) (Hydrogen peroxide reductase) (EC 1.11.1.-) (Superoxide dismutase) (EC 1.15.1.1)
[sod1-a] Superoxide dismutase [Cu-Zn] A (XSODA) (EC 1.15.1.1)
[SOD2] Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1)
[CCS At1g12520 F5O11.26 T12C24.6] Copper chaperone for superoxide dismutase, chloroplastic/cytosolic (AtCCS) (Superoxide dismutase copper chaperone)
[Sod2 Sod-2] Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1)
[Sod2] Superoxide dismutase [Mn], mitochondrial (EC 1.15.1.1)
[sodB sod sodA Rv3846 MTCY01A6.22c] Superoxide dismutase [Fe] (EC 1.15.1.1)
[NECI] Nectarin-1 (EC 1.15.1.1) (Superoxide dismutase [Mn])
[sodA sod] Superoxide dismutase [Mn/Fe] (EC 1.15.1.1)
[sodF1 sodB sodF SCO2633 SC8E4A.03] Superoxide dismutase [Fe-Zn] 1 (EC 1.15.1.1) (FeSOD I) (SOD2)
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[al-3 B8P8.010 NCU01427] Geranylgeranyl pyrophosphate synthase (GGPP synthase) (GGPPSase) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Albino-3 protein) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10)
[aro-1 aro-2 aro-4 aro-5 aro-9 B14H13.20 NCU016321] Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
[sod1 sod VNG_1190G] Superoxide dismutase [Mn] 1 (EC 1.15.1.1)
[al-2 B22I21.230 NCU00585] Bifunctional lycopene cyclase/phytoene synthase (Protein albino-2) [Includes: Lycopene beta-cyclase (EC 5.5.1.19) (Carotene cyclase) (Lycopene cyclase); Phytoene synthase (EC 2.5.1.32)]
[T 90C4.150 NCU00776] Tyrosinase (EC 1.14.18.1) (Monophenol monooxygenase)
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]

Bibliography :
[9003353] The Cu,Zn superoxide dismutase from Escherichia coli retains monomeric structure at high protein concentration. Evidence for altered subunit interaction in all the bacteriocupreins.
[2071047] Induction of superoxide dismutases in Photobacterium leiognathi.
[2071040] The rate of Cu,Zn superoxide dismutase evolution.
[3805055] Bacteriocuprein superoxide dismutase of Photobacterium leiognathi. Isolation and sequence of the gene and evidence for a precursor form.
[3298151] Comparison of chloroplast and cytosolic Cu/Zn superoxide dismutase isozymes from tomato in relation to superoxide dismutase evolution.
[3790249] Primary structure of Cu-Zn superoxide dismutase of Brassica oleracea proves homology with corresponding enzymes of animals, fungi and prokaryotes.
[3511030] Strain variation in bacteriocuprein superoxide dismutase from symbiotic Photobacterium leiognathi.
[3997777] Bacteriocuprein superoxide dismutases in pseudomonads.
[6510412] The amino-acid sequence of copper/zinc superoxide dismutase from swordfish liver. Comparison of copper/zinc superoxide dismutase sequences.
[7050107] Copper-zinc superoxide dismutase from Caulobacter crescentus CB15. A novel bacteriocuprein form of the enzyme.