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Protein

Superoxide dismutase [Cu-Zn]

Gene

sodC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Protein has several cofactor binding sites:
  • Cu cationNote: Binds 1 copper ion per subunit.
  • Zn2+Note: Binds 1 zinc ion per subunit.

Temperature dependencei

Highly thermostable.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi67 – 671Copper; catalytic
Metal bindingi69 – 691Copper; catalytic
Metal bindingi92 – 921Copper; catalytic
Metal bindingi92 – 921Zinc; structural
Metal bindingi101 – 1011Zinc; structural
Metal bindingi109 – 1091Zinc; structural
Metal bindingi112 – 1121Zinc; structural
Metal bindingi147 – 1471Copper; catalytic

GO - Molecular functioni

  • copper ion binding Source: EcoliWiki
  • superoxide dismutase activity Source: EcoliWiki
  • zinc ion binding Source: EcoliWiki

GO - Biological processi

  • superoxide metabolic process Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:G6886-MONOMER.
ECOL316407:JW1638-MONOMER.
MetaCyc:G6886-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Cu-Zn] (EC:1.15.1.1)
Alternative name(s):
Bacteriocuprein
Gene namesi
Name:sodC
Ordered Locus Names:b1646, JW1638
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13419. sodC.

Subcellular locationi

GO - Cellular componenti

  • outer membrane-bounded periplasmic space Source: EcoCyc
  • periplasmic space Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 173154Superoxide dismutase [Cu-Zn]PRO_0000032824Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi74 ↔ 1691 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiP0AGD1.
PaxDbiP0AGD1.
PRIDEiP0AGD1.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi4259604. 8 interactions.
STRINGi511145.b1646.

Structurei

Secondary structure

1
173
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi21 – 3010Combined sources
Beta strandi33 – 4614Combined sources
Beta strandi49 – 568Combined sources
Beta strandi61 – 644Combined sources
Beta strandi66 – 727Combined sources
Beta strandi80 – 823Combined sources
Helixi87 – 893Combined sources
Beta strandi106 – 1083Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi128 – 1303Combined sources
Helixi136 – 1394Combined sources
Beta strandi142 – 1498Combined sources
Beta strandi153 – 1586Combined sources
Helixi159 – 1624Combined sources
Beta strandi165 – 1728Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ESOX-ray2.00A20-173[»]
ProteinModelPortaliP0AGD1.
SMRiP0AGD1. Positions 20-173.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AGD1.

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108Z7T. Bacteria.
COG2032. LUCA.
HOGENOMiHOG000263449.
InParanoidiP0AGD1.
KOiK04565.
OMAiGARYACG.
OrthoDBiEOG6K13RS.
PhylomeDBiP0AGD1.

Family and domain databases

Gene3Di2.60.40.200. 1 hit.
InterProiIPR024134. SOD_Cu/Zn_/chaperone.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003. PTHR10003. 1 hit.
PfamiPF00080. Sod_Cu. 1 hit.
[Graphical view]
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AGD1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRFSLAILA LVVATGAQAA SEKVEMNLVT SQGVGQSIGS VTITETDKGL
60 70 80 90 100
EFSPDLKALP PGEHGFHIHA KGSCQPATKD GKASAAESAG GHLDPQNTGK
110 120 130 140 150
HEGPEGAGHL GDLPALVVNN DGKATDAVIA PRLKSLDEIK DKALMVHVGG
160 170
DNMSDQPKPL GGGGERYACG VIK
Length:173
Mass (Da):17,681
Last modified:December 20, 2005 - v1
Checksum:i9A0CB65F03AAB197
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51242 Genomic DNA. Translation: AAB03729.1.
U00096 Genomic DNA. Translation: AAC74718.1.
AP009048 Genomic DNA. Translation: BAE76489.1.
X97766 Genomic DNA. Translation: CAA66363.1.
PIRiJC6004.
RefSeqiNP_416163.1. NC_000913.3.
WP_001296937.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74718; AAC74718; b1646.
BAE76489; BAE76489; BAE76489.
GeneIDi945343.
KEGGiecj:JW1638.
eco:b1646.
PATRICi32118594. VBIEscCol129921_1717.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51242 Genomic DNA. Translation: AAB03729.1.
U00096 Genomic DNA. Translation: AAC74718.1.
AP009048 Genomic DNA. Translation: BAE76489.1.
X97766 Genomic DNA. Translation: CAA66363.1.
PIRiJC6004.
RefSeqiNP_416163.1. NC_000913.3.
WP_001296937.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ESOX-ray2.00A20-173[»]
ProteinModelPortaliP0AGD1.
SMRiP0AGD1. Positions 20-173.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259604. 8 interactions.
STRINGi511145.b1646.

Proteomic databases

EPDiP0AGD1.
PaxDbiP0AGD1.
PRIDEiP0AGD1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74718; AAC74718; b1646.
BAE76489; BAE76489; BAE76489.
GeneIDi945343.
KEGGiecj:JW1638.
eco:b1646.
PATRICi32118594. VBIEscCol129921_1717.

Organism-specific databases

EchoBASEiEB3195.
EcoGeneiEG13419. sodC.

Phylogenomic databases

eggNOGiENOG4108Z7T. Bacteria.
COG2032. LUCA.
HOGENOMiHOG000263449.
InParanoidiP0AGD1.
KOiK04565.
OMAiGARYACG.
OrthoDBiEOG6K13RS.
PhylomeDBiP0AGD1.

Enzyme and pathway databases

BioCyciEcoCyc:G6886-MONOMER.
ECOL316407:JW1638-MONOMER.
MetaCyc:G6886-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AGD1.
PROiP0AGD1.

Family and domain databases

Gene3Di2.60.40.200. 1 hit.
InterProiIPR024134. SOD_Cu/Zn_/chaperone.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003. PTHR10003. 1 hit.
PfamiPF00080. Sod_Cu. 1 hit.
[Graphical view]
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and analysis of sodC, encoding the copper-zinc superoxide dismutase of Escherichia coli."
    Imlay K.R.C., Imlay J.A.
    J. Bacteriol. 178:2564-2571(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 20-36.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "The Cu,Zn superoxide dismutase from Escherichia coli retains monomeric structure at high protein concentration. Evidence for altered subunit interaction in all the bacteriocupreins."
    Battistoni A., Folcarelli S., Gabbianelli R., Capo C., Rotilio G.
    Biochem. J. 320:713-716(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-173.
    Strain: QC871.
  5. "Escherichia coli expresses a copper- and zinc-containing superoxide dismutase."
    Benov L.T., Fridovich I.
    J. Biol. Chem. 269:25310-25314(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "Copper, zinc superoxide dismutase in Escherichia coli: periplasmic localization."
    Benov L.T., Chang L.Y., Day B., Fridovich I.
    Arch. Biochem. Biophys. 319:508-511(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "Isolation of an active and heat-stable monomeric form of Cu,Zn superoxide dismutase from the periplasmic space of Escherichia coli."
    Battistoni A., Rotilio G.
    FEBS Lett. 374:199-202(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. "Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealed by X-ray crystallography."
    Pesce A., Capasso C., Battistoni A., Folcarelli S., Rotilio G., Desideri A., Bolognesi M.
    J. Mol. Biol. 274:408-420(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 20-173, DISULFIDE BOND.

Entry informationi

Entry nameiSODC_ECOLI
AccessioniPrimary (citable) accession number: P0AGD1
Secondary accession number(s): P53635, P96756, Q2MB67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: July 6, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.