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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)DescriptionActionsGraphical viewLength
Metal bindingi67Copper; catalytic1
Metal bindingi69Copper; catalytic1
Metal bindingi92Copper; catalytic1
Metal bindingi92Zinc; structural1
Metal bindingi101Zinc; structural1
Metal bindingi109Zinc; structural1
Metal bindingi112Zinc; structural1
Metal bindingi147Copper; catalytic1

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 191 PublicationAdd BLAST19
ChainiPRO_000003282420 – 173Superoxide dismutase [Cu-Zn]Add BLAST154

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi74 ↔ 1691 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiP0AGD1.
PaxDbiP0AGD1.
PRIDEiP0AGD1.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi4259604. 8 interactors.
STRINGi511145.b1646.

Structurei

Secondary structure

1173
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi21 – 30Combined sources10
Beta strandi33 – 46Combined sources14
Beta strandi49 – 56Combined sources8
Beta strandi61 – 64Combined sources4
Beta strandi66 – 72Combined sources7
Beta strandi80 – 82Combined sources3
Helixi87 – 89Combined sources3
Beta strandi106 – 108Combined sources3
Beta strandi116 – 118Combined sources3
Beta strandi128 – 130Combined sources3
Helixi136 – 139Combined sources4
Beta strandi142 – 149Combined sources8
Beta strandi153 – 158Combined sources6
Helixi159 – 162Combined sources4
Beta strandi165 – 172Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ESOX-ray2.00A20-173[»]
ProteinModelPortaliP0AGD1.
SMRiP0AGD1.
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.
PhylomeDBiP0AGD1.

Family and domain databases

CDDicd00305. Cu-Zn_Superoxide_Dismutase. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ESOX-ray2.00A20-173[»]
ProteinModelPortaliP0AGD1.
SMRiP0AGD1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259604. 8 interactors.
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.
PhylomeDBiP0AGD1.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0AGD1.
PROiP0AGD1.

Family and domain databases

CDDicd00305. Cu-Zn_Superoxide_Dismutase. 1 hit.
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...

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: November 2, 2016
This is version 97 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.