sodC:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

SodC

Synonyms

superoxide dismutase, Cu, Zn[1], B1646[2][1], SodC[2][1], Bacteriocuprein[2][1] , ECK1642, JW1638, b1646

Product description

superoxide dismutase precursor (Cu-Zn)[2][3]

Superoxide dismutase, Cu, Zn, periplasmic; mutants are sensitive to exogenous hydrogen peroxide in early stationary phase[4]

EC number (for enzymes)
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Notes

Function

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<protect> Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0030288

outer membrane-bounded periplasmic space

PMID:7786035[5]

IDA: Inferred from Direct Assay

C

Seeded from Riley et al 2006 [1].

complete

GO:0004784

superoxide dismutase activity

PMID:7929223[6]

IDA: Inferred from Direct Assay

F

complete

GO:0004784

superoxide dismutase activity

PMID:8626323[7]

IDA: Inferred from Direct Assay

F

complete

GO:0042597

periplasmic space

PMID:8791100[8]

IDA: Inferred from Direct Assay

C

complete

GO:0042597

periplasmic space

PMID:7786035[5]

IDA: Inferred from Direct Assay

C

complete

GO:0004784

superoxide dismutase activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:1.15.1.1

F

Seeded from EcoCyc (v14.0)

complete

GO:0005507

copper ion binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0186

F

Seeded from EcoCyc (v14.0)

complete

GO:0006801

superoxide metabolic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001424

P

Seeded from EcoCyc (v14.0)

complete

GO:0008270

zinc ion binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0862

F

Seeded from EcoCyc (v14.0)

complete

GO:0016209

antioxidant activity

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0049

F

Seeded from EcoCyc (v14.0)

complete

GO:0055114

oxidation reduction

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001424

P

Seeded from EcoCyc (v14.0)

complete

GO:0055114

oxidation reduction

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0560

P

Seeded from EcoCyc (v14.0)

complete

GO:0005507

copper ion binding

PMID:8791100[8]

IDA: Inferred from Direct Assay

F

complete

GO:0008270

zinc ion binding

PMID:9405149[9]

IDA: Inferred from Direct Assay

F

complete

GO:0006801

superoxide metabolic process

PMID:8791100[8]

IDA: Inferred from Direct Assay

P

complete

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Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence
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Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Reference/Source Notes

periplasm

Periplasm

PMID:8626323[7]

EchoLocation:sodC


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Notes

Structure and Physical Properties

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<protect> Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence

at EcoCyc 

MKRFSLAILA LVVATGAQAA SEKVEMNLVT SQGVGQSIGS VTITETDKGL EFSPDLKALP
PGEHGFHIHA KGSCQPATKD GKASAAESAG GHLDPQNTGK HEGPEGAGHL GDLPALVVNN
DGKATDAVIA PRLKSLDEIK DKALMVHVGG DNMSDQPKPL GGGGERYACG VIK
Length

173

Mol. Wt

17.68 kDa

pI

6.4 (calculated)

Extinction coefficient

1,490 - 1,740 (calc based on 1 Y, 0 W, and 2 C residues)

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Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

motif

1-19

UniProt Manual:Signal Peptides

UniProt:P0AGD1

Domain

17..172

PF00080 Copper/zinc superoxide dismutase (SODC)

PMID:19920124[10]

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Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=sodC taxon=562,83333 </beststructure>

Models

View models at:

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Structure figures

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Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16129604

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:945343

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0005505

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P0AGD1

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:G6886

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG13419

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:945343

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120003475

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB3195

Escherichia coli str. K-12 substr. MG1655

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Notes

Links

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References

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See Help:References for how to manage references in EcoliWiki.

  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. ↑ 5.0 5.1 Benov, L et al. (1995) Copper, zinc superoxide dismutase in Escherichia coli: periplasmic localization. Arch. Biochem. Biophys. 319 508-11 PubMed
  6. ↑ Benov, LT & Fridovich, I (1994) Escherichia coli expresses a copper- and zinc-containing superoxide dismutase. J. Biol. Chem. 269 25310-4 PubMed
  7. ↑ 7.0 7.1 Imlay, KR & Imlay, JA (1996) Cloning and analysis of sodC, encoding the copper-zinc superoxide dismutase of Escherichia coli. J. Bacteriol. 178 2564-71 PubMed
  8. ↑ 8.0 8.1 8.2 Benov, LT et al. (1996) Purification and characterization of the Cu,Zn SOD from Escherichia coli. Free Radic. Biol. Med. 21 117-21 PubMed
  9. ↑ Pesce, A et al. (1997) Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealed by X-ray crystallography. J. Mol. Biol. 274 408-20 PubMed
  10. ↑ Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

Categories

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