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ECOLI:SODM

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) sodA
Protein Name(s) Superoxide dismutase [Mn]

MnSOD

External Links
UniProt P00448
EMBL X03951
M20984
L19201
U00096
AP009048
X60699
M85158
PIR A24141
RefSeq NP_418344.3
YP_491542.1
PDB 1D5N
1EN4
1EN5
1EN6
1I08
1I0H
1IX9
1IXB
1MMM
1VEW
1ZLZ
3K9S
3OT7
PDBsum 1D5N
1EN4
1EN5
1EN6
1I08
1I0H
1IX9
1IXB
1MMM
1VEW
1ZLZ
3K9S
3OT7
ProteinModelPortal P00448
SMR P00448
IntAct P00448
STRING 511145.b3908
SWISS-2DPAGE P00448
PaxDb P00448
PRIDE P00448
EnsemblBacteria AAC76890
BAE77401
GeneID 12933233
948403
KEGG ecj:Y75_p3278
eco:b3908
PATRIC 32123327
EchoBASE EB0946
EcoGene EG10953
eggNOG COG0605
HOGENOM HOG000013583
InParanoid P00448
KO K04564
OMA KHHNAYT
OrthoDB EOG63NMNT
PhylomeDB P00448
BioCyc EcoCyc:SUPEROX-DISMUTMN-MONOMER
ECOL316407:JW3879-MONOMER
MetaCyc:SUPEROX-DISMUTMN-MONOMER
EvolutionaryTrace P00448
PRO PR:P00448
Proteomes UP000000318
UP000000625
Genevestigator P00448
GO GO:0005737
GO:0016209
GO:0003677
GO:0030145
GO:0046872
GO:0004784
GO:0071291
GO:0055114
GO:0019430
GO:0010447
GO:0009408
GO:0006979
GO:0006801
InterPro IPR001189
IPR019833
IPR019832
IPR019831
PANTHER PTHR11404
Pfam PF02777
PF00081
PIRSF PIRSF000349
PRINTS PR01703
SUPFAM SSF46609
SSF54719
PROSITE PS00088

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

involved_in

GO:0055114

oxidation-reduction process

PMID:4943714[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

PMID:4921969[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0019430

removal of superoxide radicals

PMID:4943714[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006801

superoxide metabolic process

PMID:4196244[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:4580575[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004784

superoxide dismutase activity

PMID:4921969[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0071291

cellular response to selenium ion

PMID:11872706[5]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0030145

manganese ion binding

PMID:9548935[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0030145

manganese ion binding

PMID:9220980[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0016209

antioxidant activity

PMID:3011417[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0010447

response to acidic pH

PMID:20305033[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009408

response to heat

PMID:7768839[10]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006979

response to oxidative stress

PMID:7730258[11]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[12]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004784

superoxide dismutase activity

PMID:330499[13]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

PMID:7961811[14]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004784

superoxide dismutase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001189
InterPro:IPR019831
InterPro:IPR019832
InterPro:IPR019833

F

Seeded From UniProt

complete

involved_in

GO:0006801

superoxide metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001189
InterPro:IPR019831
InterPro:IPR019832
InterPro:IPR019833

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001189
InterPro:IPR019831
InterPro:IPR019832
InterPro:IPR019833

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001189
InterPro:IPR019831
InterPro:IPR019832
InterPro:IPR019833

P

Seeded From UniProt

complete

enables

GO:0004784

superoxide dismutase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.15.1.1

F

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 Beauchamp, C & Fridovich, I (1971) Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal. Biochem. 44 276-87 PubMed GONUTS page
  2. 2.0 2.1 Keele, BB Jr et al. (1970) Superoxide dismutase from escherichia coli B. A new manganese-containing enzyme. J. Biol. Chem. 245 6176-81 PubMed GONUTS page
  3. Gregory, EM & Fridovich, I (1973) Induction of superoxide dismutase by molecular oxygen. J. Bacteriol. 114 543-8 PubMed GONUTS page
  4. Gregory, EM et al. (1973) Superoxide dismutases of Escherichia coli: intracellular localization and functions. J. Bacteriol. 115 987-91 PubMed GONUTS page
  5. Bébien, M et al. (2002) Involvement of superoxide dismutases in the response of Escherichia coli to selenium oxides. J. Bacteriol. 184 1556-64 PubMed GONUTS page
  6. Vance, CK & Miller, AF (1998) Spectroscopic comparisons of the pH dependencies of Fe-substituted (Mn)superoxide dismutase and Fe-superoxide dismutase. Biochemistry 37 5518-27 PubMed GONUTS page
  7. Whittaker, MM & Whittaker, JW (1997) Mutagenesis of a proton linkage pathway in Escherichia coli manganese superoxide dismutase. Biochemistry 36 8923-31 PubMed GONUTS page
  8. Carlioz, A & Touati, D (1986) Isolation of superoxide dismutase mutants in Escherichia coli: is superoxide dismutase necessary for aerobic life? EMBO J. 5 623-30 PubMed GONUTS page
  9. Bruno-Bárcena, JM et al. (2010) Role of antioxidant enzymes in bacterial resistance to organic acids. Appl. Environ. Microbiol. 76 2747-53 PubMed GONUTS page
  10. Benov, L & Fridovich, I (1995) Superoxide dismutase protects against aerobic heat shock in Escherichia coli. J. Bacteriol. 177 3344-6 PubMed GONUTS page
  11. Touati, D et al. (1995) Lethal oxidative damage and mutagenesis are generated by iron in delta fur mutants of Escherichia coli: protective role of superoxide dismutase. J. Bacteriol. 177 2305-14 PubMed GONUTS page
  12. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  13. Britton, L & Fridovich, I (1977) Intracellular localization of the superoxide dismutases of Escherichia coli: a reevaluation. J. Bacteriol. 131 815-20 PubMed GONUTS page
  14. Steinman, HM et al. (1994) The manganese superoxide dismutase of Escherichia coli K-12 associates with DNA. J. Biol. Chem. 269 28629-34 PubMed GONUTS page