Superoxide dismutase [Mn] - Escherichia coli (strain K12)

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P00448 (SODM_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 141. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Superoxide dismutase [Mn]
EC=1.15.1.1

Alternative name(s):
MnSOD

Gene names

Name:	sodA
Ordered Locus Names:	b3908, JW3879

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	206 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic activity	2 superoxide + 2 H⁺ = O₂ + H₂O₂.
Cofactor	Binds 1 manganese ion per subunit.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the iron/manganese superoxide dismutase family.

Ontologies

Keywords
Ligand	Manganese Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to selenium ion Inferred from expression pattern PubMed 11872706. Source: EcoCyc removal of superoxide radicals Inferred from direct assay PubMed 4943714. Source: EcoliWiki response to acidity Inferred from mutant phenotype PubMed 20305033. Source: EcoCyc response to heat Inferred from mutant phenotype PubMed 7768839. Source: EcoCyc
Cellular_component	cytoplasm Inferred from direct assay PubMed 4580575. Source: EcoliWiki
Molecular_function	DNA binding Inferred from direct assay PubMed 7961811. Source: EcoCyc manganese ion binding Inferred from direct assay PubMed 9220980 PubMed 9548935. Source: EcoCyc superoxide dismutase activity Inferred from direct assay PubMed 330499. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.5 Ref.9 Ref.10

Chain

2 – 206

205

Superoxide dismutase [Mn]

PRO_0000160030

Sites

Metal binding

Manganese

Metal binding

Manganese

Metal binding

168

Manganese

Metal binding

172

Manganese

Natural variations

Natural variant

165

M → L in strain: B.

Experimental info

Sequence conflict

81 – 82

NH → HN Ref.6

Secondary structure

206

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P00448 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 082DAF56EA3C15CC
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FASTA

206

23,097

        10         20         30         40         50         60 
MSYTLPSLPY AYDALEPHFD KQTMEIHHTK HHQTYVNNAN AALESLPEFA NLPVEELITK 

        70         80         90        100        110        120 
LDQLPADKKT VLRNNAGGHA NHSLFWKGLK KGTTLQGDLK AAIERDFGSV DNFKAEFEKA 

       130        140        150        160        170        180 
AASRFGSGWA WLVLKGDKLA VVSTANQDSP LMGEAISGAS GFPIMGLDVW EHAYYLKFQN 

       190        200 
RRPDYIKEFW NVVNWDEAAA RFAAKK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and gene expression of the E. coli Mn-superoxide dismutase gene." Takeda Y., Avila H. Nucleic Acids Res. 14:4577-4589(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes." Plunkett G. III, Burland V., Daniels D.L., Blattner F.R. Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"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.
[5]	"The amino acid sequence of mangano superoxide dismutase from Escherichia coli B." Steinman H.M. J. Biol. Chem. 253:8708-8720(1978) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-206. Strain: B.
[6]	"Nucleotide sequence of the rhaR-sodA interval specifying rhaT in Escherichia coli." Garcia C., Baldoma L., Badia J., Aguilar J. J. Gen. Microbiol. 138:1109-1116(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-96. Strain: K12.
[7]	"Mapping, cloning, expression, and sequencing of the rhaT gene, which encodes a novel L-rhamnose-H+ transport protein in Salmonella typhimurium and Escherichia coli." Tate C.G., Muiry J.A.R., Henderson P.J.F. J. Biol. Chem. 267:6923-6932(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-63. Strain: K12.
[8]	"Transcriptional and posttranscriptional regulation of manganese superoxide dismutase biosynthesis in Escherichia coli, studied with operon and protein fusions." Touati D. J. Bacteriol. 170:2511-2520(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-2.
[9]	Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F. Submitted (SEP-1994) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-11. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[10]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Strain: K12 / EMG2.
[11]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[12]	"Outer sphere mutations perturb metal reactivity in manganese superoxide dismutase." Edwards R.A., Whittaker M.M., Whittaker J.W., Baker E.N., Jameson G.B. Biochemistry 40:15-27(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS PHE-35; LEU-147 AND HIS-147.
[13]	"Removing a hydrogen bond in the dimer interface of Escherichia coli manganese superoxide dismutase alters structure and reactivity." Edwards R.A., Whittaker M.M., Whittaker J.W., Baker E.N., Jameson G.B. Biochemistry 40:4622-4632(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF MUTANTS ALA-31 AND PHE-175.
[14]	"Paramagnetic NMR spectroscopy of native and cobalt substituted manganese superoxide dismutase from Escherichia coli." Renault J.P., Verchere-Beau R., Morgenstern-Badarau I., Piccioli M. FEBS Lett. 401:15-19(1997) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[15]	"Crystal structure of Escherichia coli manganese superoxide dismutase at 2.1-A resolution." Edwards R.A., Baker H.M., Whittaker M.M., Whittaker J.W., Jameson G.B., Baker E.N. J. Biol. Inorg. Chem. 3:161-171(1998) Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[16]	"Cryo-trapping the six-coordinate, distorted-octahedral active site of manganese superoxide dismutase." Borgstahl G.E., Pokross M., Chehab R., Sekher A., Snell E.H. J. Mol. Biol. 296:951-959(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X03951 Genomic DNA. Translation: CAA27580.1.
M20984 Genomic DNA. No translation available.
L19201 Genomic DNA. Translation: AAB03041.1.
U00096 Genomic DNA. Translation: AAC76890.1.
AP009048 Genomic DNA. Translation: BAE77401.1.
X60699 Genomic DNA. Translation: CAA43108.1.
M85158 Genomic DNA. Translation: AAA24528.1. Sequence problems.

PIR

DSECN. A24141.

RefSeq

NP_418344.3. NC_000913.2.
YP_491542.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D5N	X-ray	1.55	A/B/C/D	2-206	[»]
1EN4	X-ray	2.00	A/B/C/D	2-206	[»]
1EN5	X-ray	2.30	A/B/C/D	2-206	[»]
1EN6	X-ray	2.00	A/B/C/D	2-206	[»]
1I08	X-ray	2.20	A/B/C/D	2-206	[»]
1I0H	X-ray	1.35	A/B	2-206	[»]
1IX9	X-ray	0.90	A/B	2-206	[»]
1IXB	X-ray	0.90	A/B	2-206	[»]
1MMM	X-ray	2.20	A/B	2-206	[»]
1VEW	X-ray	2.10	A/B/C/D	2-206	[»]
1ZLZ	X-ray	1.55	A/B	2-206	[»]
3K9S	X-ray	1.55	A/B/C/D	2-206	[»]
3OT7	X-ray	1.90	A/B/C/D	2-206	[»]

ProteinModelPortal

P00448.

SMR

P00448. Positions 2-206.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00448. 7 interactions.

STRING

511145.b3908.

2D gel databases

SWISS-2DPAGE

P00448.

Proteomic databases

PaxDb

P00448.

PRIDE

P00448.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76890; AAC76890; b3908.
BAE77401; BAE77401; BAE77401.

GeneID

12933233.
948403.

KEGG

ecj:Y75_p3278.
eco:b3908.

PATRIC

32123327. VBIEscCol129921_4024.

Organism-specific databases

EchoBASE

EB0946.

EcoGene

EG10953. sodA.

Phylogenomic databases

eggNOG

COG0605.

HOGENOM

HOG000013583.

K04564.

OMA

ETMTIHH.

ProtClustDB

PRK10925.

Enzyme and pathway databases

BioCyc

EcoCyc:SUPEROX-DISMUTMN-MONOMER.
ECOL316407:JW3879-MONOMER.
MetaCyc:SUPEROX-DISMUTMN-MONOMER.

Gene expression databases

Genevestigator

P00448.

Family and domain databases

InterPro

IPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]

PANTHER

PTHR11404. PTHR11404. 1 hit.

Pfam

PF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000349. SODismutase. 1 hit.

PRINTS

PR01703. MNSODISMTASE.

SUPFAM

SSF46609. SODismutase. 1 hit.
SSF54719. SODismutase. 1 hit.

PROSITE

PS00088. SOD_MN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00448.

Entry information

Entry name

SODM_ECOLI

Accession

Primary (citable) accession number: P00448
Secondary accession number(s): Q2M8K5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 141 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents