Reviewed, UniProtKB/Swiss-Prot P0AGD3 (SODF_ECOLI)

Names and origin

Protein names

Recommended name:
    Superoxide dismutase [Fe]
    EC=1.15.1.1

Gene names

Name:	sodB
Ordered Locus Names:	b1656, JW1648

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	193 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 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 iron ion per subunit.
Subunit structure	Homodimer. Ref.11
Sequence similarities	Belongs to the iron/manganese superoxide dismutase family.

Ontologies

Keywords
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW superoxide metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB membrane Inferred from direct assay. Source: UniProtKB
Molecular function	iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW superoxide dismutase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5 Ref.7 Ref.8

Chain

2 – 193

192

Superoxide dismutase [Fe]

PRO_0000159979

Sites

Metal binding

27

1

Iron

Metal binding

74

1

Iron

Metal binding

157

1

Iron

Metal binding

161

1

Iron

Amino acid modifications

Modified residue

51

1

N6-acetyllysine Ref.10

Secondary structure

1

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193

Helix Strand Turn

Details...

Turn

12 – 18

7

Helix

21 – 29

9

Helix

31 – 43

13

Turn

47 – 50

4

Helix

53 – 57

5

Helix

62 – 79

18

Helix

91 – 101

11

Helix

104 – 117

14

Beta strand

120 – 128

9

Beta strand

134 – 140

7

Helix

145 – 147

3

Beta strand

151 – 157

7

Helix

160 – 162

3

Helix

164 – 167

4

Helix

171 – 179

9

Helix

184 – 192

9

Sequences

	Sequence		Length	Mass (Da)
	P0AGD3-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 91236D2A8FE61474	FASTA	193	21,266
	10 20 30 40 50 60 MSFELPALPY AKDALAPHIS AETIEYHYGK HHQTYVTNLN NLIKGTAFEG KSLEEIIRSS 70 80 90 100 110 120 EGGVFNNAAQ VWNHTFYWNC LAPNAGGEPT GKVAEAIAAS FGSFADFKAQ FTDAAIKNFG 130 140 150 160 170 180 SGWTWLVKNS DGKLAIVSTS NAGTPLTTDA TPLLTVDVWE HAYYIDYRNA RPGYLEHFWA 190 LVNWEFVAKN LAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Iron superoxide dismutase. Nucleotide sequence of the gene from Escherichia coli K12 and correlations with crystal structures." Carlioz A., Ludwig M.L., Stallings W.C., Fee J.A., Steinman H.M., Touati D. J. Biol. Chem. 263:1555-1562(1988) [PubMed: 2447093] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: K12.
[2]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:363-377(1996) [PubMed: 9097039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[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: 9278503] [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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"The primary structure of iron superoxide dismutase from Escherichia coli." Schinina M.E., Maffey L., Barra D., Bossa F., Puget K., Michelson A.M. FEBS Lett. 221:87-90(1987) [PubMed: 3305077] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-193.
[6]	"Sequence homologies among bacterial and mitochondrial superoxide dismutases." Steinman H.M., Hill R.L. Proc. Natl. Acad. Sci. U.S.A. 70:3725-3729(1973) [PubMed: 4590170] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE.
[7]	"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: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Strain: K12 / EMG2.
[8]	"Protein identification with N and C-terminal sequence tags in proteome projects." Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F. J. Mol. Biol. 278:599-608(1998) [PubMed: 9600841] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-5. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[9]	"Spectroscopic measurement of a long-predicted active site pK in iron-superoxide dismutase from Escherichia coli." Sorkin D.L., Miller A.-F. Biochemistry 36:4916-4924(1997) [PubMed: 9125513] [Abstract] Cited for: SPECTROSCOPIC MEASUREMENT OF ACTIVE SITE PK.
[10]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51, MASS SPECTROMETRY.
[11]	"Iron superoxide dismutase from Escherichia coli at 3.1-A resolution: a structure unlike that of copper/zinc protein at both monomer and dimer levels." Stallings W.C., Powers T.B., Pattridge K.A., Fee J.A., Ludwig M.L. Proc. Natl. Acad. Sci. U.S.A. 80:3884-3888(1983) [PubMed: 6346322] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH IRON ION, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

J03511 Genomic DNA. Translation: AAA24637.1.
U00096 Genomic DNA. Translation: AAC74728.1.
AP009048 Genomic DNA. Translation: BAA15422.1.

PIR

DSECF. A29940.

RefSeq

AP_002278.1.
NP_416173.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ISA	X-ray	1.80	A/B	1-193	[»]
1ISB	X-ray	1.85	A/B	1-193	[»]
1ISC	X-ray	1.80	A/B	1-193	[»]
1ZA5	X-ray	1.80	A/B	2-192	[»]
2BKB	X-ray	1.70	A/B/C/D	2-192	[»]
2NYB	X-ray	1.10	A/B/C/D	2-192	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0AGD3. 6 interactions.

STRING

P0AGD3.

2-D gel databases

SWISS-2DPAGE

P0AGD3.

ECO2DBASE

F021.3. 6TH EDITION.

Genome annotation databases

GeneID

944953.

GenomeReviews

Gene locus JW1648 in contig AP009048_GR.
Gene locus b1656 in contig U00096_GR.

KEGG

ecj:JW1648.
eco:b1656.

Organism-specific databases

EchoBASE

EB0947.

EcoGene

EG10954. sodB.

CMR

Search...

Phylogenomic databases

HOGENOM

HBG507761.

OMA

VNWKFAE.

Enzyme and pathway databases

BioCyc

EcoCyc:SUPEROX-DISMUTFE-MON.
ECOL168927:B1656-MON.
MetaCyc:SUPEROX-DISMUTFE-MON.

Gene expression databases

Genevestigator

P0AGD3.

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. SODismutase. 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.

PROSITE

PS00088. SOD_MN. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SODF_ECOLI

Accession

Primary (citable) accession number: P0AGD3
Secondary accession number(s): P09157

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	January 23, 2007
Last modified:	December 15, 2009
This is version 45 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)