RegulonDB

Gene
Name:	sodA
Synonym(s):	ECK3901, EG10953, b3908
Genome position(nucleotides):	4100810 --> 4101430
Strand:	forward
Sequence:	Get nucleotide sequence FastaFormat
GC content %:	53.3
External database links:

ASAP:	ABE-0012761
CGSC:	17593
ECHOBASE:	EB0946
ECOLIHUB:	sodA
MIM:	612634
OU-MICROARRAY:	b3908
STRING:	511145.b3908
COLOMBOS:	sodA

Gene

Name:

sodA

Synonym(s):

ECK3901, EG10953, b3908

Genome position(nucleotides):

4100810 --> 4101430

Strand:

forward

Sequence:

Get nucleotide sequence FastaFormat

GC content %:

53.3

External database links:

ASAP:

CGSC:

ECHOBASE:

ECOLIHUB:

MIM:

OU-MICROARRAY:

STRING:

COLOMBOS:

Product

Name:

superoxide dismutase (Mn)

Synonym(s):

MnSOD, SodA

Sequence:

Get amino acid sequence Fasta Format

Cellular location:

cytosol

Molecular weight:

23.097

Isoelectric point:

6.971

Motif(s):

Type	Positions	Sequence	Comment
	2 -> 206	SYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPEFANLPVEELITKLDQLPADKKTVLRNNAGGHANHSLFWKGLKKGTTLQGDLKAAIERDFGSVDNFKAEFEKAAASRFGSGWAWLVLKGDKLAVVSTANQDSPLMGEAISGASGFPIMGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAAKK	UniProt: Superoxide dismutase [Mn].
	81 -> 82	NH	UniProt: In Ref. 6..
	96 -> 201	QGDLKAAIERDFGSVDNFKAEFEKAAASRFGSGWAWLVLKGDKLAVVSTANQDSPLMGEAISGASGFPIMGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAAR
	165 -> 165	M	UniProt: In strain: B..

Classification:

Multifun Terms (GenProtEC)
Multifun Terms (GenProtEC)		5 - cell processes --> 5.6 - protection --> 5.6.2 - detoxification
Gene Ontology Terms (GO)
	cellular_component	GO:0005737 - cytoplasm GO:0005829 - cytosol
	molecular_function	GO:0003677 - DNA binding GO:0046872 - metal ion binding GO:0016491 - oxidoreductase activity GO:0016209 - antioxidant activity GO:0004784 - superoxide dismutase activity GO:0030145 - manganese ion binding GO:0042803 - protein homodimerization activity
	biological_process	GO:0006979 - response to oxidative stress GO:0009408 - response to heat GO:0006801 - superoxide metabolic process GO:0019430 - removal of superoxide radicals GO:0010447 - response to acidic pH GO:0071291 - cellular response to selenium ion

Note(s):

Note(s): ...[more].

Reference(s):

[1] Baez A., et al., 2013
[2] Bertrand R., et al., 2012
[3] Chaithawiwat K., et al., 2016
[4] Clares MP., et al., 2015
[5] Gardner PR., et al., 1987
[6] Gomez-Sagasti MT., et al., 2014
[7] Gravina F., et al., 2017
[8] Kahrstrom CT. 2012
[9] Lin CN., et al., 2010
[10] Privalle CT., et al., 1989
[11] Privalle CT., et al., 1992
[12] Privalle CT., et al., 1990
[13] Privalle CT., et al., 1988
[14] Rodriguez-Moya M., et al., 2015
[15] Sharma A., et al., 2013
[16] Smolik AC., et al., 2014
[17] Sun H., et al., 2016
[18] Tetteh AY., et al., 2014
[19] Wang JH., et al., 2014
[20] Yost AD., et al., 2015

External database links:

ALPHAFOLD:

P00448

ECOCYC:

SUPEROX-DISMUTMN-MONOMER

ECOLIWIKI:

INTERPRO:

INTERPRO:

INTERPRO:

INTERPRO:

INTERPRO:

INTERPRO:

MODBASE:

PDB:

PDB:

PDB:

PDB:

PDB:

PDB:

PDB:

PDB:

PDB:

PDB:

PDB:

PDB:

PDB:

PFAM:

PFAM:

PRIDE:

PRINTS:

PRODB:

PROSITE:

REFSEQ:

SMR:

UNIPROT:

Transcriptional Regulation
	Display Regulation
Activated by:	SoxR, CRP, MarA, Rob, SoxS
Repressed by:	Fur, FNR, IHF, ArcA

Transcriptional Regulation

Display Regulation

Activated by:

SoxR, CRP, MarA, Rob, SoxS

Repressed by:

Fur, FNR, IHF, ArcA

RNA cis-regulatory element

Attenuation:	Translational

RNA cis-regulatory element

Attenuation:

Translational

Reference(s)
[1] Baez A., Shiloach J., 2013, Escherichia coli avoids high dissolved oxygen stress by activation of SoxRS and manganese-superoxide dismutase., Microb Cell Fact 12:23
[2] Bertrand R., Danielson D., Gong V., Olynik B., Eze MO., 2012, Sodium nitroprusside may modulate Escherichia coli antioxidant enzyme expression by interacting with the ferric uptake regulator., Med Hypotheses 78(1):130-3
[3] Chaithawiwat K., Vangnai A., McEvoy JM., Pruess B., Krajangpan S., Khan E., 2016, Role of oxidative stress in inactivation of Escherichia coli BW25113 by nanoscale zero-valent iron., Sci Total Environ 565:857-862
[4] Clares MP., Serena C., Blasco S., Nebot A., del Castillo L., Soriano C., Domenech A., Sanchez-Sanchez AV., Soler-Calero L., Mullor JL., Garcia-Espana A., Garcia-Espana E., 2015, Mn(II) complexes of scorpiand-like ligands. A model for the MnSOD active centre with high in vitro and in vivo activity., J Inorg Biochem 143:1-8
[5] Gardner PR., Fridovich I., 1987, Controls on the biosynthesis of the manganese-containing superoxide dismutase of Escherichia coli. Effects of thiols., J Biol Chem 262(36):17591-5
[6] Gomez-Sagasti MT., Becerril JM., Martin I., Epelde L., Garbisu C., 2014, cDNA microarray assessment of early gene expression profiles in Escherichia coli cells exposed to a mixture of heavy metals., Cell Biol Toxicol 30(4):207-32
[7] Gravina F., Dobrzanski T., Olchanheski LR., Galvao CW., Reche PM., Pileggi SA., Azevedo RA., Sadowsky MJ., Pileggi M., 2017, Metabolic Interference of sod gene mutations on catalase activity in Escherichia coli exposed to Gramoxone® (paraquat) herbicide., Ecotoxicol Environ Saf 139:89-96
[8] Kahrstrom CT., 2012, Cellular microbiology: Ironing out Hfq regulation., Nat Rev Microbiol 10(5):310-1
[9] Lin CN., Syu WJ., Sun WS., Chen JW., Chen TH., Don MJ., Wang SH., 2010, A role of ygfZ in the Escherichia coli response to plumbagin challenge., J Biomed Sci 17:84
[10] Privalle CT., Beyer WF., Fridovich I., 1989, Anaerobic induction of ProMn-superoxide dismutase in Escherichia coli., J Biol Chem 264(5):2758-63
[11] Privalle CT., Fridovich I., 1992, Transcriptional and maturational effects of manganese and iron on the biosynthesis of manganese-superoxide dismutase in Escherichia coli., J Biol Chem 267(13):9140-5
[12] Privalle CT., Fridovich I., 1990, Anaerobic biosynthesis of the manganese-containing superoxide dismutase in Escherichia coli. Effects of diazenedicarboxylic acid bis(N,N'-dimethylamide) (diamide)., J Biol Chem 265(35):21966-70
[13] Privalle CT., Fridovich I., 1988, Inductions of superoxide dismutases in Escherichia coli under anaerobic conditions. Accumulation of an inactive form of the manganese enzyme., J Biol Chem 263(9):4274-9
[14] Rodriguez-Moya M., Gonzalez R., 2015, Proteomic analysis of the response of Escherichia coli to short-chain fatty acids., J Proteomics 122:86-99
[15] Sharma A., Gaidamakova EK., Matrosova VY., Bennett B., Daly MJ., Hoffman BM., 2013, Responses of Mn2+ speciation in Deinococcus radiodurans and Escherichia coli to γ-radiation by advanced paramagnetic resonance methods., Proc Natl Acad Sci U S A 110(15):5945-50
[16] Smolik AC., Bengez-Pudja L., Cheng I., Mascotti DP., 2014, Characterization of E. coli manganese superoxide dismutase binding to RNA and DNA., Biochim Biophys Acta 1844(12):2251-6
[17] Sun H., Li G., An T., Zhao H., Wong PK., 2016, Unveiling the photoelectrocatalytic inactivation mechanism of Escherichia coli: Convincing evidence from responses of parent and anti-oxidation single gene knockout mutants., Water Res 88:135-143
[18] Tetteh AY., Sun KH., Hung CY., Kittur FS., Ibeanu GC., Williams D., Xie J., 2014, Transcriptional Response of Selenopolypeptide Genes and Selenocysteine Biosynthesis Machinery Genes in Escherichia coli during Selenite Reduction., Int J Microbiol 394835
[19] Wang JH., Singh R., Benoit M., Keyhan M., Sylvester M., Hsieh M., Thathireddy A., Hsieh YJ., Matin AC., 2014, Sigma S-dependent antioxidant defense protects stationary-phase Escherichia coli against the bactericidal antibiotic gentamicin., Antimicrob Agents Chemother 58(10):5964-75
[20] Yost AD., Joshi SG., 2015, Atmospheric Nonthermal Plasma-Treated PBS Inactivates Escherichia coli by Oxidative DNA Damage., PLoS One 10(10):e0139903

Reference(s)

[1] Baez A., Shiloach J., 2013, Escherichia coli avoids high dissolved oxygen stress by activation of SoxRS and manganese-superoxide dismutase., Microb Cell Fact 12:23