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P09738 (SODM_STRMU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Superoxide dismutase [Mn/Fe]
EC=1.15.1.1
Gene names
Name:sodA
Synonyms:sod
Ordered Locus Names:SMU_629
OrganismStreptococcus mutans serotype c (strain ATCC 700610 / UA159) [Complete proteome] [HAMAP]
Taxonomic identifier210007 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus ›

Protein attributes

Sequence length203 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 or iron ion per subunit By similarity.

Sequence similarities

Belongs to the iron/manganese superoxide dismutase family.

Ontologies

Keywords
   LigandIron
Manganese
Metal-binding
   Molecular functionOxidoreductase
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processsuperoxide metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionmetal 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 203202Superoxide dismutase [Mn/Fe]
PRO_0000160094

Sites

Metal binding271Manganese or iron By similarity
Metal binding811Manganese or iron By similarity
Metal binding1631Manganese or iron By similarity
Metal binding1671Manganese or iron By similarity

Experimental info

Sequence conflict41L → T AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
P09738 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: CC86C35928C415A6

FASTA20322,626
        10         20         30         40         50         60 
MAILLPDLPY AYDALEPYID AETMTLHHDK HHATYVANAN AALEKHPEIG ENLEVLLADV 

        70         80         90        100        110        120 
EQIPADIRQS LINNGGGHLN HALFWELLSP EKTKVTAEVA AAINEAFGSF DDFKAAFTAA 

       130        140        150        160        170        180 
ATTRFGSGWA WLVVDKEGKL EVTSTANQDT PISQGLKPIL ALDVWEHAYY LNYRNVRPNY 

       190        200 
IKAFFEVINW NTVARLYAEA LTK

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of Streptococcus mutans superoxide dismutase gene and isolation of insertion mutants."
Nakayama K.
J. Bacteriol. 174:4928-4934(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: GS-5.
[2]"Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen."
Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.
Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700610 / UA159.
[3]"A Streptococcus mutans superoxide dismutase that is active with either manganese or iron as a cofactor."
Martin M.E., Byers B.R., Olson M.O.J., Salin M.L., Arceneaux J.E.L., Tolbert C.
J. Biol. Chem. 261:9361-9367(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-23.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D01037 Genomic DNA. Translation: BAB86870.1.
AE014133 Genomic DNA. Translation: AAN58363.1.
PIRA42710.
RefSeqNP_721057.1. NC_004350.2.
YP_006489870.1. NC_018089.1.

3D structure databases

ProteinModelPortalP09738.
SMRP09738. Positions 5-199.
ModBaseSearch...

Protein-protein interaction databases

STRING210007.SMU.629.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN58363; AAN58363; SMU_629.
GeneID1029605.
13299631.
KEGGsmu:SMU_629.
smut:SMUGS5_02755.
PATRIC19663445. VBIStrMut61772_0555.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0605.
KOK04564.
OMAETMTIHH.
ProtClustDBCLSK2756239.

Family and domain databases

InterProIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERPTHR11404. PTHR11404. 1 hit.
PfamPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFPIRSF000349. SODismutase. 1 hit.
PRINTSPR01703. MNSODISMTASE.
SUPFAMSSF46609. SODismutase. 1 hit.
SSF54719. SODismutase. 1 hit.
PROSITEPS00088. SOD_MN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSODM_STRMU
AccessionPrimary (citable) accession number: P09738
Secondary accession number(s): Q59791
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 102 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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