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Protein

Superoxide dismutase [Mn/Fe]

Gene

sodA

Organism
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Mn2+By similarity, Fe2+By similarityNote: Binds 1 Mn2+ or Fe2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi27 – 271Manganese or ironBy similarity
Metal bindingi81 – 811Manganese or ironBy similarity
Metal bindingi163 – 1631Manganese or ironBy similarity
Metal bindingi167 – 1671Manganese or ironBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Iron, Manganese, Metal-binding

Enzyme and pathway databases

BioCyciSMUT210007:GC7Z-613-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Mn/Fe] (EC:1.15.1.1)
Gene namesi
Name:sodA
Synonyms:sod
Ordered Locus Names:SMU_629
OrganismiStreptococcus mutans serotype c (strain ATCC 700610 / UA159)
Taxonomic identifieri210007 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000002512 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 203202Superoxide dismutase [Mn/Fe]PRO_0000160094Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi210007.SMU_629.

Structurei

Secondary structure

1
203
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni12 – 187Combined sources
Helixi21 – 299Combined sources
Helixi31 – 4515Combined sources
Helixi47 – 493Combined sources
Helixi53 – 586Combined sources
Helixi59 – 624Combined sources
Helixi65 – 8723Combined sources
Helixi97 – 10711Combined sources
Helixi110 – 12314Combined sources
Beta strandi126 – 1349Combined sources
Beta strandi140 – 1467Combined sources
Helixi151 – 1544Combined sources
Beta strandi157 – 1637Combined sources
Helixi166 – 1683Combined sources
Helixi170 – 1734Combined sources
Helixi177 – 1848Combined sources
Helixi185 – 1873Combined sources
Helixi190 – 20213Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4YIPX-ray2.15A/B/C/D1-202[»]
ProteinModelPortaliP09738.
SMRiP09738. Positions 5-199.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CK4. Bacteria.
COG0605. LUCA.
KOiK04564.
OMAiVIDWVEV.
OrthoDBiEOG63NMNT.
PhylomeDBiP09738.

Family and domain databases

InterProiIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERiPTHR11404. PTHR11404. 1 hit.
PfamiPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000349. SODismutase. 1 hit.
PRINTSiPR01703. MNSODISMTASE.
SUPFAMiSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEiPS00088. SOD_MN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09738-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAILLPDLPY AYDALEPYID AETMTLHHDK HHATYVANAN AALEKHPEIG
60 70 80 90 100
ENLEVLLADV EQIPADIRQS LINNGGGHLN HALFWELLSP EKTKVTAEVA
110 120 130 140 150
AAINEAFGSF DDFKAAFTAA ATTRFGSGWA WLVVDKEGKL EVTSTANQDT
160 170 180 190 200
PISQGLKPIL ALDVWEHAYY LNYRNVRPNY IKAFFEVINW NTVARLYAEA

LTK
Length:203
Mass (Da):22,626
Last modified:January 23, 2007 - v3
Checksum:iCC86C35928C415A6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41L → T AA sequence (PubMed:3722201).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D01037 Genomic DNA. Translation: BAB86870.1.
AE014133 Genomic DNA. Translation: AAN58363.1.
PIRiA42710.
RefSeqiNP_721057.1. NC_004350.2.
WP_002261912.1. NC_004350.2.

Genome annotation databases

EnsemblBacteriaiAAN58363; AAN58363; SMU_629.
GeneIDi1029605.
KEGGismu:SMU_629.
PATRICi19663445. VBIStrMut61772_0555.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D01037 Genomic DNA. Translation: BAB86870.1.
AE014133 Genomic DNA. Translation: AAN58363.1.
PIRiA42710.
RefSeqiNP_721057.1. NC_004350.2.
WP_002261912.1. NC_004350.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4YIPX-ray2.15A/B/C/D1-202[»]
ProteinModelPortaliP09738.
SMRiP09738. Positions 5-199.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi210007.SMU_629.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN58363; AAN58363; SMU_629.
GeneIDi1029605.
KEGGismu:SMU_629.
PATRICi19663445. VBIStrMut61772_0555.

Phylogenomic databases

eggNOGiENOG4105CK4. Bacteria.
COG0605. LUCA.
KOiK04564.
OMAiVIDWVEV.
OrthoDBiEOG63NMNT.
PhylomeDBiP09738.

Enzyme and pathway databases

BioCyciSMUT210007:GC7Z-613-MONOMER.

Family and domain databases

InterProiIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERiPTHR11404. PTHR11404. 1 hit.
PfamiPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000349. SODismutase. 1 hit.
PRINTSiPR01703. MNSODISMTASE.
SUPFAMiSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEiPS00088. SOD_MN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiSODM_STRMU
AccessioniPrimary (citable) accession number: P09738
Secondary accession number(s): Q59791
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: April 13, 2016
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.