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Protein

Superoxide dismutase [Mn/Fe]

Gene

sodA

Organism
Propionibacterium freudenreichii subsp. shermanii
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+, Fe2+Note: Binds 1 Mn2+ or Fe2+ ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi27 – 271Manganese or iron
Metal bindingi75 – 751Manganese or iron
Metal bindingi161 – 1611Manganese or iron
Metal bindingi165 – 1651Manganese or iron

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Iron, Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Mn/Fe] (EC:1.15.1.1)
Gene namesi
Name:sodA
OrganismiPropionibacterium freudenreichii subsp. shermanii
Taxonomic identifieri1752 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaPropionibacterialesPropionibacteriaceaePropionibacterium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 201201Superoxide dismutase [Mn/Fe]PRO_0000160066Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi754252.PFREUD_06110.

Structurei

Secondary structure

1
201
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni12 – 187Combined sources
Helixi21 – 299Combined sources
Helixi31 – 5222Combined sources
Helixi58 – 8023Combined sources
Helixi94 – 10411Combined sources
Helixi107 – 11913Combined sources
Beta strandi122 – 13211Combined sources
Turni133 – 1364Combined sources
Beta strandi137 – 1448Combined sources
Turni145 – 1473Combined sources
Beta strandi155 – 1617Combined sources
Helixi164 – 1663Combined sources
Helixi168 – 1714Combined sources
Helixi175 – 1839Combined sources
Helixi188 – 19710Combined sources
Turni198 – 2003Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AR4X-ray1.90A/B1-201[»]
1AR5X-ray1.60A/B1-201[»]
1AVMX-ray1.55A/B1-201[»]
1BS3X-ray1.55A/B1-201[»]
1BSMX-ray1.35A/B1-201[»]
1BT8X-ray1.85A/B1-201[»]
ProteinModelPortaliP80293.
SMRiP80293. Positions 1-201.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80293.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CK4. Bacteria.
COG0605. LUCA.

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.

P80293-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
AVYTLPELPY DYSALEPYIS GEIMELHHDK HHKAYVDGAN TALDKLAEAR
60 70 80 90 100
DKADFGAINK LEKDLAFNLA GHVNHSVFWK NMAPKGSAPE RPTDELGAAI
110 120 130 140 150
DEFFGSFDNM KAQFTAAATG IQGSGWASLV WDPLGKRINT LQFYDHQNNL
160 170 180 190 200
PAGSIPLLQL DMWEHAFYLQ YKNVKGDYVK SWWNVVNWDD VALRFSEARV

A
Length:201
Mass (Da):22,633
Last modified:February 1, 1994 - v1
Checksum:i5BFEF424C7B32E00
GO

Sequence databases

PIRiJC4396.

Cross-referencesi

Sequence databases

PIRiJC4396.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AR4X-ray1.90A/B1-201[»]
1AR5X-ray1.60A/B1-201[»]
1AVMX-ray1.55A/B1-201[»]
1BS3X-ray1.55A/B1-201[»]
1BSMX-ray1.35A/B1-201[»]
1BT8X-ray1.85A/B1-201[»]
ProteinModelPortaliP80293.
SMRiP80293. Positions 1-201.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi754252.PFREUD_06110.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CK4. Bacteria.
COG0605. LUCA.

Miscellaneous databases

EvolutionaryTraceiP80293.

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...

Entry informationi

Entry nameiSODM_PROFR
AccessioniPrimary (citable) accession number: P80293
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: September 7, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.