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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)DescriptionActionsGraphical viewLength
Metal bindingi27Manganese or iron1
Metal bindingi75Manganese or iron1
Metal bindingi161Manganese or iron1
Metal bindingi165Manganese or iron1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001600661 – 201Superoxide dismutase [Mn/Fe]Add BLAST201

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi754252.PFREUD_06110.

Structurei

Secondary structure

1201
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni12 – 18Combined sources7
Helixi21 – 29Combined sources9
Helixi31 – 52Combined sources22
Helixi58 – 80Combined sources23
Helixi94 – 104Combined sources11
Helixi107 – 119Combined sources13
Beta strandi122 – 132Combined sources11
Turni133 – 136Combined sources4
Beta strandi137 – 144Combined sources8
Turni145 – 147Combined sources3
Beta strandi155 – 161Combined sources7
Helixi164 – 166Combined sources3
Helixi168 – 171Combined sources4
Helixi175 – 183Combined sources9
Helixi188 – 197Combined sources10
Turni198 – 200Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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
PDB 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.
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: November 2, 2016
This is version 90 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.