P80293 (SODM_PROFR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Superoxide dismutase [Mn/Fe]
EC=1.15.1.1

Gene names

Name:

sodA

Organism

Propionibacterium freudenreichii subsp. shermanii

Taxonomic identifier

1752 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Propionibacterineae › Propionibacteriaceae › Propionibacterium › Propionibacterium freudenreichii

Protein attributes

Sequence length	201 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Subunit structure	Homotetramer.
Sequence similarities	Belongs to the iron/manganese superoxide dismutase family.

Ontologies

Keywords
Ligand	Iron Manganese Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	superoxide metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	metal 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 201

201

Superoxide dismutase [Mn/Fe]

PRO_0000160066

Sites

Metal binding

27

1

Manganese or iron

Metal binding

75

1

Manganese or iron

Metal binding

161

1

Manganese or iron

Metal binding

165

1

Manganese or iron

Secondary structure

1

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201

Helix Strand Turn

Details...

Turn

12 – 18

7

Helix

21 – 29

9

Helix

31 – 52

22

Helix

58 – 80

23

Helix

94 – 104

11

Helix

107 – 119

13

Beta strand

122 – 132

11

Turn

133 – 136

4

Beta strand

137 – 144

8

Turn

145 – 147

3

Beta strand

155 – 161

7

Helix

164 – 166

3

Helix

168 – 171

4

Helix

175 – 183

9

Helix

188 – 197

10

Turn

198 – 200

3

Sequences

	Sequence		Length	Mass (Da)
	P80293 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: 5BFEF424C7B32E00	FASTA	201	22,633
	10 20 30 40 50 60 AVYTLPELPY DYSALEPYIS GEIMELHHDK HHKAYVDGAN TALDKLAEAR DKADFGAINK 70 80 90 100 110 120 LEKDLAFNLA GHVNHSVFWK NMAPKGSAPE RPTDELGAAI DEFFGSFDNM KAQFTAAATG 130 140 150 160 170 180 IQGSGWASLV WDPLGKRINT LQFYDHQNNL PAGSIPLLQL DMWEHAFYLQ YKNVKGDYVK 190 200 SWWNVVNWDD VALRFSEARV A

References

[1]	"In vivo incorporation of copper into the iron-exchangeable and manganese-exchangeable superoxide dismutase from Propionibacterium shermanii. Amino acid sequence and identity of the protein moieties." Meier B., Sehn A.P., Schinina M.E., Barra D. Eur. J. Biochem. 219:463-468(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: PZ3.
[2]	"X-ray structure of the cambialistic superoxide dismutase from Propionibacterium shermanii active with Fe or Mn." Schmidt M., Meier B., Parak F. J. Biol. Inorg. Chem. 1:532-541(1996) Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[3]	Schmidt M., Scherk C., Iakovleva O., Nolting H.F., Meier B., Parak F. Submitted (SEP-1997) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
[4]	"Manipulating the coordination mumber of the ferric iron within the cambialistic superoxide dismutase of Propionibacterium shermanii by changing the pH-value. A crystallographic analysis." Schmidt M. Eur. J. Biochem. 262:117-127(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).

Cross-references

Sequence databases

PIR

JC4396.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AR4	X-ray	1.90	A/B	1-201	[»]
1AR5	X-ray	1.60	A/B	1-201	[»]
1AVM	X-ray	1.55	A/B	1-201	[»]
1BS3	X-ray	1.55	A/B	1-201	[»]
1BSM	X-ray	1.35	A/B	1-201	[»]
1BT8	X-ray	1.85	A/B	1-201	[»]

ProteinModelPortal

P80293.

SMR

P80293. Positions 1-201.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]

PANTHER

PTHR11404. PTHR11404. 1 hit.

Pfam

PF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000349. SODismutase. 1 hit.

PRINTS

PR01703. MNSODISMTASE.

SUPFAM

SSF46609. SODismutase. 1 hit.
SSF54719. SODismutase. 1 hit.

PROSITE

PS00088. SOD_MN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P80293.

Entry information

Entry name

SODM_PROFR

Accession

Primary (citable) accession number: P80293

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	April 3, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program