Q9RUV2 (SODM_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Superoxide dismutase [Mn]
EC=1.15.1.1

Alternative name(s):
MnSOD

Gene names

Name:	sodA
Ordered Locus Names:	DR_1279

Organism

Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) [Reference proteome] [HAMAP]

Taxonomic identifier

243230 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus › Deinococcus radiodurans

Protein attributes

Sequence length	211 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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 By similarity.
Catalytic activity	2 superoxide + 2 H+ = O2 + H2O2.
Cofactor	Binds 1 manganese ion per subunit By similarity.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the iron/manganese superoxide dismutase family.

Ontologies

Keywords
Ligand	Manganese Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
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

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 211

210

Superoxide dismutase [Mn]

PRO_0000160029

Sites

Metal binding

27

1

Manganese By similarity

Metal binding

81

1

Manganese By similarity

Metal binding

173

1

Manganese By similarity

Metal binding

177

1

Manganese By similarity

Secondary structure

1

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211

Helix Strand Turn

Details...

Turn

12 – 18

7

Helix

21 – 29

9

Helix

31 – 43

13

Turn

47 – 50

4

Helix

53 – 56

4

Turn

60 – 62

3

Helix

65 – 67

3

Helix

68 – 86

19

Helix

102 – 112

11

Helix

115 – 128

14

Beta strand

131 – 140

10

Beta strand

143 – 150

8

Helix

155 – 157

3

Helix

159 – 162

4

Beta strand

166 – 173

8

Helix

176 – 178

3

Helix

180 – 183

4

Helix

187 – 194

8

Helix

195 – 197

3

Helix

200 – 210

11

Sequences

	Sequence		Length	Mass (Da)
	Q9RUV2 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: A71F22F516A1897E	FASTA	211	23,478
	10 20 30 40 50 60 MAYTLPQLPY AYDALEPHID ARTMEIHHTK HHQTYVDNAN KALEGTEFAD LPVEQLIQQL 70 80 90 100 110 120 DRVPADKKGA LRNNAGGHAN HSMFWQIMGQ GQGQNGANQP SGELLDAINS AFGSFDAFKQ 130 140 150 160 170 180 KFEDAAKTRF GSGWAWLVVK DGKLDVVSTA NQDNPLMGEA IAGVSGTPIL GVDVWEHAYY 190 200 210 LNYQNRRPDY LAAFWNVVNW DEVSKRYAAA K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1." White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., Vamathevan J.J., Lam P. , McDonald L.A., Utterback T.R., Zalewski C., Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D., Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Science 286:1571-1577(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
[2]	Joshi B.S., Apte S.K., Schmid R., Altendorf K. Submitted (APR-2003) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-13. Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000513 Genomic DNA. Translation: AAF10851.1.

PIR

B75415.

RefSeq

NP_295003.1. NC_001263.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Y67	X-ray	1.85	A/B/C/D	2-210	[»]
2AW9	X-ray	2.70	A/B	2-210	[»]
2CDY	X-ray	2.00	A/B/C/D	2-211	[»]
2CE4	X-ray	2.20	A/B	2-211	[»]
3KKY	X-ray	1.80	A/B	1-211	[»]

ProteinModelPortal

Q9RUV2.

SMR

Q9RUV2. Positions 2-211.

ModBase

Search...

Protein-protein interaction databases

STRING

243230.DR_1279.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAF10851; AAF10851; DR_1279.

GeneID

1797407.

KEGG

dra:DR_1279.

PATRIC

21630152. VBIDeiRad64572_1475.

Phylogenomic databases

eggNOG

COG0605.

HOGENOM

HOG000013583.

KO

K04564.

OMA

ETMTIHH.

ProtClustDB

CLSK444979.

Enzyme and pathway databases

BioCyc

DRAD243230:GH46-1649-MONOMER.

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

Q9RUV2.

Entry information

Entry name

SODM_DEIRA

Accession

Primary (citable) accession number: Q9RUV2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2003
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 92 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program