P15453 (SODC_BRUAB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Superoxide dismutase [Cu-Zn]
EC=1.15.1.1

Gene names

Name:	sodC
Ordered Locus Names:	BruAb2_0527

Organism

Brucella abortus biovar 1 (strain 9-941) [Complete proteome] [HAMAP]

Taxonomic identifier

262698 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	173 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 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 copper ion per subunit By similarity. Binds 1 zinc ion per subunit By similarity.
Subunit structure	Homodimer.
Subcellular location	Periplasm.
Sequence similarities	Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Ligand	Copper Metal-binding Zinc
Molecular function	Antioxidant Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	superoxide metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
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

Signal peptide

1 – 19

19

Ref.2

Chain

20 – 173

154

Superoxide dismutase [Cu-Zn]

PRO_0000032820

Sites

Metal binding

67

1

Copper; catalytic By similarity

Metal binding

69

1

Copper; catalytic By similarity

Metal binding

92

1

Copper; catalytic By similarity

Metal binding

92

1

Zinc; structural By similarity

Metal binding

101

1

Zinc; structural By similarity

Metal binding

109

1

Zinc; structural By similarity

Metal binding

112

1

Zinc; structural By similarity

Metal binding

147

1

Copper; catalytic By similarity

Amino acid modifications

Disulfide bond

74 ↔ 169

By similarity

Secondary structure

1

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173

Helix Strand Turn

Details...

Beta strand

21 – 30

10

Beta strand

33 – 44

12

Beta strand

49 – 56

8

Beta strand

61 – 64

4

Beta strand

66 – 72

7

Beta strand

77 – 79

3

Beta strand

82 – 84

3

Helix

87 – 89

3

Beta strand

106 – 108

3

Beta strand

116 – 118

3

Beta strand

124 – 130

7

Helix

136 – 139

4

Beta strand

142 – 149

8

Beta strand

153 – 158

6

Helix

159 – 162

4

Beta strand

165 – 172

8

Sequences

	Sequence		Length	Mass (Da)
	P15453 [UniParc]. Last modified June 21, 2005. Version 2. Checksum: BA78F7E0FB62C69A	FASTA	173	18,131
	10 20 30 40 50 60 MKSLFIASTM VLMAFPAFAE STTVKMYEAL PTGPGKEVGT VVISEAPGGL HFKVNMEKLT 70 80 90 100 110 120 PGYHGFHVHE NPSCAPGEKD GKIVPALAAG GHYDPGNTHH HLGPEGDGHM GDLPRLSANA 130 140 150 160 170 DGKVSETVVA PHLKKLAEIK QRSLMVHVGG DNYSDKPEPL GGGGARFACG VIE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis." Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C. J. Bacteriol. 187:2715-2726(2005) [PubMed: 15805518] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 9-941.
[2]	"A protein isolated from Brucella abortus is a Cu-Zn superoxide dismutase." Beck B.L., Tabatabai L.B., Mayfield J.E. Biochemistry 29:372-376(1990) [PubMed: 2105741] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-173.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE017224 Genomic DNA. Translation: AAX75946.1.

PIR

A33893.

RefSeq

YP_223307.1. NC_006933.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AQM	X-ray	1.10	A	20-173	[»]

ProteinModelPortal

P15453.

SMR

P15453. Positions 20-173.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3341416.

GenomeReviews

Gene locus BruAb2_0527 in contig AE017224_GR.

KEGG

bmb:BruAb2_0527.

PATRIC

17827316. VBIBruAbo15061_2836.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

HBG609879.

OMA

DKAGMND.

PhylomeDB

P15453.

ProtClustDB

CLSK898879.

Enzyme and pathway databases

BioCyc

BABO262698:BRUAB2_0527-MONOMER.

Family and domain databases

InterPro

IPR024136. SOD_Cu/Zn.
IPR024134. SOD_Cu/Zn_/chaperones.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]

Gene3D

G3DSA:2.60.40.200. SOD_Cu_Zn. 1 hit.

KO

K04565.

PANTHER

PTHR10003:SF11. PTHR10003:SF11. 1 hit.
PTHR10003. SOD_Cu_Zn. 1 hit.

Pfam

PF00080. Sod_Cu. 1 hit.
[Graphical view]

SUPFAM

SSF49329. SOD_Cu_Zn. 1 hit.

PROSITE

PS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SODC_BRUAB

Accession

Primary (citable) accession number: P15453
Secondary accession number(s): Q578I8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	June 21, 2005
Last modified:	January 25, 2012
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program