Superoxide dismutase [Ni] precursor - Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)

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P80735 (SODN_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 88. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Superoxide dismutase [Ni]
EC=1.15.1.1

Alternative name(s):
NiSOD
Nickel-containing superoxide dismutase

Gene names

Name:	sodN
Synonyms:	sod1
Ordered Locus Names:	SCO5254
ORF Names:	2SC7G11.16c

Organism

Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]

Taxonomic identifier

100226 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces ›

Protein attributes

Sequence length	131 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)

Catalytic activity	2 superoxide + 2 H⁺ = O₂ + H₂O₂.
Cofactor	Nickel.
Subunit structure	Homohexamer. The hexameric protein has a roughly the shape of a hollow sphere with an outer diameter of 60 angstroms and a large interior cavity. Ref.5
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the nickel superoxide dismutase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Nickel
Molecular function	Antioxidant Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	nickel cation binding Inferred from electronic annotation. Source: InterPro 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

Propeptide

1 – 14

PRO_0000032906

Chain

15 – 131

117

Superoxide dismutase [Ni]

PRO_0000032907

Sites

Metal binding

Nickel; catalytic

Metal binding

Nickel; catalytic

Metal binding

Nickel; catalytic

Experimental info

Sequence conflict

C → G AA sequence Ref.3

Sequence conflict

C → G AA sequence Ref.4

Sequence conflict

C → G AA sequence Ref.3

Sequence conflict

C → G AA sequence Ref.4

Secondary structure

131

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P80735 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 8DA21AFBAC0D7EF6
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FASTA

131

14,703

        10         20         30         40         50         60 
MLSRLFAPKV TVSAHCDLPC GVYDPAQARI EAESVKAVQE KMAGNDDPHF QTRATVIKEQ 

        70         80         90        100        110        120 
RAELAKHHVS VLWSDYFKPP HFEKYPELHQ LVNDTLKALS AAKGSKDPAT GQKALDYIAQ 

       130 
IDKIFWETKK A

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Transcriptional and post-transcriptional regulation by nickel of sodN gene encoding nickel-containing superoxide dismutase from Streptomyces coelicolor Muller." Kim E.-J., Chung H.-J., Suh B., Hah Y.C., Roe J.-H. Mol. Microbiol. 27:187-195(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 10147 / DSM 41007 / JCM 4020 / NBRC 3176 / KCC S-0020 and ATCC BAA-471 / A3(2) / M145.
[2]	"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)." Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. Hopwood D.A. Nature 417:141-147(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-471 / A3(2) / M145.
[3]	"A novel nickel-containing superoxide dismutase from Streptomyces spp." Youn H.-D., Kim E.-J., Roe J.-H., Hah Y.C., Kang S.-O. Biochem. J. 318:889-896(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 15-28. Strain: ATCC 10147 / DSM 41007 / JCM 4020 / NBRC 3176 / KCC S-0020.
[4]	"Differential expression of superoxide dismutases containing Ni and Fe/Zn in Streptomyces coelicolor." Kim F.-J., Kim H.-P., Hah Y.V., Roe J.-H. Eur. J. Biochem. 241:178-185(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 15-28. Strain: ATCC 10147 / DSM 41007 / JCM 4020 / NBRC 3176 / KCC S-0020.
[5]	"Nickel superoxide dismutase structure and mechanism." Barondeau D.P., Kassmann C.J., Bruns C.K., Tainer J.A., Getzoff E.D. Biochemistry 43:8038-8047(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 15-131 IN COMPLEX WITH NICKEL IONS, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF012193 Genomic DNA. Translation: AAC38082.1.
AF104994 Genomic DNA. Translation: AAF25537.1.
AL939123 Genomic DNA. Translation: CAC05965.1.

RefSeq

NP_629400.1. NC_003888.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1T6I	X-ray	2.81	A/B/C	15-131	[»]
1T6Q	X-ray	2.05	A/B/C	15-131	[»]
1T6U	X-ray	1.30	A/B/C/D/E/F/G/H/I/J/K/L	15-131	[»]
3G4X	X-ray	2.01	A/B/C	15-131	[»]
3G4Z	X-ray	1.87	A/B/C	15-131	[»]
3G50	X-ray	1.90	A/B/C	15-131	[»]

ProteinModelPortal

P80735.

SMR

P80735. Positions 15-131.

ModBase

Search...

Protein-protein interaction databases

STRING

100226.SCO5254.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAC05965; CAC05965; CAC05965.

GeneID

1100695.

KEGG

sco:SCO5254.

PATRIC

23740360. VBIStrCoe124346_5338.

Phylogenomic databases

eggNOG

NOG39351.

HOGENOM

HOG000020289.

K00518.

OMA

WTDYFKP.

ProtClustDB

CLSK902881.

Family and domain databases

Gene3D

1.20.120.400. 1 hit.

InterPro

IPR014123. Superoxide_dismutase_Ni-type.
[Graphical view]

Pfam

PF09055. Sod_Ni. 1 hit.
[Graphical view]

SUPFAM

SSF109770. Superoxide_dismutase_Ni-type. 1 hit.

TIGRFAMs

TIGR02753. sodN. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P80735.

Entry information

Entry name

SODN_STRCO

Accession

Primary (citable) accession number: P80735
Secondary accession number(s): O51921

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents