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Protein

Superoxide dismutase [Cu-Zn]

Gene

sodC

Organism
Neisseria meningitidis serogroup B (strain MC58)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Destroys radicals which are normally produced within the cells and which are toxic to biological systems.By similarity

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Protein has several cofactor binding sites:
  • Cu cationBy similarityNote: Binds 1 copper ion per subunit.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi79 – 791Copper; catalyticBy similarity
Metal bindingi81 – 811Copper; catalyticBy similarity
Metal bindingi104 – 1041Copper; catalyticBy similarity
Metal bindingi104 – 1041Zinc; structuralBy similarity
Metal bindingi113 – 1131Zinc; structuralBy similarity
Metal bindingi122 – 1221Zinc; structuralBy similarity
Metal bindingi125 – 1251Zinc; structuralBy similarity
Metal bindingi160 – 1601Copper; catalyticBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciNMEN122586:GHGG-1436-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Cu-Zn] (EC:1.15.1.1)
Gene namesi
Name:sodC
Ordered Locus Names:NMB1398
OrganismiNeisseria meningitidis serogroup B (strain MC58)
Taxonomic identifieri122586 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
Proteomesi
  • UP000000425 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Chaini23 – 186164Superoxide dismutase [Cu-Zn]PRO_0000032834Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi86 ↔ 182By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ59623.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi122586.NMB1398.

Structurei

Secondary structure

1
186
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 4011Combined sources
Turni43 – 453Combined sources
Beta strandi48 – 5811Combined sources
Beta strandi61 – 688Combined sources
Beta strandi73 – 764Combined sources
Beta strandi78 – 847Combined sources
Beta strandi89 – 913Combined sources
Beta strandi94 – 963Combined sources
Helixi99 – 1013Combined sources
Beta strandi129 – 1313Combined sources
Beta strandi141 – 1433Combined sources
Helixi149 – 1524Combined sources
Beta strandi155 – 1628Combined sources
Beta strandi166 – 1716Combined sources
Helixi172 – 1754Combined sources
Beta strandi178 – 1858Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AQRX-ray1.75A/B/C23-186[»]
2AQSX-ray1.70A/B23-186[»]
ProteinModelPortaliQ59623.
SMRiQ59623. Positions 32-186.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ59623.

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108Z7T. Bacteria.
COG2032. LUCA.
HOGENOMiHOG000263449.
KOiK04565.
OMAiGARYACG.
OrthoDBiEOG6K13RS.

Family and domain databases

Gene3Di2.60.40.200. 1 hit.
InterProiIPR024134. SOD_Cu/Zn_/chaperone.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003. PTHR10003. 1 hit.
PfamiPF00080. Sod_Cu. 1 hit.
[Graphical view]
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q59623-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNMKTLLALA VSAVCSVGVA QAHEHNTIPK GASIEVKVQQ LDPVNGNKDV
60 70 80 90 100
GTVTITESNY GLVFTPDLQG LSEGLHGFHI HENPSCEPKE KEGKLTAGLG
110 120 130 140 150
AGGHWDPKGA KQHGYPWQDD AHLGDLPALT VLHDGTATNP VLAPRLKHLD
160 170 180
DVRGHSIMIH TGGDNHSDHP APLGGGGPRM ACGVIK
Length:186
Mass (Da):19,520
Last modified:July 15, 1999 - v2
Checksum:i6499049BFAC3427C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001313 Genomic DNA. Translation: CAA04674.1.
AE002098 Genomic DNA. Translation: AAF41762.1.
X83126 Genomic DNA. Translation: CAA58207.1.
PIRiF81088.
RefSeqiNP_274412.1. NC_003112.2.
WP_002216968.1. NC_003112.2.

Genome annotation databases

EnsemblBacteriaiAAF41762; AAF41762; NMB1398.
GeneIDi903820.
KEGGinme:NMB1398.
PATRICi20358483. VBINeiMen85645_1753.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001313 Genomic DNA. Translation: CAA04674.1.
AE002098 Genomic DNA. Translation: AAF41762.1.
X83126 Genomic DNA. Translation: CAA58207.1.
PIRiF81088.
RefSeqiNP_274412.1. NC_003112.2.
WP_002216968.1. NC_003112.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AQRX-ray1.75A/B/C23-186[»]
2AQSX-ray1.70A/B23-186[»]
ProteinModelPortaliQ59623.
SMRiQ59623. Positions 32-186.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi122586.NMB1398.

Proteomic databases

PaxDbiQ59623.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF41762; AAF41762; NMB1398.
GeneIDi903820.
KEGGinme:NMB1398.
PATRICi20358483. VBINeiMen85645_1753.

Phylogenomic databases

eggNOGiENOG4108Z7T. Bacteria.
COG2032. LUCA.
HOGENOMiHOG000263449.
KOiK04565.
OMAiGARYACG.
OrthoDBiEOG6K13RS.

Enzyme and pathway databases

BioCyciNMEN122586:GHGG-1436-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ59623.

Family and domain databases

Gene3Di2.60.40.200. 1 hit.
InterProiIPR024134. SOD_Cu/Zn_/chaperone.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003. PTHR10003. 1 hit.
PfamiPF00080. Sod_Cu. 1 hit.
[Graphical view]
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Periplasmic superoxide dismutase in meningococcal pathogenicity."
    Wilks K.E., Dunn K.L., Farrant J.L., Reddin K.M., Gorringe A.R., Langford P.R., Kroll J.S.
    Infect. Immun. 66:213-217(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: MC58.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MC58.
  3. "Bacterial [Cu,Zn]-superoxide dismutase: phylogenetically distinct from the eukaryotic enzyme, and not so rare after all!"
    Kroll J.S., Langford P.R., Wilks K.E., Keil A.D.
    Microbiology 141:2271-2279(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 87-173.
    Strain: MC58.

Entry informationi

Entry nameiSODC_NEIMB
AccessioniPrimary (citable) accession number: Q59623
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 15, 1999
Last modified: November 11, 2015
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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.