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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)DescriptionActionsGraphical viewLength
Metal bindingi79Copper; catalyticBy similarity1
Metal bindingi81Copper; catalyticBy similarity1
Metal bindingi104Copper; catalyticBy similarity1
Metal bindingi104Zinc; structuralBy similarity1
Metal bindingi113Zinc; structuralBy similarity1
Metal bindingi122Zinc; structuralBy similarity1
Metal bindingi125Zinc; structuralBy similarity1
Metal bindingi160Copper; catalyticBy similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Zinc

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
ChainiPRO_000003283423 – 186Superoxide dismutase [Cu-Zn]Add BLAST164

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

1186
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi30 – 40Combined sources11
Turni43 – 45Combined sources3
Beta strandi48 – 58Combined sources11
Beta strandi61 – 68Combined sources8
Beta strandi73 – 76Combined sources4
Beta strandi78 – 84Combined sources7
Beta strandi89 – 91Combined sources3
Beta strandi94 – 96Combined sources3
Helixi99 – 101Combined sources3
Beta strandi129 – 131Combined sources3
Beta strandi141 – 143Combined sources3
Helixi149 – 152Combined sources4
Beta strandi155 – 162Combined sources8
Beta strandi166 – 171Combined sources6
Helixi172 – 175Combined sources4
Beta strandi178 – 185Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AQRX-ray1.75A/B/C23-186[»]
2AQSX-ray1.70A/B23-186[»]
ProteinModelPortaliQ59623.
SMRiQ59623.
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.
OrthoDBiPOG091H05JR.

Family and domain databases

CDDicd00305. Cu-Zn_Superoxide_Dismutase. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AQRX-ray1.75A/B/C23-186[»]
2AQSX-ray1.70A/B23-186[»]
ProteinModelPortaliQ59623.
SMRiQ59623.
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.
OrthoDBiPOG091H05JR.

Miscellaneous databases

EvolutionaryTraceiQ59623.

Family and domain databases

CDDicd00305. Cu-Zn_Superoxide_Dismutase. 1 hit.
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...

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 2, 2016
This is version 120 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.