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Protein

Superoxide dismutase [Cu-Zn]

Gene

sodC

Organism
Mycobacterium leprae (strain TN)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Destroys radicals which are normally produced within the cells and which are toxic to biological systems. May play a role in favoring mycobacterial survival in phagocytes (By similarity).By similarity

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Protein has several cofactor binding sites:
  • Cu cationCuratedNote: Binds 1 copper ion per subunit.Curated
  • Zn2+CuratedNote: Binds 1 zinc ion per subunit.Curated

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi116Copper; catalyticBy similarity1
Metal bindingi118Copper; catalyticBy similarity1
Metal bindingi195Copper; 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:ML1925
OrganismiMycobacterium leprae (strain TN)
Taxonomic identifieri272631 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000000806 Componenti: Chromosome

Organism-specific databases

LepromaiML1925.

Subcellular locationi

  • Cell membrane PROSITE-ProRule annotation; Lipid-anchor PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 32PROSITE-ProRule annotationAdd BLAST32
ChainiPRO_000003283833 – 240Superoxide dismutase [Cu-Zn]Add BLAST208

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi33N-palmitoyl cysteinePROSITE-ProRule annotation1
Lipidationi33S-diacylglycerol cysteinePROSITE-ProRule annotation1
Disulfide bondi123 ↔ 234By similarity

Keywords - PTMi

Disulfide bond, Lipoprotein, Palmitate

Interactioni

Protein-protein interaction databases

STRINGi272631.ML1925.

Structurei

3D structure databases

ProteinModelPortaliQ9CBI6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105H08. Bacteria.
COG2032. LUCA.
HOGENOMiHOG000263448.
KOiK04565.
OMAiIHADADN.
OrthoDBiPOG091H05EB.

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.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 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.

Q9CBI6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKLAGHRNV AAVTRSALSL SFVAACVALL SACIQNQPPA TLPGTTPTVW
60 70 80 90 100
TGSPAPSGML GAEAESMGPP NIITRLNAPD GTQVATAKFE FNNGFATITI
110 120 130 140 150
ATTGVGHLAP GFHGVHIHKV GKCEPSSAGP TGGAPGDFLS AGGHFQVPGH
160 170 180 190 200
TVEPASGNLT SLQVRKDGIG TLVTTTDAFT MNDLLAGQKT AIIIHAGADN
210 220 230 240
FGNIPPERYS QVNGTPGPDA TTISTGDAGK RVACGVIGAD
Length:240
Mass (Da):24,087
Last modified:June 1, 2001 - v1
Checksum:iF042C680D80799DD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL583923 Genomic DNA. Translation: CAC30880.1.
PIRiH87149.
RefSeqiNP_302298.1. NC_002677.1.
WP_010908619.1. NC_002677.1.

Genome annotation databases

EnsemblBacteriaiCAC30880; CAC30880; CAC30880.
GeneIDi910108.
KEGGimle:ML1925.
PATRICi18057442. VBIMycLep78757_3645.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL583923 Genomic DNA. Translation: CAC30880.1.
PIRiH87149.
RefSeqiNP_302298.1. NC_002677.1.
WP_010908619.1. NC_002677.1.

3D structure databases

ProteinModelPortaliQ9CBI6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272631.ML1925.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC30880; CAC30880; CAC30880.
GeneIDi910108.
KEGGimle:ML1925.
PATRICi18057442. VBIMycLep78757_3645.

Organism-specific databases

LepromaiML1925.

Phylogenomic databases

eggNOGiENOG4105H08. Bacteria.
COG2032. LUCA.
HOGENOMiHOG000263448.
KOiK04565.
OMAiIHADADN.
OrthoDBiPOG091H05EB.

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.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSODC_MYCLE
AccessioniPrimary (citable) accession number: Q9CBI6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: June 1, 2001
Last modified: October 5, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Lacks three conserved histidine residues and one conserved aspartate residue that bind copper and zinc.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.