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Q9CBI6

- SODC_MYCLE

UniProt

Q9CBI6 - SODC_MYCLE

Protein

Superoxide dismutase [Cu-Zn]

Gene

sodC

Organism
Mycobacterium leprae (strain TN)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    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

    Binds 1 copper ion per subunit.Curated
    Binds 1 zinc ion per subunit.Curated

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi116 – 1161Copper; catalyticBy similarity
    Metal bindingi118 – 1181Copper; catalyticBy similarity
    Metal bindingi195 – 1951Copper; catalyticBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. superoxide dismutase activity Source: UniProtKB-EC

    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 lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
    ProteomesiUP000000806: Chromosome

    Organism-specific databases

    LepromaiML1925.

    Subcellular locationi

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

    GO - Cellular componenti

    1. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3232PROSITE-ProRule annotationAdd
    BLAST
    Chaini33 – 240208Superoxide dismutase [Cu-Zn]PRO_0000032838Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi33 – 331N-palmitoyl cysteinePROSITE-ProRule annotation
    Lipidationi33 – 331S-diacylglycerol cysteinePROSITE-ProRule annotation
    Disulfide bondi123 ↔ 234By similarity

    Keywords - PTMi

    Disulfide bond, Lipoprotein, Palmitate

    Interactioni

    Protein-protein interaction databases

    STRINGi272631.ML1925.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CBI6.
    SMRiQ9CBI6. Positions 71-239.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the Cu-Zn superoxide dismutase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2032.
    HOGENOMiHOG000263448.
    KOiK04565.
    OMAiYNQTNGT.
    OrthoDBiEOG6K13RS.

    Family and domain databases

    Gene3Di2.60.40.200. 1 hit.
    InterProiIPR018152. SOD_Cu/Zn_BS.
    IPR001424. SOD_Cu_Zn_dom.
    [Graphical view]
    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

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    MSKLAGHRNV AAVTRSALSL SFVAACVALL SACIQNQPPA TLPGTTPTVW    50
    TGSPAPSGML GAEAESMGPP NIITRLNAPD GTQVATAKFE FNNGFATITI 100
    ATTGVGHLAP GFHGVHIHKV GKCEPSSAGP TGGAPGDFLS AGGHFQVPGH 150
    TVEPASGNLT SLQVRKDGIG TLVTTTDAFT MNDLLAGQKT AIIIHAGADN 200
    FGNIPPERYS QVNGTPGPDA TTISTGDAGK RVACGVIGAD 240
    Length:240
    Mass (Da):24,087
    Last modified:June 1, 2001 - v1
    Checksum:iF042C680D80799DD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL583923 Genomic DNA. Translation: CAC30880.1 .
    PIRi H87149.
    RefSeqi NP_302298.1. NC_002677.1.
    WP_010908619.1. NC_002677.1.

    3D structure databases

    ProteinModelPortali Q9CBI6.
    SMRi Q9CBI6. Positions 71-239.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272631.ML1925.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAC30880 ; CAC30880 ; CAC30880 .
    GeneIDi 910108.
    KEGGi mle:ML1925.
    PATRICi 18057442. VBIMycLep78757_3645.

    Organism-specific databases

    Lepromai ML1925.

    Phylogenomic databases

    eggNOGi COG2032.
    HOGENOMi HOG000263448.
    KOi K04565.
    OMAi YNQTNGT.
    OrthoDBi EOG6K13RS.

    Family and domain databases

    Gene3Di 2.60.40.200. 1 hit.
    InterProi IPR018152. SOD_Cu/Zn_BS.
    IPR001424. SOD_Cu_Zn_dom.
    [Graphical view ]
    Pfami PF00080. Sod_Cu. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49329. SSF49329. 1 hit.
    PROSITEi PS51257. PROKAR_LIPOPROTEIN. 1 hit.
    PS00332. SOD_CU_ZN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: TN.

    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 1, 2014
    This is version 91 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

    External Data

    Dasty 3