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Protein

Superoxide dismutase [Cu-Zn]

Gene

sodC

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 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. May play a role in favoring mycobacterial survival in phagocytes (By similarity).By similarity

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Cu cationNote: Binds 1 copper ion per subunit.

Enzyme regulationi

Inhibited by the copper chelator diethyl dithiocarbamate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi116 – 1161Copper; catalytic
Metal bindingi118 – 1181Copper; catalytic
Metal bindingi144 – 1441Copper; catalytic
Metal bindingi195 – 1951Copper; catalytic

GO - Molecular functioni

  • copper ion binding Source: GO_Central
  • superoxide dismutase activity Source: MTBBASE
  • zinc ion binding Source: GO_Central

GO - Biological processi

  • cell redox homeostasis Source: MTBBASE
  • evasion or tolerance by symbiont of host-produced nitric oxide Source: MTBBASE
  • evasion or tolerance by symbiont of host-produced reactive oxygen species Source: MTBBASE
  • interaction with host Source: Reactome
  • removal of superoxide radicals Source: GOC
  • response to host Source: MTBBASE
  • response to host immune response Source: Reactome
  • response to hydroperoxide Source: MTBBASE
  • response to oxidative stress Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-1222387. Tolerance of reactive oxygen produced by macrophages.

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Cu-Zn] (EC:1.15.1.1)
Gene namesi
Name:sodC
Ordered Locus Names:Rv0432
ORF Names:MTCY22G10.29
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv0432.

Subcellular locationi

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

GO - Cellular componenti

  • cell wall Source: MTBBASE
  • extracellular region Source: MTBBASE
  • extracellular space Source: GO_Central
  • plasma membrane Source: MTBBASE
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232CuratedAdd
BLAST
Chaini33 – 240208Superoxide dismutase [Cu-Zn]PRO_0000032840Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi33 – 331N-palmitoyl cysteineCurated
Lipidationi33 – 331S-diacylglycerol cysteineCurated
Disulfide bondi123 ↔ 234

Keywords - PTMi

Disulfide bond, Lipoprotein, Palmitate

Proteomic databases

PaxDbiP9WGE9.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi83332.Rv0432.

Structurei

Secondary structure

1
240
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi71 – 777Combined sources
Beta strandi83 – 9210Combined sources
Beta strandi95 – 10814Combined sources
Beta strandi110 – 1134Combined sources
Beta strandi115 – 1206Combined sources
Beta strandi125 – 1273Combined sources
Helixi139 – 1413Combined sources
Beta strandi152 – 1543Combined sources
Beta strandi162 – 1643Combined sources
Beta strandi171 – 1788Combined sources
Helixi181 – 1855Combined sources
Beta strandi191 – 1977Combined sources
Turni206 – 2083Combined sources
Helixi220 – 2256Combined sources
Beta strandi230 – 23910Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PZSX-ray1.63A33-240[»]
ProteinModelPortaliP9WGE9.
SMRiP9WGE9. Positions 70-240.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105H08. Bacteria.
COG2032. LUCA.
KOiK04565.
OMAiIHADADN.
PhylomeDBiP9WGE9.

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.
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.

P9WGE9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKPADHRNH AAVSTSVLSA LFLGAGAALL SACSSPQHAS TVPGTTPSIW
60 70 80 90 100
TGSPAPSGLS GHDEESPGAQ SLTSTLTAPD GTKVATAKFE FANGYATVTI
110 120 130 140 150
ATTGVGKLTP GFHGLHIHQV GKCEPNSVAP TGGAPGNFLS AGGHYHVPGH
160 170 180 190 200
TGTPASGDLA SLQVRGDGSA MLVTTTDAFT MDDLLSGAKT AIIIHAGADN
210 220 230 240
FANIPPERYV QVNGTPGPDE TTLTTGDAGK RVACGVIGSG
Length:240
Mass (Da):23,844
Last modified:April 16, 2014 - v1
Checksum:iAFC08C0B302B84FC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP43163.1.
PIRiF70631.
RefSeqiNP_214946.1. NC_000962.3.
WP_003402198.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP43163; CCP43163; Rv0432.
GeneIDi886358.
KEGGimtu:Rv0432.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP43163.1.
PIRiF70631.
RefSeqiNP_214946.1. NC_000962.3.
WP_003402198.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PZSX-ray1.63A33-240[»]
ProteinModelPortaliP9WGE9.
SMRiP9WGE9. Positions 70-240.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv0432.

Proteomic databases

PaxDbiP9WGE9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP43163; CCP43163; Rv0432.
GeneIDi886358.
KEGGimtu:Rv0432.

Organism-specific databases

TubercuListiRv0432.

Phylogenomic databases

eggNOGiENOG4105H08. Bacteria.
COG2032. LUCA.
KOiK04565.
OMAiIHADADN.
PhylomeDBiP9WGE9.

Enzyme and pathway databases

ReactomeiR-HSA-1222387. Tolerance of reactive oxygen produced by macrophages.

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

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  2. "Lipid modification of the Cu,Zn superoxide dismutase from Mycobacterium tuberculosis."
    D'Orazio M., Folcarelli S., Mariani F., Colizzi V., Rotilio G., Battistoni A.
    Biochem. J. 359:17-22(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.
  4. "Unique features of the sodC-encoded superoxide dismutase from Mycobacterium tuberculosis, a fully functional copper-containing enzyme lacking zinc in the active site."
    Spagnolo L., Toro I., D'Orazio M., O'Neill P., Pedersen J.Z., Carugo O., Rotilio G., Battistoni A., Djinovic-Carugo K.
    J. Biol. Chem. 279:33447-33455(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 33-240 IN COMPLEX WITH COPPER IONS, ABSENCE OF ZINC BINDING, SUBUNIT.

Entry informationi

Entry nameiSODC_MYCTU
AccessioniPrimary (citable) accession number: P9WGE9
Secondary accession number(s): L0T6G1, P0A608, P96278
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: February 17, 2016
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Does not bind zinc ions. Has normal enzyme activity in the absence of zinc ions.

Caution

Lacks two conserved histidine residues that bind copper and zinc.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.