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Protein

Superoxide dismutase [Cu-Zn]

Gene

sodC

Organism
Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
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 bindingi103Copper; catalyticBy similarity1
Metal bindingi105Copper; catalyticBy similarity1
Metal bindingi145Zinc; structuralBy similarity1
Metal bindingi182Copper; 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:MAP_3921
OrganismiMycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
Taxonomic identifieri262316 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium avium complex (MAC)
Proteomesi
  • UP000000580 Componenti: Chromosome

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 – 19PROSITE-ProRule annotationAdd BLAST19
ChainiPRO_000003283920 – 227Superoxide dismutase [Cu-Zn]Add BLAST208

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi20N-palmitoyl cysteinePROSITE-ProRule annotation1
Lipidationi20S-diacylglycerol cysteinePROSITE-ProRule annotation1
Disulfide bondi110 ↔ 221By similarity

Keywords - PTMi

Disulfide bond, Lipoprotein, Palmitate

Interactioni

Protein-protein interaction databases

STRINGi262316.MAP3921.

Structurei

3D structure databases

ProteinModelPortaliQ9AGW2.
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.
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]
PRINTSiPR00068. CUZNDISMTASE.
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.

Q9AGW2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKLLPPVVL AGCVVALGAC SSPQHASSLP GTTPAVWTGS PSPSGAGAAE
60 70 80 90 100
AAPAAAPSIT THLKAPDGTQ VATAKFEFSN GYATVTIETT ANGVLTPGFH
110 120 130 140 150
GVHIHKVGKC EPSSVAPTGG APGDFLSAGG HFQAPGHTGE PASGDLTSLQ
160 170 180 190 200
VRKDGSGTLV TTTDAFTMED LLGGRKTAII IHAGADNFAN IPAERYNQTN
210 220
GTPGPDEMTM STGDAGKRVA CGVIGAG
Length:227
Mass (Da):22,466
Last modified:March 15, 2004 - v2
Checksum:iE5EE567880C00D5E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti16 – 18ALG → GC in AAK20038 (PubMed:11549243).Curated3
Sequence conflicti186D → N in AAK20038 (PubMed:11549243).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF326234 Genomic DNA. Translation: AAK20038.1.
AE016958 Genomic DNA. Translation: AAS06471.1.
RefSeqiWP_003873788.1. NC_002944.2.

Genome annotation databases

EnsemblBacteriaiAAS06471; AAS06471; MAP_3921.
GeneIDi2719337.
KEGGimpa:MAP_3921.
PATRICi18000734. VBIMycAvi108102_4173.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF326234 Genomic DNA. Translation: AAK20038.1.
AE016958 Genomic DNA. Translation: AAS06471.1.
RefSeqiWP_003873788.1. NC_002944.2.

3D structure databases

ProteinModelPortaliQ9AGW2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi262316.MAP3921.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAS06471; AAS06471; MAP_3921.
GeneIDi2719337.
KEGGimpa:MAP_3921.
PATRICi18000734. VBIMycAvi108102_4173.

Phylogenomic databases

eggNOGiENOG4105H08. Bacteria.
COG2032. LUCA.
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]
PRINTSiPR00068. CUZNDISMTASE.
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSODC_MYCPA
AccessioniPrimary (citable) accession number: Q9AGW2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: March 15, 2004
Last modified: November 2, 2016
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Lacks three conserved histidine residues 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.