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Q9AGW2

- SODC_MYCPA

UniProt

Q9AGW2 - SODC_MYCPA

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Protein

Superoxide dismutase [Cu-Zn]

Gene

sodC

Organism
Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi103 – 1031Copper; catalyticBy similarity
Metal bindingi105 – 1051Copper; catalyticBy similarity
Metal bindingi145 – 1451Zinc; structuralBy similarity
Metal bindingi182 – 1821Copper; catalyticBy similarity

GO - Molecular functioni

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

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMAVI262316:GCQR-3966-MONOMER.

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 lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium avium complex (MAC)
ProteomesiUP000000580: Chromosome

Subcellular locationi

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

GO - Cellular componenti

  1. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919PROSITE-ProRule annotationAdd
BLAST
Chaini20 – 227208Superoxide dismutase [Cu-Zn]PRO_0000032839Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi20 – 201N-palmitoyl cysteinePROSITE-ProRule annotation
Lipidationi20 – 201S-diacylglycerol cysteinePROSITE-ProRule annotation
Disulfide bondi110 ↔ 221By similarity

Keywords - PTMi

Disulfide bond, Lipoprotein, Palmitate

Interactioni

Protein-protein interaction databases

STRINGi262316.MAP3921.

Structurei

3D structure databases

ProteinModelPortaliQ9AGW2.
SMRiQ9AGW2. Positions 58-227.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2032.
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]
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 183ALG → GC in AAK20038. (PubMed:11549243)Curated
Sequence conflicti186 – 1861D → N in AAK20038. (PubMed:11549243)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF326234 Genomic DNA. Translation: AAK20038.1.
AE016958 Genomic DNA. Translation: AAS06471.1.
RefSeqiNP_962855.1. NC_002944.2.

Genome annotation databases

EnsemblBacteriaiAAS06471; AAS06471; MAP_3921.
GeneIDi2719337.
KEGGimpa:MAP3921.
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 .
RefSeqi NP_962855.1. NC_002944.2.

3D structure databases

ProteinModelPortali Q9AGW2.
SMRi Q9AGW2. Positions 58-227.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 262316.MAP3921.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAS06471 ; AAS06471 ; MAP_3921 .
GeneIDi 2719337.
KEGGi mpa:MAP3921.
PATRICi 18000734. VBIMycAvi108102_4173.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci MAVI262316:GCQR-3966-MONOMER.

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 ]
PRINTSi PR00068. CUZNDISMTASE.
SUPFAMi SSF49329. SSF49329. 1 hit.
PROSITEi PS51257. PROKAR_LIPOPROTEIN. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification, cloning and expression of sodC from an alkaline phosphatase gene fusion library of Mycobacterium avium subspecies paratuberculosis."
    Dupont C., Murray A.
    Microbios 106:7-19(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete genome sequence of Mycobacterium avium subspecies paratuberculosis."
    Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N., Kanjilal S., Kapur V.
    Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-968 / K-10.

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 26, 2014
This is version 100 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

External Data

Dasty 3