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Database: UniProt
Entry: SODC_MYCPA
LinkDB: SODC_MYCPA
Original site: SODC_MYCPA 
ID   SODC_MYCPA              Reviewed;         227 AA.
AC   Q9AGW2;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2004, sequence version 2.
DT   10-APR-2019, entry version 120.
DE   RecName: Full=Superoxide dismutase [Cu-Zn];
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=sodC; OrderedLocusNames=MAP_3921;
OS   Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11549243;
RA   Dupont C., Murray A.;
RT   "Identification, cloning and expression of sodC from an alkaline
RT   phosphatase gene fusion library of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Microbios 106:7-19(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D.,
RA   Banerji N., Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems. May play a role
CC       in favoring mycobacterial survival in phagocytes (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000305};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000305};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Lacks three conserved histidine residues that bind copper
CC       and zinc. {ECO:0000305}.
DR   EMBL; AF326234; AAK20038.1; -; Genomic_DNA.
DR   EMBL; AE016958; AAS06471.1; -; Genomic_DNA.
DR   RefSeq; WP_003873788.1; NC_002944.2.
DR   ProteinModelPortal; Q9AGW2; -.
DR   SMR; Q9AGW2; -.
DR   STRING; 262316.MAP_3921; -.
DR   EnsemblBacteria; AAS06471; AAS06471; MAP_3921.
DR   GeneID; 2719337; -.
DR   KEGG; mpa:MAP_3921; -.
DR   eggNOG; ENOG4105H08; Bacteria.
DR   eggNOG; COG2032; LUCA.
DR   KO; K04565; -.
DR   OMA; HADADNF; -.
DR   BioCyc; MAVI262316:G1G0E-4110-MONOMER; -.
DR   Proteomes; UP000000580; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Antioxidant; Cell membrane; Complete proteome; Copper; Disulfide bond;
KW   Lipoprotein; Membrane; Metal-binding; Oxidoreductase; Palmitate;
KW   Reference proteome; Signal; Zinc.
FT   SIGNAL        1     19       {ECO:0000255|PROSITE-ProRule:PRU00303}.
FT   CHAIN        20    227       Superoxide dismutase [Cu-Zn].
FT                                /FTId=PRO_0000032839.
FT   METAL       103    103       Copper; catalytic. {ECO:0000250}.
FT   METAL       105    105       Copper; catalytic. {ECO:0000250}.
FT   METAL       145    145       Zinc; structural. {ECO:0000250}.
FT   METAL       182    182       Copper; catalytic. {ECO:0000250}.
FT   LIPID        20     20       N-palmitoyl cysteine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00303}.
FT   LIPID        20     20       S-diacylglycerol cysteine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00303}.
FT   DISULFID    110    221       {ECO:0000250}.
FT   CONFLICT     16     18       ALG -> GC (in Ref. 1; AAK20038).
FT                                {ECO:0000305}.
FT   CONFLICT    186    186       D -> N (in Ref. 1; AAK20038).
FT                                {ECO:0000305}.
SQ   SEQUENCE   227 AA;  22466 MW;  E5EE567880C00D5E CRC64;
     MPKLLPPVVL AGCVVALGAC SSPQHASSLP GTTPAVWTGS PSPSGAGAAE AAPAAAPSIT
     THLKAPDGTQ VATAKFEFSN GYATVTIETT ANGVLTPGFH GVHIHKVGKC EPSSVAPTGG
     APGDFLSAGG HFQAPGHTGE PASGDLTSLQ VRKDGSGTLV TTTDAFTMED LLGGRKTAII
     IHAGADNFAN IPAERYNQTN GTPGPDEMTM STGDAGKRVA CGVIGAG
//
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