ID   SODM_MYCPA              Reviewed;         207 AA.
AC   P53647; Q9AM00; Q9F9R1;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
GN   Name=sodA; Synonyms=sod; OrderedLocusNames=MAP_0187c;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=11520620; DOI=10.1111/j.1574-6968.2001.tb10809.x;
RA   Liu X., Feng Z., Harris N.B., Cirillo J.D., Bercovier H., Barletta R.G.;
RT   "Identification of a secreted superoxide dismutase in Mycobacterium avium
RT   ssp. paratuberculosis.";
RL   FEMS Microbiol. Lett. 202:233-238(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Shin S.J., Dheenadhayalan V., Chang Y.F.;
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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., Banerji N.,
RA   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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-165.
RC   STRAIN=ATCC 19851 / CIP 103964 / NCTC 8578 / JC31;
RA   Bull T.J., Shanson D.C., Archard L.C.;
RT   "Rapid identification of mycobacteria from AIDS patients by capillary
RT   electrophoretic profiling of amplified SOD gene.";
RL   Clin. Mol. Pathol. 48:124-132(1995).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological systems.
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=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11520620}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; AF180816; AAG09425.1; -; Genomic_DNA.
DR   EMBL; AF333434; AAG50084.2; -; Genomic_DNA.
DR   EMBL; AE016958; AAS02504.1; -; Genomic_DNA.
DR   EMBL; Z48212; CAA88245.1; -; Genomic_DNA.
DR   PIR; S52370; S52370.
DR   RefSeq; WP_010948769.1; NC_002944.2.
DR   AlphaFoldDB; P53647; -.
DR   SMR; P53647; -.
DR   STRING; 262316.MAP_0187c; -.
DR   MoonProt; P53647; -.
DR   EnsemblBacteria; AAS02504; AAS02504; MAP_0187c.
DR   KEGG; mpa:MAP_0187c; -.
DR   PATRIC; fig|262316.17.peg.196; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_2_2_11; -.
DR   OMA; KWGSFDK; -.
DR   Proteomes; UP000000580; Chromosome.
DR   GO; GO:0005576; C:extracellular region; 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   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 3.55.40.20; -; 1.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019833; Mn/Fe_SOD_BS.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Manganese; Metal-binding; Oxidoreductase;
KW   Reference proteome; Secreted.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:11520620"
FT   CHAIN           2..207
FT                   /note="Superoxide dismutase [Mn]"
FT                   /id="PRO_0000160056"
FT   BINDING         28
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         76
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   207 AA;  23030 MW;  EDA8C2EB40ED428D CRC64;
     MAEYTLPDLD WDYAALEPHI SGQINEIHHT KHHATYVKGV NDALAKLEEA RANEDHAAIF
     LNEKNLAFHL GGHVNHSIWW KNLSPDGGDK PTGELAAAID DAFGSFDKFR AQFSAAANGL
     QGSGWAVLGY DTVGSRLLTF QLYDQQANVP LGIIPLLQVD MWEHAFYLQY KNVKADYVKA
     FWNVVNWADV QKRYAAATSK AQGLIFG