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 27-MAR-2024, entry version 136.
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; Actinomycetota; Actinomycetes; Mycobacteriales; 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; NZ_CP106873.1.
DR AlphaFoldDB; P53647; -.
DR SMR; P53647; -.
DR STRING; 262316.MAP_0187c; -.
DR MoonProt; P53647; -.
DR KEGG; mpa:MAP_0187c; -.
DR PATRIC; fig|262316.17.peg.196; -.
DR eggNOG; COG0605; Bacteria.
DR HOGENOM; CLU_031625_2_2_11; -.
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; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 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 PANTHER; PTHR11404; SUPEROXIDE DISMUTASE 2; 1.
DR PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL; 1.
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; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 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
//
