ID   SODM_XANC8              Reviewed;         203 AA.
AC   P0C0F9; Q4UVM3;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
GN   Name=sodA; Synonyms=sod; OrderedLocusNames=XC_1837;
OS   Xanthomonas campestris pv. campestris (strain 8004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=314565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8810073; DOI=10.1094/mpmi-9-0584;
RA   Smith S.G., Wilson T.J., Dow J.M., Daniels M.J.;
RT   "A gene for superoxide dismutase from Xanthomonas campestris pv. campestris
RT   and its expression during bacterial-plant interactions.";
RL   Mol. Plant Microbe Interact. 9:584-593(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8004;
RX   PubMed=15899963; DOI=10.1101/gr.3378705;
RA   Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q.,
RA   Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S.,
RA   Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B., Fang R.,
RA   Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.;
RT   "Comparative and functional genomic analyses of the pathogenicity of
RT   phytopathogen Xanthomonas campestris pv. campestris.";
RL   Genome Res. 15:757-767(2005).
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   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; U42464; AAB47971.1; -; Genomic_DNA.
DR   EMBL; CP000050; AAY48900.1; -; Genomic_DNA.
DR   RefSeq; WP_011037422.1; NC_007086.1.
DR   AlphaFoldDB; P0C0F9; -.
DR   SMR; P0C0F9; -.
DR   EnsemblBacteria; AAY48900; AAY48900; XC_1837.
DR   GeneID; 58013145; -.
DR   KEGG; xcb:XC_1837; -.
DR   HOGENOM; CLU_031625_0_1_6; -.
DR   OMA; YEGWKGE; -.
DR   OrthoDB; 1440645at2; -.
DR   Proteomes; UP000000420; Chromosome.
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   3: Inferred from homology;
KW   Manganese; Metal-binding; Oxidoreductase.
FT   CHAIN           1..203
FT                   /note="Superoxide dismutase [Mn]"
FT                   /id="PRO_0000160110"
FT   BINDING         27
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         81
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"
FT   BINDING         168
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        53
FT                   /note="V -> I (in Ref. 1; AAB47971)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        88
FT                   /note="M -> L (in Ref. 1; AAB47971)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        123
FT                   /note="L -> V (in Ref. 1; AAB47971)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        141
FT                   /note="V -> L (in Ref. 1; AAB47971)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        180
FT                   /note="D -> E (in Ref. 1; AAB47971)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        188
FT                   /note="V -> A (in Ref. 1; AAB47971)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        192
FT                   /note="D -> E (in Ref. 1; AAB47971)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   203 AA;  22721 MW;  C2CA1F9FB150C880 CRC64;
     MAYTLPQLPY AYDALEPNID AQTMEIHHTK HHQTYINNVN AALEGTEYAD LPVEELVSKL
     KSLPENLQGP VRNNGGGHAN HSLFWTVMSP NGGGEPKGEV AKAIDKDIGG FEKFKEAFTK
     AALSRFGSGW AWLSVTPDKK VVVESTANQD SPLFEGNTPI LGLDVWEHAY YLKYQNRRPD
     YIGAFYNVVN WDEVERRYHA AIA