ID   G0CJT7_XANCA            Unreviewed;       192 AA.
AC   G0CJT7;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=XCR_2830 {ECO:0000313|EMBL:AEL07698.1};
OS   Xanthomonas campestris pv. raphani 756C.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=990315 {ECO:0000313|EMBL:AEL07698.1, ECO:0000313|Proteomes:UP000001633};
RN   [1] {ECO:0000313|EMBL:AEL07698.1, ECO:0000313|Proteomes:UP000001633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=756C {ECO:0000313|EMBL:AEL07698.1,
RC   ECO:0000313|Proteomes:UP000001633};
RX   PubMed=21784931; DOI=10.1128/JB.05262-11;
RA   Bogdanove A.J., Koebnik R., Lu H., Furutani A., Angiuoli S.V., Patil P.B.,
RA   Van Sluys M.A., Ryan R.P., Meyer D.F., Han S.W., Aparna G., Rajaram M.,
RA   Delcher A.L., Phillippy A.M., Puiu D., Schatz M.C., Shumway M.,
RA   Sommer D.D., Trapnell C., Benahmed F., Dimitrov G., Madupu R., Radune D.,
RA   Sullivan S., Jha G., Ishihara H., Lee S.W., Pandey A., Sharma V.,
RA   Sriariyanun M., Szurek B., Vera-Cruz C.M., Dorman K.S., Ronald P.C.,
RA   Verdier V., Dow J.M., Sonti R.V., Tsuge S., Brendel V.P., Rabinowicz P.D.,
RA   Leach J.E., White F.F., Salzberg S.L.;
RT   "Two new complete genome sequences offer insight into host and tissue
RT   specificity of plant pathogenic Xanthomonas spp.";
RL   J. Bacteriol. 193:5450-5464(2011).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000414}.
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         Evidence={ECO:0000256|RuleBase:RU000414};
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00008714, ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; CP002789; AEL07698.1; -; Genomic_DNA.
DR   RefSeq; WP_012437975.1; NC_017271.1.
DR   AlphaFoldDB; G0CJT7; -.
DR   KEGG; xcp:XCR_2830; -.
DR   PATRIC; fig|990315.4.peg.2668; -.
DR   HOGENOM; CLU_031625_0_1_6; -.
DR   Proteomes; UP000001633; 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; 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; PTHR42769; SUPEROXIDE DISMUTASE; 1.
DR   PANTHER; PTHR42769:SF3; SUPEROXIDE DISMUTASE [FE] 2, CHLOROPLASTIC; 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   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000349-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN          7..81
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          91..190
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   BINDING         27
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         74
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         157
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         161
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ   SEQUENCE   192 AA;  21590 MW;  7E8ADFF6B07D2BC3 CRC64;
     MPIEHLALPY SRAALEPHLS AATVDAHHGV CHRSEVERLN ARIEGSEFAE LMLEEIIAQA
     QGTLFQLAAQ VWNHNFYWQC LRPRGGGEPL GRLADSIAAS FGDFVHFKQE FNRIALGTVG
     SGWVWLVQRP DGRLAVVATP NASTPLTGPD TALLACDLWE HAYYLDHQQD RAQYLDAFWK
     LINWDFVASR LR
//