ID   A5HZ65_CLOBH            Unreviewed;       216 AA.
AC   A5HZ65; A7G150;
DT   26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=superoxide dismutase {ECO:0000256|ARBA:ARBA00012682};
DE            EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682};
GN   OrderedLocusNames=CBO0521 {ECO:0000313|EMBL:CAL82074.1};
OS   Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441771 {ECO:0000313|EMBL:CAL82074.1, ECO:0000313|Proteomes:UP000001986};
RN   [1] {ECO:0000313|EMBL:CAL82074.1, ECO:0000313|Proteomes:UP000001986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger]
RC   {ECO:0000313|Proteomes:UP000001986};
RX   PubMed=17519437; DOI=10.1101/gr.6282807;
RA   Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA   Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA   Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA   Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA   Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA   Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA   White B., Whithead S., Parkhill J.;
RT   "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT   Hall A and comparative analysis of the clostridial genomes.";
RL   Genome Res. 17:1082-1092(2007).
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00008714}.
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DR   EMBL; AM412317; CAL82074.1; -; Genomic_DNA.
DR   RefSeq; WP_003355842.1; NC_009698.1.
DR   RefSeq; YP_001253064.1; NC_009495.1.
DR   RefSeq; YP_001386477.1; NC_009698.1.
DR   AlphaFoldDB; A5HZ65; -.
DR   GeneID; 5184776; -.
DR   KEGG; cbh:CLC_0594; -.
DR   KEGG; cbo:CBO0521; -.
DR   PATRIC; fig|413999.7.peg.523; -.
DR   HOGENOM; CLU_031625_2_2_9; -.
DR   Proteomes; UP000001986; 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; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
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   PIRSF; PIRSF000349; SODismutase; 1.
DR   SUPFAM; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR   SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 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:0000313|EMBL:CAL82074.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001986}.
FT   DOMAIN          90..188
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   BINDING         23
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         155
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         159
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ   SEQUENCE   216 AA;  25152 MW;  74E1BC574A611018 CRC64;
     MIVAKKYPFD NVKGISLKQL TEHYKLYDGY VNMINKIWSI PNNSKDFKDS NATFSKLRCI
     KLGESYALDG VKLHELYFQN MTSGHIPING PILDKILEDF NSVENFTELF KETGKSMRGW
     VVLGIDPLDK KLHIFGSDSH DNGAIWLAYP LLVMDVYEHA YFMDFGTDKG KYMDAFLQNV
     NWNLINNRLG MYYTLINALK HNILLNNKMK HRNMFY
//