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SODM1_BACAN
ID   SODM1_BACAN             Reviewed;         203 AA.
AC   Q81LW0; Q6HTB2; Q6KMK4;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Superoxide dismutase [Mn] 1;
DE            EC=1.15.1.1;
GN   Name=sodA1; Synonyms=sodA-1; OrderedLocusNames=BA_4499, GBAA_4499, BAS4177;
OS   Bacillus anthracis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1392;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames / isolate Porton;
RX   PubMed=12721629; DOI=10.1038/nature01586;
RA   Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA   Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA   Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA   Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA   DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA   Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA   Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA   Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA   White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA   Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT   "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT   related bacteria.";
RL   Nature 423:81-86(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames ancestor;
RX   PubMed=18952800; DOI=10.1128/jb.01347-08;
RA   Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA   Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT   "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL   J. Bacteriol. 191:445-446(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sterne;
RA   Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA   Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA   Richardson P., Rubin E., Tice H.;
RT   "Complete genome sequence of Bacillus anthracis Sterne.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; AE016879; AAP28210.1; -; Genomic_DNA.
DR   EMBL; AE017334; AAT33618.1; -; Genomic_DNA.
DR   EMBL; AE017225; AAT56477.1; -; Genomic_DNA.
DR   RefSeq; NP_846724.1; NC_003997.3.
DR   RefSeq; WP_001052031.1; NZ_WXXJ01000027.1.
DR   RefSeq; YP_030426.1; NC_005945.1.
DR   PDB; 1XUQ; X-ray; 1.80 A; A/B=1-203.
DR   PDBsum; 1XUQ; -.
DR   AlphaFoldDB; Q81LW0; -.
DR   SMR; Q81LW0; -.
DR   STRING; 260799.BAS4177; -.
DR   DNASU; 1088022; -.
DR   EnsemblBacteria; AAP28210; AAP28210; BA_4499.
DR   EnsemblBacteria; AAT33618; AAT33618; GBAA_4499.
DR   GeneID; 59155151; -.
DR   GeneID; 64199622; -.
DR   GeneID; 67508913; -.
DR   KEGG; ban:BA_4499; -.
DR   KEGG; bar:GBAA_4499; -.
DR   KEGG; bat:BAS4177; -.
DR   PATRIC; fig|198094.11.peg.4467; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_0_1_9; -.
DR   OMA; YEGWKGE; -.
DR   EvolutionaryTrace; Q81LW0; -.
DR   Proteomes; UP000000427; Chromosome.
DR   Proteomes; UP000000594; 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   1: Evidence at protein level;
KW   3D-structure; Manganese; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..203
FT                   /note="Superoxide dismutase [Mn] 1"
FT                   /id="PRO_0000160012"
FT   BINDING         28
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         83
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   TURN            13..19
FT                   /evidence="ECO:0007829|PDB:1XUQ"
FT   HELIX           22..30
FT                   /evidence="ECO:0007829|PDB:1XUQ"
FT   HELIX           32..44
FT                   /evidence="ECO:0007829|PDB:1XUQ"
FT   HELIX           48..51
FT                   /evidence="ECO:0007829|PDB:1XUQ"
FT   HELIX           55..60
FT                   /evidence="ECO:0007829|PDB:1XUQ"
FT   HELIX           62..64
FT                   /evidence="ECO:0007829|PDB:1XUQ"
FT   HELIX           67..88
FT                   /evidence="ECO:0007829|PDB:1XUQ"
FT   HELIX           100..110
FT                   /evidence="ECO:0007829|PDB:1XUQ"
FT   HELIX           113..126
FT                   /evidence="ECO:0007829|PDB:1XUQ"
FT   STRAND          129..138
FT                   /evidence="ECO:0007829|PDB:1XUQ"
FT   STRAND          141..148
FT                   /evidence="ECO:0007829|PDB:1XUQ"
FT   HELIX           153..156
FT                   /evidence="ECO:0007829|PDB:1XUQ"
FT   STRAND          159..165
FT                   /evidence="ECO:0007829|PDB:1XUQ"
FT   HELIX           168..170
FT                   /evidence="ECO:0007829|PDB:1XUQ"
FT   HELIX           172..175
FT                   /evidence="ECO:0007829|PDB:1XUQ"
FT   HELIX           179..186
FT                   /evidence="ECO:0007829|PDB:1XUQ"
FT   TURN            187..189
FT                   /evidence="ECO:0007829|PDB:1XUQ"
FT   HELIX           192..201
FT                   /evidence="ECO:0007829|PDB:1XUQ"
SQ   SEQUENCE   203 AA;  22664 MW;  61B0B7D44A090D97 CRC64;
     MAKHELPNLP YAYDALEPHF DKETMNIHHT KHHNTYITNL NAALEGHAEL ADKSVEELVA
     NLNEVPEAIR TAVRNNGGGH ANHTFFWTIL SPNGGGQPVG ELATAIEAKF GSFDAFKEEF
     AKAGATRFGS GWAWLVVNNG ELEVTSTPNQ DSPLTEGKTP VIGLDVWEHA YYLNYQNRRP
     DYIGAFWNVV DWNAAEKRYQ EAK
 
 
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