SODM2_BACAN
ID SODM2_BACAN Reviewed; 208 AA.
AC Q81JK8; Q6HQ51; Q6KJJ4;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Superoxide dismutase [Mn] 2;
DE EC=1.15.1.1;
GN Name=sodA2; Synonyms=sodA-2; OrderedLocusNames=BA_5696, GBAA_5696, BAS5300;
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; AAP29328.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT34855.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT57587.1; -; Genomic_DNA.
DR RefSeq; NP_847842.1; NC_003997.3.
DR RefSeq; WP_000094049.1; NZ_WXXJ01000017.1.
DR RefSeq; YP_031537.1; NC_005945.1.
DR PDB; 1XRE; X-ray; 1.80 A; A/B=1-208.
DR PDBsum; 1XRE; -.
DR AlphaFoldDB; Q81JK8; -.
DR SMR; Q81JK8; -.
DR STRING; 260799.BAS5300; -.
DR DNASU; 1085438; -.
DR EnsemblBacteria; AAP29328; AAP29328; BA_5696.
DR EnsemblBacteria; AAT34855; AAT34855; GBAA_5696.
DR GeneID; 45025271; -.
DR KEGG; ban:BA_5696; -.
DR KEGG; bar:GBAA_5696; -.
DR KEGG; bat:BAS5300; -.
DR PATRIC; fig|198094.11.peg.5658; -.
DR eggNOG; COG0605; Bacteria.
DR HOGENOM; CLU_031625_0_1_9; -.
DR OMA; FGTGWVW; -.
DR EvolutionaryTrace; Q81JK8; -.
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..208
FT /note="Superoxide dismutase [Mn] 2"
FT /id="PRO_0000160013"
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:1XRE"
FT HELIX 22..30
FT /evidence="ECO:0007829|PDB:1XRE"
FT HELIX 32..44
FT /evidence="ECO:0007829|PDB:1XRE"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1XRE"
FT HELIX 55..60
FT /evidence="ECO:0007829|PDB:1XRE"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:1XRE"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:1XRE"
FT HELIX 70..88
FT /evidence="ECO:0007829|PDB:1XRE"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:1XRE"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:1XRE"
FT STRAND 129..138
FT /evidence="ECO:0007829|PDB:1XRE"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:1XRE"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:1XRE"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:1XRE"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:1XRE"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:1XRE"
FT HELIX 179..186
FT /evidence="ECO:0007829|PDB:1XRE"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:1XRE"
FT HELIX 192..202
FT /evidence="ECO:0007829|PDB:1XRE"
SQ SEQUENCE 208 AA; 24023 MW; 870D8FF1C721FD73 CRC64;
MSSFQLPKLS YDYDELEPYI DSNTLSIHHG KHHATYVNNL NAALENYSEL HNKSLEELLC
NLETLPKEIV TAVRNNGGGH YCHSLFWEVM SPRGGGEPNG DVAKVIDYYF NTFDNLKDQL
SKAAISRFGS GYGWLVLDGE ELSVMSTPNQ DTPLQEGKIP LLVIDVWEHA YYLKYQNRRP
EFVTNWWHTV NWDRVNEKYL QAIQSQKH