ID   SODM_HAEDU              Reviewed;         213 AA.
AC   O30826;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
GN   Name=sodA; OrderedLocusNames=HD_0321;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RX   PubMed=9511768; DOI=10.1016/s0378-1119(97)00642-2;
RA   San Mateo L.R., Toffer K.L., Kawula T.H.;
RT   "The sodA gene of Haemophilus ducreyi encodes a hydrogen peroxide-
RT   inhibitable superoxide dismutase.";
RL   Gene 207:251-257(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) 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   -!- ACTIVITY REGULATION: Inhibited by hydrogen peroxide.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; AF017750; AAC46219.1; -; Genomic_DNA.
DR   EMBL; AE017143; AAP95298.1; -; Genomic_DNA.
DR   PIR; JC6542; JC6542.
DR   RefSeq; WP_010944351.1; NC_002940.2.
DR   AlphaFoldDB; O30826; -.
DR   SMR; O30826; -.
DR   STRING; 233412.HD_0321; -.
DR   EnsemblBacteria; AAP95298; AAP95298; HD_0321.
DR   GeneID; 60733624; -.
DR   KEGG; hdu:HD_0321; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_0_1_6; -.
DR   OMA; YEGWKGE; -.
DR   Proteomes; UP000001022; 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; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..213
FT                   /note="Superoxide dismutase [Mn]"
FT                   /id="PRO_0000160039"
FT   BINDING         27
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         82
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   BINDING         172
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        111
FT                   /note="E -> K (in Ref. 1; AAC46219)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   213 AA;  24107 MW;  3CE142A1B032E458 CRC64;
     MTYQLPELGY AYDALEPYFD KETMEIHHSK HHQAYVNNSN ALLEKHPELL EKCPGALLKD
     LTQVPAEKRT AVRNNLGGHV NHTLFWKGLK TGTTLQGALK DAIIRDFGSV EAFQAEFEQA
     AATRFGSGWA WLVLEEGKLA VVSTANQDSP IMGKDVAGVS GYPIFTLDVW EHAYYLHYQN
     RRPDYIKAFW NVVNWDEASR RFEEKQAGCG CTK