ID   SODM_HALMA              Reviewed;         203 AA.
AC   Q03302; Q5V3T9;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
GN   Name=sod; Synonyms=sodA; OrderedLocusNames=rrnAC0831;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8449865; DOI=10.1128/jb.175.6.1561-1571.1993;
RA   Joshi P.B., Dennis P.P.;
RT   "Characterization of paralogous and orthologous members of the superoxide
RT   dismutase gene family from genera of the halophilic archaebacteria.";
RL   J. Bacteriol. 175:1561-1571(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
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   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; M97485; AAA73374.1; -; Genomic_DNA.
DR   EMBL; AY596297; AAV45813.1; -; Genomic_DNA.
DR   PIR; T50044; T50044.
DR   RefSeq; WP_004961502.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q03302; -.
DR   SMR; Q03302; -.
DR   STRING; 272569.rrnAC0831; -.
DR   EnsemblBacteria; AAV45813; AAV45813; rrnAC0831.
DR   GeneID; 40151856; -.
DR   GeneID; 64822514; -.
DR   KEGG; hma:rrnAC0831; -.
DR   PATRIC; fig|272569.17.peg.1569; -.
DR   eggNOG; arCOG04147; Archaea.
DR   HOGENOM; CLU_031625_2_1_2; -.
DR   OMA; YEGWKGE; -.
DR   Proteomes; UP000001169; Chromosome I.
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   CHAIN           1..203
FT                   /note="Superoxide dismutase [Mn]"
FT                   /id="PRO_0000160113"
FT   BINDING         31
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         79
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
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   CONFLICT        66..67
FT                   /note="MG -> WV (in Ref. 1; AAA73374)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        76..77
FT                   /note="HY -> QD (in Ref. 1; AAA73374)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        134
FT                   /note="V -> C (in Ref. 1; AAA73374)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   203 AA;  22726 MW;  A20197A10C2948E0 CRC64;
     MSEHSNPELP PLPYDYDALE PHISEQVLTW HHDTHHQGYV NGLESAEETL AENRDAGDFG
     SSAAAMGNVT HNGCGHYLHT LFWENMDPNG GGEPEGELLD RIEEDFGSYE GWKGEFEAAA
     SAAGGWALLV YDPVAKQLRN VPVDKHDQGA LWGSHPILAL DVWEHSYYYD YGPARGDFID
     AFFEVVDWDK AAEEYEKSVS HFE