ID   SODM2_HALVD             Reviewed;         199 AA.
AC   Q03301; D4GXS2;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 2.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=Superoxide dismutase [Mn] 2;
DE            EC=1.15.1.1;
GN   Name=sod2; OrderedLocusNames=HVO_2913;
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
RC   VKM B-1768 / DS2;
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 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
RC   VKM B-1768 / DS2;
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
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; M97487; AAA73376.1; -; Genomic_DNA.
DR   EMBL; CP001956; ADE03299.1; -; Genomic_DNA.
DR   PIR; T50046; T50046.
DR   RefSeq; WP_013035375.1; NC_013967.1.
DR   AlphaFoldDB; Q03301; -.
DR   SMR; Q03301; -.
DR   STRING; 309800.HVO_2913; -.
DR   PaxDb; 309800-C498_00215; -.
DR   EnsemblBacteria; ADE03299; ADE03299; HVO_2913.
DR   GeneID; 8924540; -.
DR   KEGG; hvo:HVO_2913; -.
DR   HOGENOM; CLU_031625_2_0_2; -.
DR   Proteomes; UP000008243; 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; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR   Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 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   NCBIfam; NF041312; Superox_dis_Halo; 1.
DR   PANTHER; PTHR11404; SUPEROXIDE DISMUTASE 2; 1.
DR   PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL; 1.
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; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR   SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   3: Inferred from homology;
KW   Manganese; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..199
FT                   /note="Superoxide dismutase [Mn] 2"
FT                   /id="PRO_0000160117"
FT   BINDING         28
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
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   CONFLICT        42..43
FT                   /note="AE -> DD (in Ref. 1; AAA73376)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        62
FT                   /note="L -> V (in Ref. 1; AAA73376)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        93
FT                   /note="A -> L (in Ref. 1; AAA73376)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        120
FT                   /note="G -> A (in Ref. 1; AAA73376)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   199 AA;  22297 MW;  6315C33F3B7265CB CRC64;
     MSYELDPLPY EYDALEPHIS EQVLTWHHDT HHQGYVNGWN AAEETLAENR EAGEFGSSAG
     ALRNVTHNGS GHILHDLFWQ NMSPEGGDEP EGALAERIAE DFGSYEAWKG EFEAAAGAAG
     GWALLVYDSF SNQLRNVVVD KHDQGALWGS HPILALDVWE HSYYHDYGPA RGDFVSAFFE
     VVDWDEPAAR YEQAVELFE
//