ID   Q6ARI0_DESPS            Unreviewed;       197 AA.
AC   Q6ARI0;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=DP0316 {ECO:0000313|EMBL:CAG35045.1};
OS   Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC   Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC   Desulfocapsaceae; Desulfotalea.
OX   NCBI_TaxID=177439 {ECO:0000313|EMBL:CAG35045.1, ECO:0000313|Proteomes:UP000000602};
RN   [1] {ECO:0000313|Proteomes:UP000000602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12343 / LSv54 {ECO:0000313|Proteomes:UP000000602};
RX   PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA   Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA   Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA   Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT   "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT   permanently cold Arctic sediments.";
RL   Environ. Microbiol. 6:887-902(2004).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000414}.
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         Evidence={ECO:0000256|RuleBase:RU000414};
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00008714, ECO:0000256|RuleBase:RU000414}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR522870; CAG35045.1; -; Genomic_DNA.
DR   RefSeq; WP_011187561.1; NC_006138.1.
DR   AlphaFoldDB; Q6ARI0; -.
DR   STRING; 177439.DP0316; -.
DR   KEGG; dps:DP0316; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_0_0_7; -.
DR   OrthoDB; 9803125at2; -.
DR   Proteomes; UP000000602; 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   PANTHER; PTHR42769; SUPEROXIDE DISMUTASE; 1.
DR   PANTHER; PTHR42769:SF3; SUPEROXIDE DISMUTASE [FE] 2, CHLOROPLASTIC; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000349-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000602}.
FT   DOMAIN          4..87
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          94..194
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   BINDING         27
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         79
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         161
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         165
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ   SEQUENCE   197 AA;  22047 MW;  3E3DC95E1BA70880 CRC64;
     MSITLPELPY LKNALAPYIS SETLDFHHGK HHSTYVTNLN KLIAGTELEN ATLEEIIKKT
     VNDASKSGVF NNAAQIWNHT FYWQSMKAEG GGMPRGAIAE KIDADFGSYD NFVEQLKNAG
     LTQFGSGWAW LVLNNNKLEI MKTANADTPI AHGLQALLTV DVWEHAYYLD YQNGRGTYLD
     AFFNNLINWD FVNANLA
//