ID   D3DHT9_HYDTT            Unreviewed;       174 AA.
AC   D3DHT9;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=sodC {ECO:0000313|EMBL:BAI69391.1};
GN   OrderedLocusNames=HTH_0932 {ECO:0000313|EMBL:BAI69391.1};
OS   Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6).
OC   Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae;
OC   Hydrogenobacter.
OX   NCBI_TaxID=608538 {ECO:0000313|EMBL:BAI69391.1, ECO:0000313|Proteomes:UP000002574};
RN   [1] {ECO:0000313|EMBL:BAI69391.1, ECO:0000313|Proteomes:UP000002574}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6534 / IAM 12695 / TK-6 [Tokyo]
RC   {ECO:0000313|Proteomes:UP000002574};
RX   PubMed=20348262; DOI=10.1128/JB.00158-10;
RA   Arai H., Kanbe H., Ishii M., Igarashi Y.;
RT   "Complete genome sequence of the thermophilic, obligately
RT   chemolithoautotrophic hydrogen-oxidizing bacterium Hydrogenobacter
RT   thermophilus TK-6.";
RL   J. Bacteriol. 192:2651-2652(2010).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000393}.
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:RU000393};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00010457, ECO:0000256|RuleBase:RU000393}.
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DR   EMBL; AP011112; BAI69391.1; -; Genomic_DNA.
DR   RefSeq; WP_012963571.1; NC_017161.1.
DR   AlphaFoldDB; D3DHT9; -.
DR   STRING; 608538.HTH_0932; -.
DR   KEGG; hth:HTH_0932; -.
DR   PATRIC; fig|608538.5.peg.948; -.
DR   eggNOG; COG2032; Bacteria.
DR   OrthoDB; 9792957at2; -.
DR   Proteomes; UP000002574; Chromosome.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003:SF71; SUPEROXIDE DISMUTASE; 1.
DR   PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002574};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..174
FT                   /note="Superoxide dismutase [Cu-Zn]"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003043296"
FT   DOMAIN          41..173
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
SQ   SEQUENCE   174 AA;  18617 MW;  59F44A66E8E32125 CRC64;
     MGGLSCLSSG MALCAVLFSF SIAQELKAHA DIVNQKGEKI GKAELIQTNS GVLIKLEASN
     LPPNAELAFH IHELGKCDPP DFMSAKGHFN PFKKKHGLLN PDGPHAGDMP NVFTDANGNL
     KVHVLNTFVT LERGKENSLL KDGGTALMIH HHRDDYRTDP AGDAGARIAC GVIK
//