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Database: UniProt
Entry: F2F9N4_SOLSS
LinkDB: F2F9N4_SOLSS
Original site: F2F9N4_SOLSS 
ID   F2F9N4_SOLSS            Unreviewed;       179 AA.
AC   F2F9N4;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   OrderedLocusNames=SSIL_3609 {ECO:0000313|EMBL:BAK18032.1};
OS   Solibacillus silvestris (strain StLB046) (Bacillus silvestris).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Solibacillus.
OX   NCBI_TaxID=1002809 {ECO:0000313|EMBL:BAK18032.1, ECO:0000313|Proteomes:UP000006691};
RN   [1] {ECO:0000313|Proteomes:UP000006691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=StLB046 {ECO:0000313|Proteomes:UP000006691};
RA   Morohoshi T., Someya N., Ikeda T.;
RT   "Genome sequence of Solibacillus silvestris StLB046.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAK18032.1, ECO:0000313|Proteomes:UP000006691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=StLB046 {ECO:0000313|EMBL:BAK18032.1,
RC   ECO:0000313|Proteomes:UP000006691};
RX   PubMed=22019407; DOI=10.1016/j.jbiosc.2011.09.006;
RA   Morohoshi T., Tominaga Y., Someya N., Ikeda T.;
RT   "Complete genome sequence and characterization of the N-acylhomoserine
RT   lactone-degrading gene of the potato leaf-associated Solibacillus
RT   silvestris.";
RL   J. Biosci. Bioeng. 113:20-25(2012).
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; AP012157; BAK18032.1; -; Genomic_DNA.
DR   RefSeq; WP_014824895.1; NC_018065.1.
DR   AlphaFoldDB; F2F9N4; -.
DR   STRING; 1002809.SSIL_3609; -.
DR   KEGG; siv:SSIL_3609; -.
DR   PATRIC; fig|1002809.3.peg.3655; -.
DR   eggNOG; COG2032; Bacteria.
DR   HOGENOM; CLU_056632_8_1_9; -.
DR   OMA; KWVAFHV; -.
DR   Proteomes; UP000006691; 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 [CU-ZN]; 1.
DR   PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006691};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..179
FT                   /note="Superoxide dismutase [Cu-Zn]"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003282546"
FT   DOMAIN          47..178
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
SQ   SEQUENCE   179 AA;  19192 MW;  89BEA11406FF2B49 CRC64;
     MRVISLFVCV LLLSGCNLFQ KETVPVSAPE ALSAKAQMYD TKNNLVGEIL FKESSKGVEL
     TAVLNNLPPG DHGIHLHEFG KCESPSFESA GAHFNPTKKQ HGVDNPAGPH LGDLPNITVD
     DAGEVELNFV TADFTLEKGK ENSLFDEDGT SVVIHEKADD YKTDPSGNSG ARIVCGVIK
//
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