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Database: UniProt/TrEMBL
Entry: A0A075JXI4_9BACI
LinkDB: A0A075JXI4_9BACI
Original site: A0A075JXI4_9BACI 
ID   A0A075JXI4_9BACI        Unreviewed;       203 AA.
AC   A0A075JXI4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   25-OCT-2017, entry version 14.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=X953_17910 {ECO:0000313|EMBL:AIF44773.1};
OS   Virgibacillus sp. SK37.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=403957 {ECO:0000313|EMBL:AIF44773.1, ECO:0000313|Proteomes:UP000027985};
RN   [1] {ECO:0000313|EMBL:AIF44773.1, ECO:0000313|Proteomes:UP000027985}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK37 {ECO:0000313|EMBL:AIF44773.1,
RC   ECO:0000313|Proteomes:UP000027985};
RA   Phrommao E., Yongsawatdigul J., Rodtong S., Steele J.L.;
RT   "Complete genome sequence of Virgibacillus sp. SK37, a moderately
RT   halophilic bacterium isolated from Thai fish sauce fermentation.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {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.
CC       {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.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
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DR   EMBL; CP007161; AIF44773.1; -; Genomic_DNA.
DR   RefSeq; WP_019379305.1; NZ_CP007161.1.
DR   EnsemblBacteria; AIF44773; AIF44773; X953_17910.
DR   KEGG; vir:X953_17910; -.
DR   KO; K04565; -.
DR   Proteomes; UP000027985; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; -; 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; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000027985};
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:UP000027985};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25    203       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5001707429.
FT   DOMAIN       65    201       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   203 AA;  21518 MW;  AECA52341AD4877A CRC64;
     MKRSLLLVFS VLLIMVLAAC GGNEEEKPNK DNNQENEESS ETMADQNKSD STDKEDVLVS
     LKNKDGDVVA TATLTEDEEG VHVALEGEKL PAGTHGFHIH EKGACEAPDF KSAGGHFNPT
     DAKHGFDVPE GPHAGDMKNI EVGEDGTVQT ERLADMVTLK KGEANSLFKE GGTALVIHSG
     ADDYKSQPSG DAGERIACGV IGE
//
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