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Database: UniProt/TrEMBL
Entry: A0A1J0H5T8_VIRHA
LinkDB: A0A1J0H5T8_VIRHA
Original site: A0A1J0H5T8_VIRHA 
ID   A0A1J0H5T8_VIRHA        Unreviewed;       203 AA.
AC   A0A1J0H5T8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   25-OCT-2017, entry version 7.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=BME96_17385 {ECO:0000313|EMBL:APC49859.1};
OS   Virgibacillus halodenitrificans (Bacillus halodenitrificans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=1482 {ECO:0000313|EMBL:APC49859.1, ECO:0000313|Proteomes:UP000182945};
RN   [1] {ECO:0000313|EMBL:APC49859.1, ECO:0000313|Proteomes:UP000182945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PDB-F2 {ECO:0000313|EMBL:APC49859.1,
RC   ECO:0000313|Proteomes:UP000182945};
RA   Sun Z., Zhou Y., Li H.;
RT   "Complete genome sequencing of Virgibacillus halodenitrificans PDB-
RT   F2.";
RL   Submitted (NOV-2016) 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; CP017962; APC49859.1; -; Genomic_DNA.
DR   RefSeq; WP_071649771.1; NZ_CP017962.1.
DR   KEGG; vhl:BME96_17385; -.
DR   KO; K04565; -.
DR   Proteomes; UP000182945; 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:UP000182945};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
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_5009612150.
FT   DOMAIN       65    201       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   203 AA;  21532 MW;  AE5423711AD4863F CRC64;
     MKRSLLLVFS VLLIMVLAAC GGNEEEKPNK DNNQENEESS ETMADQNKSD STDKEDVLVS
     LKNKDGEVVA TATLTEDEEG VHVALEGEKL PAGTHGFHIH EKGACEAPDF KSAGGHFNPT
     DAKHGFDVPE GPHAGDMKNI EVGEDGTVQT ERLADMVTLK KGEANSLFKE GGTALVIHSG
     ADDYKSQPSG DAGERIACGV IGE
//
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