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Database: UniProt/TrEMBL
Entry: A0A1G9TZ96_9PSED
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ID   A0A1G9TZ96_9PSED        Unreviewed;       173 AA.
AC   A0A1G9TZ96;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   25-OCT-2017, entry version 6.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=SAMN05660875_105403 {ECO:0000313|EMBL:SDM53002.1};
OS   Pseudomonas balearica DSM 6083.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1123016 {ECO:0000313|EMBL:SDM53002.1, ECO:0000313|Proteomes:UP000182276};
RN   [1] {ECO:0000313|EMBL:SDM53002.1, ECO:0000313|Proteomes:UP000182276}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6083 {ECO:0000313|EMBL:SDM53002.1,
RC   ECO:0000313|Proteomes:UP000182276};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FNHO01000005; SDM53002.1; -; Genomic_DNA.
DR   RefSeq; WP_043220920.1; NZ_FNHO01000005.1.
DR   KEGG; pbm:CL52_12445; -.
DR   KO; K04565; -.
DR   Proteomes; UP000182276; Unassembled WGS sequence.
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   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000182276};
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:UP000182276};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    173       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5010288859.
FT   DOMAIN       34    172       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   173 AA;  17640 MW;  547D105ADA09C4F3 CRC64;
     MNKWIIAALA SCVAAAAQAE TLNVQMNAVG ADGVGKSVGQ VSIETSDYGL VFRPQLSDLQ
     PGVHGFHIHA KGSCETAEID GKTTPAGAAG GHWDPKNTGK HGEPWGDGHM GDLPALYVES
     GGTAKQPVLA PRLKSLGDIK GLALMVHQGG DNHADHPQPL GGGGARVACG LIK
//
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