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Database: UniProt/TrEMBL
Entry: A0A1U6XZM1_AERHY
LinkDB: A0A1U6XZM1_AERHY
Original site: A0A1U6XZM1_AERHY 
ID   A0A1U6XZM1_AERHY        Unreviewed;       171 AA.
AC   A0A1U6XZM1;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-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=V469_10980 {ECO:0000313|EMBL:AJE36338.1};
OS   Aeromonas hydrophila J-1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=1419584 {ECO:0000313|EMBL:AJE36338.1, ECO:0000313|Proteomes:UP000031528};
RN   [1] {ECO:0000313|EMBL:AJE36338.1, ECO:0000313|Proteomes:UP000031528}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J-1 {ECO:0000313|EMBL:AJE36338.1,
RC   ECO:0000313|Proteomes:UP000031528};
RA   Pang M., Hu M., Kwok A.H.Y., Jiang J., Leung F.C.C., Lu C., Liu Y.;
RT   "Genome sequencing of Aeromonas hydrophila J-1.";
RL   Submitted (NOV-2013) 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; CP006883; AJE36338.1; -; Genomic_DNA.
DR   RefSeq; WP_043158995.1; NZ_CP006883.1.
DR   KEGG; ahj:V469_10980; -.
DR   KO; K04565; -.
DR   Proteomes; UP000031528; 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   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:UP000031528};
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     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23    171       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5010581885.
FT   DOMAIN       32    170       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   171 AA;  17225 MW;  227B4C13991881B0 CRC64;
     MNNRLSKVML AAVLVTSVNA TAATVTMKDL ASGAVVGHVE LSESPYGAVF TPALSSLPAG
     LHGFHVHANG SCDSSMKDGQ SVAGGAAGGH YDPQQTGRHG APWQDDAHKG DLPPLYVDDA
     GKAVQPVLAP RLTLAELSGK ALMVHAGGDN HSDHPAPLGG GGARVVCGII P
//
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