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Database: UniProt/TrEMBL
Entry: C6CSI4_PAESJ
LinkDB: C6CSI4_PAESJ
Original site: C6CSI4_PAESJ 
ID   C6CSI4_PAESJ            Unreviewed;       186 AA.
AC   C6CSI4;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   25-OCT-2017, entry version 56.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
DE   Flags: Precursor;
GN   OrderedLocusNames=Pjdr2_0456 {ECO:0000313|EMBL:ACS99136.1};
OS   Paenibacillus sp. (strain JDR-2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=324057 {ECO:0000313|EMBL:ACS99136.1, ECO:0000313|Proteomes:UP000002510};
RN   [1] {ECO:0000313|Proteomes:UP000002510}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JDR-2 {ECO:0000313|Proteomes:UP000002510};
RX   PubMed=22675593; DOI=10.4056/sigs.2374349;
RA   Chow V., Nong G., St John F.J., Rice J.D., Dickstein E., Chertkov O.,
RA   Bruce D., Detter C., Brettin T., Han J., Woyke T., Pitluck S.,
RA   Nolan M., Pati A., Martin J., Copeland A., Land M.L., Goodwin L.,
RA   Jones J.B., Ingram L.O., Shanmugam K.T., Preston J.F.;
RT   "Complete genome sequence of Paenibacillus sp. strain JDR-2.";
RL   Stand. Genomic Sci. 6:1-10(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: 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; CP001656; ACS99136.1; -; Genomic_DNA.
DR   RefSeq; WP_012772458.1; NC_012914.1.
DR   ProteinModelPortal; C6CSI4; -.
DR   STRING; 324057.Pjdr2_0456; -.
DR   EnsemblBacteria; ACS99136; ACS99136; Pjdr2_0456.
DR   KEGG; pjd:Pjdr2_0456; -.
DR   eggNOG; ENOG4108Z7T; Bacteria.
DR   eggNOG; COG2032; LUCA.
DR   HOGENOM; HOG000263448; -.
DR   KO; K04565; -.
DR   OMA; HKGDIGN; -.
DR   OrthoDB; POG091H05EB; -.
DR   BioCyc; PSP324057:GH5H-496-MONOMER; -.
DR   Proteomes; UP000002510; 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; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002510};
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:UP000002510};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     25       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        26    186       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002960985.
FT   DOMAIN       48    184       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   186 AA;  19589 MW;  33E9B64D6574E890 CRC64;
     MNKSMMLCSL GFLVASCGFS SAAMASQGHG HHTRSHVMEA KAAFIDTKGN QIGTVVLTEE
     KDGVHLKLEA KGLTPGVHGI HFHNVGKCEA PSFESAGSHL NPKNKQHGFD NPQGFHDGDL
     PNITVDKDGT VKADIISKNV TLDTEAPNSL LPAAGTALVI HEKADDYKTD PSGNSGSRIA
     CGVIQH
//
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