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Database: UniProt
Entry: A0PZP2_CLONN
LinkDB: A0PZP2_CLONN
Original site: A0PZP2_CLONN 
ID   A0PZP2_CLONN            Unreviewed;       191 AA.
AC   A0PZP2;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   16-JAN-2019, entry version 73.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   OrderedLocusNames=NT01CX_1771 {ECO:0000313|EMBL:ABK60604.1};
OS   Clostridium novyi (strain NT).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=386415 {ECO:0000313|EMBL:ABK60604.1, ECO:0000313|Proteomes:UP000008220};
RN   [1] {ECO:0000313|EMBL:ABK60604.1, ECO:0000313|Proteomes:UP000008220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NT {ECO:0000313|EMBL:ABK60604.1,
RC   ECO:0000313|Proteomes:UP000008220};
RX   PubMed=17115055; DOI=10.1038/nbt1256;
RA   Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A.,
RA   Zhang X., Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W.,
RA   Vogelstein B., Zhou S.;
RT   "The genome and transcriptomes of the anti-tumor agent Clostridium
RT   novyi-NT.";
RL   Nat. Biotechnol. 24:1573-1580(2006).
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:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC         Evidence={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; CP000382; ABK60604.1; -; Genomic_DNA.
DR   RefSeq; WP_011721849.1; NC_008593.1.
DR   ProteinModelPortal; A0PZP2; -.
DR   STRING; 386415.NT01CX_1771; -.
DR   EnsemblBacteria; ABK60604; ABK60604; NT01CX_1771.
DR   GeneID; 4541761; -.
DR   KEGG; cno:NT01CX_1771; -.
DR   PATRIC; fig|386415.7.peg.874; -.
DR   eggNOG; ENOG4108Z7T; Bacteria.
DR   eggNOG; COG2032; LUCA.
DR   HOGENOM; HOG000263448; -.
DR   KO; K04565; -.
DR   OMA; GKSVIIH; -.
DR   OrthoDB; 2015673at2; -.
DR   BioCyc; CNOV386415:G1G6M-892-MONOMER; -.
DR   Proteomes; UP000008220; 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:UP000008220};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393,
KW   ECO:0000313|EMBL:ABK60604.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008220};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       53    188       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   191 AA;  21214 MW;  FD3F1C6E948F42F6 CRC64;
     MYFNFEYPYF DTCYPYPRTP YTNFYRNSSL DTNVKRPNIN IAVSYIKGGP SYPNIKGIVS
     FVSVPGGTEV SVYVEGLPNY KPATKTTQPI GPFGFHIHSV GCCDIGNPND PFTCASGHWN
     PDNQPHGNHA GDFPVLFSNH GMCKMSFFTD RFKPKDIIGL SVIIHESPDD YRSQPSGNSG
     KRIACGIIKT I
//
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