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Database: UniProt/TrEMBL
Entry: A5HZ65_CLOBH
LinkDB: A5HZ65_CLOBH
Original site: A5HZ65_CLOBH 
ID   A5HZ65_CLOBH            Unreviewed;       216 AA.
AC   A5HZ65; A7G150;
DT   26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2007, sequence version 1.
DT   28-MAR-2018, entry version 76.
DE   SubName: Full=Superoxide dismutase [fe] {ECO:0000313|EMBL:CAL82074.1};
DE            EC=1.15.1.1 {ECO:0000313|EMBL:CAL82074.1};
GN   OrderedLocusNames=CBO0521 {ECO:0000313|EMBL:CAL82074.1};
OS   Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441771 {ECO:0000313|Proteomes:UP000001986};
RN   [1] {ECO:0000313|EMBL:CAL82074.1, ECO:0000313|Proteomes:UP000001986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger]
RC   {ECO:0000313|Proteomes:UP000001986};
RX   PubMed=17519437; DOI=10.1101/gr.6282807;
RA   Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA   Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA   Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J.,
RA   Cerdeno-Tarraga A.M., Churcher C., Quail M.A., Chillingworth T.,
RA   Feltwell T., Fraser A., Goodhead I., Hance Z., Jagels K., Larke N.,
RA   Maddison M., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E.,
RA   Sanders M., Simmonds M., White B., Whithead S., Parkhill J.;
RT   "Genome sequence of a proteolytic (Group I) Clostridium botulinum
RT   strain Hall A and comparative analysis of the clostridial genomes.";
RL   Genome Res. 17:1082-1092(2007).
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DR   EMBL; AM412317; CAL82074.1; -; Genomic_DNA.
DR   RefSeq; WP_003355842.1; NC_009698.1.
DR   RefSeq; YP_001253064.1; NC_009495.1.
DR   RefSeq; YP_001386477.1; NC_009698.1.
DR   ProteinModelPortal; A5HZ65; -.
DR   GeneID; 5184776; -.
DR   GeneID; 5399682; -.
DR   KEGG; cbh:CLC_0594; -.
DR   KEGG; cbo:CBO0521; -.
DR   PATRIC; fig|413999.7.peg.523; -.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; YEHAYFI; -.
DR   BioCyc; CBOT441771:G1G97-556-MONOMER; -.
DR   Proteomes; UP000001986; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.40.500.20; -; 1.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001986};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1};
KW   Oxidoreductase {ECO:0000313|EMBL:CAL82074.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001986}.
FT   DOMAIN       90    188       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        23     23       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        74     74       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       155    155       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       159    159       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   216 AA;  25152 MW;  74E1BC574A611018 CRC64;
     MIVAKKYPFD NVKGISLKQL TEHYKLYDGY VNMINKIWSI PNNSKDFKDS NATFSKLRCI
     KLGESYALDG VKLHELYFQN MTSGHIPING PILDKILEDF NSVENFTELF KETGKSMRGW
     VVLGIDPLDK KLHIFGSDSH DNGAIWLAYP LLVMDVYEHA YFMDFGTDKG KYMDAFLQNV
     NWNLINNRLG MYYTLINALK HNILLNNKMK HRNMFY
//
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