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Database: UniProt
Entry: C5ZWG9_9HELI
LinkDB: C5ZWG9_9HELI
Original site: C5ZWG9_9HELI 
ID   C5ZWG9_9HELI            Unreviewed;       208 AA.
AC   C5ZWG9;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   16-JAN-2019, entry version 38.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodF {ECO:0000313|EMBL:EES89487.1};
GN   ORFNames=HCAN_0773 {ECO:0000313|EMBL:EES89487.1};
OS   Helicobacter canadensis MIT 98-5491.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=537970 {ECO:0000313|EMBL:EES89487.1, ECO:0000313|Proteomes:UP000007032};
RN   [1] {ECO:0000313|EMBL:EES89487.1, ECO:0000313|Proteomes:UP000007032}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13241 {ECO:0000313|Proteomes:UP000007032};
RX   PubMed=19542273; DOI=10.1128/JB.00729-09;
RA   Loman N.J., Snyder L.A., Linton J.D., Langdon R., Lawson A.J.,
RA   Weinstock G.M., Wren B.W., Pallen M.J.;
RT   "Genome sequence of the emerging pathogen Helicobacter canadensis.";
RL   J. Bacteriol. 191:5566-5567(2009).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000414}.
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:RU000414};
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; CM000776; EES89487.1; -; Genomic_DNA.
DR   RefSeq; WP_006655475.1; NZ_DS990368.1.
DR   STRING; 537970.HCAN_0773; -.
DR   EnsemblBacteria; EES89487; EES89487; HCAN_0773.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   OrthoDB; 1440645at2; -.
DR   Proteomes; UP000007032; 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; 1.10.287.990; -; 1.
DR   Gene3D; 2.40.500.20; -; 1.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019833; Mn/Fe_SOD_BS.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007032};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007032}.
FT   DOMAIN        2     79       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       87    186       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        24     24       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        71     71       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       154    154       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       158    158       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   208 AA;  24117 MW;  EB3BF37585DC0F86 CRC64;
     MFNLRKLPFN EIQGFISKET CEFHYGKHHQ TYINNLNNLI KGTEFESASL FEIVTKAQGG
     IFNNAAQVYN HDFYWDCLSP KETPLSNELQ EAINESFGSF DKFKETFLQS ATTLFGSGWC
     WVVYNPNSKK LEIVQTSNAQ TPVTQGLIPV LVVDVWEHAY YVDYRNARPA YLEKFFSHIH
     WDFVSKSLEW AKKEGLNSVN FYMNSLHA
//
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