ID Q5NGG3_FRATT Unreviewed; 185 AA.
AC Q5NGG3; A0A0G2RMJ6;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN Name=sodC {ECO:0000313|EMBL:CAG45512.1};
GN OrderedLocusNames=FTT_0879 {ECO:0000313|EMBL:CAG45512.1};
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416 {ECO:0000313|EMBL:CAG45512.1, ECO:0000313|Proteomes:UP000001174};
RN [1] {ECO:0000313|EMBL:CAG45512.1, ECO:0000313|Proteomes:UP000001174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4 {ECO:0000313|Proteomes:UP000001174};
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M., Duffield M., Fuxelius H.H.,
RA Garcia E., Halltorp G., Johansson D., Isherwood K., Karp P., Larsson E.,
RA Lui Y., Michell S., Prior J., Prior R., Sjostedt A., Svensson K.,
RA Thompson N., Vergez L., Wagg J., Wren B., Lindler L.E., Andersson S.G.,
RA Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
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. {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. {ECO:0000256|RuleBase:RU000393};
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000256|ARBA:ARBA00010457, ECO:0000256|RuleBase:RU000393}.
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DR EMBL; AJ749949; CAG45512.1; -; Genomic_DNA.
DR RefSeq; WP_003014586.1; NZ_CP010290.1.
DR RefSeq; YP_169879.1; NC_006570.2.
DR AlphaFoldDB; Q5NGG3; -.
DR SMR; Q5NGG3; -.
DR DNASU; 3190715; -.
DR EnsemblBacteria; CAG45512; CAG45512; FTT_0879.
DR KEGG; ftu:FTT_0879; -.
DR PATRIC; fig|177416.36.peg.1986; -.
DR OrthoDB; 5431326at2; -.
DR Proteomes; UP000001174; Chromosome.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
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; Superoxide dismutase, copper/zinc binding domain; 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:SF71; SUPEROXIDE DISMUTASE; 1.
DR PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000393};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000393};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000393,
KW ECO:0000313|EMBL:CAG45512.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001174};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000393}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..185
FT /note="Superoxide dismutase [Cu-Zn]"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030175878"
FT DOMAIN 51..183
FT /note="Superoxide dismutase copper/zinc binding"
FT /evidence="ECO:0000259|Pfam:PF00080"
SQ SEQUENCE 185 AA; 19887 MW; 73D892A8BF54403B CRC64;
MTAFYKLCGM SMLSLVLADC TFLSANKPYD RDHDGELIVH MKDVNTHKEV GTITISPYIH
DGNQEGMLIT PHLYNLPANT THGMHIHINP SCEDNGIAAG GHWDPDNTQK HLGPYNDNGH
KGDLPVLVVN ADGTATEPVV APKLNSLEEL AGHSLMLHAG GDNYSDKPQP LGGGGARMWC
GVIAD
//
