SODC_CAUVC
ID SODC_CAUVC Reviewed; 174 AA.
AC P20379;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Superoxide dismutase [Cu-Zn];
DE EC=1.15.1.1;
DE Flags: Precursor;
GN Name=sodC; OrderedLocusNames=CC_1579;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=2345128; DOI=10.1128/jb.172.6.2901-2910.1990;
RA Steinman H.M., Ely B.;
RT "Copper-zinc superoxide dismutase of Caulobacter crescentus: cloning,
RT sequencing, and mapping of the gene and periplasmic location of the
RT enzyme.";
RL J. Bacteriol. 172:2901-2910(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
RN [3]
RP PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=7050107; DOI=10.1016/s0021-9258(18)34017-1;
RA Steinman H.M.;
RT "Copper-zinc superoxide dismutase from Caulobacter crescentus CB15. A novel
RT bacteriocuprein form of the enzyme.";
RL J. Biol. Chem. 257:10283-10293(1982).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems (By similarity). May
CC function against extracytoplasmic toxic oxygen species. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; M55259; AAA23054.1; -; Genomic_DNA.
DR EMBL; AE005673; AAK23558.1; -; Genomic_DNA.
DR PIR; A35383; A35383.
DR RefSeq; NP_420390.1; NC_002696.2.
DR RefSeq; WP_010919453.1; NC_002696.2.
DR AlphaFoldDB; P20379; -.
DR SMR; P20379; -.
DR STRING; 190650.CC_1579; -.
DR EnsemblBacteria; AAK23558; AAK23558; CC_1579.
DR KEGG; ccr:CC_1579; -.
DR PATRIC; fig|190650.5.peg.1607; -.
DR eggNOG; COG2032; Bacteria.
DR HOGENOM; CLU_056632_8_1_5; -.
DR OMA; AQRGFHI; -.
DR BioCyc; CAULO:CC1579-MON; -.
DR Proteomes; UP000001816; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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; PS00087; SOD_CU_ZN_1; 1.
DR PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE 1: Evidence at protein level;
KW Antioxidant; Copper; Direct protein sequencing; Disulfide bond;
KW Metal-binding; Oxidoreductase; Periplasm; Reference proteome; Signal; Zinc.
FT SIGNAL 1..23
FT CHAIN 24..174
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000032823"
FT BINDING 68
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT DISULFID 75..170
FT /evidence="ECO:0000250"
SQ SEQUENCE 174 AA; 17100 MW; F3B3C79EF3E3642C CRC64;
MIRLSAAAAL GLAAALAASP ALAQTSATAV VKAGDGKDAG AVTVTEAPHG VLLKLELKGL
TPGWHAAHFH EKGDCGTPDF KSAGAHVHTA ATTVHGLLNP DANDSGDLPN IFAAADGAAT
AEIYSPLVSL KGAGGRPALL DADGSSIVVH ANPDDHKTQP IGGAGARVAC GVIK
