SODC_NEIMB
ID SODC_NEIMB Reviewed; 186 AA.
AC Q59623;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Superoxide dismutase [Cu-Zn];
DE EC=1.15.1.1;
DE Flags: Precursor;
GN Name=sodC; OrderedLocusNames=NMB1398;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=9423860; DOI=10.1128/iai.66.1.213-217.1998;
RA Wilks K.E., Dunn K.L., Farrant J.L., Reddin K.M., Gorringe A.R.,
RA Langford P.R., Kroll J.S.;
RT "Periplasmic superoxide dismutase in meningococcal pathogenicity.";
RL Infect. Immun. 66:213-217(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 87-173.
RC STRAIN=MC58;
RX PubMed=7496539; DOI=10.1099/13500872-141-9-2271;
RA Kroll J.S., Langford P.R., Wilks K.E., Keil A.D.;
RT "Bacterial [Cu,Zn]-superoxide dismutase: phylogenetically distinct from the
RT eukaryotic enzyme, and not so rare after all!";
RL Microbiology 141:2271-2279(1995).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems. {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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; AJ001313; CAA04674.1; -; Genomic_DNA.
DR EMBL; AE002098; AAF41762.1; -; Genomic_DNA.
DR EMBL; X83126; CAA58207.1; -; Genomic_DNA.
DR PIR; F81088; F81088.
DR RefSeq; NP_274412.1; NC_003112.2.
DR RefSeq; WP_002216968.1; NC_003112.2.
DR PDB; 2AQR; X-ray; 1.75 A; A/B/C=23-186.
DR PDB; 2AQS; X-ray; 1.70 A; A/B=23-186.
DR PDBsum; 2AQR; -.
DR PDBsum; 2AQS; -.
DR AlphaFoldDB; Q59623; -.
DR SMR; Q59623; -.
DR STRING; 122586.NMB1398; -.
DR PaxDb; Q59623; -.
DR EnsemblBacteria; AAF41762; AAF41762; NMB1398.
DR KEGG; nme:NMB1398; -.
DR PATRIC; fig|122586.8.peg.1753; -.
DR HOGENOM; CLU_056632_7_1_4; -.
DR OMA; AQRGFHI; -.
DR EvolutionaryTrace; Q59623; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
DR GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
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 3D-structure; Antioxidant; Copper; Disulfide bond; Metal-binding;
KW Oxidoreductase; Periplasm; Reference proteome; Signal; Zinc.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..186
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000032834"
FT BINDING 79
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
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 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT DISULFID 86..182
FT /evidence="ECO:0000250"
FT STRAND 30..40
FT /evidence="ECO:0007829|PDB:2AQS"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:2AQS"
FT STRAND 48..58
FT /evidence="ECO:0007829|PDB:2AQS"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:2AQS"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:2AQS"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:2AQS"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:2AQS"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2AQS"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:2AQS"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:2AQS"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:2AQS"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:2AQS"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:2AQS"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:2AQS"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:2AQS"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:2AQS"
SQ SEQUENCE 186 AA; 19520 MW; 6499049BFAC3427C CRC64;
MNMKTLLALA VSAVCSVGVA QAHEHNTIPK GASIEVKVQQ LDPVNGNKDV GTVTITESNY
GLVFTPDLQG LSEGLHGFHI HENPSCEPKE KEGKLTAGLG AGGHWDPKGA KQHGYPWQDD
AHLGDLPALT VLHDGTATNP VLAPRLKHLD DVRGHSIMIH TGGDNHSDHP APLGGGGPRM
ACGVIK
