SODC_NEIMA
ID SODC_NEIMA Reviewed; 186 AA.
AC P57005; A1ISJ6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Superoxide dismutase [Cu-Zn];
DE EC=1.15.1.1;
DE Flags: Precursor;
GN Name=sodC; OrderedLocusNames=NMA1617;
OS Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS Z2491).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122587;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15465 / Z2491;
RX PubMed=10761919; DOI=10.1038/35006655;
RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA Barrell B.G.;
RT "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT Z2491.";
RL Nature 404:502-506(2000).
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; AL157959; CAM08755.1; -; Genomic_DNA.
DR PIR; E81855; E81855.
DR RefSeq; WP_002220801.1; NC_003116.1.
DR PDB; 2AQN; X-ray; 1.40 A; A/B/C=23-186.
DR PDB; 2AQP; X-ray; 1.30 A; A/B=23-186.
DR PDB; 2AQQ; X-ray; 1.65 A; A/B/C=23-186.
DR PDB; 2AQT; X-ray; 1.80 A; A/B/C=23-186.
DR PDBsum; 2AQN; -.
DR PDBsum; 2AQP; -.
DR PDBsum; 2AQQ; -.
DR PDBsum; 2AQT; -.
DR AlphaFoldDB; P57005; -.
DR SMR; P57005; -.
DR EnsemblBacteria; CAM08755; CAM08755; NMA1617.
DR KEGG; nma:NMA1617; -.
DR HOGENOM; CLU_056632_7_1_4; -.
DR OMA; AQRGFHI; -.
DR BioCyc; NMEN122587:NMA_RS08080-MON; -.
DR EvolutionaryTrace; P57005; -.
DR Proteomes; UP000000626; 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 3D-structure; Antioxidant; Copper; Disulfide bond; Metal-binding;
KW Oxidoreductase; Periplasm; Signal; Zinc.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..186
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000032833"
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 33..40
FT /evidence="ECO:0007829|PDB:2AQP"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:2AQP"
FT STRAND 48..58
FT /evidence="ECO:0007829|PDB:2AQP"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:2AQP"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:2AQP"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:2AQP"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:2AQP"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2AQP"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:2AQP"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:2AQP"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:2AQP"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:2AQP"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:2AQP"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:2AQP"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:2AQP"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:2AQP"
SQ SEQUENCE 186 AA; 19550 MW; 04C84AB87FC7522D CRC64;
MNMKTLLALA VSAVCSVSVA QAHEHNTIPK GASIEVKVQQ LDPVNGNKDV GTVTITESNY
GLVFTPDLQG LSEGLHGFHI HENPSCEPKE KEGKLTAGLG AGGHWDPKGA KQHGYPWQDD
AHLGDLPALT VLHDGTATNP VLAPRLKHLD DVRGHSIMIH TGGDNHSDHP APLGGGGPRM
ACGVIK
