SODC_HAEDU
ID SODC_HAEDU Reviewed; 199 AA.
AC Q59452; Q59449; Q59453;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Superoxide dismutase [Cu-Zn];
DE EC=1.15.1.1;
DE Flags: Precursor;
GN Name=sodC; OrderedLocusNames=HD_0848;
OS Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=233412;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724;
RX PubMed=9143881; DOI=10.1111/j.1574-695x.1997.tb01017.x;
RA Langford P.R., Kroll J.S.;
RT "Distribution, cloning, characterisation and mutagenesis of sodC, the gene
RT encoding copper/zinc superoxide dismutase, a potential determinant of
RT virulence, in Haemophilus ducreyi.";
RL FEMS Immunol. Med. Microbiol. 17:235-242(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724;
RX PubMed=8996084; DOI=10.1016/s0378-1119(96)00417-9;
RA Stevens M.K., Hassett D.J., Radolf J.D., Hansen E.J.;
RT "Cloning and sequencing of the gene encoding the Cu,Zn-superoxide dismutase
RT of Haemophilus ducreyi.";
RL Gene 183:35-40(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724;
RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA Nguyen D., Wang J., Forst C., Hood L.;
RT "The complete genome sequence of Haemophilus ducreyi.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 100-186.
RC STRAIN=35000HP / ATCC 700724;
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. May play a role in the
CC interactive biology of organisms with their hosts and so contribute to
CC their capacity to cause disease.
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.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X98737; CAA67289.1; -; Genomic_DNA.
DR EMBL; U47664; AAB41293.1; -; Genomic_DNA.
DR EMBL; AE017143; AAP95739.1; -; Genomic_DNA.
DR EMBL; X83125; CAA58206.1; -; Genomic_DNA.
DR PIR; JC5718; JC5718.
DR RefSeq; WP_010944789.1; NC_002940.2.
DR PDB; 1Z9N; X-ray; 1.50 A; A/B/C/D=23-199.
DR PDB; 1Z9P; X-ray; 1.50 A; A/B=45-199.
DR PDBsum; 1Z9N; -.
DR PDBsum; 1Z9P; -.
DR AlphaFoldDB; Q59452; -.
DR SMR; Q59452; -.
DR STRING; 233412.HD_0848; -.
DR EnsemblBacteria; AAP95739; AAP95739; HD_0848.
DR KEGG; hdu:HD_0848; -.
DR eggNOG; COG2032; Bacteria.
DR HOGENOM; CLU_056632_7_1_6; -.
DR OMA; AQRGFHI; -.
DR EvolutionaryTrace; Q59452; -.
DR Proteomes; UP000001022; 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; Reference proteome; Signal; Zinc.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..199
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000032828"
FT BINDING 92
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT DISULFID 99..195
FT /evidence="ECO:0000250"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:1Z9N"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:1Z9N"
FT STRAND 61..71
FT /evidence="ECO:0007829|PDB:1Z9N"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:1Z9N"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:1Z9N"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:1Z9N"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1Z9P"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:1Z9N"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1Z9N"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1Z9N"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:1Z9N"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:1Z9N"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:1Z9N"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:1Z9N"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:1Z9N"
FT STRAND 191..198
FT /evidence="ECO:0007829|PDB:1Z9N"
SQ SEQUENCE 199 AA; 21402 MW; 841D3210AB2BC06C CRC64;
MKLTKVALFS LGLFGFSSMA LAHGDHMHNH DTKMDTMSKD MMSMEKIVVP VQQLDPQNGN
KDVGTVEITE SAYGLVFTPK LHDLAHGLHG FHIHEKPSCE PKEKDGKLVA GLGAGGHWDP
KQTQKHGYPW SDDAHMGDLP ALFVMHDGSA TTPVLAPRLK KLAEVKGHSL MIHAGGDNHS
DHPAPLGGGG PRMACGVIK
