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Database: UniProt/SWISS-PROT
Entry: SODC_HAEDU
LinkDB: SODC_HAEDU
Original site: 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   25-OCT-2017, entry version 126.
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
RT   gene encoding copper/zinc superoxide dismutase, a potential
RT   determinant of 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
RT   dismutase 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.,
RA   Johnson L., 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
RT   from the 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
CC       in the interactive biology of organisms with their hosts and so
CC       contribute to their capacity to cause disease.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
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}.
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   ProteinModelPortal; Q59452; -.
DR   SMR; Q59452; -.
DR   STRING; 233412.HD0848; -.
DR   EnsemblBacteria; AAP95739; AAP95739; HD_0848.
DR   GeneID; 24944082; -.
DR   KEGG; hdu:HD_0848; -.
DR   eggNOG; ENOG4108Z7T; Bacteria.
DR   eggNOG; COG2032; LUCA.
DR   KO; K04565; -.
DR   OMA; HKGDIGN; -.
DR   OrthoDB; POG091H05JR; -.
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; Complete proteome; Copper; Disulfide bond;
KW   Metal-binding; Oxidoreductase; Periplasm; Reference proteome; Signal;
KW   Zinc.
FT   SIGNAL        1     22       {ECO:0000255}.
FT   CHAIN        23    199       Superoxide dismutase [Cu-Zn].
FT                                /FTId=PRO_0000032828.
FT   METAL        92     92       Copper; catalytic. {ECO:0000250}.
FT   METAL        94     94       Copper; catalytic. {ECO:0000250}.
FT   METAL       117    117       Copper; catalytic. {ECO:0000250}.
FT   METAL       117    117       Zinc; structural. {ECO:0000250}.
FT   METAL       126    126       Zinc; structural. {ECO:0000250}.
FT   METAL       135    135       Zinc; structural. {ECO:0000250}.
FT   METAL       138    138       Zinc; structural. {ECO:0000250}.
FT   METAL       173    173       Copper; catalytic. {ECO:0000250}.
FT   DISULFID     99    195       {ECO:0000250}.
FT   STRAND       47     53       {ECO:0000244|PDB:1Z9N}.
FT   TURN         56     58       {ECO:0000244|PDB:1Z9N}.
FT   STRAND       61     71       {ECO:0000244|PDB:1Z9N}.
FT   STRAND       74     81       {ECO:0000244|PDB:1Z9N}.
FT   STRAND       86     89       {ECO:0000244|PDB:1Z9N}.
FT   STRAND       91     97       {ECO:0000244|PDB:1Z9N}.
FT   STRAND      102    104       {ECO:0000244|PDB:1Z9P}.
FT   STRAND      105    109       {ECO:0000244|PDB:1Z9N}.
FT   HELIX       112    114       {ECO:0000244|PDB:1Z9N}.
FT   STRAND      142    144       {ECO:0000244|PDB:1Z9N}.
FT   STRAND      154    156       {ECO:0000244|PDB:1Z9N}.
FT   HELIX       162    165       {ECO:0000244|PDB:1Z9N}.
FT   STRAND      168    175       {ECO:0000244|PDB:1Z9N}.
FT   STRAND      179    184       {ECO:0000244|PDB:1Z9N}.
FT   HELIX       185    188       {ECO:0000244|PDB:1Z9N}.
FT   STRAND      191    198       {ECO:0000244|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
//
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