SODC_ACTPL
ID SODC_ACTPL Reviewed; 190 AA.
AC P24702; Q59135;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Superoxide dismutase [Cu-Zn];
DE EC=1.15.1.1;
DE Flags: Precursor;
GN Name=sodC;
OS Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=715;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serotype III / Isolate 1421 (Nielsen);
RX PubMed=8945543; DOI=10.1128/iai.64.12.5035-5041.1996;
RA Langford P.R., Loynds B.M., Kroll J.S.;
RT "Cloning and molecular characterization of Cu,Zn superoxide dismutase from
RT Actinobacillus pleuropneumoniae.";
RL Infect. Immun. 64:5035-5041(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27088 / DSM 13472 / CCM 5869 / S4074 / Serotype 1;
RA Helie M.C., Sirois M., Ouellet C., Boissinot M.;
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 180-190.
RC STRAIN=Serotype III / Isolate 1421 (Nielsen);
RX PubMed=1741300; DOI=10.1093/nar/20.3.615;
RA Loynds B.M., Langford P.R., Kroll J.S.;
RT "recF in Actinobacillus pleuropneumoniae.";
RL Nucleic Acids Res. 20:615-615(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 91-177.
RC STRAIN=Serotype III / Isolate 1421 (Nielsen);
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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=10656823; DOI=10.1006/jmbi.1999.3448;
RA Forest K.T., Langford P.R., Kroll J.S., Getzoff E.D.;
RT "Cu,Zn superoxide dismutase structure from a microbial pathogen establishes
RT a class with a conserved dimer interface.";
RL J. Mol. Biol. 296:145-153(2000).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems.
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;
CC Note=Binds 1 copper ion per subunit.;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
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; X99396; CAA67771.1; -; Genomic_DNA.
DR EMBL; U51440; AAB02816.1; -; Genomic_DNA.
DR EMBL; X63626; CAA45174.1; -; Genomic_DNA.
DR EMBL; X83123; CAA58204.1; -; Genomic_DNA.
DR PIR; I39650; I39650.
DR RefSeq; WP_005603006.1; NZ_UIFY01000002.1.
DR PDB; 2APS; X-ray; 1.90 A; A/B=29-190.
DR PDBsum; 2APS; -.
DR AlphaFoldDB; P24702; -.
DR SMR; P24702; -.
DR STRING; 228399.appser1_190; -.
DR EvolutionaryTrace; P24702; -.
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..23
FT CHAIN 24..190
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000032817"
FT REGION 162..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 83
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT BINDING 85
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT BINDING 108
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT BINDING 164
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT DISULFID 90..186
FT CONFLICT 113
FT /note="E -> D (in Ref. 2; AAB02816)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="N -> D (in Ref. 2; AAB02816)"
FT /evidence="ECO:0000305"
FT CONFLICT 134..136
FT /note="FVE -> TIA (in Ref. 2; AAB02816)"
FT /evidence="ECO:0000305"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:2APS"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2APS"
FT STRAND 52..62
FT /evidence="ECO:0007829|PDB:2APS"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:2APS"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:2APS"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:2APS"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:2APS"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:2APS"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:2APS"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:2APS"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:2APS"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:2APS"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:2APS"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:2APS"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:2APS"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:2APS"
SQ SEQUENCE 190 AA; 20207 MW; 5FC1F3148972DC83 CRC64;
MKLTNLALAF TLFGASAVAF AHADHDHKKA DNSSVEKLVV QVQQLDPVKG NKDVGTVEIT
ESAYGLVFTP HLHGLAQGLH GFHIHQNPSC EPKEKDGKLV AGLGAGGHWD PKETKQHGYP
WSDNAHLGDL PALFVEHDGS ATNPVLAPRL KKLDEVKGHS LMIHEGGDNH SDHPAPLGGG
GPRMACGVIK
