SODC_PHOLE
ID SODC_PHOLE Reviewed; 173 AA.
AC P00446;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Superoxide dismutase [Cu-Zn];
DE EC=1.15.1.1;
DE Flags: Precursor;
GN Name=sodC;
OS Photobacterium leiognathi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=553611;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3805055; DOI=10.1016/s0021-9258(19)75722-6;
RA Steinman H.M.;
RT "Bacteriocuprein superoxide dismutase of Photobacterium leiognathi.
RT Isolation and sequence of the gene and evidence for a precursor form.";
RL J. Biol. Chem. 262:1882-1887(1987).
RN [2]
RP PROTEIN SEQUENCE OF 23-173.
RX PubMed=6884993; DOI=10.1515/bchm2.1983.364.1.675;
RA Steffens G.J., Bannister J.V., Bannister W.H., Flohe L., Gunzler W.A.,
RA Kim S.-M.A., Otting F.;
RT "The primary structure of Cu-Zn superoxide dismutase from Photobacterium
RT leiognathi: evidence for a separate evolution of Cu-Zn superoxide dismutase
RT in bacteria.";
RL Hoppe-Seyler's Z. Physiol. Chem. 364:675-690(1983).
RN [3]
RP DISCUSSION OF POSSIBLE GENE TRANSFER FROM EUKARYOTES.
RX PubMed=3855538; DOI=10.1073/pnas.82.1.149;
RA Bannister J.V., Parker M.W.;
RT "The presence of a copper/zinc superoxide dismutase in the bacterium
RT Photobacterium leiognathi: a likely case of gene transfer from eukaryotes
RT to prokaryotes.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:149-152(1985).
RN [4]
RP DISCUSSION OF POSSIBLE GENE TRANSFER FROM EUKARYOTES.
RA Leunissen J.A.M., de Jong W.W.;
RT "Copper/zinc superoxide dismutase: how likely is gene transfer from
RT ponyfish to Photobacterium leiognathi.";
RL J. Mol. Evol. 23:250-258(1986).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=8917495; DOI=10.1073/pnas.93.23.12774;
RA Bourne Y., Redford S.M., Steinman H.M., Lepock J.R., Tainer J.A.,
RA Getzoff E.D.;
RT "Novel dimeric interface and electrostatic recognition in bacterial Cu,Zn
RT superoxide dismutase.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:12774-12779(1996).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=9878406; DOI=10.1006/jmbi.1998.2267;
RA Bordo D., Matak D., Djinovic-Carugo K., Rosano C., Pesce A., Bolognesi M.,
RA Stroppolo M.E., Falconi M., Battistoni A., Desideri A.;
RT "Evolutionary constraints for dimer formation in prokaryotic Cu,Zn
RT superoxide dismutase.";
RL J. Mol. Biol. 285:283-296(1999).
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; J02658; AAA25632.1; -; Genomic_DNA.
DR PIR; A26689; DSFOCL.
DR RefSeq; WP_023934797.1; NZ_PYOJ01000018.1.
DR PDB; 1BZO; X-ray; 2.10 A; A=23-173.
DR PDB; 1IB5; X-ray; 2.45 A; A=23-173.
DR PDB; 1IBB; X-ray; 2.10 A; A=23-173.
DR PDB; 1IBD; X-ray; 2.00 A; A=23-173.
DR PDB; 1IBF; X-ray; 2.20 A; A=23-173.
DR PDB; 1IBH; X-ray; 2.00 A; A=23-173.
DR PDB; 1OAJ; X-ray; 1.73 A; A=23-173.
DR PDB; 1OAL; X-ray; 1.50 A; A=23-173.
DR PDB; 1YAI; X-ray; 1.90 A; A/B/C=23-173.
DR PDBsum; 1BZO; -.
DR PDBsum; 1IB5; -.
DR PDBsum; 1IBB; -.
DR PDBsum; 1IBD; -.
DR PDBsum; 1IBF; -.
DR PDBsum; 1IBH; -.
DR PDBsum; 1OAJ; -.
DR PDBsum; 1OAL; -.
DR PDBsum; 1YAI; -.
DR AlphaFoldDB; P00446; -.
DR SMR; P00446; -.
DR STRING; 553611.GCA_001557755_03507; -.
DR OrthoDB; 2015673at2; -.
DR EvolutionaryTrace; P00446; -.
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; Direct protein sequencing;
KW Disulfide bond; Metal-binding; Oxidoreductase; Periplasm; Signal; Zinc.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:6884993"
FT CHAIN 23..173
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000032836"
FT BINDING 67
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT BINDING 69
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT BINDING 92
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT BINDING 147
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT DISULFID 74..169
FT STRAND 24..31
FT /evidence="ECO:0007829|PDB:1OAL"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:1OAL"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:1OAL"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:1OAL"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:1OAL"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:1OAL"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1OAL"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1OAL"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:1OAL"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:1OAL"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:1OAL"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:1OAL"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:1OAL"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:1OAL"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:1OAL"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:1OAL"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:1OAL"
SQ SEQUENCE 173 AA; 18109 MW; 5931576F1E2A8F47 CRC64;
MNKAKTLLFT ALAFGLSHQA LAQDLTVKMT DLQTGKPVGT IELSQNKYGV VFTPELADLT
PGMHGFHIHQ NGSCASSEKD GKVVLGGAAG GHYDPEHTNK HGFPWTDDNH KGDLPALFVS
ANGLATNPVL APRLTLKELK GHAIMIHAGG DNHSDMPKAL GGGGARVACG VIQ
