SODF_PHOLE
ID SODF_PHOLE Reviewed; 193 AA.
AC P09213;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Superoxide dismutase [Fe];
DE EC=1.15.1.1;
GN Name=sodB;
OS Photobacterium leiognathi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=553611;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=3542995; DOI=10.1016/s0021-9258(19)75740-8;
RA Barra D., Schinina M.E., Bannister W.H., Bannister J.V., Bossa F.;
RT "The primary structure of iron-superoxide dismutase from Photobacterium
RT leiognathi.";
RL J. Biol. Chem. 262:1001-1009(1987).
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the 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=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Note=Binds 1 Fe cation per subunit.;
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR PIR; A26707; A26707.
DR AlphaFoldDB; P09213; -.
DR SMR; P09213; -.
DR STRING; 553611.GCA_001557755_03767; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.287.990; -; 1.
DR Gene3D; 3.55.40.20; -; 1.
DR InterPro; IPR001189; Mn/Fe_SOD.
DR InterPro; IPR019833; Mn/Fe_SOD_BS.
DR InterPro; IPR019832; Mn/Fe_SOD_C.
DR InterPro; IPR019831; Mn/Fe_SOD_N.
DR InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR InterPro; IPR036314; SOD_C_sf.
DR Pfam; PF02777; Sod_Fe_C; 1.
DR Pfam; PF00081; Sod_Fe_N; 1.
DR PIRSF; PIRSF000349; SODismutase; 1.
DR PRINTS; PR01703; MNSODISMTASE.
DR SUPFAM; SSF46609; SSF46609; 1.
DR SUPFAM; SSF54719; SSF54719; 1.
DR PROSITE; PS00088; SOD_MN; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Iron; Metal-binding; Oxidoreductase.
FT CHAIN 1..193
FT /note="Superoxide dismutase [Fe]"
FT /id="PRO_0000159992"
FT BINDING 26
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 73
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 157
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 161
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
SQ SEQUENCE 193 AA; 21342 MW; 66FEDB570290399B CRC64;
AFELPALPFA MNALEPHISQ ETLEYHYGKH HNTYVVKLNG LVEGTELAEK SLEEIIKTST
GGVFNNAAQV WNHTFYWNCL APNAGGEPTG EVAAAIEKAF GSFAEFKAKF TDSAINNFGS
SWTWLVKNAN GSLAIVNTSN AGCPITEEGV TPLLTVDLWE HAYYIDYRNL RPSYMDGFWA
LVNWDFVSKN LAA