SODF_STRCO
ID SODF_STRCO Reviewed; 213 AA.
AC O51917;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Superoxide dismutase [Fe-Zn] 1;
DE EC=1.15.1.1;
DE AltName: Full=FeSOD I;
DE AltName: Full=SOD2;
GN Name=sodF1; Synonyms=sodB, sodF; OrderedLocusNames=SCO2633;
GN ORFNames=SC8E4A.03;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10147 / DSM 41007 / JCM 4020 / NBRC 3176 / KCC S-0020;
RX PubMed=9555880; DOI=10.1128/jb.180.8.2014-2020.1998;
RA Kim E.-J., Chung H.-J., Suh B., Hah Y.C., Roe J.-H.;
RT "Expression and regulation of the sodF gene encoding iron- and zinc-
RT containing superoxide dismutase in Streptomyces coelicolor Muller.";
RL J. Bacteriol. 180:2014-2020(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A3(2) / NRRL B-16638;
RX PubMed=10231572; DOI=10.1016/s0378-1119(99)00088-8;
RA Chung H.J., Kim E.J., Suh B., Choi J.H., Roe J.H.;
RT "Duplicate genes for Fe-containing superoxide dismutase in Streptomyces
RT coelicolor A3(2).";
RL Gene 231:87-93(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [4]
RP PROTEIN SEQUENCE OF 2-16.
RC STRAIN=ATCC 10147 / DSM 41007 / JCM 4020 / NBRC 3176 / KCC S-0020;
RX PubMed=8898904; DOI=10.1111/j.1432-1033.1996.0178t.x;
RA Kim F.-J., Kim H.-P., Hah Y.V., Roe J.-H.;
RT "Differential expression of superoxide dismutases containing Ni and Fe/Zn
RT in Streptomyces coelicolor.";
RL Eur. J. Biochem. 241:178-185(1996).
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(3+); Xref=ChEBI:CHEBI:29034;
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 Fe(3+) or Zn(2+) ion per subunit.;
CC -!- SUBUNIT: Tetramer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Inhibited by nickel.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; AF012087; AAC46274.1; -; Genomic_DNA.
DR EMBL; AF099014; AAD33128.1; -; Genomic_DNA.
DR EMBL; AL939113; CAB71808.1; -; Genomic_DNA.
DR PIR; T42080; T42080.
DR RefSeq; NP_626869.1; NC_003888.3.
DR RefSeq; WP_003976168.1; NZ_VNID01000020.1.
DR AlphaFoldDB; O51917; -.
DR SMR; O51917; -.
DR STRING; 100226.SCO2633; -.
DR GeneID; 1098067; -.
DR KEGG; sco:SCO2633; -.
DR PATRIC; fig|100226.15.peg.2680; -.
DR eggNOG; COG0605; Bacteria.
DR HOGENOM; CLU_031625_2_2_11; -.
DR InParanoid; O51917; -.
DR OMA; KWGSFDK; -.
DR PhylomeDB; O51917; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
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 Cytoplasm; Direct protein sequencing; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8898904"
FT CHAIN 2..213
FT /note="Superoxide dismutase [Fe-Zn] 1"
FT /id="PRO_0000160001"
FT BINDING 28
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:P9WGE7"
FT BINDING 76
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:P9WGE7"
FT BINDING 165
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:P9WGE7"
FT BINDING 169
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:P9WGE7"
SQ SEQUENCE 213 AA; 23527 MW; 9E2E208E1E8CF5B4 CRC64;
MSVYTLPELP YDYSALAPVI SPEIIELHHD KHHAAYVKGA NDTLEQLAEA RDKETWGSIN
GLEKNLAFHL SGHILHSIYW HNMTGDGGGE PLDKDGVGEL ADAIAESFGS FAGFRAQLTK
AAATTQGSGW GVLAYEPLSG RLIVEQIYDH QGNVGQGSTP ILVFDAWEHA FYLQYKNQKV
DFIDAMWAVV NWQDVARRYE AAKSRTNTLL LAP
