SODF_PSEAE
ID SODF_PSEAE Reviewed; 193 AA.
AC P53641;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Superoxide dismutase [Fe];
DE EC=1.15.1.1 {ECO:0000269|PubMed:8244935};
GN Name=sodB {ECO:0000303|PubMed:8244935}; OrderedLocusNames=PA4366;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP INDUCTION.
RC STRAIN=FRD1;
RX PubMed=8244935; DOI=10.1128/jb.175.23.7658-7665.1993;
RA Hassett D.J., Woodruff W.A., Wozniak D.J., Vasil M.L., Cohen M.S.,
RA Ohman D.E.;
RT "Cloning and characterization of the Pseudomonas aeruginosa sodA and sodB
RT genes encoding manganese- and iron-cofactored superoxide dismutase:
RT demonstration of increased manganese superoxide dismutase activity in
RT alginate-producing bacteria.";
RL J. Bacteriol. 175:7658-7665(1993).
RN [2]
RP CATALYTIC ACTIVITY, AND INDUCTION.
RC STRAIN=CHA;
RX PubMed=8806672; DOI=10.1006/bbrc.1996.1393;
RA Polack B., Dacheux D., Delic-Attree I., Toussaint B., Vignais P.M.;
RT "The Pseudomonas aeruginosa fumC and sodA genes belong to an iron-
RT responsive operon.";
RL Biochem. Biophys. Res. Commun. 226:555-560(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems
CC (Probable). Partially complements double sodA-sodB deletions in E.coli
CC (PubMed:8244935). {ECO:0000269|PubMed:8244935,
CC ECO:0000305|PubMed:8244935}.
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; Evidence={ECO:0000269|PubMed:8244935,
CC ECO:0000269|PubMed:8806672};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INDUCTION: By growth in a high-phosphate succinate medium (at protein
CC level) (PubMed:8244935). Strongly induced by growth on medium
CC containing FeSO(4) (at protein level) (PubMed:8806672).
CC {ECO:0000269|PubMed:8244935, ECO:0000269|PubMed:8806672}.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; L25675; AAA16786.1; -; Unassigned_DNA.
DR EMBL; AE004091; AAG07754.1; -; Genomic_DNA.
DR PIR; B53294; B53294.
DR PIR; E83100; E83100.
DR RefSeq; NP_253056.1; NC_002516.2.
DR RefSeq; WP_003094005.1; NZ_QZGE01000004.1.
DR AlphaFoldDB; P53641; -.
DR SMR; P53641; -.
DR STRING; 287.DR97_1543; -.
DR PaxDb; P53641; -.
DR PRIDE; P53641; -.
DR EnsemblBacteria; AAG07754; AAG07754; PA4366.
DR GeneID; 881397; -.
DR KEGG; pae:PA4366; -.
DR PATRIC; fig|208964.12.peg.4573; -.
DR PseudoCAP; PA4366; -.
DR HOGENOM; CLU_031625_0_0_6; -.
DR InParanoid; P53641; -.
DR OMA; YLHSIFW; -.
DR PhylomeDB; P53641; -.
DR BioCyc; PAER208964:G1FZ6-4452-MON; -.
DR Proteomes; UP000002438; Chromosome.
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 Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..193
FT /note="Superoxide dismutase [Fe]"
FT /id="PRO_0000159994"
FT BINDING 27
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CONFLICT 30..31
FT /note="KH -> NN (in Ref. 1; AAA16786)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="N -> T (in Ref. 1; AAA16786)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="A -> G (in Ref. 1; AAA16786)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="A -> G (in Ref. 1; AAA16786)"
FT /evidence="ECO:0000305"
FT CONFLICT 118..123
FT /note="TFGSGW -> HLRFRS (in Ref. 1; AAA16786)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="A -> P (in Ref. 1; AAA16786)"
FT /evidence="ECO:0000305"
FT CONFLICT 169..176
FT /note="NLRPKYVE -> TASEVRR (in Ref. 1; AAA16786)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 193 AA; 21351 MW; 81A0FB516972188C CRC64;
MAFELPPLPY EKNALEPHIS AETLEYHHDK HHNTYVVNLN NLIPGTEFEG KSLEEIVKSS
SGGIFNNAAQ VWNHTFYWNC LSPNGGGQPT GALADAINAA FGSFDKFKEE FTKTSVGTFG
SGWGWLVKKA DGSLALASTI GAGNPLTSGD TPLLTCDVWE HAYYIDYRNL RPKYVEAFWN
LVNWDFVAKN FAA
