SODM_PSEAE
ID SODM_PSEAE Reviewed; 203 AA.
AC P53652; P77920;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Superoxide dismutase [Mn];
DE EC=1.15.1.1 {ECO:0000269|PubMed:8244935};
GN Name=sodA {ECO:0000303|PubMed:8244935}; OrderedLocusNames=PA4468;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA], 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=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer.
CC -!- INDUCTION: By growth in a high-phosphate succinate medium; more highly
CC expressed in mucoid than non-mucoid cells in both Y and LTG mdia (at
CC protein level) (PubMed:8244935). Part of the fumC-PA4469-sodA operon
CC which is repressed by iron (PubMed:8806672).
CC {ECO:0000269|PubMed:8244935, ECO:0000269|PubMed:8806672}.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=L25672; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L25672; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; U72494; AAB17391.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07856.1; -; Genomic_DNA.
DR PIR; A53294; A53294.
DR PIR; D83088; D83088.
DR RefSeq; NP_253158.1; NC_002516.2.
DR RefSeq; WP_003098862.1; NZ_QZGE01000004.1.
DR AlphaFoldDB; P53652; -.
DR SMR; P53652; -.
DR STRING; 287.DR97_1647; -.
DR PaxDb; P53652; -.
DR PRIDE; P53652; -.
DR EnsemblBacteria; AAG07856; AAG07856; PA4468.
DR GeneID; 881040; -.
DR KEGG; pae:PA4468; -.
DR PATRIC; fig|208964.12.peg.4678; -.
DR PseudoCAP; PA4468; -.
DR HOGENOM; CLU_031625_0_1_6; -.
DR InParanoid; P53652; -.
DR OMA; YEGWKGE; -.
DR PhylomeDB; P53652; -.
DR BioCyc; PAER208964:G1FZ6-4557-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0004784; F:superoxide dismutase activity; IDA:UniProtKB.
DR GO; GO:0019430; P:removal of superoxide radicals; IDA:UniProtKB.
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 Manganese; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..203
FT /note="Superoxide dismutase [Mn]"
FT /id="PRO_0000160067"
FT BINDING 27
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
SQ SEQUENCE 203 AA; 22506 MW; AA52FFB4B3CAB2B9 CRC64;
MPHALPPLPY AYDALEPHID ALTMEIHHSK HHQTYVNNLN AALEGTPYAE QPVESLLRQL
AGLPEKLRTP VVNNGGGHAN HSLFWTVMSP QGGGRPDGDL GRAIDEQLGG FEAFKDAFTK
AALTRFGSGW AWLSVTPQGS LLVESSGNQD SPLMNGNTPI LGLDVWEHAY YLKYQNRRPE
YIGAFYNVID WREVARRYAQ ALA
