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Database: UniProt
Entry: P53652
LinkDB: P53652
Original site: P53652 
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   05-DEC-2018, entry version 111.
DE   RecName: Full=Superoxide dismutase [Mn];
DE            EC=1.15.1.1;
GN   Name=sodA; OrderedLocusNames=PA4468;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 /
OS   JCM 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].
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
RT   sodB genes encoding manganese- and iron-cofactored superoxide
RT   dismutase: demonstration of increased manganese superoxide dismutase
RT   activity in alginate-producing bacteria.";
RL   J. Bacteriol. 175:7658-7665(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 /
RC   1C / 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.,
RA   Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an
RT   opportunistic 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
CC       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=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
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; NC_002516.2.
DR   ProteinModelPortal; P53652; -.
DR   SMR; P53652; -.
DR   STRING; 208964.PA4468; -.
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   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   InParanoid; P53652; -.
DR   KO; K04564; -.
DR   OMA; YEGWKGE; -.
DR   PhylomeDB; P53652; -.
DR   BioCyc; PAER208964:G1FZ6-4557-MONOMER; -.
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; 2.40.500.20; -; 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   3: Inferred from homology;
KW   Complete proteome; Manganese; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN         1    203       Superoxide dismutase [Mn].
FT                                /FTId=PRO_0000160067.
FT   METAL        27     27       Manganese. {ECO:0000250}.
FT   METAL        81     81       Manganese. {ECO:0000250}.
FT   METAL       164    164       Manganese. {ECO:0000250}.
FT   METAL       168    168       Manganese. {ECO:0000250}.
FT   CONFLICT     42     65       ALEGTPYAEQPVESLLRQLAGLPE -> RWRARPMPSSRWK
FT                                VCCGNWLVCRR (in Ref. 1). {ECO:0000305}.
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
//
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