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Database: UniProt
Entry: P22799
LinkDB: P22799
Original site: P22799 
ID   SODM_RAOPL              Reviewed;         170 AA.
AC   P22799;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   05-DEC-2018, entry version 80.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
DE   Flags: Fragment;
GN   Name=sodA;
OS   Raoultella planticola (Klebsiella planticola).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Raoultella.
OX   NCBI_TaxID=575;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-26.
RX   PubMed=7764218; DOI=10.1271/bbb.57.1454;
RA   Lee S.O., Kim S.W., Uno I., Lee T.H.;
RT   "Direct sequencing of superoxide dismutase genes from two bacterial
RT   strains amplified by polymerase chain reaction.";
RL   Biosci. Biotechnol. Biochem. 57:1454-1460(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-16, SUBUNIT, AND CHARACTERIZATION.
RC   STRAIN=ATCC 8329 / NBRC 3317 / NCIB 8153;
RX   PubMed=1368658; DOI=10.1271/bbb1961.55.101;
RA   Kim S.W., Lee S.O., Lee T.H.;
RT   "Purification and characterization of superoxide dismutase from
RT   Aerobacter aerogenes.";
RL   Agric. Biol. Chem. 55:101-108(1991).
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=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1368658}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   PIR; PN0615; PN0615.
DR   PRIDE; P22799; -.
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; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Iron; Metal-binding; Oxidoreductase.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:1368658,
FT                                ECO:0000269|PubMed:7764218}.
FT   CHAIN         2   >170       Superoxide dismutase [Fe].
FT                                /FTId=PRO_0000160036.
FT   METAL        27     27       Iron. {ECO:0000250}.
FT   METAL        81     81       Iron. {ECO:0000250}.
FT   METAL       163    163       Iron. {ECO:0000250}.
FT   METAL       167    167       Iron. {ECO:0000250}.
FT   NON_TER     170    170
SQ   SEQUENCE   170 AA;  18468 MW;  7DE4F44E733EA16D CRC64;
     MAYELPQLPY AYDALEPHID AKTXEIHHSK HHNTYVTNLN AAVEGTEFAD KDINDLIAML
     DALPADKQTA VRNNGGGHAN HTLFWEVIAP GGSNTPVGEV AKAIDAKFGS FDAFKEEFAK
     AATTRFGSGW AWLIVDGDSV AVTSTPNQDS PVMEGKTPVL GLDVWEHAYY
//
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