ID   K8CHP3_CROSK            Unreviewed;        74 AA.
AC   K8CHP3;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Manganese superoxide dismutase {ECO:0000313|EMBL:CCK04729.1};
DE            EC=1.15.1.1 {ECO:0000313|EMBL:CCK04729.1};
GN   ORFNames=BN129_3514 {ECO:0000313|EMBL:CCK04729.1};
OS   Cronobacter sakazakii 701.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=1208663 {ECO:0000313|EMBL:CCK04729.1, ECO:0000313|Proteomes:UP000009355};
RN   [1] {ECO:0000313|EMBL:CCK04729.1, ECO:0000313|Proteomes:UP000009355}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=701 {ECO:0000313|EMBL:CCK04729.1,
RC   ECO:0000313|Proteomes:UP000009355};
RX   PubMed=23166675; DOI=10.1371/journal.pone.0049455;
RA   Joseph S., Desai P., Ji Y., Cummings C.A., Shih R., Degoricija L., Rico A.,
RA   Brzoska P., Hamby S.E., Masood N., Hariri S., Sonbol H., Chuzhanova N.,
RA   McClelland M., Furtado M.R., Forsythe S.J.;
RT   "Comparative analysis of genome sequences covering the seven cronobacter
RT   species.";
RL   PLoS ONE 7:e49455-e49455(2012).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological systems.
CC       {ECO:0000256|ARBA:ARBA00002170}.
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         Evidence={ECO:0000256|ARBA:ARBA00001605};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCK04729.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CALE01000616; CCK04729.1; -; Genomic_DNA.
DR   AlphaFoldDB; K8CHP3; -.
DR   Proteomes; UP000009355; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1.
DR   InterPro; IPR019833; Mn/Fe_SOD_BS.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR036314; SOD_C_sf.
DR   PANTHER; PTHR43595; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43595:SF2; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   SUPFAM; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:CCK04729.1}.
FT   DOMAIN          5..69
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
SQ   SEQUENCE   74 AA;  8379 MW;  DA32D9EC52102DAD CRC64;
     MLKGDKLAVV STANQDSPLM GEAISGASGY PILGLDVWEH AYYLKFQNRR PDYIKEFWNV
     VNWDEAAARF ASQK
//