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Database: UniProt/TrEMBL
Entry: A0A0H3HCH2_KLEOK
LinkDB: A0A0H3HCH2_KLEOK
Original site: A0A0H3HCH2_KLEOK 
ID   A0A0H3HCH2_KLEOK        Unreviewed;       193 AA.
AC   A0A0H3HCH2;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   25-OCT-2017, entry version 14.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=KOX_22125 {ECO:0000313|EMBL:AEX06145.1};
OS   Klebsiella oxytoca (strain ATCC 8724 / DSM 4798 / JCM 20051 / NBRC
OS   3318 / NRRL B-199 / KCTC 1686).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=1006551 {ECO:0000313|EMBL:AEX06145.1, ECO:0000313|Proteomes:UP000007843};
RN   [1] {ECO:0000313|Proteomes:UP000007843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / NRRL B-199 /
RC   KCTC 1686 {ECO:0000313|Proteomes:UP000007843};
RA   Shin S.H., Kim S., Kim J.Y., Yang K.-S., Seo J.-S.;
RT   "Complete genome sequence of Klebsiella oxytoca strain KCTC 1686.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; CP003218; AEX06145.1; -; Genomic_DNA.
DR   RefSeq; WP_014229605.1; NC_016612.1.
DR   STRING; 1006551.KOX_22125; -.
DR   EnsemblBacteria; AEX06145; AEX06145; KOX_22125.
DR   KEGG; kox:KOX_22125; -.
DR   PATRIC; fig|1006551.4.peg.4434; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   Proteomes; UP000007843; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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 {ECO:0000313|Proteomes:UP000007843};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        2     82       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       89    189       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        74     74       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       157    157       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       161    161       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   193 AA;  21159 MW;  201CFB6524BB3A28 CRC64;
     MSFELPALPY AKDALAPHIS AETLEYHYGK HHQAYVTNLN NLIKGTPFEG KTLEEIVRSS
     DGGVFNNAAQ VWNHTFYWNC LAPNAGGEPQ GELAAAIAKS FGSFADFKAK FTDAAAKNFG
     AGWTWLVKNA DGSLAIVSTS NAGTPLTSDA TPLLTVDVWE HAYYIDYRNA RPNYLEHFWA
     LVNWKFVAAN LAA
//
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