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Database: UniProt/TrEMBL
Entry: A0A1V2Z4M5_9ENTR
LinkDB: A0A1V2Z4M5_9ENTR
Original site: A0A1V2Z4M5_9ENTR 
ID   A0A1V2Z4M5_9ENTR        Unreviewed;       206 AA.
AC   A0A1V2Z4M5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-SEP-2017, entry version 4.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=BZY71_09530 {ECO:0000313|EMBL:OOB87344.1};
OS   Leclercia adecarboxylata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Leclercia.
OX   NCBI_TaxID=83655 {ECO:0000313|EMBL:OOB87344.1, ECO:0000313|Proteomes:UP000188927};
RN   [1] {ECO:0000313|EMBL:OOB87344.1, ECO:0000313|Proteomes:UP000188927}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=I1 {ECO:0000313|EMBL:OOB87344.1,
RC   ECO:0000313|Proteomes:UP000188927};
RA   Hoyos-Mallecot Y., Rojo-Martin M.D., Bonnin R., Navarro Mari J.M.,
RA   Naas T.;
RT   "Draft genome sequence of a NDM-1 producing Leclercia adecarboxylata
RT   from Spain.";
RL   Submitted (JAN-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OOB87344.1}.
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DR   EMBL; MUFS01000022; OOB87344.1; -; Genomic_DNA.
DR   RefSeq; WP_032615319.1; NZ_MUFS01000022.1.
DR   GeneID; 31869989; -.
DR   KEGG; lax:APT61_00450; -.
DR   KO; K04564; -.
DR   Proteomes; UP000188927; Unassembled WGS sequence.
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   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:UP000188927};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        2     89       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       96    201       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        82     82       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       168    168       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       172    172       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   206 AA;  22974 MW;  3A48B00356D5AC10 CRC64;
     MSYTLPSLPY AYDALEPHFD KQTMEIHHTK HHQTYVNNAN AALESLPEFA SLPAEELITK
     LDQLPADKKT VLRNNAGGHA NHSFFWKGLK TGTTLQGDLK AAIERDFGSV DNFKAEFEKA
     AATRFGSGWA WLVLKGDKLA VVSTANQDSP LMGEAISGAS GFPIVGLDVW EHAYYLKFQN
     RRPDYIKAFW DVVNWDEAAA RFAAKK
//
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