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Database: UniProt
Entry: K1LNX7_9LACT
LinkDB: K1LNX7_9LACT
Original site: K1LNX7_9LACT 
ID   K1LNX7_9LACT            Unreviewed;       201 AA.
AC   K1LNX7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   05-DEC-2018, entry version 25.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=HMPREF9707_01575 {ECO:0000313|EMBL:EKB53822.1};
OS   Facklamia ignava CCUG 37419.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Aerococcaceae;
OC   Facklamia.
OX   NCBI_TaxID=883112 {ECO:0000313|EMBL:EKB53822.1, ECO:0000313|Proteomes:UP000005147};
RN   [1] {ECO:0000313|EMBL:EKB53822.1, ECO:0000313|Proteomes:UP000005147}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 37419 {ECO:0000313|EMBL:EKB53822.1,
RC   ECO:0000313|Proteomes:UP000005147};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B.,
RA   Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA   Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Facklamia ignava CCUG 37419.";
RL   Submitted (JUL-2012) 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:
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|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:EKB53822.1}.
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DR   EMBL; AGZE01000037; EKB53822.1; -; Genomic_DNA.
DR   RefSeq; WP_006702208.1; NZ_JH932301.1.
DR   ProteinModelPortal; K1LNX7; -.
DR   EnsemblBacteria; EKB53822; EKB53822; HMPREF9707_01575.
DR   PATRIC; fig|883112.3.peg.1573; -.
DR   OrthoDB; POG091H03Q7; -.
DR   Proteomes; UP000005147; 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   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 {ECO:0000313|Proteomes:UP000005147};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005147}.
FT   DOMAIN        3     88       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      100    196       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        81     81       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       164    164       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       168    168       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   201 AA;  23379 MW;  E68FD7B741CA1319 CRC64;
     MAFELPKLPY EYDALEPVID KQTMEIHHTK HHQAYVTNLN KVIEGTEYES LELEELVKKI
     DTLPESIQTA VRNNGGGHLN HSLFWNLLQS PNEETTIPSE LSDKLIEDFG SIESFKEKFE
     ASAKGRFGSG WAWLVDNQGT LEVIDLPNQD NPLMIGKTPL FGLDVWEHAY YLNYQNRRPE
     YVSNFWKVVN WEQVNKLWKE I
//
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