GenomeNet

Database: UniProt
Entry: F9VBP4_LACGL
LinkDB: F9VBP4_LACGL
Original site: F9VBP4_LACGL 
ID   F9VBP4_LACGL            Unreviewed;       202 AA.
AC   F9VBP4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   16-JAN-2019, entry version 35.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=LCGL_0285 {ECO:0000313|EMBL:BAK59745.1};
OS   Lactococcus garvieae (strain Lg2) (Enterococcus seriolicida).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=420890 {ECO:0000313|EMBL:BAK59745.1, ECO:0000313|Proteomes:UP000008520};
RN   [1] {ECO:0000313|EMBL:BAK59745.1, ECO:0000313|Proteomes:UP000008520}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lg2 {ECO:0000313|EMBL:BAK59745.1,
RC   ECO:0000313|Proteomes:UP000008520};
RX   PubMed=21829716; DOI=10.1371/journal.pone.0023184;
RA   Morita H., Toh H., Oshima K., Yoshizaki M., Kawanishi M., Nakaya K.,
RA   Suzuki T., Miyauchi E., Ishii Y., Tanabe S., Murakami M., Hattori M.;
RT   "Complete genome sequence and comparative analysis of the fish
RT   pathogen Lactococcus garvieae.";
RL   PLoS ONE 6:E23184-E23184(2011).
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   -----------------------------------------------------------------------
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; AP009333; BAK59745.1; -; Genomic_DNA.
DR   RefSeq; WP_014024256.1; NC_017490.1.
DR   STRING; 420890.LCGL_0285; -.
DR   EnsemblBacteria; BAK59745; BAK59745; LCGL_0285.
DR   GeneID; 34203832; -.
DR   KEGG; lgv:LCGL_0285; -.
DR   PATRIC; fig|420890.5.peg.283; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; 1440645at2; -.
DR   BioCyc; LGAR420890:G1H60-291-MONOMER; -.
DR   Proteomes; UP000008520; Chromosome.
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:UP000008520};
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:UP000008520}.
FT   DOMAIN        2     89       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       97    196       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       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   202 AA;  23006 MW;  FC1EDC8E28AF342F CRC64;
     MAYTLPELPY AYDALEPFFD EETMHLHHDK HHQTYVNNLN AAIEKHPEFF DKTVEELVAY
     LDRLPEDIRV AVRNNGGGHL NHTMFWEWLA PNAGGAPTGD IAAAIDEAFG SFDDFKAEFK
     AAATGRFGSG WAWLVLDYGK LKVVSTANQD NPISDGQIPV LGLDVWEHAY YLKYHNVRPD
     YIEAFFNLIN WDKVNELYAK AK
//
DBGET integrated database retrieval system