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Database: UniProt/TrEMBL
Entry: A0A0B4XLG0_9GAMM
LinkDB: A0A0B4XLG0_9GAMM
Original site: A0A0B4XLG0_9GAMM 
ID   A0A0B4XLG0_9GAMM        Unreviewed;       192 AA.
AC   A0A0B4XLG0;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   25-OCT-2017, entry version 13.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=S7S_05475 {ECO:0000313|EMBL:AJD47515.1};
OS   Alcanivorax pacificus W11-5.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=391936 {ECO:0000313|EMBL:AJD47515.1, ECO:0000313|Proteomes:UP000006764};
RN   [1] {ECO:0000313|EMBL:AJD47515.1, ECO:0000313|Proteomes:UP000006764}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W11-5 {ECO:0000313|EMBL:AJD47515.1};
RX   PubMed=23209202; DOI=10.1128/JB.01845-12;
RA   Lai Q., Shao Z.;
RT   "Genome sequence of an alkane-degrading bacterium, Alcanivorax
RT   pacificus type strain W11-5, isolated from deep sea sediment.";
RL   J. Bacteriol. 194:6936-6936(2012).
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; CP004387; AJD47515.1; -; Genomic_DNA.
DR   RefSeq; WP_008737498.1; NZ_CP004387.1.
DR   ProteinModelPortal; A0A0B4XLG0; -.
DR   EnsemblBacteria; AJD47515; AJD47515; S7S_05475.
DR   KEGG; apac:S7S_05475; -.
DR   KO; K04564; -.
DR   Proteomes; UP000006764; 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:UP000006764};
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:UP000006764}.
FT   DOMAIN        3     83       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       90    189       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        75     75       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   192 AA;  21148 MW;  38F02BEEE7C5988F CRC64;
     MAFELPALPY AKDALAPHMS AETLEFHYGK HHQTYVTKLN ELVAGTDKEG QSLEDIIKGA
     GPGPLFNNAA QVWNHTFFWN SLSPNGGGEP TGALADAINA KWGSFDKFKE AFTNSAIGNF
     GSGWTWLVKN GNELEIVNTS NAATPLTDGK TALLTVDVWE HAYYIDYRNA RPKYLEGFWA
     LVNWEFAASN FA
//
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