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Database: UniProt/TrEMBL
Entry: A0A1J0GLQ6_9CLOT
LinkDB: A0A1J0GLQ6_9CLOT
Original site: A0A1J0GLQ6_9CLOT 
ID   A0A1J0GLQ6_9CLOT        Unreviewed;       218 AA.
AC   A0A1J0GLQ6;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-SEP-2017, entry version 6.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=A7L45_20725 {ECO:0000313|EMBL:APC42308.1};
OS   Clostridium estertheticum subsp. estertheticum.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1552 {ECO:0000313|EMBL:APC42308.1, ECO:0000313|Proteomes:UP000182569};
RN   [1] {ECO:0000313|Proteomes:UP000182569}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8809 {ECO:0000313|Proteomes:UP000182569};
RX   PubMed=27891116;
RA   Yu Z., Gunn L., Brennan E., Reid R., Wall P.G., Gaora O.P., Hurley D.,
RA   Bolton D., Fanning S.;
RT   "Complete Genome Sequence of Clostridium estertheticum DSM 8809, a
RT   Microbe Identified in Spoiled Vacuum Packed Beef.";
RL   Front. Microbiol. 7:1764-1764(2016).
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; CP015756; APC42308.1; -; Genomic_DNA.
DR   RefSeq; WP_071614598.1; NZ_CP015756.1.
DR   KEGG; ceu:A7L45_20725; -.
DR   KO; K04564; -.
DR   Proteomes; UP000182569; 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; 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   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000182569};
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:UP000182569}.
FT   DOMAIN        3     83       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       90    190       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        25     25       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        76     76       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   218 AA;  25614 MW;  39F35E60909C1961 CRC64;
     MYNLKPKTFD FESVQGISKK QLDEHYKLYT GYVTKLNEIW NTPYTPDNYN DSNPTYSKMR
     SLKRGETYSL NGVKLHNLYF ENMTGGNNTP YGPIFNAIIN QFLSYDNFIS YLTNVGLSMR
     GWAVLTLDLL DNSLHIVGSD SHDNGAVWLS CPILIMDVYE HAYFMDFGTN RKKYISTFIE
     NINWNVLNER FERYISPLKS MDMMSKNIKK NRYYPYSY
//
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