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Database: UniProt/TrEMBL
Entry: F2NCX7_DESAR
LinkDB: F2NCX7_DESAR
Original site: F2NCX7_DESAR 
ID   F2NCX7_DESAR            Unreviewed;       216 AA.
AC   F2NCX7;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   07-JUN-2017, entry version 35.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=Desac_1710 {ECO:0000313|EMBL:AEB09551.1};
OS   Desulfobacca acetoxidans (strain ATCC 700848 / DSM 11109 / ASRB2).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophaceae; Desulfobacca.
OX   NCBI_TaxID=880072 {ECO:0000313|EMBL:AEB09551.1, ECO:0000313|Proteomes:UP000000483};
RN   [1] {ECO:0000313|Proteomes:UP000000483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700848 / DSM 11109 / ASRB2
RC   {ECO:0000313|Proteomes:UP000000483};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA   Teshima H., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schueler E.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Desulfobacca acetoxidans DSM 11109.";
RL   Submitted (MAR-2011) 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}.
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DR   EMBL; CP002629; AEB09551.1; -; Genomic_DNA.
DR   RefSeq; WP_013706661.1; NC_015388.1.
DR   ProteinModelPortal; F2NCX7; -.
DR   STRING; 880072.Desac_1710; -.
DR   EnsemblBacteria; AEB09551; AEB09551; Desac_1710.
DR   KEGG; dao:Desac_1710; -.
DR   eggNOG; ENOG4107XIJ; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OMA; YEHAYFI; -.
DR   OrthoDB; POG091H03Q7; -.
DR   BioCyc; DACE880072:GHK9-1684-MONOMER; -.
DR   Proteomes; UP000000483; 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:UP000000483};
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:UP000000483};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     25       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        26    216       Superoxide dismutase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5003282525.
FT   DOMAIN       45    104       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      112    213       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        52     52       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        97     97       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       180    180       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       184    184       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   216 AA;  24163 MW;  C369640E1C384150 CRC64;
     MPITMKSVLA FLTILTLFVV TTAAAAPVTY QAKDFSRLRG MKGFSDQALE LHFVLYQGYV
     KNTNAMLETL AQIASSTPAY AEMKRRLGWE YNGMRLHELY FGNLGGDGKI PPDSKIAKRL
     TEQFGSLESW ANDFKATGAM RGIGWVVLYE DQASGRLINT WINEHDLGHL AGGQPLLVMD
     VFEHAFIPDY GLKKGDYIEA FFQNIDWKAV DARLGK
//
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