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Database: UniProt
Entry: A0M6S2_GRAFK
LinkDB: A0M6S2_GRAFK
Original site: A0M6S2_GRAFK 
ID   A0M6S2_GRAFK            Unreviewed;       202 AA.
AC   A0M6S2;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   16-JAN-2019, entry version 79.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodA {ECO:0000313|EMBL:CAL68317.1};
GN   OrderedLocusNames=GFO_3377 {ECO:0000313|EMBL:CAL68317.1};
OS   Gramella forsetii (strain KT0803).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Gramella.
OX   NCBI_TaxID=411154 {ECO:0000313|EMBL:CAL68317.1, ECO:0000313|Proteomes:UP000000755};
RN   [1] {ECO:0000313|EMBL:CAL68317.1, ECO:0000313|Proteomes:UP000000755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT0803 {ECO:0000313|EMBL:CAL68317.1,
RC   ECO:0000313|Proteomes:UP000000755};
RX   PubMed=17107561; DOI=10.1111/j.1462-2920.2006.01152.x;
RA   Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E.,
RA   Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K.,
RA   Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I.,
RA   Gloeckner F.O.;
RT   "Whole genome analysis of the marine Bacteroidetes'Gramella forsetii'
RT   reveals adaptations to degradation of polymeric organic matter.";
RL   Environ. Microbiol. 8:2201-2213(2006).
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}.
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DR   EMBL; CU207366; CAL68317.1; -; Genomic_DNA.
DR   RefSeq; WP_011711218.1; NC_008571.1.
DR   ProteinModelPortal; A0M6S2; -.
DR   STRING; 411154.GFO_3377; -.
DR   EnsemblBacteria; CAL68317; CAL68317; GFO_3377.
DR   KEGG; gfo:GFO_3377; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; 1440645at2; -.
DR   BioCyc; GFOR411154:G1GJG-3215-MONOMER; -.
DR   Proteomes; UP000000755; 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:UP000000755};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:CAL68317.1}.
FT   DOMAIN        2     85       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       92    197       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        77     77       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;  22364 MW;  7CD0317A5D4A6C27 CRC64;
     MSFELPKLKY AFDALEPHID AKTMEIHHGK HHAGYTKKLN AAIEGTDMDG KNIENILKNL
     DKSNKAVRNN GGGFYNHSLF WEIMSPDGGG KPEGELASAI DAAYGSFEAF KEEFSKAAAG
     QFGSGWAWLC VHNGGKVEVC STPNQDNPLM PEVGCGGAPI LGLDVWEHAY YLNYQNKRPE
     YIDAFFNVID WKEVSSRYAK AK
//
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