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Database: UniProt
Entry: A0A1D7XSK4_9FLAO
LinkDB: A0A1D7XSK4_9FLAO
Original site: A0A1D7XSK4_9FLAO 
ID   A0A1D7XSK4_9FLAO        Unreviewed;       202 AA.
AC   A0A1D7XSK4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   16-JAN-2019, entry version 9.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=FORMA_11420 {ECO:0000313|EMBL:AOR26305.1};
OS   Formosa sp. Hel3_A1_48.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Formosa.
OX   NCBI_TaxID=1336795 {ECO:0000313|EMBL:AOR26305.1, ECO:0000313|Proteomes:UP000094318};
RN   [1] {ECO:0000313|EMBL:AOR26305.1, ECO:0000313|Proteomes:UP000094318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hel3_A1_48 {ECO:0000313|EMBL:AOR26305.1,
RC   ECO:0000313|Proteomes:UP000094318};
RA   Unfried F., Harder J., Teeling H., Hahnke R.L., Markert S.,
RA   Kappelmann L., Chafee M.;
RT   "Glycan utilization in Formosa spp.";
RL   Submitted (SEP-2016) 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:
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; CP017259; AOR26305.1; -; Genomic_DNA.
DR   RefSeq; WP_069674705.1; NZ_CP017259.1.
DR   EnsemblBacteria; AOR26305; AOR26305; FORMA_11420.
DR   KEGG; foh:FORMA_11420; -.
DR   PATRIC; fig|1336795.4.peg.1092; -.
DR   KO; K04564; -.
DR   OrthoDB; 1440645at2; -.
DR   Proteomes; UP000094318; 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:UP000094318};
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:UP000094318}.
FT   DOMAIN        3     85       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       93    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;  22388 MW;  6BB44779C76BF711 CRC64;
     MAFELPKLNY AYDALEPNID ARTMEIHHSK HHNGYTTKLN AAISGTALEN QSIESILSSL
     DMSNKAVRNN GGGFYNHSLF WEVMSPIDKG ELSGELKDAI LEAYGSFEDF KSAFSNAAAT
     QFGSGWAWLC VHKGGKVEVC ATPNQDNPLM PGVSCGGTPI LGIDVWEHAY YLNYQNRRPD
     YINAFFNVIN WNEVAKRFAA AK
//
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