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Database: UniProt
Entry: A0A0A2E0J8_9PORP
LinkDB: A0A0A2E0J8_9PORP
Original site: A0A0A2E0J8_9PORP 
ID   A0A0A2E0J8_9PORP        Unreviewed;       200 AA.
AC   A0A0A2E0J8;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   28-MAR-2018, entry version 15.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=HQ37_04585 {ECO:0000313|EMBL:KGN70004.1};
OS   Porphyromonas sp. COT-239 OH1446.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC   Porphyromonadaceae; Porphyromonas.
OX   NCBI_TaxID=1515613 {ECO:0000313|EMBL:KGN70004.1, ECO:0000313|Proteomes:UP000030150};
RN   [1] {ECO:0000313|EMBL:KGN70004.1, ECO:0000313|Proteomes:UP000030150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COT-239 OH1446 {ECO:0000313|Proteomes:UP000030150};
RA   Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA   Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S.,
RA   Eisen J.A.;
RT   "Porphyromonas sp. COT-239_OH1446 Genome sequencing.";
RL   Submitted (AUG-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KGN70004.1}.
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DR   EMBL; JRAO01000016; KGN70004.1; -; Genomic_DNA.
DR   EnsemblBacteria; KGN70004; KGN70004; HQ37_04585.
DR   Proteomes; UP000030150; Unassembled WGS sequence.
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:UP000030150};
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:UP000030150}.
FT   DOMAIN        2     78       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       88    187       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        25     25       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        72     72       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       156    156       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       160    160       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   200 AA;  22490 MW;  C3B02FDB799D41F1 CRC64;
     MKLIELPYAT DALSPVISKA TIELHHGKHL AGYVNNLNRL IKGTEFEGMA LGEIVCKSKG
     GIFNNAGQTL NHNLYFLQFA PKPRHSQPIG RLAQAIQRQW GGFAALRQVM EQTGGKLFGS
     GWLWLVVNTE GQLEVVTEAN GSNPIVRGMN PLLGFDLWEH AYYLDYQNRR ADHIKALWQI
     IDWEIIELRY QSSNTSCGIN
//
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