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Database: UniProt
Entry: J4VTS0_9PORP
LinkDB: J4VTS0_9PORP
Original site: J4VTS0_9PORP 
ID   J4VTS0_9PORP            Unreviewed;       244 AA.
AC   J4VTS0;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   16-JAN-2019, entry version 25.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=HMPREF1323_0376 {ECO:0000313|EMBL:EJU17971.1};
OS   Porphyromonas sp. oral taxon 279 str. F0450.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC   Porphyromonadaceae; Porphyromonas.
OX   NCBI_TaxID=1125723 {ECO:0000313|EMBL:EJU17971.1, ECO:0000313|Proteomes:UP000004156};
RN   [1] {ECO:0000313|EMBL:EJU17971.1, ECO:0000313|Proteomes:UP000004156}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0450 {ECO:0000313|EMBL:EJU17971.1,
RC   ECO:0000313|Proteomes:UP000004156};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B.,
RA   Sutton G., Nelson K.E.;
RL   Submitted (JUL-2012) 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}.
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:EJU17971.1}.
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DR   EMBL; ALKJ01000009; EJU17971.1; -; Genomic_DNA.
DR   RefSeq; WP_009432293.1; NZ_ALKJ01000009.1.
DR   ProteinModelPortal; J4VTS0; -.
DR   EnsemblBacteria; EJU17971; EJU17971; HMPREF1323_0376.
DR   PATRIC; fig|1125723.3.peg.181; -.
DR   Proteomes; UP000004156; 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:UP000004156};
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:UP000004156};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22    244       Superoxide dismutase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5003781271.
FT   DOMAIN       44    122       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      133    234       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        68     68       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       115    115       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       201    201       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       205    205       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   244 AA;  27337 MW;  CA8EE091FC53F503 CRC64;
     MRIRSLALLL TGALAISSLS AQTKTTKATA TAPAATAEPA KPAFQLFDLS YATDALAPVI
     SQRTVELHYG KHVVGYLHKL NKLVHENDIK ERDLARLVRF SSGAIFDNAG QLLNHLLYFK
     QFRPYEAGRV TEPQGALRAA LLRSYKDFDA FKADFEKAGG EIFGSGWLWL STDEAGDIYV
     EKTSNAGTPV TRGRVPLLAI DIWEHAYYLD YENRRADHLR AIWQIIDWEV VGRRYEARAK
     GVQL
//
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