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Database: UniProt
Entry: J6H2F7_9PORP
LinkDB: J6H2F7_9PORP
Original site: J6H2F7_9PORP 
ID   J6H2F7_9PORP            Unreviewed;       191 AA.
AC   J6H2F7;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   13-FEB-2019, entry version 24.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodB {ECO:0000313|EMBL:EJU17298.1};
GN   ORFNames=HMPREF1323_1162 {ECO:0000313|EMBL:EJU17298.1};
OS   Porphyromonas sp. oral taxon 279 str. F0450.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC   Porphyromonadaceae; Porphyromonas.
OX   NCBI_TaxID=1125723 {ECO:0000313|EMBL:EJU17298.1, ECO:0000313|Proteomes:UP000004156};
RN   [1] {ECO:0000313|EMBL:EJU17298.1, ECO:0000313|Proteomes:UP000004156}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0450 {ECO:0000313|EMBL:EJU17298.1,
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:EJU17298.1}.
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DR   EMBL; ALKJ01000016; EJU17298.1; -; Genomic_DNA.
DR   RefSeq; WP_009432751.1; NZ_ALKJ01000016.1.
DR   ProteinModelPortal; J6H2F7; -.
DR   EnsemblBacteria; EJU17298; EJU17298; HMPREF1323_1162.
DR   PATRIC; fig|1125723.3.peg.649; -.
DR   BioCyc; GCF_000292995-HMP:HMPREF1323_RS03320-MONOMER; -.
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   ECO:0000313|EMBL:EJU17298.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004156}.
FT   DOMAIN        2     81       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       89    190       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        74     74       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       157    157       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       161    161       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   191 AA;  21296 MW;  3FA8FD654B73ED8A CRC64;
     MKYELIQLPY APNALEPAIS AETLSFHHGK HLAGYVNTLN GLIEGTEYAE LPLEELVRKS
     EGPIFNNAGQ LLNHNLYFTQ FGPNKGGQPT GKLLDAIVAK WGSFEAFQQE FLTACTTLFG
     SGWAWLAAKA DGELVITKEP NGSNPVVQGL RPLFGVDVWE HAYYLSYQNR RADHVKDLWA
     IVDWDVVASR Y
//
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