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Database: UniProt
Entry: P19665
LinkDB: P19665
Original site: P19665 
ID   SODF_PORGI              Reviewed;         191 AA.
AC   P19665;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 2.
DT   16-JAN-2019, entry version 140.
DE   RecName: Full=Superoxide dismutase [Mn/Fe];
DE            EC=1.15.1.1;
GN   Name=sodB; OrderedLocusNames=PG_1545;
OS   Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC   Porphyromonadaceae; Porphyromonas.
OX   NCBI_TaxID=242619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2265754; DOI=10.1016/0378-1119(90)90357-W;
RA   Nakayama K.;
RT   "The superoxide dismutase-encoding gene of the obligately anaerobic
RT   bacterium Bacteroides gingivalis.";
RL   Gene 96:149-150(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1840572;
RA   Choi J.I., Takahashi N., Kato T., Kuramitsu H.K.;
RT   "Isolation, expression, and nucleotide sequence of the sod gene from
RT   Porphyromonas gingivalis.";
RL   Infect. Immun. 59:1564-1566(1991).
RN   [3]
RP   PROTEIN SEQUENCE.
RC   STRAIN=381;
RX   PubMed=2226833; DOI=10.1016/0014-5793(90)80488-5;
RA   Amano A., Shizukuishi S., Tsunemitsu A., Maekawa K., Tsunasawa S.;
RT   "The primary structure of superoxide dismutase purified from
RT   anaerobically maintained Bacteroides gingivalis.";
RL   FEBS Lett. 272:217-220(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-308 / W83;
RX   PubMed=12949112; DOI=10.1128/JB.185.18.5591-5601.2003;
RA   Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA   Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA   Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA   Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J.,
RA   Dewhirst F.E., Fraser C.M.;
RT   "Complete genome sequence of the oral pathogenic bacterium
RT   Porphyromonas gingivalis strain W83.";
RL   J. Bacteriol. 185:5591-5601(2003).
RN   [5]
RP   PROTEIN SEQUENCE OF 1-12.
RX   PubMed=2307656; DOI=10.1128/jb.172.3.1457-1463.1990;
RA   Amano A., Shizukuishi S., Tamagawa H., Iwakura K., Tsunasawa S.,
RA   Tsunemitsu A.;
RT   "Characterization of superoxide dismutases purified from either
RT   anaerobically maintained or aerated Bacteroides gingivalis.";
RL   J. Bacteriol. 172:1457-1463(1990).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   PubMed=10848964; DOI=10.1046/j.1432-1327.2000.01373.x;
RA   Sugio S., Hiraoka B.Y., Yamakura F.;
RT   "Crystal structure of cambialistic superoxide dismutase from
RT   Porphyromonas gingivalis.";
RL   Eur. J. Biochem. 267:3487-3495(2000).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       systems.
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC       Note=Binds 1 Mn(2+) or Fe(2+) ion per subunit.;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; D90152; BAA14182.1; -; Genomic_DNA.
DR   EMBL; M60401; AAA25651.1; -; Genomic_DNA.
DR   EMBL; AE015924; AAQ66583.1; -; Genomic_DNA.
DR   PIR; A43585; A43585.
DR   RefSeq; WP_004585361.1; NC_002950.2.
DR   PDB; 1QNN; X-ray; 1.80 A; A/B/C/D=1-191.
DR   PDB; 1UER; X-ray; 1.60 A; A/B/C/D=1-191.
DR   PDB; 1UES; X-ray; 1.60 A; A/B/C/D=1-191.
DR   PDBsum; 1QNN; -.
DR   PDBsum; 1UER; -.
DR   PDBsum; 1UES; -.
DR   ProteinModelPortal; P19665; -.
DR   SMR; P19665; -.
DR   STRING; 242619.PG1545; -.
DR   EnsemblBacteria; AAQ66583; AAQ66583; PG_1545.
DR   GeneID; 29255789; -.
DR   KEGG; pgi:PG_1545; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OMA; YEGWKGE; -.
DR   OrthoDB; 1440645at2; -.
DR   EvolutionaryTrace; P19665; -.
DR   Proteomes; UP000000588; 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   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Direct protein sequencing; Iron;
KW   Manganese; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN         1    191       Superoxide dismutase [Mn/Fe].
FT                                /FTId=PRO_0000159993.
FT   METAL        27     27       Manganese or iron.
FT   METAL        74     74       Manganese or iron.
FT   METAL       157    157       Manganese or iron.
FT   METAL       161    161       Manganese or iron.
FT   CONFLICT     13     13       D -> Y (in Ref. 2; AAA25651).
FT                                {ECO:0000305}.
FT   CONFLICT     29     29       G -> E (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    112    112       N -> D (in Ref. 2; AAA25651).
FT                                {ECO:0000305}.
FT   TURN         12     19       {ECO:0000244|PDB:1UER}.
FT   HELIX        21     27       {ECO:0000244|PDB:1UER}.
FT   TURN         28     30       {ECO:0000244|PDB:1UER}.
FT   HELIX        31     42       {ECO:0000244|PDB:1UER}.
FT   TURN         43     45       {ECO:0000244|PDB:1UER}.
FT   TURN         47     50       {ECO:0000244|PDB:1UER}.
FT   HELIX        53     59       {ECO:0000244|PDB:1UER}.
FT   HELIX        62     79       {ECO:0000244|PDB:1UER}.
FT   HELIX        91    101       {ECO:0000244|PDB:1UER}.
FT   HELIX       104    117       {ECO:0000244|PDB:1UER}.
FT   STRAND      120    128       {ECO:0000244|PDB:1UER}.
FT   STRAND      134    140       {ECO:0000244|PDB:1UER}.
FT   HELIX       145    148       {ECO:0000244|PDB:1UER}.
FT   STRAND      151    157       {ECO:0000244|PDB:1UER}.
FT   HELIX       160    162       {ECO:0000244|PDB:1UER}.
FT   HELIX       164    167       {ECO:0000244|PDB:1UER}.
FT   HELIX       171    178       {ECO:0000244|PDB:1UER}.
FT   HELIX       179    181       {ECO:0000244|PDB:1UER}.
FT   HELIX       184    190       {ECO:0000244|PDB:1UER}.
SQ   SEQUENCE   191 AA;  21501 MW;  AA53419397BF6BA1 CRC64;
     MTHELISLPY AVDALAPVIS KETVEFHHGK HLKTYVDNLN KLIIGTEFEN ADLNTIVQKS
     EGGIFNNAGQ TLNHNLYFTQ FRPGKGGAPK GKLGEAIDKQ FGSFEKFKEE FNTAGTTLFG
     SGWVWLASDA NGKLSIEKEP NAGNPVRKGL NPLLGFDVWE HAYYLTYQNR RADHLKDLWS
     IVDWDIVESR Y
//
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