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SODF_PORGI
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   03-AUG-2022, entry version 152.
DE   RecName: Full=Superoxide dismutase [Mn/Fe];
DE            EC=1.15.1.1 {ECO:0000305|PubMed:2307656};
GN   Name=sodB; Synonyms=sod {ECO:0000303|PubMed:1840572};
GN   OrderedLocusNames=PG_1545;
OS   Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   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].
RC   STRAIN=ATCC 53977;
RX   PubMed=1840572; DOI=10.1128/iai.59.4.1564-1566.1991;
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 anaerobically
RT   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., Dewhirst F.E.,
RA   Fraser C.M.;
RT   "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT   gingivalis strain W83.";
RL   J. Bacteriol. 185:5591-5601(2003).
RN   [5]
RP   PROTEIN SEQUENCE OF 1-12, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP   REGULATION, AND SUBUNIT.
RC   STRAIN=381;
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] {ECO:0007744|PDB:1QNN}
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH IRON, AND COFACTOR.
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 Porphyromonas
RT   gingivalis.";
RL   Eur. J. Biochem. 267:3487-3495(2000).
RN   [7] {ECO:0007744|PDB:1UER, ECO:0007744|PDB:1UES}
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF WILD-TYPE AND MUTANT THR-155 IN
RP   COMPLEX WITH IRON OR MANGANESE, COFACTOR, AND MUTAGENESIS OF GLY-155.
RX   PubMed=12962504; DOI=10.1021/bi0349625;
RA   Yamakura F., Sugio S., Hiraoka B.Y., Ohmori D., Yokota T.;
RT   "Pronounced conversion of the metal-specific activity of superoxide
RT   dismutase from Porphyromonas gingivalis by the mutation of a single amino
RT   acid (Gly155Thr) located apart from the active site.";
RL   Biochemistry 42:10790-10799(2003).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological systems.
CC       Catalyzes the dismutation of superoxide anion radicals into O2 and H2O2
CC       by successive reduction and oxidation of the transition metal ion at
CC       the active site.
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:0000305|PubMed:2307656};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20697;
CC         Evidence={ECO:0000305|PubMed:2307656};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:10848964, ECO:0000269|PubMed:2307656};
CC       Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC         Evidence={ECO:0000269|PubMed:10848964, ECO:0000269|PubMed:12962504,
CC         ECO:0000269|PubMed:2307656};
CC       Note=Binds 1 Mn(2+) or Fe(3+) ion per subunit.
CC       {ECO:0000269|PubMed:10848964, ECO:0000269|PubMed:12962504};
CC   -!- ACTIVITY REGULATION: Inhibited by hydrogen peroxide.
CC       {ECO:0000269|PubMed:2307656}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:2307656}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
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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   AlphaFoldDB; P19665; -.
DR   SMR; P19665; -.
DR   STRING; 242619.PG_1545; -.
DR   EnsemblBacteria; AAQ66583; AAQ66583; PG_1545.
DR   GeneID; 29255789; -.
DR   KEGG; pgi:PG_1545; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_0_0_10; -.
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; 3.55.40.20; -; 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; Direct protein sequencing; Iron; Manganese; Metal-binding;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..191
FT                   /note="Superoxide dismutase [Mn/Fe]"
FT                   /id="PRO_0000159993"
FT   BINDING         27
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000269|PubMed:12962504,
FT                   ECO:0007744|PDB:1QNN, ECO:0007744|PDB:1UER"
FT   BINDING         27
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000269|PubMed:12962504,
FT                   ECO:0007744|PDB:1UES"
FT   BINDING         74
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000269|PubMed:12962504,
FT                   ECO:0007744|PDB:1QNN, ECO:0007744|PDB:1UER"
FT   BINDING         74
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000269|PubMed:12962504,
FT                   ECO:0007744|PDB:1UES"
FT   BINDING         157
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000269|PubMed:12962504,
FT                   ECO:0007744|PDB:1QNN, ECO:0007744|PDB:1UER"
FT   BINDING         157
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000269|PubMed:12962504,
FT                   ECO:0007744|PDB:1UES"
FT   BINDING         161
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000269|PubMed:12962504,
FT                   ECO:0007744|PDB:1QNN, ECO:0007744|PDB:1UER"
FT   BINDING         161
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000269|PubMed:12962504,
FT                   ECO:0007744|PDB:1UES"
FT   MUTAGEN         155
FT                   /note="G->T: Converts the metal-specific activity of the
FT                   enzyme from a cambialistic type (showing the same activity
FT                   with Fe and Mn) to an Fe-specific type."
FT                   /evidence="ECO:0000269|PubMed:12962504"
FT   CONFLICT        13
FT                   /note="D -> Y (in Ref. 2; AAA25651)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        29
FT                   /note="G -> E (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        112
FT                   /note="N -> D (in Ref. 2; AAA25651)"
FT                   /evidence="ECO:0000305"
FT   TURN            12..19
FT                   /evidence="ECO:0007829|PDB:1UER"
FT   HELIX           21..27
FT                   /evidence="ECO:0007829|PDB:1UER"
FT   TURN            28..30
FT                   /evidence="ECO:0007829|PDB:1UER"
FT   HELIX           31..42
FT                   /evidence="ECO:0007829|PDB:1UER"
FT   TURN            43..45
FT                   /evidence="ECO:0007829|PDB:1UER"
FT   TURN            47..50
FT                   /evidence="ECO:0007829|PDB:1UER"
FT   HELIX           53..59
FT                   /evidence="ECO:0007829|PDB:1UER"
FT   HELIX           62..79
FT                   /evidence="ECO:0007829|PDB:1UER"
FT   HELIX           91..101
FT                   /evidence="ECO:0007829|PDB:1UER"
FT   HELIX           104..117
FT                   /evidence="ECO:0007829|PDB:1UER"
FT   STRAND          120..128
FT                   /evidence="ECO:0007829|PDB:1UER"
FT   STRAND          134..140
FT                   /evidence="ECO:0007829|PDB:1UER"
FT   HELIX           145..148
FT                   /evidence="ECO:0007829|PDB:1UER"
FT   STRAND          151..157
FT                   /evidence="ECO:0007829|PDB:1UER"
FT   HELIX           160..162
FT                   /evidence="ECO:0007829|PDB:1UER"
FT   HELIX           164..167
FT                   /evidence="ECO:0007829|PDB:1UER"
FT   HELIX           171..178
FT                   /evidence="ECO:0007829|PDB:1UER"
FT   HELIX           179..181
FT                   /evidence="ECO:0007829|PDB:1UER"
FT   HELIX           184..190
FT                   /evidence="ECO:0007829|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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