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SODM2_BACAN
ID   SODM2_BACAN             Reviewed;         208 AA.
AC   Q81JK8; Q6HQ51; Q6KJJ4;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Superoxide dismutase [Mn] 2;
DE            EC=1.15.1.1;
GN   Name=sodA2; Synonyms=sodA-2; OrderedLocusNames=BA_5696, GBAA_5696, BAS5300;
OS   Bacillus anthracis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1392;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames / isolate Porton;
RX   PubMed=12721629; DOI=10.1038/nature01586;
RA   Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA   Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA   Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA   Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA   DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA   Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA   Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA   Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA   White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA   Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT   "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT   related bacteria.";
RL   Nature 423:81-86(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames ancestor;
RX   PubMed=18952800; DOI=10.1128/jb.01347-08;
RA   Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA   Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT   "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL   J. Bacteriol. 191:445-446(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sterne;
RA   Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA   Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA   Richardson P., Rubin E., Tice H.;
RT   "Complete genome sequence of Bacillus anthracis Sterne.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological 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; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; AE016879; AAP29328.1; -; Genomic_DNA.
DR   EMBL; AE017334; AAT34855.1; -; Genomic_DNA.
DR   EMBL; AE017225; AAT57587.1; -; Genomic_DNA.
DR   RefSeq; NP_847842.1; NC_003997.3.
DR   RefSeq; WP_000094049.1; NZ_WXXJ01000017.1.
DR   RefSeq; YP_031537.1; NC_005945.1.
DR   PDB; 1XRE; X-ray; 1.80 A; A/B=1-208.
DR   PDBsum; 1XRE; -.
DR   AlphaFoldDB; Q81JK8; -.
DR   SMR; Q81JK8; -.
DR   STRING; 260799.BAS5300; -.
DR   DNASU; 1085438; -.
DR   EnsemblBacteria; AAP29328; AAP29328; BA_5696.
DR   EnsemblBacteria; AAT34855; AAT34855; GBAA_5696.
DR   GeneID; 45025271; -.
DR   KEGG; ban:BA_5696; -.
DR   KEGG; bar:GBAA_5696; -.
DR   KEGG; bat:BAS5300; -.
DR   PATRIC; fig|198094.11.peg.5658; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_0_1_9; -.
DR   OMA; FGTGWVW; -.
DR   EvolutionaryTrace; Q81JK8; -.
DR   Proteomes; UP000000427; Chromosome.
DR   Proteomes; UP000000594; 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; Manganese; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..208
FT                   /note="Superoxide dismutase [Mn] 2"
FT                   /id="PRO_0000160013"
FT   BINDING         28
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         83
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   TURN            13..19
FT                   /evidence="ECO:0007829|PDB:1XRE"
FT   HELIX           22..30
FT                   /evidence="ECO:0007829|PDB:1XRE"
FT   HELIX           32..44
FT                   /evidence="ECO:0007829|PDB:1XRE"
FT   HELIX           48..50
FT                   /evidence="ECO:0007829|PDB:1XRE"
FT   HELIX           55..60
FT                   /evidence="ECO:0007829|PDB:1XRE"
FT   HELIX           62..64
FT                   /evidence="ECO:0007829|PDB:1XRE"
FT   TURN            67..69
FT                   /evidence="ECO:0007829|PDB:1XRE"
FT   HELIX           70..88
FT                   /evidence="ECO:0007829|PDB:1XRE"
FT   HELIX           100..110
FT                   /evidence="ECO:0007829|PDB:1XRE"
FT   HELIX           113..125
FT                   /evidence="ECO:0007829|PDB:1XRE"
FT   STRAND          129..138
FT                   /evidence="ECO:0007829|PDB:1XRE"
FT   STRAND          141..148
FT                   /evidence="ECO:0007829|PDB:1XRE"
FT   HELIX           153..156
FT                   /evidence="ECO:0007829|PDB:1XRE"
FT   STRAND          159..165
FT                   /evidence="ECO:0007829|PDB:1XRE"
FT   HELIX           168..170
FT                   /evidence="ECO:0007829|PDB:1XRE"
FT   HELIX           172..175
FT                   /evidence="ECO:0007829|PDB:1XRE"
FT   HELIX           179..186
FT                   /evidence="ECO:0007829|PDB:1XRE"
FT   HELIX           187..189
FT                   /evidence="ECO:0007829|PDB:1XRE"
FT   HELIX           192..202
FT                   /evidence="ECO:0007829|PDB:1XRE"
SQ   SEQUENCE   208 AA;  24023 MW;  870D8FF1C721FD73 CRC64;
     MSSFQLPKLS YDYDELEPYI DSNTLSIHHG KHHATYVNNL NAALENYSEL HNKSLEELLC
     NLETLPKEIV TAVRNNGGGH YCHSLFWEVM SPRGGGEPNG DVAKVIDYYF NTFDNLKDQL
     SKAAISRFGS GYGWLVLDGE ELSVMSTPNQ DTPLQEGKIP LLVIDVWEHA YYLKYQNRRP
     EFVTNWWHTV NWDRVNEKYL QAIQSQKH
 
 
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