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Database: UniProt
Entry: Q65RU9_MANSM
LinkDB: Q65RU9_MANSM
Original site: Q65RU9_MANSM 
ID   Q65RU9_MANSM            Unreviewed;       208 AA.
AC   Q65RU9;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   16-JAN-2019, entry version 90.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=sodC {ECO:0000313|EMBL:AAU38311.1};
GN   OrderedLocusNames=MS1704 {ECO:0000313|EMBL:AAU38311.1};
OS   Mannheimia succiniciproducens (strain MBEL55E).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Basfia.
OX   NCBI_TaxID=221988 {ECO:0000313|EMBL:AAU38311.1, ECO:0000313|Proteomes:UP000000607};
RN   [1] {ECO:0000313|EMBL:AAU38311.1, ECO:0000313|Proteomes:UP000000607}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBEL55E {ECO:0000313|EMBL:AAU38311.1,
RC   ECO:0000313|Proteomes:UP000000607};
RX   PubMed=15378067; DOI=10.1038/nbt1010;
RA   Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K.,
RA   Kim C.H., Jeong H., Hur C.G., Kim J.J.;
RT   "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT   succiniciproducens.";
RL   Nat. Biotechnol. 22:1275-1281(2004).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000393}.
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:RU000393};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 copper ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
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DR   EMBL; AE016827; AAU38311.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q65RU9; -.
DR   STRING; 221988.MS1704; -.
DR   EnsemblBacteria; AAU38311; AAU38311; MS1704.
DR   KEGG; msu:MS1704; -.
DR   eggNOG; ENOG4108Z7T; Bacteria.
DR   eggNOG; COG2032; LUCA.
DR   HOGENOM; HOG000263449; -.
DR   KO; K04565; -.
DR   OMA; HKGDIGN; -.
DR   Proteomes; UP000000607; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000607};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000607};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       69    207       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   208 AA;  21978 MW;  53B1EC2D135AD1A9 CRC64;
     MFIFHTMIVS LWHLPTFYLF TGAYMKKTVI LLGLFTLSGA AIAEEAKNVQ TEIKSKVIEV
     SLLDPVKGDK AIGQVVVTES PYGLVFTPEL NGLTAGLHGF HLHQNPSCAA GEKDGKKVAG
     LGAGGHWDPK EAKRHGFPWE DNAHLGDLPA LAVNADGTAS NPVLAPRLKS LDEIADKSIM
     IHVGGDNHSD HPAALGGGGA RMACGVIK
//
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