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Database: UniProt
Entry: A0A0U5JBL0_9BACT
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ID   A0A0U5JBL0_9BACT        Unreviewed;       209 AA.
AC   A0A0U5JBL0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   16-JAN-2019, entry version 12.
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:CUI16493.1};
GN   ORFNames=PNK_0868 {ECO:0000313|EMBL:CUI16493.1};
OS   Candidatus Protochlamydia naegleriophila.
OC   Bacteria; Chlamydiae; Parachlamydiales; Parachlamydiaceae;
OC   Candidatus Protochlamydia.
OX   NCBI_TaxID=389348 {ECO:0000313|EMBL:CUI16493.1, ECO:0000313|Proteomes:UP000069902};
RN   [1] {ECO:0000313|EMBL:CUI16493.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KNic {ECO:0000313|EMBL:CUI16493.1};
RA   Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA   Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA   Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL   Submitted (SEP-2015) 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: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; LN879502; CUI16493.1; -; Genomic_DNA.
DR   RefSeq; WP_032125362.1; NZ_LN879502.1.
DR   EnsemblBacteria; CUI16493; CUI16493; PNK_0868.
DR   KEGG; pnl:PNK_0868; -.
DR   PATRIC; fig|389348.3.peg.951; -.
DR   KO; K04565; -.
DR   OrthoDB; 2015673at2; -.
DR   Proteomes; UP000069902; Chromosome cPNK.
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   PRINTS; PR00068; CUZNDISMTASE.
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:UP000069902};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393,
KW   ECO:0000313|EMBL:CUI16493.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000069902};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       72    205       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   209 AA;  22147 MW;  54CAF2F6652FAFD6 CRC64;
     MLKKHLPTSF CHALKFSRFF VGALLITAVT SCACTDSRKP HARNGNNKNN EIADAGVIQA
     RQVKKAEAVV HGIKSDVKGI VTFTKVPGGV KIVADIDGLT PGKHGFHVHE HGDCGGEDGM
     AAGAHFNPTN HKHGGPDSPE RHVGDFGNLE ADAKGHAHYE RVDNLIELEG DNSIIGRSIM
     IHADEDDLVS QPSGNSGARI GCGVIESKP
//
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