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Database: UniProt
Entry: A0A090D360_9BACT
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ID   A0A090D360_9BACT        Unreviewed;       182 AA.
AC   A0A090D360;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   10-APR-2019, entry version 19.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=sodc3 {ECO:0000313|EMBL:CDR34968.1};
GN   ORFNames=CSEC_2162 {ECO:0000313|EMBL:CDR34968.1};
OS   Criblamydia sequanensis CRIB-18.
OC   Bacteria; Chlamydiae; Parachlamydiales; Criblamydiaceae; Criblamydia.
OX   NCBI_TaxID=1437425 {ECO:0000313|EMBL:CDR34968.1};
RN   [1] {ECO:0000313|EMBL:CDR34968.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRIB-18 {ECO:0000313|EMBL:CDR34968.1};
RA   Linke B.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDR34968.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRIB-18 {ECO:0000313|EMBL:CDR34968.1};
RA   Bertelli C., Goesmann A., Greub G.;
RT   "Criblamydia sequanensis harbors a mega-plasmid encoding arsenite
RT   resistance.";
RL   Submitted (SEP-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:CDR34968.1}.
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DR   EMBL; CCEJ010000011; CDR34968.1; -; Genomic_DNA.
DR   RefSeq; WP_041018526.1; NZ_CCEJ010000011.1.
DR   STRING; 1437425.CSEC_2162; -.
DR   EnsemblBacteria; CDR34968; CDR34968; CSEC_2162.
DR   OrthoDB; 2015673at2; -.
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   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393,
KW   ECO:0000313|EMBL:CDR34968.1}; Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       43    174       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   182 AA;  19585 MW;  CF683953BB6F1B73 CRC64;
     MNQVLRFHIL LAAALIFFGC QSKKEESAPP IKKAKAILLP TEGNEAVGEV YFEETGEGVL
     ITAVITKLKT GKHGFHIHEK GDCSAKDASS AGAHFNPDNE PHAGPLDKKR HVGDLGNLEA
     DESGVARYKR MDKVVQLNGS KSIIGRSVIV HEKEDDFVTQ PTGDAGGRLA CGVILPFDEE
     AK
//
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