GenomeNet

Database: UniProt
Entry: K8EPK1_9CHLO
LinkDB: K8EPK1_9CHLO
Original site: K8EPK1_9CHLO 
ID   K8EPK1_9CHLO            Unreviewed;       208 AA.
AC   K8EPK1;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   10-APR-2019, entry version 28.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=Bathy15g00500 {ECO:0000313|EMBL:CCO19981.1};
OS   Bathycoccus prasinos.
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Bathycoccaceae; Bathycoccus.
OX   NCBI_TaxID=41875 {ECO:0000313|EMBL:CCO19981.1};
RN   [1] {ECO:0000313|EMBL:CCO19981.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC 1105 {ECO:0000313|EMBL:CCO19981.1};
RA   Genoscope - CEA;
RL   Submitted (OCT-2011) 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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; FO082264; CCO19981.1; -; Genomic_DNA.
DR   RefSeq; XP_007508895.1; XM_007508833.1.
DR   STRING; 41875.XP_007508895.1; -.
DR   GeneID; 19011539; -.
DR   KEGG; bpg:Bathy15g00500; -.
DR   KO; K04565; -.
DR   OrthoDB; 1574423at2759; -.
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; 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   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       61    204       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   208 AA;  21456 MW;  45B6543324B5F4E7 CRC64;
     MNALLTARII DSLFTREYND NIINNNNIHR LKTVSKAARK TPVAFAVNAE QKAVVVLTGT
     AGVAGTLTLT QDDPSGATTV VGDITGLAPG KHGLHVHEFG DTTNGCMSTG PHFNPNKMTH
     GAPTDSVRHA GDLGNVIADA GGCKFTIKDM QIPLSGANSI VGRAFVIHEL EDDLGKGDNS
     EIGTQGKTSS TTGNAGARLA CGVVGLTP
//
DBGET integrated database retrieval system