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Database: UniProt
Entry: X5MHC6_9RHIZ
LinkDB: X5MHC6_9RHIZ
Original site: X5MHC6_9RHIZ 
ID   X5MHC6_9RHIZ            Unreviewed;       172 AA.
AC   X5MHC6;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   16-JAN-2019, entry version 22.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=BN1012_Phect2882 {ECO:0000313|EMBL:CDO61094.1};
OS   Candidatus Phaeomarinobacter ectocarpi.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhodobiaceae; Candidatus Phaeomarinobacter.
OX   NCBI_TaxID=1458461 {ECO:0000313|EMBL:CDO61094.1, ECO:0000313|Proteomes:UP000032160};
RN   [1] {ECO:0000313|EMBL:CDO61094.1, ECO:0000313|Proteomes:UP000032160}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ec32 {ECO:0000313|EMBL:CDO61094.1};
RX   PubMed=25120558; DOI=10.3389/fgene.2014.00241;
RA   Dittami S.M., Barbeyron T., Boyen C., Cambefort J., Collet G.,
RA   Delage L., Gobet A., Groisillier A., Leblanc C., Michel G.,
RA   Scornet D., Siegel A., Tapia J.E., Tonon T.;
RT   "Genome and metabolic network of "Candidatus Phaeomarinobacter
RT   ectocarpi" Ec32, a new candidate genus of Alphaproteobacteria
RT   frequently associated with brown algae.";
RL   Front. Genet. 5:241-241(2014).
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; HG966617; CDO61094.1; -; Genomic_DNA.
DR   RefSeq; WP_043948983.1; NZ_HG966617.1.
DR   EnsemblBacteria; CDO61094; CDO61094; BN1012_Phect2882.
DR   PATRIC; fig|1458461.3.peg.2888; -.
DR   OrthoDB; 2015673at2; -.
DR   Proteomes; UP000032160; 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; 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; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000032160};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393,
KW   ECO:0000313|EMBL:CDO61094.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032160};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23    172       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004959538.
FT   DOMAIN       33    170       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   172 AA;  17492 MW;  F48CCE5E3084A084 CRC64;
     MKHCIAALAC AGLIAGASSA LAEPLEVDII GGEGTSIGTA TLHDAPTGVL MRIEIGEDGL
     EPGWHGMHLH SVGDCSDVGT FKLSKGHINF DDQEHGLLNE NGPDNADLPN IHADDDGAVS
     AELLTTLVSM TGDRGLLDED GSALVIHANE DDHMTQPIGG AGGRVACGVI GG
//
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