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Database: UniProt
Entry: A0A1G5M9R9_AFIMA
LinkDB: A0A1G5M9R9_AFIMA
Original site: A0A1G5M9R9_AFIMA 
ID   A0A1G5M9R9_AFIMA        Unreviewed;       179 AA.
AC   A0A1G5M9R9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   13-FEB-2019, entry version 5.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=SAMN03080610_00347 {ECO:0000313|EMBL:SCZ21923.1};
OS   Afifella marina DSM 2698.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhodobiaceae; Afifella.
OX   NCBI_TaxID=1120955 {ECO:0000313|EMBL:SCZ21923.1, ECO:0000313|Proteomes:UP000199347};
RN   [1] {ECO:0000313|EMBL:SCZ21923.1, ECO:0000313|Proteomes:UP000199347}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2698 {ECO:0000313|EMBL:SCZ21923.1,
RC   ECO:0000313|Proteomes:UP000199347};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FMVW01000001; SCZ21923.1; -; Genomic_DNA.
DR   BioCyc; GCF_900102695:BLP76_RS01715-MONOMER; -.
DR   Proteomes; UP000199347; Unassembled WGS sequence.
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:UP000199347};
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:UP000199347};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     18       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        19    179       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5011522876.
FT   DOMAIN       37    172       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   179 AA;  18710 MW;  E3537DC038ABC29F CRC64;
     MRLLAIAACA LMASPALAQD VSENSAFSGP ITGKDGTIGE AHLTDTPNGV LVQVVINEGA
     LKPGEHALHF HETGDCSDAP DFKKSGGHYN PTDAKHGIMT EGGMHAGDMP NFEVVDGQAT
     NIDVFNTRVR FNEGDAPLMD DDGSALMIHA GADDYTSQPS GDAGSRVGCM VIDDERAQQ
//
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