GenomeNet

Database: UniProt
Entry: A0A1M4ZTW3_9FLAO
LinkDB: A0A1M4ZTW3_9FLAO
Original site: A0A1M4ZTW3_9FLAO 
ID   A0A1M4ZTW3_9FLAO        Unreviewed;       184 AA.
AC   A0A1M4ZTW3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   05-DEC-2018, 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=SAMN05444377_10518 {ECO:0000313|EMBL:SHF21385.1};
OS   Flavobacterium fontis.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1124188 {ECO:0000313|EMBL:SHF21385.1, ECO:0000313|Proteomes:UP000184147};
RN   [1] {ECO:0000313|EMBL:SHF21385.1, ECO:0000313|Proteomes:UP000184147}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25660 {ECO:0000313|EMBL:SHF21385.1,
RC   ECO:0000313|Proteomes:UP000184147};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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}.
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; FQVQ01000005; SHF21385.1; -; Genomic_DNA.
DR   Proteomes; UP000184147; 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   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   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000184147};
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:UP000184147};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       48    182       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   184 AA;  19438 MW;  AA28D2546F8C4A1C CRC64;
     MLGINIFEIK KMKISILRLL VLTGLLISCK SSTEPDKTVT IALQPKSNSV VAGTALFTEK
     KGTVQLKVSL SGLQPGVHAI HIHEKADCSA ADATSAGGHW NPTFSKHGKW GEGEYHKGDI
     GNFTADAQGN ATVEFATDQW CIGCGDPNKD ILNKGLIVHE KADDFVSQPT GNAGGRVACA
     GIIK
//
DBGET integrated database retrieval system