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Database: UniProt
Entry: A0A251XAS4_9GAMM
LinkDB: A0A251XAS4_9GAMM
Original site: A0A251XAS4_9GAMM 
ID   A0A251XAS4_9GAMM        Unreviewed;       173 AA.
AC   A0A251XAS4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=TPSD3_06725 {ECO:0000313|EMBL:OUD14642.1};
OS   Thioflexithrix psekupsensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Thioflexithrix.
OX   NCBI_TaxID=1570016 {ECO:0000313|EMBL:OUD14642.1, ECO:0000313|Proteomes:UP000194798};
RN   [1] {ECO:0000313|EMBL:OUD14642.1, ECO:0000313|Proteomes:UP000194798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D3 {ECO:0000313|EMBL:OUD14642.1};
RA   Fomenkov A., Vincze T., Grabovich M., Anton B.P., Dubinina G., Orlova M.,
RA   Belousova E., Roberts R.J.;
RT   "Thioflexothrix psekupsii D3 genome sequencing and assembly.";
RL   Submitted (DEC-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. {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. {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00010457, ECO:0000256|RuleBase:RU000393}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OUD14642.1}.
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DR   EMBL; MSLT01000012; OUD14642.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A251XAS4; -.
DR   Proteomes; UP000194798; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
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; Superoxide dismutase, copper/zinc binding domain; 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:SF71; SUPEROXIDE DISMUTASE [CU-ZN]; 1.
DR   PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 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   Reference proteome {ECO:0000313|Proteomes:UP000194798};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN          40..172
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
SQ   SEQUENCE   173 AA;  17786 MW;  F9681828EDB12C69 CRC64;
     MASFAADHSS HNHTPAAAVE NGVVVTLHLI SNQGIEKEIG TVTLSDSSYG LLLTPQLTDL
     TAGIHGFHVH QNGSCEPLEK DGQMVAGLAA GGHFDPHNTG KHLGPYADGH LGDLPPLVAN
     ENGEATLQVL APRLKVADIL GKSLMVHVGG DNYSDDPKPL GGGGPRLACG VIS
//
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