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Database: UniProt/TrEMBL
Entry: A0A127W4F4_SPOPS
LinkDB: A0A127W4F4_SPOPS
Original site: A0A127W4F4_SPOPS 
ID   A0A127W4F4_SPOPS        Unreviewed;       175 AA.
AC   A0A127W4F4;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   25-OCT-2017, entry version 10.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=AZE41_02065 {ECO:0000313|EMBL:AMQ08391.1};
OS   Sporosarcina psychrophila (Bacillus psychrophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae;
OC   Sporosarcina.
OX   NCBI_TaxID=1476 {ECO:0000313|EMBL:AMQ08391.1, ECO:0000313|Proteomes:UP000071057};
RN   [1] {ECO:0000313|EMBL:AMQ08391.1, ECO:0000313|Proteomes:UP000071057}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6497 {ECO:0000313|EMBL:AMQ08391.1,
RC   ECO:0000313|Proteomes:UP000071057};
RA   Yan W.;
RT   "Complete genome sequence of the Sporosarcina psychrophila DSM6497, a
RT   psychrophila Bacillus that can mediate the Ca2+ precipitation.";
RL   Submitted (MAR-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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {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; CP014616; AMQ08391.1; -; Genomic_DNA.
DR   RefSeq; WP_067213806.1; NZ_CP014616.1.
DR   EnsemblBacteria; AMQ08391; AMQ08391; AZE41_02065.
DR   KEGG; spsy:AZE41_02065; -.
DR   KO; K04565; -.
DR   Proteomes; UP000071057; Chromosome.
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:UP000071057};
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:UP000071057};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       37    172       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   175 AA;  18288 MW;  4659CC5AE4DB8C11 CRC64;
     MLSALLIAGG CGKNGVKLPV TGESVQSVMS PILNTKGDKI GEANFVEGID GVTINIQAEG
     LSPGKHGVHI HEMAVCTPPD FKSAGDHFNP GHKEHGFDNP KGFHLGDLPN LEVDADGKVT
     AEVTTALVTL KPDVKNSLLD ADGSSLVIHE KVDDYKTDPS GNSGDRIACA VIKKK
//
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