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Database: UniProt
Entry: A0A0M0G9E5_SPOGL
LinkDB: A0A0M0G9E5_SPOGL
Original site: A0A0M0G9E5_SPOGL 
ID   A0A0M0G9E5_SPOGL        Unreviewed;       187 AA.
AC   A0A0M0G9E5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   05-DEC-2018, entry version 12.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=AF332_06530 {ECO:0000313|EMBL:KON86515.1};
OS   Sporosarcina globispora (Bacillus globisporus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae;
OC   Sporosarcina.
OX   NCBI_TaxID=1459 {ECO:0000313|EMBL:KON86515.1, ECO:0000313|Proteomes:UP000037109};
RN   [1] {ECO:0000313|Proteomes:UP000037109}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4 {ECO:0000313|Proteomes:UP000037109};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J.,
RA   Ge C., Shi H., Pan Z., Liu X.;
RT   "Fjat-10036 dsm4.";
RL   Submitted (JUL-2015) 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   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KON86515.1}.
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DR   EMBL; LGUF01000007; KON86515.1; -; Genomic_DNA.
DR   RefSeq; WP_053433877.1; NZ_LGUF01000007.1.
DR   EnsemblBacteria; KON86515; KON86515; AF332_06530.
DR   PATRIC; fig|1459.3.peg.1387; -.
DR   Proteomes; UP000037109; 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:UP000037109};
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:UP000037109};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       33    167       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   187 AA;  19975 MW;  7A1A43CC48598180 CRC64;
     MRKALMLSLI LLLSGCGEEK ITNTEVEMFN AAGDSLGTIK VQEQASGVKL SGNLSGLPPG
     ELAIHIHEVA KCEPPDFKSA GNHFNPDNKE HGLLHPKGSH AGDLPNLIVE DDGKVKIDFM
     APQVTLKEDK NSLLTKEGTS IVIHDGPDDG MTQPAGDSGE RIACGRISKD KDEKGQKKAQ
     DDQSAEE
//
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