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Database: UniProt
Entry: A0A2S9KHE5_9BURK
LinkDB: A0A2S9KHE5_9BURK
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ID   A0A2S9KHE5_9BURK        Unreviewed;       188 AA.
AC   A0A2S9KHE5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=C6P61_04020 {ECO:0000313|EMBL:PRD69870.1};
OS   Malikia spinosa.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Malikia.
OX   NCBI_TaxID=86180 {ECO:0000313|EMBL:PRD69870.1, ECO:0000313|Proteomes:UP000238326};
RN   [1] {ECO:0000313|EMBL:PRD69870.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=83 {ECO:0000313|EMBL:PRD69870.1};
RA   Suzuki S., Ishii S., Walworth N., Bird L., Kuenen J.G., Nealson K.H.;
RT   "Comparative genomics illustrates the genes involved in a hyperalkaliphilic
RT   mechanisms of Serpentinomonas isolated from highly-alkaline calcium-rich
RT   serpentinized springs.";
RL   Submitted (MAR-2018) 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:PRD69870.1}.
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DR   EMBL; PVLR01000011; PRD69870.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S9KHE5; -.
DR   OrthoDB; 5431326at2; -.
DR   Proteomes; UP000238326; 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; PS51257; PROKAR_LIPOPROTEIN; 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   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..188
FT                   /note="Superoxide dismutase [Cu-Zn]"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015419042"
FT   DOMAIN          53..185
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
SQ   SEQUENCE   188 AA;  19688 MW;  E086650128EDE376 CRC64;
     MTMKYKKTAF LSAALALAAL SGCSYLPTQL TPQLPGQQPV AKAMLEPRSG SQVSGKVSFT
     PVGDKLLVEA YVTGLTPGEH GFHVHEGGDC SAADASGAKG HFNPAGMPHG HHHQMHHSKR
     HAGDLPNLVA DSSGQAYYRA EVTWLKLDGS ARGIVGRSVI VHADADDYQS QPAGNSGRRV
     ACGVIKAP
//
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