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Database: UniProt/TrEMBL
Entry: A0A1D8JAV8_9BURK
LinkDB: A0A1D8JAV8_9BURK
Original site: A0A1D8JAV8_9BURK 
ID   A0A1D8JAV8_9BURK        Unreviewed;       203 AA.
AC   A0A1D8JAV8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=BI380_05690 {ECO:0000313|EMBL:AOV05818.1};
OS   Delftia tsuruhatensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=180282 {ECO:0000313|EMBL:AOV05818.1, ECO:0000313|Proteomes:UP000095607};
RN   [1] {ECO:0000313|EMBL:AOV05818.1, ECO:0000313|Proteomes:UP000095607}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM13 {ECO:0000313|EMBL:AOV05818.1,
RC   ECO:0000313|Proteomes:UP000095607};
RA   Saffarian A.;
RT   "Complete genome sequence of Deltia acidovorans CM13 isolated from murine
RT   proximal colonic tissue.";
RL   Submitted (SEP-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}.
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DR   EMBL; CP017420; AOV05818.1; -; Genomic_DNA.
DR   RefSeq; WP_046240174.1; NZ_LATT01000228.1.
DR   AlphaFoldDB; A0A1D8JAV8; -.
DR   KEGG; dts:BI380_05690; -.
DR   OrthoDB; 5431326at2; -.
DR   Proteomes; UP000095607; Chromosome.
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   PRINTS; PR00068; CUZNDISMTASE.
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..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..203
FT                   /note="Superoxide dismutase [Cu-Zn]"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009108941"
FT   DOMAIN          69..200
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
SQ   SEQUENCE   203 AA;  20381 MW;  3A1146D03FA4E030 CRC64;
     MRLNASPSTP STAVKLLMAA GMVLALGACG SQAKPPATAA ASTPAAVTAA PAARNVAMAQ
     LQPTQGSKVS GSLQFTAQAD GSVRVQGSVQ GLAPNSEHGF HVHEKGDCSS PDGLSAGGHF
     NPTGHAHGRF DSAVHHAGDL PSLRSDAQGM ASIDFVSRGL ALDQSPNSVV GRGLIVHKDP
     DDYTTQPTGN SGARLACAVI TRG
//
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