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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//