ID M9YI84_AZOVI Unreviewed; 180 AA.
AC M9YI84;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN Name=sodA {ECO:0000313|EMBL:AGK18813.1};
GN ORFNames=AvCA6_30470 {ECO:0000313|EMBL:AGK18813.1};
OS Azotobacter vinelandii CA6.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=1283331 {ECO:0000313|EMBL:AGK18813.1, ECO:0000313|Proteomes:UP000012988};
RN [1] {ECO:0000313|EMBL:AGK18813.1, ECO:0000313|Proteomes:UP000012988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CA6 {ECO:0000313|EMBL:AGK18813.1,
RC ECO:0000313|Proteomes:UP000012988};
RX PubMed=23792740; DOI=10.1128/genomeA.00313-13;
RA Noar J.D., Bruno-Barcena J.M.;
RT "Complete Genome Sequences of Azotobacter vinelandii Wild-Type Strain CA
RT and Tungsten-Tolerant Mutant Strain CA6.";
RL Genome Announc. 1:E00313-E00313(2013).
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; CP005095; AGK18813.1; -; Genomic_DNA.
DR AlphaFoldDB; M9YI84; -.
DR SMR; M9YI84; -.
DR KEGG; avd:AvCA6_30470; -.
DR PATRIC; fig|1283331.3.peg.2908; -.
DR HOGENOM; CLU_056632_7_1_6; -.
DR Proteomes; UP000012988; 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; 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; PS00087; SOD_CU_ZN_1; 1.
DR PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000393};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000393};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000393}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..180
FT /note="Superoxide dismutase [Cu-Zn]"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004104657"
FT DOMAIN 46..179
FT /note="Superoxide dismutase copper/zinc binding"
FT /evidence="ECO:0000259|Pfam:PF00080"
SQ SEQUENCE 180 AA; 18310 MW; 4C9747C6A4EE4189 CRC64;
MYNKEMPMKK RLIAAMIASC ALPLQAAPLS VALNAVGADG IGAALGTVSI EQSEYGLVFT
PNLSGLQPGI HGFHIHASGD CGTTEKEGQK VAAGAAGGHW DPQNATRHGQ PWGEGHLGDL
PALYVDANGK ATQPVLAPRL KDLEAIKGRA LMVHAGGDNH ADSPAPLGGG GARVACGVIK
//
