ID A0A0E1NMW9_YERPA Unreviewed; 189 AA.
AC A0A0E1NMW9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
DE Flags: Precursor;
GN OrderedLocusNames=YPA_2873 {ECO:0000313|EMBL:ABG14835.1};
OS Yersinia pestis bv. Antiqua (strain Antiqua).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG14835.1, ECO:0000313|Proteomes:UP000001971};
RN [1] {ECO:0000313|EMBL:ABG14835.1, ECO:0000313|Proteomes:UP000001971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Antiqua {ECO:0000313|EMBL:ABG14835.1,
RC ECO:0000313|Proteomes:UP000001971};
RX PubMed=16740952; DOI=10.1128/JB.00124-06;
RA Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(2006).
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; CP000308; ABG14835.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E1NMW9; -.
DR KEGG; ypa:YPA_2873; -.
DR PATRIC; fig|360102.15.peg.1562; -.
DR HOGENOM; CLU_056632_7_1_6; -.
DR OMA; AQRGFHI; -.
DR Proteomes; UP000001971; 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 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|RuleBase:RU000393};
KW Metal-binding {ECO:0000256|RuleBase:RU000393};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000393,
KW ECO:0000313|EMBL:ABG14835.1}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|RuleBase:RU000393}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..189
FT /note="Superoxide dismutase [Cu-Zn]"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010416323"
FT DOMAIN 54..188
FT /note="Superoxide dismutase copper/zinc binding"
FT /evidence="ECO:0000259|Pfam:PF00080"
SQ SEQUENCE 189 AA; 19378 MW; B14965FE9E8C7C00 CRC64;
MKLSTLLLPV ILYSSATLAA NMAGMNDKAS MNGKASMTVK INESLPQGNG KALGTVTVTE
TAYGLLFTPH LTGLAPGIHG FHLHEKPSCA PGMKDGKAVP ALAAGGHLDP NKTGVHLGPY
NDKGHLGDLP GLVVNADGTA TYPVLAPRLK SLSEVKQHAL MIHAGGDNYS DHPMPLGGGG
ARMACGVIE
//