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Database: UniProt/TrEMBL
Entry: W0QDC1_9PAST
LinkDB: W0QDC1_9PAST
Original site: W0QDC1_9PAST 
ID   W0QDC1_9PAST            Unreviewed;       179 AA.
AC   W0QDC1;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=X808_13380 {ECO:0000313|EMBL:AHG75860.1};
OS   Mannheimia varigena USDA-ARS-USMARC-1296.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Mannheimia.
OX   NCBI_TaxID=1433287 {ECO:0000313|EMBL:AHG75860.1, ECO:0000313|Proteomes:UP000066995};
RN   [1] {ECO:0000313|EMBL:AHG75860.1, ECO:0000313|Proteomes:UP000066995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USDA-ARS-USMARC-1296 {ECO:0000313|EMBL:AHG75860.1,
RC   ECO:0000313|Proteomes:UP000066995};
RA   Harhay G.P., Clawson M.L., Murray R.W., Lubbers B.V., Heaton M.P.,
RA   Chitko-Mckown C.G., Harhay D.M., Smith T.P.L.;
RT   "Annotation of the Mannheimia varigena USDA-ARS-USMARC-1296 complete
RT   genome.";
RL   Submitted (DEC-2013) 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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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; CP006943; AHG75860.1; -; Genomic_DNA.
DR   RefSeq; WP_025217567.1; NZ_CP006943.1.
DR   AlphaFoldDB; W0QDC1; -.
DR   STRING; 1433287.X808_13380; -.
DR   KEGG; mvi:X808_13380; -.
DR   PATRIC; fig|1433287.3.peg.1340; -.
DR   eggNOG; COG2032; Bacteria.
DR   HOGENOM; CLU_056632_7_1_6; -.
DR   OrthoDB; 5431326at2; -.
DR   Proteomes; UP000066995; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..179
FT                   /note="Superoxide dismutase [Cu-Zn]"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004794692"
FT   DOMAIN          44..178
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
SQ   SEQUENCE   179 AA;  18910 MW;  BB7B3D870E3AD2AD CRC64;
     MKMKTALAIA LGSLFSFSAA ATEPAKIVVQ VQQLDVEKGN KDVGTIEITE SKYGLVFTPN
     LKDLTEGLHG FHIHENPSCD AKEKDGKLTA GLAAGGHWNP SKVEHHGFPW SDDAHLGDLP
     ALTVLHDGTS TNPVLAPRLK KLDEIKGRSL MIHAGGDNHS DHPAPLGGGG ARMACGVIK
//
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