ID   B2FHC6_STRMK            Unreviewed;       189 AA.
AC   B2FHC6;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   02-SEP-2026, entry version 91.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=sodC1 {ECO:0000313|EMBL:CAQ43769.1};
GN   OrderedLocusNames=Smlt0160 {ECO:0000313|EMBL:CAQ43769.1};
OS   Stenotrophomonas maltophilia (strain K279a).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Lysobacterales; Lysobacteraceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=522373 {ECO:0000313|EMBL:CAQ43769.1, ECO:0000313|Proteomes:UP000008840};
RN   [1] {ECO:0000313|EMBL:CAQ43769.1, ECO:0000313|Proteomes:UP000008840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K279a {ECO:0000313|EMBL:CAQ43769.1,
RC   ECO:0000313|Proteomes:UP000008840};
RX   PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA   Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA   Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA   Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA   Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA   Parkhill J., Thomson N.R., Avison M.B.;
RT   "The complete genome, comparative and functional analysis of
RT   Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT   resistance determinants.";
RL   Genome Biol. 9:R74.1-R74.13(2008).
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 superoxide + 2 H(+) = 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; AM743169; CAQ43769.1; -; Genomic_DNA.
DR   RefSeq; WP_012478734.1; NC_010943.1.
DR   AlphaFoldDB; B2FHC6; -.
DR   EnsemblBacteria; CAQ43769; CAQ43769; Smlt0160.
DR   KEGG; sml:Smlt0160; -.
DR   PATRIC; fig|522373.3.peg.150; -.
DR   eggNOG; COG2032; Bacteria.
DR   HOGENOM; CLU_056632_8_2_6; -.
DR   Proteomes; UP000008840; 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; 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   Lipoprotein {ECO:0000256|PROSITE-ProRule:PRU00303};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393,
KW   ECO:0000313|EMBL:CAQ43769.1};
KW   Palmitate {ECO:0000256|PROSITE-ProRule:PRU00303};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008840};
KW   Signal {ECO:0000256|PROSITE-ProRule:PRU00303, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..189
FT                   /note="Superoxide dismutase [Cu-Zn]"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00303,
FT                   ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002777739"
FT   DOMAIN          55..185
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
FT   REGION          97..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           19
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00303"
FT   LIPID           19
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   189 AA;  18992 MW;  2A7D8BC07C5958CA CRC64;
     MRLSFAILPL SAAVLLSACG SAPKKTEPTP PPPTVVSAAK QGEANIAPAS ASIVSGRIAL
     MVEPGGIHIT GLIGGLQPMQ QAGFHIHERG DCSAVDASSA GNHFNPGGAA HGRAGTGKHH
     LGDMDNLRAD AQGRANVDIH LKGVTLGGGA ATDIAGRALV VHANADDYRS QPAGNAGVRI
     ACGVIRVVR
//