ID I3E2J0_BACMT Unreviewed; 187 AA.
AC I3E2J0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, 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=PB1_10142 {ECO:0000313|EMBL:EIJ80711.1};
OS Bacillus methanolicus PB1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=997296 {ECO:0000313|EMBL:EIJ80711.1, ECO:0000313|Proteomes:UP000010523};
RN [1] {ECO:0000313|EMBL:EIJ80711.1, ECO:0000313|Proteomes:UP000010523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB1 {ECO:0000313|EMBL:EIJ80711.1,
RC ECO:0000313|Proteomes:UP000010523};
RX PubMed=22610424; DOI=10.1128/AEM.00703-12;
RA Heggeset T.M., Krog A., Balzer S., Wentzel A., Ellingsen T.E.,
RA Brautaset T.;
RT "Genome Sequence of Thermotolerant Bacillus methanolicus: Features and
RT Regulation Related to Methylotrophy and Production of L-Lysine and L-
RT Glutamate from Methanol.";
RL Appl. Environ. Microbiol. 78:5170-5181(2012).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIJ80711.1}.
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DR EMBL; AFEU01000002; EIJ80711.1; -; Genomic_DNA.
DR RefSeq; WP_003352209.1; NZ_AFEU01000002.1.
DR AlphaFoldDB; I3E2J0; -.
DR STRING; 997296.PB1_10142; -.
DR PATRIC; fig|997296.3.peg.2150; -.
DR eggNOG; COG2032; Bacteria.
DR OrthoDB; 9792957at2; -.
DR Proteomes; UP000010523; Unassembled WGS sequence.
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; PS51257; PROKAR_LIPOPROTEIN; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000393}.
FT DOMAIN 37..167
FT /note="Superoxide dismutase copper/zinc binding"
FT /evidence="ECO:0000259|Pfam:PF00080"
FT REGION 145..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 187 AA; 20104 MW; D3A70AAFA181F44B CRC64;
MKKGWMIILM ILLAGCAEDN PKSVDVEMFN TVGDSLGKIK ITEQASGVKL EVNLEGLPPG
EHAMHIHETG KCEPPDFQSA GNHFDPDNKQ HGLLHPKGAH AGDLPNLIVE DDGKAKAEIM
APQVTLQNGK TSLFTKEGTS IVIHEEKDDG MTQPAGDSGS RIACGKISND KGQTEQKKAQ
DDKQGEQ
//
