ID A0A0G1SW50_9BACT Unreviewed; 201 AA.
AC A0A0G1SW50;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=superoxide dismutase {ECO:0000256|ARBA:ARBA00012682};
DE EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682};
GN ORFNames=UX98_C0005G0088 {ECO:0000313|EMBL:KKU73712.1};
OS Parcubacteria group bacterium GW2011_GWA2_47_26.
OC Bacteria.
OX NCBI_TaxID=1618844 {ECO:0000313|EMBL:KKU73712.1, ECO:0000313|Proteomes:UP000034356};
RN [1] {ECO:0000313|EMBL:KKU73712.1, ECO:0000313|Proteomes:UP000034356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000256|ARBA:ARBA00008714}.
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:KKU73712.1}.
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DR EMBL; LCOG01000005; KKU73712.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1SW50; -.
DR STRING; 1618844.UX98_C0005G0088; -.
DR Proteomes; UP000034356; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1.
DR InterPro; IPR001189; Mn/Fe_SOD.
DR InterPro; IPR019832; Mn/Fe_SOD_C.
DR InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR InterPro; IPR036314; SOD_C_sf.
DR PANTHER; PTHR11404; SUPEROXIDE DISMUTASE 2; 1.
DR PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL; 1.
DR Pfam; PF02777; Sod_Fe_C; 1.
DR PIRSF; PIRSF000349; SODismutase; 1.
DR SUPFAM; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000349-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 89..188
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
FT BINDING 24
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 75
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 156
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 160
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ SEQUENCE 201 AA; 22813 MW; 4E750198C735C8CA CRC64;
MEKQVKPLKY KSLNGLSEKQ LAEHHDVLYA GYVKKVNEIN GKLQGVDLGA PNATHSDLRE
LKLEETFALN GVKLHEGYFD NLGGGGGEPT GEIAEMIKQD FGSIARWREE FKALGICARG
WVVLAYDWDE KILCNILCDA HNQGGVWNCS ALLILDVYEH AYFLDYATGR KAYIETFMKN
MDWAFVNDLI KKMRIVEHRK S
//
