ID A0A0L0LFE0_9BACT Unreviewed; 197 AA.
AC A0A0L0LFE0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=superoxide dismutase {ECO:0000256|ARBA:ARBA00012682};
DE EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682};
GN ORFNames=AB198_00205 {ECO:0000313|EMBL:KND48729.1};
OS Parcubacteria bacterium C7867-003.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1659197 {ECO:0000313|EMBL:KND48729.1, ECO:0000313|Proteomes:UP000036964};
RN [1] {ECO:0000313|EMBL:KND48729.1, ECO:0000313|Proteomes:UP000036964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7867-003 {ECO:0000313|EMBL:KND48729.1};
RX PubMed=26257709; DOI=10.3389/fmicb.2015.00713;
RA Nelson W.C., Stegen J.C.;
RT "The reduced genomes of Parcubacteria (OD1) contain signatures of a
RT symbiotic lifestyle.";
RL Front. Microbiol. 6:713-713(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:KND48729.1}.
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DR EMBL; LFCM01000026; KND48729.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0LFE0; -.
DR STRING; 1659197.AB198_00205; -.
DR Proteomes; UP000036964; 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; 1.10.287.990; Fe,Mn superoxide dismutase (SOD) domain; 1.
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,
KW ECO:0000313|EMBL:KND48729.1}.
FT DOMAIN 91..192
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
FT BINDING 25
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 158
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 162
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ SEQUENCE 197 AA; 23028 MW; 399CAB8D20A079BF CRC64;
MKPFEEKKFN IPELKGISAK TIEEHLKLYS GYVKNANLVG TKLGEMWTED KEKHMYAMSE
LARRFSFEYN GMRNHEVYFD ILSDGTTPLS DGELKKAIEK SYGTVETFLE IFKAMAMTRG
VGWAMVWYDK QEDRLINSWV DEQHLGQLQG CALILGLDMW EHSFVYDYQP SGKKQYVEDF
FANLNWSKVE ENFNKAK
//
