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Database: UniProt
Entry: B9E4T8_CLOK1
LinkDB: B9E4T8_CLOK1
Original site: B9E4T8_CLOK1 
ID   B9E4T8_CLOK1            Unreviewed;       218 AA.
AC   B9E4T8;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 70.
DE   RecName: Full=superoxide dismutase {ECO:0000256|ARBA:ARBA00012682};
DE            EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682};
GN   OrderedLocusNames=CKR_2462 {ECO:0000313|EMBL:BAH07513.1};
OS   Clostridium kluyveri (strain NBRC 12016).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=583346 {ECO:0000313|EMBL:BAH07513.1, ECO:0000313|Proteomes:UP000007969};
RN   [1] {ECO:0000313|Proteomes:UP000007969}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 12016 {ECO:0000313|Proteomes:UP000007969};
RA   Inui M., Nonaka H., Shinoda Y., Ikenaga Y., Abe M., Naito K., Vertes A.A.,
RA   Yukawa H.;
RT   "Complete genome sequence of Clostridium kluyveri and comparative genomics
RT   of Clostridia species.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00008714}.
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DR   EMBL; AP009049; BAH07513.1; -; Genomic_DNA.
DR   RefSeq; WP_012103112.1; NC_011837.1.
DR   AlphaFoldDB; B9E4T8; -.
DR   SMR; B9E4T8; -.
DR   KEGG; ckr:CKR_2462; -.
DR   HOGENOM; CLU_031625_2_2_9; -.
DR   Proteomes; UP000007969; Chromosome.
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          91..190
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         76
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         157
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         161
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ   SEQUENCE   218 AA;  25664 MW;  79C85E73A8F75DD0 CRC64;
     MYNMKPEVFN FNSVKGISQR QLNEHYKLYV GYVNILNQIW NTDYTPQNYT DSNPTYSKMR
     SLKLGETYAL NGVKLHNLYF KNMTGGNTTP HGPVLNSIIN QFSSYDNFLS YLTNVGLSMR
     GWAILSIDSL DNKFHIIGSD LHDKGSVWIS YPILVMDVYE HAYFMDFGTN KKEYISTFIK
     NINWTVVNKR FQKYLHLLQI LNINHNRYIP YEFLNRHI
//
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