ID C0A181_CLOPF Unreviewed; 184 AA.
AC C0A181;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Superoxide dismutase {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
DE EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
DE Flags: Fragment;
GN Name=sodF {ECO:0000313|EMBL:BAH28679.1};
GN Synonyms=sod {ECO:0000313|EMBL:AFP72716.1}, sodA
GN {ECO:0000313|EMBL:AFV13923.1};
OS Clostridium perfringens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1502 {ECO:0000313|EMBL:BAH28679.1};
RN [1] {ECO:0000313|EMBL:BAH28679.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NCTC8081 {ECO:0000313|EMBL:BAH28679.1}, NCTC8239
RC {ECO:0000313|EMBL:BAH28681.1}, NCTC8798 {ECO:0000313|EMBL:BAH28684.1},
RC OSA1 {ECO:0000313|EMBL:BAH28688.1}, OSA2
RC {ECO:0000313|EMBL:BAH28689.1}, OSA3 {ECO:0000313|EMBL:BAH28690.1},
RC OSA4 {ECO:0000313|EMBL:BAH28691.1}, W4232
RC {ECO:0000313|EMBL:BAH28699.1}, W5834 {ECO:0000313|EMBL:BAH28700.1},
RC and W6205 {ECO:0000313|EMBL:BAH28701.1};
RX PubMed=19479065; DOI=10.1371/journal.pone.0005598;
RA Deguchi A., Miyamoto K., Kuwahara T., Miki Y., Kaneko I., Li J.,
RA McClane B.A., Akimoto S.;
RT "Genetic characterization of type A enterotoxigenic Clostridium perfringens
RT strains.";
RL PLoS ONE 4:e5598-e5598(2009).
RN [2] {ECO:0000313|EMBL:AFP72716.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VWA001 {ECO:0000313|EMBL:AFP72716.1}, VWA019
RC {ECO:0000313|EMBL:AFP72720.1}, VWA031 {ECO:0000313|EMBL:AFP72721.1},
RC VWA085 {ECO:0000313|EMBL:AFP72724.1}, and VWA300
RC {ECO:0000313|EMBL:AFP72729.1};
RX PubMed=22865060; DOI=10.1128/AEM.01486-12;
RA Xiao Y., Wagendorp A., Moezelaar R., Abee T., Wells-Bennik M.H.;
RT "A Wide Variety of Clostridium perfringens Type A Food-Borne Isolates That
RT Carry a Chromosomal cpe Gene Belong to One Multilocus Sequence Typing
RT Cluster.";
RL Appl. Environ. Microbiol. 78:7060-7068(2012).
RN [3] {ECO:0000313|EMBL:AFV13923.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CN2076 {ECO:0000313|EMBL:AFV13923.1}, CN3748
RC {ECO:0000313|EMBL:AFV13924.1}, CN3752 {ECO:0000313|EMBL:AFV13925.1},
RC CN3753 {ECO:0000313|EMBL:AFV13926.1}, CN3758
RC {ECO:0000313|EMBL:AFV13927.1}, and CN3763
RC {ECO:0000313|EMBL:AFV13928.1};
RX PubMed=23027533; DOI=10.1128/IAI.00818-12;
RA Ma M., Li J., McClane B.A.;
RT "Genotypic and Phenotypic Characterization of Clostridium perfringens
RT Isolates from Darmbrand Cases in Post-World War II Germany.";
RL Infect. Immun. 80:4354-4363(2012).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems.
CC {ECO:0000256|RuleBase:RU000414}.
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:RU000414};
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000256|ARBA:ARBA00008714, ECO:0000256|RuleBase:RU000414}.
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DR EMBL; JX307750; AFP72716.1; -; Genomic_DNA.
DR EMBL; JX307754; AFP72720.1; -; Genomic_DNA.
DR EMBL; JX307755; AFP72721.1; -; Genomic_DNA.
DR EMBL; JX307758; AFP72724.1; -; Genomic_DNA.
DR EMBL; JX307763; AFP72729.1; -; Genomic_DNA.
DR EMBL; JX276521; AFV13923.1; -; Genomic_DNA.
DR EMBL; JX276522; AFV13924.1; -; Genomic_DNA.
DR EMBL; JX276523; AFV13925.1; -; Genomic_DNA.
DR EMBL; JX276524; AFV13926.1; -; Genomic_DNA.
DR EMBL; JX276525; AFV13927.1; -; Genomic_DNA.
DR EMBL; JX276526; AFV13928.1; -; Genomic_DNA.
DR EMBL; AB477944; BAH28679.1; -; Genomic_DNA.
DR EMBL; AB477946; BAH28681.1; -; Genomic_DNA.
DR EMBL; AB477949; BAH28684.1; -; Genomic_DNA.
DR EMBL; AB477953; BAH28688.1; -; Genomic_DNA.
DR EMBL; AB477954; BAH28689.1; -; Genomic_DNA.
DR EMBL; AB477955; BAH28690.1; -; Genomic_DNA.
DR EMBL; AB477956; BAH28691.1; -; Genomic_DNA.
DR EMBL; AB477964; BAH28699.1; -; Genomic_DNA.
DR EMBL; AB477965; BAH28700.1; -; Genomic_DNA.
DR EMBL; AB477966; BAH28701.1; -; Genomic_DNA.
DR AlphaFoldDB; C0A181; -.
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; IPR019833; Mn/Fe_SOD_BS.
DR InterPro; IPR019832; Mn/Fe_SOD_C.
DR InterPro; IPR019831; Mn/Fe_SOD_N.
DR InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR InterPro; IPR036314; SOD_C_sf.
DR PANTHER; PTHR43595; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43595:SF2; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
DR Pfam; PF02777; Sod_Fe_C; 1.
DR Pfam; PF00081; Sod_Fe_N; 1.
DR PIRSF; PIRSF000349; SODismutase; 1.
DR PRINTS; PR01703; MNSODISMTASE.
DR SUPFAM; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
DR PROSITE; PS00088; SOD_MN; 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:0000256|RuleBase:RU000414}.
FT DOMAIN 4..90
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 99..184
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
FT BINDING 28
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 83
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 165
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 169
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAH28679.1"
FT NON_TER 184
FT /evidence="ECO:0000313|EMBL:BAH28679.1"
SQ SEQUENCE 184 AA; 21102 MW; BC8B19E63E53E917 CRC64;
GEGFKLKPLD YPYDALEPSI DEETVKIHHD KHQQAYVDKL NKALEKHPEL YGKSLYDILS
NLDDMPEDIM ADLVNQGGGV YNHEFYWSIL GKGCNRPVAE IADAIDRDFG SFEEFKEKFK
QCGISTFGSG WAWLVSDKDG KLEIMSTKDQ SSPISLGLIP ILTMDVWEHA YYLKYQNKRP
EYID
//
