ID M5C6M2_THACB Unreviewed; 208 AA.
AC M5C6M2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
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};
GN Name=LbMnSOD3 {ECO:0000313|EMBL:CCO35588.1};
GN ORFNames=BN14_09706 {ECO:0000313|EMBL:CCO35588.1}, RSOLAG1IB_06174
GN {ECO:0000313|EMBL:CEL53208.1};
OS Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS rot fungus) (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=1108050 {ECO:0000313|EMBL:CCO35588.1, ECO:0000313|Proteomes:UP000012065};
RN [1] {ECO:0000313|EMBL:CCO35588.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Isolate 7/3/14 {ECO:0000313|EMBL:CCO35588.1};
RA Jelonek L.;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCO35588.1, ECO:0000313|Proteomes:UP000012065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG1-IB / isolate 7/3/14 {ECO:0000313|Proteomes:UP000012065},
RC and Isolate 7/3/14 {ECO:0000313|EMBL:CCO35588.1};
RX PubMed=23280342; DOI=10.1016/j.jbiotec.2012.12.010;
RA Wibberg D.W., Jelonek L.J., Rupp O.R., Hennig M.H., Eikmeyer F.E.,
RA Goesmann A.G., Hartmann A.H., Borriss R.B., Grosch R.G., Puehler A.P.,
RA Schlueter A.S.;
RT "Establishment and interpretation of the genome sequence of the
RT phytopathogenic fungus Rhizoctonia solani AG1-IB isolate 7/3/14.";
RL J. Biotechnol. 0:0-0(2013).
RN [3] {ECO:0000313|EMBL:CEL53208.1, ECO:0000313|Proteomes:UP000059188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rhizoctonia solani AG1-IB 7/3/14 {ECO:0000313|EMBL:CEL53208.1};
RA Wibberg Daniel;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00001605,
CC 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; CAOJ01014791; CCO35588.1; -; Genomic_DNA.
DR EMBL; LN679111; CEL53208.1; -; Genomic_DNA.
DR AlphaFoldDB; M5C6M2; -.
DR STRING; 1108050.M5C6M2; -.
DR HOGENOM; CLU_031625_2_0_1; -.
DR Proteomes; UP000012065; Unassembled WGS sequence.
DR Proteomes; UP000059188; 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; 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; PTHR11404; SUPEROXIDE DISMUTASE 2; 1.
DR PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], 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 Antioxidant {ECO:0000256|ARBA:ARBA00022862};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000349-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000414};
KW Reference proteome {ECO:0000313|Proteomes:UP000059188}.
FT DOMAIN 4..84
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 99..199
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
FT BINDING 27
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 166
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 170
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ SEQUENCE 208 AA; 23297 MW; A09ACA89FCF21F71 CRC64;
MSVTLPDLPY AYNALEPYIS EEIMTLHHKK HHQTYVNGYN TAVENLSKLV GDPSAARKQI
SLQSAVKFNG GGHLNHSLFW KNLAPAGTTG LKPDGTLETA TLASSIERDF DSFSKFKERF
NEAALGIQGS GWAWLVLNTA NQRLDIITTP NQDPVLPPYL PLFGVDMWEH AFYLQYKNVK
PDYLSAIWNV INFKEAESRL NEGLSSKL
//
