ID I7EZ11_9PEZI Unreviewed; 124 AA.
AC I7EZ11;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SOD2 {ECO:0000313|EMBL:AFP34579.1};
OS Colletotrichum theobromicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=912112 {ECO:0000313|EMBL:AFP34579.1};
RN [1] {ECO:0000313|EMBL:AFP34579.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C1262.14 {ECO:0000313|EMBL:AFP34578.1}, and C1262.15
RC {ECO:0000313|EMBL:AFP34579.1};
RX PubMed=23136459; DOI=10.3114/sim0011;
RA Weir B.S., Johnston P.R., Damm U.;
RT "The Colletotrichum gloeosporioides species complex.";
RL Stud. Mycol. 73:115-180(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|ARBA:ARBA00001605,
CC ECO:0000256|RuleBase:RU000414};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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; JX010297; AFP34578.1; -; Genomic_DNA.
DR EMBL; JX010298; AFP34579.1; -; Genomic_DNA.
DR AlphaFoldDB; I7EZ11; -.
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; IPR019831; Mn/Fe_SOD_N.
DR InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR InterPro; IPR036314; SOD_C_sf.
DR PANTHER; PTHR11404:SF29; SUPEROXIDE DISMUTASE; 1.
DR PANTHER; PTHR11404; SUPEROXIDE DISMUTASE 2; 1.
DR Pfam; PF02777; Sod_Fe_C; 1.
DR Pfam; PF00081; Sod_Fe_N; 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000414};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000414}.
FT DOMAIN 1..47
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 61..124
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFP34579.1"
FT NON_TER 124
FT /evidence="ECO:0000313|EMBL:AFP34579.1"
SQ SEQUENCE 124 AA; 13238 MW; B216F6E2C64139AE CRC64;
QTYVTNLNKA IETYNANPLQ NRIAVLAALN FNGGGHINHS LFWENLSPAS SPDASPDSAP
NLIADITRVW GGLDKFKQAF NAALLGITGS GWGWLVKDDT TGLSIITTKD QDPVTKGVPI
FGVD
//
