ID A6XIG5_HELAN Unreviewed; 228 AA.
AC A6XIG5;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 18-MAR-2008, sequence version 2.
DT 27-MAR-2024, entry version 72.
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 ORFNames=HannXRQ_Chr08g0221521 {ECO:0000313|EMBL:OTG18294.1},
GN HanXRQr2_Chr08g0335361 {ECO:0000313|EMBL:KAF5795063.1};
OS Helianthus annuus (Common sunflower).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4232 {ECO:0000313|EMBL:ABH11434.2};
RN [1] {ECO:0000313|EMBL:ABH11434.2}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21388704; DOI=10.1016/j.jplph.2011.01.020;
RA Fernandez-Ocana A., Chaki M., Luque F., Gomez-Rodriguez M.V., Carreras A.,
RA Valderrama R., Begara-Morales J.C., Hernandez L.E., Corpas F.J.,
RA Barroso J.B.;
RT "Functional analysis of superoxide dismutases (SODs) in sunflower under
RT biotic and abiotic stress conditions. Identification of two new genes of
RT mitochondrial Mn-SOD.";
RL J. Plant Physiol. 168:1303-1308(2011).
RN [2] {ECO:0000313|EMBL:KAF5795063.1, ECO:0000313|Proteomes:UP000215914}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. SF193 {ECO:0000313|Proteomes:UP000215914};
RC TISSUE=Leaves {ECO:0000313|EMBL:KAF5795063.1};
RX PubMed=28538728; DOI=10.1038/nature22380;
RA Badouin H., Gouzy J., Grassa C.J., Murat F., Staton S.E., Cottret L.,
RA Lelandais-Briere C., Owens G.L., Carrere S., Mayjonade B., Legrand L.,
RA Gill N., Kane N.C., Bowers J.E., Hubner S., Bellec A., Berard A.,
RA Berges H., Blanchet N., Boniface M.C., Brunel D., Catrice O., Chaidir N.,
RA Claudel C., Donnadieu C., Faraut T., Fievet G., Helmstetter N., King M.,
RA Knapp S.J., Lai Z., Le Paslier M.C., Lippi Y., Lorenzon L., Mandel J.R.,
RA Marage G., Marchand G., Marquand E., Bret-Mestries E., Morien E.,
RA Nambeesan S., Nguyen T., Pegot-Espagnet P., Pouilly N., Raftis F.,
RA Sallet E., Schiex T., Thomas J., Vandecasteele C., Vares D., Vear F.,
RA Vautrin S., Crespi M., Mangin B., Burke J.M., Salse J., Munos S.,
RA Vincourt P., Rieseberg L.H., Langlade N.B.;
RT "The sunflower genome provides insights into oil metabolism, flowering and
RT Asterid evolution.";
RL Nature 546:148-152(2017).
RN [3] {ECO:0000313|EMBL:OTG18294.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaves {ECO:0000313|EMBL:OTG18294.1};
RA Langlade N., Munos S.;
RT "Sunflower complete genome.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:KAF5795063.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:KAF5795063.1};
RA Gouzy J., Langlade N., Munos S.;
RT "Helianthus annuus Genome sequencing and assembly Release 2.";
RL Submitted (JUN-2020) 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; DQ812552; ABH11434.2; -; mRNA.
DR EMBL; MNCJ02000323; KAF5795063.1; -; Genomic_DNA.
DR EMBL; CM007897; OTG18294.1; -; Genomic_DNA.
DR AlphaFoldDB; A6XIG5; -.
DR SMR; A6XIG5; -.
DR STRING; 4232.A6XIG5; -.
DR EnsemblPlants; mRNA:HanXRQr2_Chr08g0335361; mRNA:HanXRQr2_Chr08g0335361; HanXRQr2_Chr08g0335361.
DR Gramene; mRNA:HanXRQr2_Chr08g0335361; mRNA:HanXRQr2_Chr08g0335361; HanXRQr2_Chr08g0335361.
DR OMA; HQTYVTA; -.
DR OrthoDB; 4839at2759; -.
DR Proteomes; UP000215914; Chromosome 8.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
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 2: Evidence at transcript level;
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:UP000215914}.
FT DOMAIN 27..108
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 119..221
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
FT BINDING 52
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 100
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 189
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 193
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ SEQUENCE 228 AA; 25379 MW; D1A2A54D9702FC15 CRC64;
MALRTLATRK TLGAFSTFPQ QLRGLQTFTL PDLAYDYGAL EPAISGDIMQ LHHQKHHQTY
ITNYNKALEQ LDDAIAKGDA STAVKLQSAI KFNGGGHVNH SIFWKNLAPT KEGGGEPPHG
SLGWAIDQSY GSVEKLIAKM NAEGAAVQGS GWVWLAVDKE LKRLVVETTA NQDPLVTKGP
SLVPLIGIDV WEHAYYLQYK NVRPDYLKNI WKVINWKYAS EIYEKECP
//
