ID A0A0F2M528_SPOSC Unreviewed; 229 AA.
AC A0A0F2M528;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=SPSK_09674 {ECO:0000313|EMBL:KJR84199.1};
OS Sporothrix schenckii 1099-18.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1397361 {ECO:0000313|EMBL:KJR84199.1, ECO:0000313|Proteomes:UP000033710};
RN [1] {ECO:0000313|EMBL:KJR84199.1, ECO:0000313|Proteomes:UP000033710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1099-18 {ECO:0000313|EMBL:KJR84199.1,
RC ECO:0000313|Proteomes:UP000033710};
RX PubMed=25351875; DOI=10.1186/1471-2164-15-943;
RA Teixeira M.M., de Almeida L.G., Kubitschek-Barreira P., Alves F.L.,
RA Kioshima E.S., Abadio A.K., Fernandes L., Derengowski L.S., Ferreira K.S.,
RA Souza R.C., Ruiz J.C., de Andrade N.C., Paes H.C., Nicola A.M.,
RA Albuquerque P., Gerber A.L., Martins V.P., Peconick L.D., Neto A.V.,
RA Chaucanez C.B., Silva P.A., Cunha O.L., de Oliveira F.F., dos Santos T.C.,
RA Barros A.L., Soares M.A., de Oliveira L.M., Marini M.M.,
RA Villalobos-Duno H., Cunha M.M., de Hoog S., da Silveira J.F., Henrissat B.,
RA Nino-Vega G.A., Cisalpino P.S., Mora-Montes H.M., Almeida S.R.,
RA Stajich J.E., Lopes-Bezerra L.M., Vasconcelos A.T., Felipe M.S.;
RT "Comparative genomics of the major fungal agents of human and animal
RT Sporotrichosis: Sporothrix schenckii and Sporothrix brasiliensis.";
RL BMC Genomics 15:943-943(2014).
RN [2] {ECO:0000313|EMBL:KJR84199.1, ECO:0000313|Proteomes:UP000033710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1099-18 {ECO:0000313|EMBL:KJR84199.1,
RC ECO:0000313|Proteomes:UP000033710};
RX PubMed=25480940;
RA Teixeira Mde M., Rodrigues A.M., Tsui C.K., de Almeida L.G.,
RA Van Diepeningen A.D., van den Ende B.G., Fernandes G.F., Kano R.,
RA Hamelin R.C., Lopes-Bezerra L.M., Vasconcelos A.T., de Hoog S.,
RA de Camargo Z.P., Felipe M.S.;
RT "Asexual propagation of a virulent clone complex in a human and feline
RT outbreak of sporotrichosis.";
RL Eukaryot. Cell 14:158-169(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJR84199.1}.
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DR EMBL; AXCR01000007; KJR84199.1; -; Genomic_DNA.
DR RefSeq; XP_016586875.1; XM_016736246.1.
DR AlphaFoldDB; A0A0F2M528; -.
DR GeneID; 27671523; -.
DR KEGG; ssck:SPSK_09674; -.
DR VEuPathDB; FungiDB:SPSK_09674; -.
DR OrthoDB; 4839at2759; -.
DR Proteomes; UP000033710; 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}.
FT DOMAIN 35..114
FT /note="Manganese/iron superoxide dismutase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 124..225
FT /note="Manganese/iron superoxide dismutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02777"
FT BINDING 58
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 106
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 192
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT BINDING 196
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ SEQUENCE 229 AA; 24694 MW; 87A41265A5A4D26E CRC64;
MASLLRSSTL RAARQARPTA AAAALSTSFV RTKATLPDLP YDYNALEPYI SSKIMELHHS
KHHQTYVSGL NAALDTIAEA NAAGDARKAA KAAPLLNFHG GGHINHSLFW ENLAPASRDG
GGDPSGALKT QIEKDFGSTE ALVKQFNAAL AGIQGSGWAW LAKDSASGTL TLVTRANQDP
VSGSLVPLLG IDAWEHAYYL QYENRKAEYF SAIWNVINWK TVGQRFEKA
//
