SODM_ASPOR
ID SODM_ASPOR Reviewed; 210 AA.
AC Q877B6; Q537X2;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE EC=1.15.1.1 {ECO:0000250|UniProtKB:P0A0J3};
DE Flags: Precursor;
GN Name=sodB; Synonyms=sodM; ORFNames=AO090003000475-A;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=OSI 1013;
RX PubMed=15388959; DOI=10.1271/bbb.68.1849;
RA Ishida H., Hata Y., Kawato A., Abe Y., Kashiwagi Y.;
RT "Isolation of a novel promoter for efficient protein production in
RT Aspergillus oryzae.";
RL Biosci. Biotechnol. Biochem. 68:1849-1857(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-166.
RX PubMed=16781873; DOI=10.1016/j.ympev.2006.05.001;
RA Frealle E., Noel C., Nolard N., Symoens F., Felipe M.S., Dei-Cas E.,
RA Camus D., Viscogliosi E., Delhaes L.;
RT "Manganese superoxide dismutase based phylogeny of pathogenic fungi.";
RL Mol. Phylogenet. Evol. 41:28-39(2006).
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems.
CC {ECO:0000250|UniProtKB:P04179}.
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:0000250|UniProtKB:P0A0J3};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9UQX0};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9UQX0};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P04179}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q9UQX0}.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC56175.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB078724; BAC56175.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AP007155; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY625481; AAU04411.1; -; Genomic_DNA.
DR AlphaFoldDB; Q877B6; -.
DR SMR; Q877B6; -.
DR STRING; 510516.Q877B6; -.
DR Proteomes; UP000006564; Chromosome 2.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0030145; F:manganese ion binding; IEA:EnsemblFungi.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.287.990; -; 1.
DR Gene3D; 3.55.40.20; -; 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 Pfam; PF02777; Sod_Fe_C; 1.
DR Pfam; PF00081; Sod_Fe_N; 1.
DR PIRSF; PIRSF000349; SODismutase; 1.
DR PRINTS; PR01703; MNSODISMTASE.
DR SUPFAM; SSF46609; SSF46609; 1.
DR SUPFAM; SSF54719; SSF54719; 1.
DR PROSITE; PS00088; SOD_MN; 1.
PE 3: Inferred from homology;
KW Antioxidant; Manganese; Metal-binding; Mitochondrion; Oxidoreductase;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN ?..210
FT /note="Superoxide dismutase [Mn], mitochondrial"
FT /id="PRO_0000043336"
FT BINDING 29
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P04179"
FT BINDING 77
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P04179"
FT BINDING 164
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P04179"
FT BINDING 168
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P04179"
FT CONFLICT 150
FT /note="D -> N (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 210 AA; 23229 MW; D12C8ECAE02BB8DA CRC64;
MATTFSLPPL PYAYDALEPV ICKQIMEIHH QKHHQTYITN LNAALSAQST ALAANNIPQL
INLQQKIKFN GGGHINHSLF WKNLAPHASP ETNIDQAAPV LKAAIEAQYG SVEKFKEAFG
ATLLGLQGSG WGWLVANGPG GKLEIVSTKD QDPVTDKVPV FGVDMWEHAY YLQYFNNKAS
YVEGIWKVLN WRTAEDRFKN GVEGSALLKL
