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Database: UniProt
Entry: Q877B6
LinkDB: Q877B6
Original site: Q877B6 
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   16-JAN-2019, entry version 74.
DE   RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE            EC=1.15.1.1;
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.
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.,
RA   Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K.,
RA   Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W.,
RA   Galagan J.E., Nierman W.C., Yu J., Archer D.B., Bennett J.W.,
RA   Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H.,
RA   Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R.,
RA   Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N.,
RA   Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I.,
RA   Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y.,
RA   Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y.,
RA   Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K.,
RA   Kuhara S., Ogasawara N., 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
CC       systems. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC56175.1; Type=Frameshift; Positions=204; Evidence={ECO:0000305};
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   ProteinModelPortal; Q877B6; -.
DR   SMR; 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   GO; GO:0001320; P:age-dependent response to reactive oxygen species involved in chronological cell aging; IEA:EnsemblFungi.
DR   GO; GO:0001302; P:replicative cell aging; IEA:EnsemblFungi.
DR   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 2.40.500.20; -; 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   Complete proteome; Manganese; Metal-binding; Mitochondrion;
KW   Oxidoreductase; Reference proteome; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion. {ECO:0000250}.
FT   CHAIN         ?    210       Superoxide dismutase [Mn], mitochondrial.
FT                                /FTId=PRO_0000043336.
FT   METAL        29     29       Manganese. {ECO:0000250}.
FT   METAL        77     77       Manganese. {ECO:0000250}.
FT   METAL       164    164       Manganese. {ECO:0000250}.
FT   METAL       168    168       Manganese. {ECO:0000250}.
FT   CONFLICT    150    150       D -> N (in Ref. 2). {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
//
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