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Database: UniProt/SWISS-PROT
Entry: SODC_EMENI
LinkDB: SODC_EMENI
Original site: SODC_EMENI 
ID   SODC_EMENI              Reviewed;         154 AA.
AC   Q9HEY7; C8VUL3; Q5BGT9; Q8X1S5; Q8X1S7;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-OCT-2017, entry version 104.
DE   RecName: Full=Superoxide dismutase [Cu-Zn];
DE            EC=1.15.1.1;
GN   Name=sodA; ORFNames=AN0241;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11094151; DOI=10.1016/S0014-5793(00)02206-7;
RA   Oberegger H., Zadra I., Schoeser M., Haas H.;
RT   "Iron starvation leads to increased expression of Cu/Zn-superoxide
RT   dismutase in Aspergillus.";
RL   FEBS Lett. 485:113-116(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA   Holdom M.D., Hobby P., Lechenne B., Zaugg C., Sutton B., Monod M.,
RA   Hamilton A.J.;
RT   "Homogeneity in 3-dimensional structure of Cu,Zn superoxide dismutases
RT   of Aspergillus fumigatus, Aspergillus flavus and Aspergillus
RT   nidulans.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-11.
RX   PubMed=8757871;
RA   Holdom M.D., Hay R.J., Hamilton A.J.;
RT   "The Cu,Zn superoxide dismutases of Aspergillus flavus, Aspergillus
RT   niger, Aspergillus nidulans, and Aspergillus terreus: purification and
RT   biochemical comparison with the Aspergillus fumigatus Cu,Zn superoxide
RT   dismutase.";
RL   Infect. Immun. 64:3326-3332(1996).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA66114.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AF305546; AAG40775.1; -; mRNA.
DR   EMBL; AF281058; AAL38992.1; -; Genomic_DNA.
DR   EMBL; AF281060; AAL38994.1; -; mRNA.
DR   EMBL; AACD01000005; EAA66114.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001308; CBF89897.1; -; Genomic_DNA.
DR   RefSeq; XP_657845.1; XM_652753.1.
DR   ProteinModelPortal; Q9HEY7; -.
DR   SMR; Q9HEY7; -.
DR   BioGrid; 1956792; 1.
DR   STRING; 162425.CADANIAP00002483; -.
DR   EnsemblFungi; CADANIAT00002483; CADANIAP00002483; CADANIAG00002483.
DR   EnsemblFungi; EAA66114; EAA66114; AN0241.2.
DR   GeneID; 2876018; -.
DR   KEGG; ani:AN0241.2; -.
DR   HOGENOM; HOG000263447; -.
DR   InParanoid; Q9HEY7; -.
DR   KO; K04565; -.
DR   OMA; IHTFGDN; -.
DR   OrthoDB; EOG092C578I; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IDA:AspGD.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; ISS:AspGD.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0010106; P:cellular response to iron ion starvation; IEP:AspGD.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEP:AspGD.
DR   GO; GO:0006801; P:superoxide metabolic process; ISS:AspGD.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   1: Evidence at protein level;
KW   Antioxidant; Complete proteome; Copper; Cytoplasm;
KW   Direct protein sequencing; Disulfide bond; Metal-binding;
KW   Oxidoreductase; Reference proteome; Zinc.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    154       Superoxide dismutase [Cu-Zn].
FT                                /FTId=PRO_0000164120.
FT   METAL        47     47       Copper. {ECO:0000250}.
FT   METAL        49     49       Copper. {ECO:0000250}.
FT   METAL        64     64       Copper. {ECO:0000250}.
FT   METAL        64     64       Zinc. {ECO:0000250}.
FT   METAL        72     72       Zinc. {ECO:0000250}.
FT   METAL        81     81       Zinc. {ECO:0000250}.
FT   METAL        84     84       Zinc. {ECO:0000250}.
FT   METAL       121    121       Copper. {ECO:0000250}.
FT   DISULFID     58    147       {ECO:0000250}.
FT   CONFLICT      8      8       Missing (in Ref. 2; AAL38992).
FT                                {ECO:0000305}.
FT   CONFLICT     26     26       N -> S (in Ref. 2; AAL38994).
FT                                {ECO:0000305}.
FT   CONFLICT    119    119       V -> A (in Ref. 2; AAL38994).
FT                                {ECO:0000305}.
SQ   SEQUENCE   154 AA;  15988 MW;  88D5F231F6F5F5E1 CRC64;
     MVKAVAVLRG DSKVSGTVTF EQADENSNTT VSWNITGNDP NAERGFHIHQ FGDNTNGCTS
     AGPHFNPFGK THGAPEDEVR HVGDLGNFKT DAEGNSKGSK TDKLIKLIGA ESVLGRTLVV
     HAGTDDLGRG DSEESKKTGN AGARPACGVI GIAA
//
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