(data stored in SCRATCH zone)

SWISSPROT: A2Q7D3_ASPNC

ID   A2Q7D3_ASPNC            Unreviewed;       351 AA.
AC   A2Q7D3;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 94.
DE   SubName: Full=Aspergillus niger contig An01c0030, genomic contig {ECO:0000313|EMBL:CAK43417.1};
DE            EC=1.7.1.1 {ECO:0000313|EMBL:CAK43417.1};
GN   ORFNames=An01g00250 {ECO:0000313|EMBL:CAK43417.1};
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011 {ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK43417.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 {ECO:0000313|Proteomes:UP000006706};
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA   Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA   van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA   Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA   Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA   Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA   van Ooyen A.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|SAAS:SAAS01057700};
CC   -!- SIMILARITY: Belongs to the cytochrome b5 family.
CC       {ECO:0000256|RuleBase:RU362121}.
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DR   EMBL; AM269950; CAK43417.1; -; Genomic_DNA.
DR   SMR; A2Q7D3; -.
DR   PaxDb; A2Q7D3; -.
DR   EnsemblFungi; CAK43417; CAK43417; An01g00250.
DR   HOGENOM; HOG000175005; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009703; F:nitrate reductase (NADH) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.10.120.10; -; 1.
DR   Gene3D; 3.40.50.80; -; 1.
DR   InterPro; IPR001834; CBR-like.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   InterPro; IPR018506; Cyt_B5_heme-BS.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00406; CYTB5RDTASE.
DR   PRINTS; PR00363; CYTOCHROMEB5.
DR   PRINTS; PR00371; FPNCR.
DR   SMART; SM01117; Cyt-b5; 1.
DR   SUPFAM; SSF52343; SSF52343; 1.
DR   SUPFAM; SSF55856; SSF55856; 1.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   3: Inferred from homology;
DR   PRODOM; A2Q7D3.
DR   SWISS-2DPAGE; A2Q7D3.
KW   FAD {ECO:0000256|SAAS:SAAS01057697};
KW   Flavoprotein {ECO:0000256|SAAS:SAAS01057691};
KW   Heme {ECO:0000256|RuleBase:RU362121, ECO:0000256|SAAS:SAAS00123300};
KW   Iron {ECO:0000256|RuleBase:RU362121, ECO:0000256|SAAS:SAAS00429729};
KW   Metal-binding {ECO:0000256|RuleBase:RU362121,
KW   ECO:0000256|SAAS:SAAS00123265}; NAD {ECO:0000256|SAAS:SAAS01094228};
KW   Oxidoreductase {ECO:0000256|SAAS:SAAS01057701,
KW   ECO:0000313|EMBL:CAK43417.1}.
FT   DOMAIN          19..91
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          107..211
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   351 AA;  38763 MW;  14F99A3571B1A79F CRC64;
     MAQSVPLEST ASMGADSQLT EYTLADIAKH NRKDDIWIAV HGQVFDITEY LQDHPGGVDV
     LLETAGSDAT TAFEDVGHSE DSREILQEYL IVVRADPHMA KGFLDSKEYQ RLPLVQKDLL
     SPNVYRFVFA LPDTKGVIGL PIGQHVAIRA NIDGNTVSRS YTPVSNNLDL GRLELVVKCY
     PDGLLSGKYL ANLTVGDEVE FRGPKGAMRY GRGLCAKIGM VAGGTGITPM YQLIRAICED
     ERDTTEISLI YANRSEGDIL LREELEDFAR KYPKNFKLWY MLDTAPEGWM YGSGYVNEAV
     LRERLPDPSA ETKIMLCGPP GMVNACKKTL GVIGFQTSGT ISKMSDQIFC F
//

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