(data stored in ACNUC7421 zone)

SWISSPROT: A2Q7Q7_ASPNC

ID   A2Q7Q7_ASPNC            Unreviewed;       984 AA.
AC   A2Q7Q7;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 76.
DE   SubName: Full=Aspergillus niger contig An01c0070, genomic contig {ECO:0000313|EMBL:CAK43530.1};
DE            EC=4.1.1.1 {ECO:0000313|EMBL:CAK43530.1};
GN   ORFNames=An01g01590 {ECO:0000313|EMBL:CAK43530.1};
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:CAK43530.1, 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   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; AM269954; CAK43530.1; -; Genomic_DNA.
DR   PaxDb; A2Q7Q7; -.
DR   EnsemblFungi; CAK43530; CAK43530; An01g01590.
DR   HOGENOM; HOG000061335; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004737; F:pyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:InterPro.
DR   InterPro; IPR013149; ADH_C.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
PE   3: Inferred from homology;
DR   PRODOM; A2Q7Q7.
DR   SWISS-2DPAGE; A2Q7Q7.
KW   Lyase {ECO:0000313|EMBL:CAK43530.1};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          45..141
FT                   /note="ADH_N"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          184..310
FT                   /note="ADH_zinc_N"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
FT   DOMAIN          394..569
FT                   /note="TPP_enzyme_N"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          595..704
FT                   /note="TPP_enzyme_M"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          779..894
FT                   /note="TPP_enzyme_C"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          890..912
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          963..984
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        963..977
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   984 AA;  107172 MW;  88221A7B066311A9 CRC64;
     MAPAHTISMP HPQLFERPRI TTSEGPSFFL DYLSLTNNLR LSPGPDEVLV NLKFSGLCHS
     TLHQWRDAHE GTGVVIAAGN EVEDIKIGDH VGIQWINRTC GGCDADKRSD FVSCPHARMT
     GYSVDGTFEE YCISQACHVV RLPKQFPLDI VAPIICVGTT CFRAVLESDA QPGSLVAVAG
     PPGGLTTLTC QYAKARGCRV LVVSTGDDSG LLYKKKLGVE YYIDYNCSAD IVAEVQGING
     NGPDAAILIE GSGALLKGAL QYVQHRGTVV VMGLPPGSPV GIDVCKLVSR MAQVKVVPYG
     GTREQIEEAI LVFTKERFYQ SCRVFALDQL PQVLKSMQNE MPEGTSPEPA LHHGGQLLGE
     AVIKMPHREA TPKPQTIAYP PTFKSTFHQT NYNIGTFLAY RLEELGVRDY FAVPGDTNFF
     LLDNLLKSPK LRMVTCCNEL NAGYAADGYA RVSSARIAVV VVPYIVGSLS ALNAVSGACS
     QYVRLIVLSG CPATGVVDSD KFLHHAPTAK NKDQALQAFM GVTAASVRLE SVETAPDVLD
     DTISKCLDSS LPVYIEIPND LAFAACTPPS PLSRKVNWKT QPHVLKEAAE AITGIWNSSK
     RPVLLLGSLA GLSLPRLHIE LLAEKLGCAV LCQPDGRCIE ESHPQYCGQF WAGMTNPEGE
     HIVMSSDLWL VIGGNWSDLH VVMSSHKQEN YRMINVDKDW VELPDGKHIK PVNIGALVAQ
     LIMSGMKPKT ESIPRPKPLL GCLPPDETET PEAPLTLRSS ISGIQGLIKG HDTLLCDAGE
     SWLIANHILL PPEANCHLQF PYCSIGWALP AGFGSQLART RGRSIILIGD GGFQMTAQAV
     SSMIRYKANP VIFVFNNLGY QIEASQTAMH QGPYNYIANW DYVKLASSFS SKPHAPSHNP
     YASKEDEERE GSPSMFALKI KTIGDLRQAL DRVDEEPDKL AFLELCIQPN DVTDDLRRLG
     RMMADRSAEA SRESQSPDTE EVDE
//

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