ID A2R6V2_ASPNC Unreviewed; 606 AA.
AC A2R6V2;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Contig An16c0060, genomic contig {ECO:0000313|EMBL:CAK42748.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:CAK42748.1};
GN ORFNames=An16g01310 {ECO:0000313|EMBL:CAK42748.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK42748.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK42748.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {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|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM270358; CAK42748.1; -; Genomic_DNA.
DR RefSeq; XP_001397444.1; XM_001397407.1.
DR AlphaFoldDB; A2R6V2; -.
DR EnsemblFungi; CAK42748; CAK42748; An16g01310.
DR GeneID; 4988524; -.
DR KEGG; ang:An16g01310; -.
DR VEuPathDB; FungiDB:An16g01310; -.
DR HOGENOM; CLU_013748_4_0_1; -.
DR OrthoDB; 1948175at2759; -.
DR Proteomes; UP000006706; Chromosome 5R.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd02002; TPP_BFDC; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF164; PYRUVATE DECARBOXYLASE; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006706};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:CAK42748.1}.
FT DOMAIN 13..144
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 222..329
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 425..603
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 606 AA; 64805 MW; 1963974336DD7565 CRC64;
MSQDTTIETA PHTVADAFLE ALAEAGVDYL FTVLGSDHPS IIEAYVRRQN DPARQYPKMV
LFQHEFVAIS AADGYARMSH KPACVIAHVD VGTAALGQGL HNASSGRAPV VIFAGVAPST
LLGEAPGSRS EHVQWYQDIR DQAALVAPYS RFSAEIKSPH NVGSLVHRAV LMATTGSPGP
VYLTATREIL ATPLPSPQAR LKPIPSCQLG SLSPQAVELI GSALLNAKSP LVVTGYLGRN
HSAVQELIKL ADTIHGLRVF DSELREVCFP ATHPACVTRG TGAAPAVQSA DVILVLDADV
PWIPRRIHPS PDAVIYHIDL DPRKERMNMF DIGAAATFHA DTGPALTQIN AHITSSARLA
DLQTNWTDRH EALRAAHAEG RARIDARATK LLETPDAPCS VDFLCSRIRE LVPDDTIFVT
DSVTNQVAMT EQLQLTRPGS HLTKGGSGLG WAGGASIGVK LATTRYDTSD RPDVRVKADT
NSPFICNITG DGSFIFSVPS AVYWASHRYG CPFLTVILNN GGWNATRQCL VDVHPGGEAA
RLSSKDLGIS LVEDGPDYGG IAKAAANGNL WATRVRSVKE LDEALREGVR VVLEEGRGAV
VDVVIQ
//
