ID   A2R395_ASPNC            Unreviewed;       708 AA.
AC   A2R395;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Contig An14c0130, genomic contig {ECO:0000313|EMBL:CAK46587.1};
DE            EC=2.2.1.3 {ECO:0000313|EMBL:CAK46587.1};
GN   ORFNames=An14g03500 {ECO:0000313|EMBL:CAK46587.1};
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:CAK46587.1, ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK46587.1, 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   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|ARBA:ARBA00007131}.
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; AM270320; CAK46587.1; -; Genomic_DNA.
DR   RefSeq; XP_001400975.1; XM_001400938.1.
DR   AlphaFoldDB; A2R395; -.
DR   EnsemblFungi; CAK46587; CAK46587; An14g03500.
DR   GeneID; 4987206; -.
DR   KEGG; ang:An14g03500; -.
DR   VEuPathDB; FungiDB:An14g03500; -.
DR   HOGENOM; CLU_009227_0_0_1; -.
DR   OrthoDB; 5399939at2759; -.
DR   Proteomes; UP000006706; Chromosome 1R.
DR   GO; GO:0047896; F:formaldehyde transketolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:UniProt.
DR   GO; GO:0006163; P:purine nucleotide metabolic process; IEA:UniProt.
DR   CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR   CDD; cd02012; TPP_TK; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR020826; Transketolase_BS.
DR   InterPro; IPR033248; Transketolase_C.
DR   InterPro; IPR033247; Transketolase_fam.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR   PANTHER; PTHR43522:SF6; TRANSKETOLASE-LIKE PYRIMIDINE-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006706};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAK46587.1}.
FT   DOMAIN          375..558
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   708 AA;  77684 MW;  7C635BC241208DD3 CRC64;
     MAVGPVPQSN GASALPLVRQ LSKDHDHVLK SFRLLISDLC QQFGGGHPGG AIGMAAIGVA
     LWRYVMQYAP HSPDYFNRDR FILSNGHTCL FQYAFLHLTG YKAMTFEQLK SYHSDRVDAL
     CPGHPEIEHE GIEVTTGPLG QGVANAVGLA MATKNLAANF NRPGYDVISN HTWCMIGDAC
     LQEGVGLEAI SFAGHLKLNN LTVIYDNNQI TCDGSVDLTN TEDINAKMRA CGWDVIDVED
     GCYDVEGIVQ ALEKARASQE KPTFINVRTV IGLGSKVEGM AAAHGAAFGA PDVADMKRKY
     GFNPDEHFVI SDTVRGFFQE LPTRGEALVQ QWNSLVKQYS AEYPELGAEF QRRMRGELPS
     NWKDLIPSSF PDKPTATRAS SGLVFNPLAK DIESFMVGTA DLSPSVNMIW PGKVDFQHPD
     LRTTCKINGN YSGRYIHFGV REHAMCAISN GLAAFAPNTF IPITSSFFMF YLYAAPAVRM
     GALQHLQVIH AATHDSIGMG EDGPTHQPIE LAALYRAMPN LLYIRPGDSE ETAGAWIAAL
     EAKKSSSIIS TSRHALPQLK QTRREGVALG AYVLEEADDA SVTLIGVGAE LSFALEVAQQ
     LKETKGIAAR VISFPCQRLF EQQPLEYKRT VLRRHQGIPA VVIEPYAPNG WERYGDAGIN
     IRRFGHSLPG KAAYKFFGYE TGVMAAKVSD YLDRLEKGEW QRGEFVDL
//