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Database: UniProt
Entry: A1DNL4_NEOFI
LinkDB: A1DNL4_NEOFI
Original site: A1DNL4_NEOFI 
ID   A1DNL4_NEOFI            Unreviewed;       583 AA.
AC   A1DNL4;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Thiamine pyrophosphate enzyme, putative {ECO:0000313|EMBL:EAW16385.1};
GN   ORFNames=NFIA_057340 {ECO:0000313|EMBL:EAW16385.1};
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW16385.1, ECO:0000313|Proteomes:UP000006702};
RN   [1] {ECO:0000313|Proteomes:UP000006702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; DS027698; EAW16385.1; -; Genomic_DNA.
DR   RefSeq; XP_001258282.1; XM_001258281.1.
DR   AlphaFoldDB; A1DNL4; -.
DR   STRING; 331117.A1DNL4; -.
DR   EnsemblFungi; EAW16385; EAW16385; NFIA_057340.
DR   GeneID; 4584797; -.
DR   KEGG; nfi:NFIA_057340; -.
DR   VEuPathDB; FungiDB:NFIA_057340; -.
DR   eggNOG; KOG1185; Eukaryota.
DR   HOGENOM; CLU_013748_4_0_1; -.
DR   OMA; DCGTLAM; -.
DR   OrthoDB; 2291769at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
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   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:UP000006702};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          21..151
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          224..329
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          431..582
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   583 AA;  63425 MW;  CD1BDE735199BAD4 CRC64;
     MNGDIQTKKR KWESDARVDS AATGFFEALV EAGVKYCFVN LGSDHPAMIE AMIKAKQENS
     TIFPTIITCP SELVALSAAL GYAQVTGSPQ CVIVHVDCGT LAMGQSIHNA SVTRVPVLCF
     AGLSPFTDSG EMLGSRTEFI HWLQDVPDQA SIVRQYCRYS GEIRTGRNIK QMVYRAMQFA
     MSDPKGPSYL TAAREVLEEQ VEIPDLGNEL MGPVTPCALP EPEVERLAAA LLGAKRPLII
     TGYMGRNPRT PPLLAELCDK LPISVIETVG SDVSLRSDHE AYLGVTVSTH PAVCEADVIL
     VMDCDVPWVP TAGKPADGTK VFHLDVDPLK QQMPVFFMQA IRRYKVSCEL ALQQLNTYLD
     KQSLDRAKYA EAFDARAARY RQWRQSLRDL EVPSPEGIVT VPYLSSRLRQ HLPDDSVIVI
     EAVTNAIPII HHLNLTKPGT LYGSGAGGLG WGGGAALGVK LAKRDSFICA IVGDGTYLFS
     QMESVYWIAR RYDIPFLLVV LNNSGWNAPK VSTLLVHKDG LASKSSRADL NLSFEPSPDY
     PVIAAAAGNA WGATVTKTDE VDSTLKKAVE AVQGGRCAVV EVR
//
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