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}.
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; 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
//