ID A0A409W2X8_9AGAR Unreviewed; 642 AA.
AC A0A409W2X8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Thiamine pyrophosphate enzyme TPP-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CVT24_012894 {ECO:0000313|EMBL:PPQ72818.1};
OS Panaeolus cyanescens.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Galeropsidaceae; Panaeolus.
OX NCBI_TaxID=181874 {ECO:0000313|EMBL:PPQ72818.1, ECO:0000313|Proteomes:UP000284842};
RN [1] {ECO:0000313|EMBL:PPQ72818.1, ECO:0000313|Proteomes:UP000284842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2629 {ECO:0000313|EMBL:PPQ72818.1,
RC ECO:0000313|Proteomes:UP000284842};
RX PubMed=30283667; DOI=10.1002/evl3.42;
RA Reynolds H.T., Vijayakumar V., Gluck-Thaler E., Korotkin H.B.,
RA Matheny P.B., Slot J.C.;
RT "Horizontal gene cluster transfer increased hallucinogenic mushroom
RT diversity.";
RL Evol. Lett. 2:88-101(2018).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PPQ72818.1}.
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DR EMBL; NHTK01005850; PPQ72818.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A409W2X8; -.
DR STRING; 181874.A0A409W2X8; -.
DR InParanoid; A0A409W2X8; -.
DR OrthoDB; 2291769at2759; -.
DR Proteomes; UP000284842; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000284842};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 235..324
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 463..596
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 642 AA; 69263 MW; FAAB3B953E6C800F CRC64;
MYTATSLFLQ ALRKLAITHL FVNWGSDHPA FLEELERQRA EDGEAHFLVV TCPNEMVALS
AAQGYAQVLG RPAAVIVHVD VGTQALAGAV HNVDRSRTPV IIFAGASPTS SEREHAGSVP
GARNEWIMWV QGQHNELLSL NLHSRKGSDI PDQAAIVRQY MRHTAQIGSL QTTENMVNRA
FQISMSAPKG PVYLWGRRDI MELPVDEATW KAAVAKAPAV PVAVSPAALS PSDLSRIAGA
LLAADSPLIV TSFLGRNVNA VAELIKLAEL LAIPVVNACP SAVNIPFSHP SYAGTTYMFK
GTHLPALDEA DLILVIECEI PWIPVCDEPR NLGNGLQVFL LDSGDPLRVN VGYWNVPAAG
IFRADAEIAL KQINESVAPI AQGIISKVDA RRLTLRTKHE RLVADIEATE ALPPPLNIDG
IPTASFTVPN LMRSLRLAIE KVTPSRGSKT LYLNESISNF PLVWNHLRTE VPGQMLTLGG
SSLGWGLGAS VGSFLASKES KLKHDLSVLI VGDGAFLFGV PSSAYWMARR YETPFLTIVL
NNGGWRSPKF SMLGVHPTGY GSHASGDRLS VGFGPDSPDY SQIAVAASSG WALGERIGGP
KWDLEVGLEN RMTALQTAIE SAIKRVFDEK RCVVLDCILE SI
//