ID A0A139AD80_GONPJ Unreviewed; 826 AA.
AC A0A139AD80;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Thiamin diphosphate-binding protein {ECO:0000313|EMBL:KXS14708.1};
GN ORFNames=M427DRAFT_32916 {ECO:0000313|EMBL:KXS14708.1};
OS Gonapodya prolifera (strain JEL478) (Monoblepharis prolifera).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Monoblepharidomycetes; Monoblepharidales;
OC Gonapodyaceae; Gonapodya.
OX NCBI_TaxID=1344416 {ECO:0000313|EMBL:KXS14708.1, ECO:0000313|Proteomes:UP000070544};
RN [1] {ECO:0000313|EMBL:KXS14708.1, ECO:0000313|Proteomes:UP000070544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL478 {ECO:0000313|EMBL:KXS14708.1,
RC ECO:0000313|Proteomes:UP000070544};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; KQ965767; KXS14708.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139AD80; -.
DR STRING; 1344416.A0A139AD80; -.
DR OrthoDB; 1328249at2759; -.
DR Proteomes; UP000070544; Unassembled WGS sequence.
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; cd02004; TPP_BZL_OCoD_HPCL; 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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF166; 2-HYDROXYACYL-COA LYASE 2; 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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000070544};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 223..337
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 464..597
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 662..801
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 826 AA; 87678 MW; 50506DC70F7CD9C4 CRC64;
MGGDLDDDID PIDEDSYEES NETNQSPPLE SFHVRDAVHS DQADDSDIQH EEKETVVEPA
SHHSIITPQV LSPSNSESRT VSAASTRPNP ANVFVAQPSL GDTAKSLDRV GQIAGHVTGG
TEQGNGSREK LRQQALRASK VATVMALSML KELALEKPIH YPILAFLGFL RLLPRFLSDA
VPNRTVFHVA ATLAAYRLWK HFISGMEIHR LITGKVDHHS PLHGGHLAAH ALRAHNVKAI
FTLAGGHVAP VLVAAEEIGI RVVDVRDEAT AVFAADGYAR LTGGVGVAVV TAGPGLTNTI
TAVKNAQMAE SPVLVISGAA ATLLKGRGAL QDIDQLAVMK PLCKSTHTAT RVRSIPPTLL
TAIQHALTPP MGPVYVELPI DTLYPISLVA KNVGASGGGG PGKGIGAALV ESLLAAYVRF
VFADAFEGFG YRQPTPAGES PLVPMHTLVP LPVPRTPFSQ RPTSRALNVL LSSRRPVLLM
GSQCVARGPE AARRVADAVR SLGVPVFLAG MSRGLLGVDG GGCQLRQVRK QALKTADVIV
LAGITPDFRL DYGRVLSRKA KIIACNANPS SLRLNAGLFW TPEVAILGDP GDFVEALAKG
VKGKAWEKDE KWVGELTEAE RKKEEENRTK SLTTTAPSTL NPLSVLYALD RHLPADAILV
ADGGDFVGTA AYILRPRGPL GWLDPGAFGT LGVGAGFAIA AKVVHPERPV WVVFGDGSFG
WAEAEVDTWV RHKLGIMAII GNDAKWAQIA REQVHMLGRP TACILSRTAD YAAAGRAMGG
RGWTVKINGE LDKVLEEAVD AAGRGEAGVL DVWIGETDFR EGSVSV
//
