ID A0A165HV68_9APHY Unreviewed; 600 AA.
AC A0A165HV68;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Thiamin diphosphate-binding protein {ECO:0000313|EMBL:KZT12231.1};
GN ORFNames=LAESUDRAFT_754721 {ECO:0000313|EMBL:KZT12231.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT12231.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT12231.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT12231.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; KV427606; KZT12231.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165HV68; -.
DR STRING; 1314785.A0A165HV68; -.
DR InParanoid; A0A165HV68; -.
DR OrthoDB; 2291769at2759; -.
DR Proteomes; UP000076871; 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:UP000076871};
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 213..338
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 435..595
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 600 AA; 64392 MW; C6A1D87BDB5D1956 CRC64;
MYTTASVLLK TLADVGVTHI FANWGNDHPA ILEDLERQRT DGGGKALLDV VTCPNEMVAL
SAAHGYSQVT GKPAAVIVHV DVGTQALAGA VHNADKGQAP VIIFAGASPF SVSGEHKGSK
NEWPMWGQDA PDQPAIVRQF MRFTAQIMSG KTVAKTVMRA WQFATSSPKG PVYLWARRET
LQEEIDPSVL QTPVDISKWP SVQPSGLSPT ALNTIVDALT NAEFPLIIAG NTGRNPQTVS
LLATLSNLRS IAVCTAISPA LCVPYSHPYL VGSSFDGRIA HLEKADVVLI IEADVPWMDT
MGSKLVDDTR VFVLDVDPLK QQFGWSHVDA EMLCRVDSAV ALGQLINAVR LADLQTSDKG
ALNARMYERG TKLRAFHEEW MKELLAAEEM AMGANGTVLT VPYVLRALRK AAQAHVPSGN
NILWLNEGIS NCDLVWNHIQ PEYPGSMIMS GGSSLGWALG AAVGARLGAQ VAGKDYELIV
AVVGDGDFLF GVPSAAYWMA RRYKTPFLTV ILNNGGWASP RYSMLGMYPN GVGSKATGQQ
LNVSFGPDMP DYAQIAAAAG DAWGRRVASA SELQSALEEG IRAVVENKRS AVVDCILEQI
//