ID A0A0P9EN04_RHOGW Unreviewed; 579 AA.
AC A0A0P9EN04;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Pyruvate decarboxylase {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=RHOBADRAFT_2550 {ECO:0000313|EMBL:KPV73287.1};
OS Rhodotorula graminis (strain WP1).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV73287.1, ECO:0000313|Proteomes:UP000053890};
RN [1] {ECO:0000313|EMBL:KPV73287.1, ECO:0000313|Proteomes:UP000053890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP1 {ECO:0000313|EMBL:KPV73287.1,
RC ECO:0000313|Proteomes:UP000053890};
RX PubMed=26441909; DOI=10.3389/fmicb.2015.00978;
RA Firrincieli A., Otillar R., Salamov A., Schmutz J., Khan Z., Redman R.S.,
RA Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT "Genome sequence of the plant growth promoting endophytic yeast Rhodotorula
RT graminis WP1.";
RL Front. Microbiol. 6:978-978(2015).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; KQ474083; KPV73287.1; -; Genomic_DNA.
DR RefSeq; XP_018269336.1; XM_018412688.1.
DR AlphaFoldDB; A0A0P9EN04; -.
DR STRING; 578459.A0A0P9EN04; -.
DR GeneID; 28973137; -.
DR OMA; PWINKLC; -.
DR OrthoDB; 2291769at2759; -.
DR Proteomes; UP000053890; 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; 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:UP000053890};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 9..139
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 216..344
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 425..575
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT NON_TER 579
FT /evidence="ECO:0000313|EMBL:KPV73287.1"
SQ SEQUENCE 579 AA; 62270 MW; 924509D665ABD00B CRC64;
MSAPTEVFTT SNVFLDVLVK AGIRKAFVNL GSDHPALLEA FASRKKYGLP SLDIVTCPNE
MVALSAAQGY AQVCGHPAAV IVHVDCGTQA LAGAVHNVST CRTPVFIYAG ASPFSENGEL
AGSRNEFIHW LQNATDQPAI VRQYMRHVGE IRSAKNTQQV VLRALQFAKS EPKGPVYVWG
QREATEEHVD PNVIGDVRAQ EIWSPIELNP LNKTAVKRIS EALLAAKSPL IITSYLGRNP
HAVNELVKLV DLLAVPVFQP TLSTVNFPFD HPSHQGVAFA GATPEWKAAV EAADCILVID
SDVPWCVPPR AFHLDVDPLK ERMAFATYPA QLRAKVDAAL ALEQLYDYLT SSSALGAHEA
AIVKRRSALV DKKKASDAAL RELEVPQEGD IMTSSTIVGR YRDLLADQGL SSLVCNEAIS
NYPQVWQHLV PTKAGECISS GASSLGWALG AAIGAQLAAE VHPEFKKDLT TVFVGDGSFI
FGVPSASFWM ARRYETPTLV FVFNNGGWKS PKLSMLGVHP NGLGAAGPTS ELNVSFGPTD
DLNPDYGAIA AAAGGAWCRK VKTASELDEA MREAVRVVR
//