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Database: UniProt
Entry: C5DC94_LACTC
LinkDB: C5DC94_LACTC
Original site: C5DC94_LACTC 
ID   C5DC94_LACTC            Unreviewed;       593 AA.
AC   C5DC94;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   SubName: Full=KLTH0B01188p {ECO:0000313|EMBL:CAR21405.1};
GN   OrderedLocusNames=KLTH0B01188g {ECO:0000313|EMBL:CAR21405.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21405.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21405.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR036565-2};
CC       Note=Binds 1 Mg(2+) per subunit. {ECO:0000256|PIRSR:PIRSR036565-2};
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; CU928166; CAR21405.1; -; Genomic_DNA.
DR   RefSeq; XP_002551843.1; XM_002551797.1.
DR   AlphaFoldDB; C5DC94; -.
DR   STRING; 559295.C5DC94; -.
DR   GeneID; 8290669; -.
DR   KEGG; lth:KLTH0B01188g; -.
DR   eggNOG; KOG1184; Eukaryota.
DR   HOGENOM; CLU_013748_0_2_1; -.
DR   InParanoid; C5DC94; -.
DR   OMA; EQRYNDI; -.
DR   OrthoDB; 1000728at2759; -.
DR   Proteomes; UP000002036; Chromosome B.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd02005; TPP_PDC_IPDC; 1.
DR   CDD; cd07038; TPP_PYR_PDC_IPDC_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; IPR012110; PDC/IPDC-like.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   InterPro; IPR047214; TPP_PDC_IPDC.
DR   InterPro; IPR047213; TPP_PYR_PDC_IPDC-like.
DR   PANTHER; PTHR43452; PYRUVATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43452:SF30; PYRUVATE DECARBOXYLASE ISOZYME 1-RELATED; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   PIRSF; PIRSF036565; Pyruvt_ip_decrb; 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   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR036565-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR036565-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          34..137
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          230..353
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          428..544
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   BINDING         57
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /ligand_label="1"
FT                   /ligand_note="substrate; ligand shared between two
FT                   neighboring subunits"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-1"
FT   BINDING         144
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /ligand_label="1"
FT                   /ligand_note="substrate; ligand shared between two
FT                   neighboring subunits"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-1"
FT   BINDING         186
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /ligand_label="2"
FT                   /ligand_note="allosteric activator"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-1"
FT   BINDING         500
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         502
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         506
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /ligand_label="1"
FT                   /ligand_note="substrate; ligand shared between two
FT                   neighboring subunits"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-1"
SQ   SEQUENCE   593 AA;  65284 MW;  DB95803C643A7F43 CRC64;
     MSDLILYCDF YKTRNLNSNR VSQNKPEITM SEITLGRYVF ERLKQVDVTT VFGLPGDFNL
     RLLDEIYEVE GMRWAGNCNE LNASYAADAY ARIKGMSCLI TTFGVGELSA LNGIAGSYAE
     HVGVLHIVGV PSVSAQAKQL LLHHTLGNGD FTVFHRMSAN ISETTAMITD LATAPSEIDR
     CIRTTYIRQR PVYLGLPSNF VDQMVPASLL DTPIDLALKP NDQQAEEEVI STLLEMIKDA
     KNPVILADAC ASRHDVKAET KKLIDITQFP SFVTPMGKGS IDEKHPRFGG VYVGTLSSPA
     VKEAVESADL VLSVGALLSD FNTGSFSYSY KTKNVVEFHS DHIKIRNATF PGVQMKFVLQ
     SLLNKVGAVV KDYKPVPVPE LPAPNAAVDP STPLKQQWLW NQVGQFLQEG DIVLTETGTS
     AFGINQTHFP NNTYGISQVL WGSIGYATGA CLGAVMAAEE LDKSKRVILF TGEGSLQLTA
     QEISTMVRWN LKPYLFVLNN KGYTIEKLIH GPTAEYNEIQ NWNHLDLLPT FGAKDYEAIR
     VSTTGEWNKL AEDKDFNKNS KIRLIELMLP VMDAPESLVK QAQLTAATNA KSA
//
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