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
//