ID A0A0D2AX28_9EURO Unreviewed; 613 AA.
AC A0A0D2AX28;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00014422};
GN ORFNames=PV06_05360 {ECO:0000313|EMBL:KIW44346.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW44346.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW44346.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW44346.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN847335; KIW44346.1; -; Genomic_DNA.
DR RefSeq; XP_016264562.1; XM_016406356.1.
DR AlphaFoldDB; A0A0D2AX28; -.
DR STRING; 215243.A0A0D2AX28; -.
DR GeneID; 27357434; -.
DR VEuPathDB; FungiDB:PV06_05360; -.
DR HOGENOM; CLU_013748_0_2_1; -.
DR OrthoDB; 2067532at2759; -.
DR Proteomes; UP000053342; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004737; F:pyruvate decarboxylase activity; IEA:UniProtKB-EC.
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:SF11; PYRUVATE DECARBOXYLASE; 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; 2.
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:UP000053342};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..113
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 204..313
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 427..505
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 360..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 468
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 495
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ SEQUENCE 613 AA; 67700 MW; D3AA59838E2C8AE7 CRC64;
MTRIPLAQYL FKRLRSQGVH AIHGVPGDFT LKALDHLPPS GVKWIGNCNE LNAGYAADGY
ARVRGLGALF TTYGVGELSA INAVAGSFSE SVPVVHIVGT PQRRLQDARA NVHHTLGDGR
PRVFAQMHRP VTVAQTDLRD ETTAPEDIDR TVAAALEHSR PVYIELPCDM VSKEVDAAGL
EVPLVDRFTT TEEFKARDED ALVADIVRRL YGSKRPLVLV DSGDGLRSPS LRREVNEFVK
RSGLPTLCMP SGSGMVDHAL GNYYGVHSGP VGQIDTMPYV NGADLVLAFG PMFSDTQTLG
WKVVPEPEKT ITMGKNHLSL PTRTSTTLSR INLHSLLPRL TKLLDKTLLS KPDVSTLGDF
RTVVPRPRPT SASTSTANED GQSDDDPIDQ TNFYLRLNPY LRPDDVVLLG NATPILGGRD
LVLPTGSQVI ASGQWFSIGH MLPAALGASL ARQQTVRNGG RTILLDGDGS FQVTAQELST
VIRYRVDLTI FLINNSGYAY ERQIHGMNED YNDLSCWNYM ELPFVFSNKP HRNDDGTTTT
TTTTTNDNRN HDEDDEYPIK SYVIRTWREM DTLLASEEFC TGKGLRFVDV RMDKFDVPEK
FRVVFKRAGE QLG
//
