ID R7YI27_CONA1 Unreviewed; 580 AA.
AC R7YI27;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00014422};
DE EC=4.1.1.1 {ECO:0000256|ARBA:ARBA00013202};
GN ORFNames=W97_00679 {ECO:0000313|EMBL:EON61464.1};
OS Coniosporium apollinis (strain CBS 100218) (Rock-inhabiting black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Coniosporium.
OX NCBI_TaxID=1168221 {ECO:0000313|EMBL:EON61464.1, ECO:0000313|Proteomes:UP000016924};
RN [1] {ECO:0000313|Proteomes:UP000016924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 100218 {ECO:0000313|Proteomes:UP000016924};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Gorbushina A., Noack S., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Coniosporium apollinis CBS 100218.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-oxocarboxylate + H(+) = an aldehyde + CO2;
CC Xref=Rhea:RHEA:11628, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:35179; EC=4.1.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001041};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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; JH767555; EON61464.1; -; Genomic_DNA.
DR RefSeq; XP_007776781.1; XM_007778591.1.
DR AlphaFoldDB; R7YI27; -.
DR STRING; 1168221.R7YI27; -.
DR GeneID; 19897990; -.
DR eggNOG; KOG4166; Eukaryota.
DR HOGENOM; CLU_013748_3_3_1; -.
DR OMA; PGPYGCL; -.
DR OrthoDB; 1328249at2759; -.
DR Proteomes; UP000016924; 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; 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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF169; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000016924};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 7..85
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 161..294
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 363..494
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 580 AA; 61705 MW; 77AC76B79E6E10BC CRC64;
MGCVDVGIEL VDTRHETVAV QAAEGYSRVS GKVGTCFVTA NSGFCNSLPG LATALADRSP
VFCVTSSAPL RDTGTNALQD FHDQVVLAKN LTKFAQRITN VGEIPRVVAL AWRTATAGAP
GPVVVDFPID ILFTPVDTDS IAWGGITAPP VSLPGPNPSA IDEAVRLYRA SERPCIIVGT
GAKDAEDEIL KLAEPTRTPI FHTSKCSTAI PYTHHLRAGL ATSLAFLQPQ NKPQPDLILL
VGVRTGFLLG GRSGAIIPNT DCKLIQIDVD GSEIGRSHYI DVGIVSDASL ALSAMHTRLA
SDSTATKAVA NEEWIRTALG LKALNARNDR DPVIDEENGR LHPYHALKRV FTSVPHNSIV
CIDGGECGVW AQQLLEHAHA HLSMATTGYM GFLGNGWGYS LGAAVADPGR MVLNIQGDGS
AGFHIAELDT YARFGLSILT VVVNNASWGM SRAGQELIFG GQTAARPAVA LSEQTRYEVV
AAGFGCAAAR VDAREVDAGG EDKGQFVLDR VGHEVHRMTM EKGPGLLNLV VSEKPVHDVT
RAMVGATGDP DVIVVPYYDN LPRPYYGRGK EADGKQYDRE
//