ID B9WM90_CANDC Unreviewed; 623 AA.
AC B9WM90;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE SubName: Full=Phenypyruvate decarboxylase, putative {ECO:0000313|EMBL:CAX40203.1};
DE EC=4.1.1.- {ECO:0000313|EMBL:CAX40203.1};
GN OrderedLocusNames=Cd36_32400 {ECO:0000313|CGD:CAL0000160094};
GN ORFNames=CD36_32400 {ECO:0000313|EMBL:CAX40203.1};
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX40203.1, ECO:0000313|Proteomes:UP000002605};
RN [1] {ECO:0000313|EMBL:CAX40203.1, ECO:0000313|Proteomes:UP000002605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC {ECO:0000313|Proteomes:UP000002605};
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(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}.
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DR EMBL; FM992695; CAX40203.1; -; Genomic_DNA.
DR RefSeq; XP_002422199.1; XM_002422154.1.
DR AlphaFoldDB; B9WM90; -.
DR GeneID; 8049348; -.
DR KEGG; cdu:CD36_32400; -.
DR CGD; CAL0000160094; Cd36_32400.
DR VEuPathDB; FungiDB:CD36_32400; -.
DR eggNOG; KOG1184; Eukaryota.
DR HOGENOM; CLU_013748_0_2_1; -.
DR OrthoDB; 1000728at2759; -.
DR Proteomes; UP000002605; Chromosome R.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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:SF3; TRANSAMINATED AMINO ACID DECARBOXYLASE; 1.
DR Pfam; PF02775; TPP_enzyme_C; 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, ECO:0000313|EMBL:CAX40203.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR036565-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036565-2}; Pyruvate {ECO:0000313|EMBL:CAX40203.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 27..136
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 455..539
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT BINDING 500
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 531
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 533
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ SEQUENCE 623 AA; 70105 MW; 8244DC2478592477 CRC64;
MTPIQQTPSV HNTIDGSSID FPNQISLGEY LFYRISQANP ILKSIFGIPG DFNLNLLEHI
YSPIISEREI KFINACNELN CAYAADGYSR VIGGMSAMIT TFGVGELSAI NGVAGAFAEH
SPVLHIVGTT SMKDRLRAPN EIYNIHHLVP NHDPLKPPNH DVYKSMVKSI SVVQESLDYD
TRNNLIKIDN VLKKVIQEAR PGYLFIPSDV PDLPVPVNML LSDPFTADTR YTNSTLSKEV
LDEVTNVILN KLYDAKNPSI FSDCLTTRFG YQNDLNRFID QIPESVKLFT ANLARNLDES
RSNLVGVYNG NGSSDDKTKQ EFESSDFILA LGFFPNEMNT GGHTSNFSKV TDVVIVHPDY
IKVNHQFYHI KQNDGERLFT LGEFLCTLTE KLDASKISVE PKDIYQYQPP QQYTTSNLDY
IPQGKLIDHF NSTLKPNDLF IIETSSFVFG LPDMKFPPNL QLLTSPYYGS IGYAIPATFG
ATLAVNDLKS DRRVILVQGD GAAQMTVQEL SSFVRYKEIL PNLPQIYLIN NDGYTIERKI
KGPNRSYNDI NGKWKWGDLL NVFGGVQGKM YESYVLKNSY ELDQFFSGKT KPMSSNKLQF
YEIIAGKYDV PQRVDNMMCI SKK
//
