ID A0A427YM77_9TREE Unreviewed; 616 AA.
AC A0A427YM77;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Pyruvate decarboxylase 1 {ECO:0000313|EMBL:RSH92195.1};
GN Name=PDC1_3 {ECO:0000313|EMBL:RSH92195.1};
GN ORFNames=EHS25_008610 {ECO:0000313|EMBL:RSH92195.1};
OS Saitozyma podzolica.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Trimorphomycetaceae; Saitozyma.
OX NCBI_TaxID=1890683 {ECO:0000313|EMBL:RSH92195.1, ECO:0000313|Proteomes:UP000279259};
RN [1] {ECO:0000313|EMBL:RSH92195.1, ECO:0000313|Proteomes:UP000279259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27192 {ECO:0000313|EMBL:RSH92195.1,
RC ECO:0000313|Proteomes:UP000279259};
RA Aliyu H., Gorte O., Ochsenreither K.;
RT "Genome sequence of Saitozyma podzolica DSM 27192.";
RL Submitted (NOV-2018) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RSH92195.1}.
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DR EMBL; RSCD01000006; RSH92195.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A427YM77; -.
DR STRING; 1890683.A0A427YM77; -.
DR Proteomes; UP000279259; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Pyruvate {ECO:0000313|EMBL:RSH92195.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000279259};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU362132};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 4..114
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 240..349
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 448..539
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 189..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 490
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 517
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 519
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ SEQUENCE 616 AA; 67397 MW; BD40C9BFA02A4489 CRC64;
MSIEFAQYLV ERLKQCGVKY VFGVPGDYNL ELLDYIERDE HLVWVGNANE LNAAYASDGY
ARVKGGLAAV ITTFGVGELS ALCGIAGALA ERVPVLHIVG APSRALQSSS ALLHHTLNLP
TSFSTFSTMS RPLSCSQALL NEIEPRDPST WTDALDMVLK DVLEQCRPGY VEIPTDAVHH
KVSADGLKKL LPSPHAAPPN ESFAASQPVG SSSDVNPNAP ASAKGQPSQA PSDDVTEYVV
EEITERFAKA KKPIIIVDAC AGRFGMAGEV RKLVEKCQIR FFETPMGKSL LDEHHPLYGG
CYAGANSLQP VREEVESADF VLFVGALKSD FNSGSFSVNI DPKITIELHS FTTNVGYASY
PTTDIRHILP LLVPSFGKVH SARSEPHGES LESKIKSGRM EPQLVEPKGE EIKHKWFWQR
MGRWFADNDI IITETGTSSF GLINVPLPSH STYVAQILWG AIGWSVGAAL GCALAATEQK
PRRTVLFVGD GSLQLTLQEI GTMIRHGVKP YLFVINNDGY EIERQIHGWT AKYNDIQLYD
HQMLLPFLAG KKSKVPYESV AVHTPAELEA LLTNEAFAKD DKIRLVEVYM PRGDAPEGLI
RQAKLTAEAN EKASEK
//
