ID A0A139I3A8_9PEZI Unreviewed; 1478 AA.
AC A0A139I3A8;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00014422};
GN ORFNames=AC579_3508 {ECO:0000313|EMBL:KXT09213.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT09213.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXT09213.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT09213.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KXT09213.1}.
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DR EMBL; LFZO01000361; KXT09213.1; -; Genomic_DNA.
DR STRING; 113226.A0A139I3A8; -.
DR Proteomes; UP000073492; 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; IPR048379; Rad26-like_C.
DR InterPro; IPR022093; Rad26-like_helical.
DR InterPro; IPR048380; Rad26-like_N.
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; PF21046; Rad26-like_C; 1.
DR Pfam; PF12331; Rad26-like_helical_rpts; 1.
DR Pfam; PF21048; Rad26-like_N; 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.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000073492};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 415..460
FT /note="Rad26-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21048"
FT DOMAIN 518..746
FT /note="Rad26-like helical repeats"
FT /evidence="ECO:0000259|Pfam:PF12331"
FT DOMAIN 754..815
FT /note="Rad26-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21046"
FT DOMAIN 910..1018
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 1107..1221
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 1306..1385
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 25..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..110
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..884
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1478 AA; 164031 MW; 171A417BB0683B10 CRC64;
MAEEDFFSDD DLDDIPANTL DRLEQQAFRS TQHFNANPQI PRHVQQQQPP QSSRPPVPLR
KQAHTASSLN RPGSAKNLPW RPPQSTFGRA SQKPPQPQIP SAPPASAPRP PSSDYGFDDE
DVIDLDEPST IIQPAPQIQS HRPSYQSRPA QRNGGRASAA LDPETAAAFA AADEELGSQT
FGRWPQVVIP QRPKATPAGA SMEMAALQAR IAELEAEQAR LRASEQQARD EARAKQGEIA
IVRSNQEKTT KQYEARISVM QRLHAEDAAK AKAELEAQRK EREKMETDNR FLQHDLAQEA
ERTKRLTGPS RAKSTQRETP RKSKRAALGD GFDDGELHMT TSPSRSRDKS RSDLTPKVGA
KRKRPAHDSP VHSLSFTQAP AQLRHESTEG QSAASFASNA APERVTAKKD GRYEFMQLLL
NHFPHEGHAT TVESLAKYSF PSKPTKTLSS IFMHDISYLS DDASLPLKVA EVCIGLWSKC
LADKYFAPFY LILELVRFAL QTQSSAARCQ LLEQAVPLCV QTIELIAIPT YRAWTNRKFA
ASLDRKAFDE QADEIDVERV LEFLQDLCDA ASLQGERIEM FWRTMEQQFV LLMLNKAQPI
GQVMTLLEML QTAALEATFG VVAQDATRQA ELERGMIDRL TNLLFEVLEA AQGEEAYGDG
ETLELRIEVL KVFRQMCQTD HGGMLLVQNR SAIGRLVRFL DAHVRKLYHT RPRYGLSGEG
KNDKSATHDL LAQCVNMTVR LIYHLLRAYG DSFDFVHKLH AVHGGYHKFL VGMTRIAFTE
QHMFEAGMED EAAEAAHRIL DSVLGPEDGE AVMKAIETPR GTRGRGSTGD TTMTMLSREL
GSSRDPQKLP YWANATVEPR SSTRSMGKEP SASRVHEKRI THGTRRHEQH ARARIATAPI
PPMAIAGSIT LAEYLFARLK QLGCQSLHGL PGDFNLTLLD HVESSGLNWV GNCNELNAGY
AADAYARIHG LGAICTTFGV GELSAVNAIA GSYAERVPVV HIVGTPSRTS QKNAALLHHT
LGNGDFRVFA RIHKEITIAQ ADLVDLATAP AEIDRVLRTC YVDSQPVYLQ IPMDMVHAKV
DATQLNAAID VSPHPSNKEA EDLALEIVLE KLYAARRPVF LVDGAAQRRR ILSAVHALIA
KAQLPVFTAP MAKGAVDEDL PNFVGVYSGA GSDPEVAQAL ESSDLIITIG TIQSDLNTVG
FTYQFSKLNK IDIEYDCVQV GYATRFEQVF FKSFIPRLEQ LLDPSKLSHE SKMIPRISPP
TPIDTNSETI IHTYLWPQLA SFLRDGDFLI TDTGTSIVGV WETRLPRNCM IINQILWSSI
GYGVGAAQGA ALAAKELGKG QRVICFEGDG SFQLTAQELS TIIRHDLDVT MFVIENDGYE
IERWIHGWDA SYNDIPQWQY SKLPEVLTLP SSKHKVRTWK ISTRSELEQL LKDPHFADGK
GLQLVEMHMP RGDAPKTLRD FAERRNGVSA TKAFTVIE
//
