ID A0A0D2L3A8_9EURO Unreviewed; 630 AA.
AC A0A0D2L3A8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00014422};
DE EC=4.1.1.1 {ECO:0000256|ARBA:ARBA00013202};
GN ORFNames=Z520_00235 {ECO:0000313|EMBL:KIY03544.1};
OS Fonsecaea multimorphosa CBS 102226.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIY03544.1, ECO:0000313|Proteomes:UP000053411};
RN [1] {ECO:0000313|EMBL:KIY03544.1, ECO:0000313|Proteomes:UP000053411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 102226 {ECO:0000313|EMBL:KIY03544.1,
RC ECO:0000313|Proteomes:UP000053411};
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 Fonsecaea multimorphosa CBS 102226.";
RL Submitted (JAN-2015) 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=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}.
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DR EMBL; KN848062; KIY03544.1; -; Genomic_DNA.
DR RefSeq; XP_016637666.1; XM_016770756.1.
DR AlphaFoldDB; A0A0D2L3A8; -.
DR STRING; 1442371.A0A0D2L3A8; -.
DR GeneID; 27705981; -.
DR VEuPathDB; FungiDB:Z520_00235; -.
DR OrthoDB; 2020042at2759; -.
DR Proteomes; UP000053411; 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; cd02004; TPP_BZL_OCoD_HPCL; 1.
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; IPR045025; HACL1-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 PANTHER; PTHR43710; 2-HYDROXYACYL-COA LYASE; 1.
DR PANTHER; PTHR43710:SF2; 2-HYDROXYACYL-COA LYASE 1; 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 Reference proteome {ECO:0000313|Proteomes:UP000053411};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 202..332
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 421..600
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 630 AA; 67085 MW; 27BEE43124BC3D26 CRC64;
MDPPPTGAKV IAQALHDLGI PVIHTLVGIP VAEIAEEAID LGIRVIGYRN EQACSYAASV
YGYLTGKPGV CLLTGGPGIL HGMAGIGNAS ANAFPLLVLG GSSESSLATK GGFQEMDAIA
LLTPHTKRAI RPTSRDPATI VAAIRNAYRI AWYGRPGPCF VDLPTELIME PTVPARRSTS
HHPPITVLSP PKPSPDPALI VAAADLLKSA SAPLVIVGKG AAYARAESSI RSLVSTHHLP
FLPTPMGKGV VPDAHPLNTS AARSAALKHA DVILLLGARL NWILHFGEAP KYRPDVKIIQ
VDISAEELGR ANSLGQPSLS IFGDIGLVVD QLCQQLGMGW KAFSRDTFRS SSPSPSSSKP
SYFSVLAASA AKNEQKSVRL ATTPTKPNAL LTYERAYHII KSQLHALSPP QDGGVVYVSE
GANTMDISRS VFPLEHPRQR LDAGTYATMG VGMGYAIAAW AAYNIPHRAA KKIVALEGDS
AFGFSGMEIE TMARHKMDVL IIVMNNSGIY KGDAADETGW KEKQAQTASD DTKIVTVPRE
GKQIDGRRGL RSTSLLYETR YECLADMVGG RGWLVRTEDE LAEATRQAFL ETEKVCVLNV
IIDPGLNSAA SFGWMETKEK HGGGGGESKL
//