ID A0A136IYK5_9PEZI Unreviewed; 573 AA.
AC A0A136IYK5;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00014422};
DE EC=4.1.1.1 {ECO:0000256|ARBA:ARBA00013202};
GN ORFNames=Micbo1qcDRAFT_184170 {ECO:0000313|EMBL:KXJ90065.1};
OS Microdochium bolleyi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ90065.1, ECO:0000313|Proteomes:UP000070501};
RN [1] {ECO:0000313|Proteomes:UP000070501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J235TASD1 {ECO:0000313|Proteomes:UP000070501};
RG DOE Joint Genome Institute;
RA David A.S., May G., Haridas S., Lim J., Wang M., Labutti K., Lipzen A.,
RA Barry K., Grigoriev I.V.;
RT "Draft genome sequence of Microdochium bolleyi, a fungal endophyte of
RT beachgrass.";
RL Submitted (FEB-2016) 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 -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; KQ964253; KXJ90065.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136IYK5; -.
DR STRING; 196109.A0A136IYK5; -.
DR InParanoid; A0A136IYK5; -.
DR OrthoDB; 2291769at2759; -.
DR Proteomes; UP000070501; 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; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF164; PYRUVATE DECARBOXYLASE; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000070501};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 19..107
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 180..310
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 387..558
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 573 AA; 61184 MW; 01DD5559C16C3F06 CRC64;
MEALAGETRR STGGPSKFPK VITVPHEFVA LSMADGFARL TGKPQCVLVH VDVGTQGLGC
AMHNSSIARS PVLVFAGLSP YTLEGELRGS RTEYIHWLQD VPDQKAIVAQ YCRFAGEFKT
GKNVKQMVNR ALQLATSDPK GPAYLMGARE VMEEEIDEYD IDQEVWHGIE PAGLSPAGVE
NIVSTLVQAE RPVIIVGYTG RNHATVPLLV QLANAVPGVR VIDALGSDLC FPFSHRAYIG
VRIGKHAAIS AADAILVIDC DVPWIPTQCP LAKGVKIIEV GVDPLKQNMP LHYIPASHRY
KADAGVALQQ LNDFLSSKHP ALVQQEPYAA RWAALEQTRA EEIAAADRLA APPSSPDTDA
ASTSYLCSQL RKTCPDNTIW CIEAVSNAMF VYDQLRVDKP GHLVNGGGGG LGWSGGGTLG
VKLASDYLAN GESQIGAEGK GSFVCEIVGD GTYLFGVPST VYWVARRYKL PTLTIVLSNK
GWNAPRISME LVHPKGHGSQ VSNEDLNISF SPTPDFSGIA KSASGNTAYS AVVRTASDLL
RVLPEAVAAV QSGVSAIIEA RVHGSSPWKG DEA
//