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Database: UniProt
Entry: D4AQP8_ARTBC
LinkDB: D4AQP8_ARTBC
Original site: D4AQP8_ARTBC 
ID   D4AQP8_ARTBC            Unreviewed;       608 AA.
AC   D4AQP8;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00014422};
DE            EC=4.1.1.1 {ECO:0000256|ARBA:ARBA00013202};
GN   ORFNames=ARB_06558 {ECO:0000313|EMBL:EFE34792.1};
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE34792.1, ECO:0000313|Proteomes:UP000008866};
RN   [1] {ECO:0000313|Proteomes:UP000008866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
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}.
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:EFE34792.1}.
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DR   EMBL; ABSU01000005; EFE34792.1; -; Genomic_DNA.
DR   RefSeq; XP_003015432.1; XM_003015386.1.
DR   AlphaFoldDB; D4AQP8; -.
DR   STRING; 663331.D4AQP8; -.
DR   GeneID; 9521159; -.
DR   KEGG; abe:ARB_06558; -.
DR   eggNOG; KOG1185; Eukaryota.
DR   HOGENOM; CLU_013748_3_3_1; -.
DR   OMA; DIGSHYI; -.
DR   OrthoDB; 2020042at2759; -.
DR   Proteomes; UP000008866; 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:UP000008866};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          5..119
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          196..324
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          401..580
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   608 AA;  64901 MW;  BC53FCB3FEC6C577 CRC64;
     MSQPTGAQAV ARALKNLGVT VIFGLVGIPV IEIAEEAINL GIRFIAFRNE QACSYAASAY
     GYITGKPGVC LVVGGPGVLH AMAGIGNSNV NAFPMLILAG SAETTLVTKG GFQEMDAISL
     LTPHTKLAVR PISVDYAESA VYDAYRTCWY GRPGTAFVDL PADLIQGKAT GSLPSAGLQL
     VHAPPKPAGD PSIIFKVAQL LRAARAPLVV VGKGSAYARA EESIRKLIDT ARLPFLPTPM
     GKGVVPDSHP LNTSSARSVA LKNADVVLLL GGRLNWILHF GEAPRWSPDV KIIQVDIHAE
     EIGRNSGSGE LGIVGDIELV VDQLLKSLGD WHYQPPNSPS SYPSLISASA TKNENKSQEK
     ALQATAAGQY LTFQRAFHII KTTLNSLSPP ENGGIVYISE GANTMDISRS AFPLQHPRQR
     LDAGTYATMG VGLGYIIAAH AAYNLPQPQG TLEAPLPKKI VALEGDSAFG FSAMEVETLA
     RHQIPALIFV MNNSGIYHGD TKTEDDWRNM QQATLLNETT SSSAGDKKGL RSTSLSYETR
     YDRLASVCGG QGFFVRNEKE LEDATRAGFL EKHKFTIVNV IVEPGIGQSI EFGWQAGKKD
     KTAQASKL
//
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