ID W9IH95_FUSOX Unreviewed; 689 AA.
AC W9IH95;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00014422};
DE EC=4.1.1.1 {ECO:0000256|ARBA:ARBA00013202};
GN ORFNames=FOYG_05789 {ECO:0000313|EMBL:EWY92204.1};
OS Fusarium oxysporum NRRL 32931.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660029 {ECO:0000313|EMBL:EWY92204.1, ECO:0000313|Proteomes:UP000030753};
RN [1] {ECO:0000313|EMBL:EWY92204.1, ECO:0000313|Proteomes:UP000030753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL Submitted (JUN-2011) 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; JH717842; EWY92204.1; -; Genomic_DNA.
DR AlphaFoldDB; W9IH95; -.
DR HOGENOM; CLU_399573_0_0_1; -.
DR OrthoDB; 1000728at2759; -.
DR Proteomes; UP000030753; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
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 PANTHER; PTHR43452; PYRUVATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43452:SF11; PYRUVATE DECARBOXYLASE; 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 Pyruvate {ECO:0000313|EMBL:EWY92204.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030753};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 337..416
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 417..518
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 594..675
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 689 AA; 74691 MW; 9A3919701EC90399 CRC64;
MADPLSIASG VAGLVSLGLT LCNGLHNYLS AVKDRYSDIE TATQGLALLQ SNICIIQSST
LKLGHRHALA ANGVNLGLRN CETQLRALEN FVEDLATAPS LSGAKQKWQK QKMFIRYPFD
QKKLFQLQEQ LSKANSTLGS FVQSFNLDLN IGISDDLQVL KRDIHANDSV THATLRMISN
QLCSISSVGQ STNVGMTTSF TLVDDQPVAT NSALGQRDIQ PLYLRNSEAE KVICRKLSTM
ECACPNSTNG AVYSRSSHTL PNVVETAGSH LVAAPPTPIP ASSHDDAFTL AQRPAISYHG
AISRFSASYS GNTHASGIFG NGPFGIGTGA MLTTGQAAAC LFRRLYEAGA RAVHGVPGDY
NLTALDYLEP AGLAWIGNCN ELNAGYAADG YGRIKGIGAL IITLGVGELS AINAILFILV
DTGASRYSMV TEVNDLVKVT GFPTAMILFG KGVVDEILRN FYGVYGTVGD HVFVDWVKNC
NLVLYIRPCE NNVNTYYFKT IPEASKTIRF EKDSLQIGCA DGEHIRWALH PVGLLRQLPN
LPALLASLPR VQKTDPLLQD TFWKRIPEFF ESGDIIMTET GTPSTGGRDF VLPRQTTPIN
SGVWLSIGYM LGSSQGVALA QRDLVAEGSS RRGRTILFEG DRSFQMTAQE LSSIIHKRLD
MIIFLINNDG YTIERLVHGK DAIYNDVAP
//