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Database: UniProt
Entry: W9IH95_FUSOX
LinkDB: W9IH95_FUSOX
Original site: W9IH95_FUSOX 
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
//
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