(data stored in SCRATCH zone)

SWISSPROT: Q4W928_ASPFU

ID   Q4W928_ASPFU            Unreviewed;       575 AA.
AC   Q4W928;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 80.
DE   SubName: Full=Pyruvate decarboxylase, putative {ECO:0000313|EMBL:EAL84191.1};
DE            EC=4.1.1.1 {ECO:0000313|EMBL:EAL84191.1};
GN   ORFNames=AFUA_6G00750 {ECO:0000313|EMBL:EAL84191.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL84191.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL84191.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR036565-2};
CC       Note=Binds 1 Mg(2+) per subunit. {ECO:0000256|PIRSR:PIRSR036565-2};
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {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:EAL84191.1}.
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DR   EMBL; AAHF01000018; EAL84191.1; -; Genomic_DNA.
DR   RefSeq; XP_731481.1; XM_726388.1.
DR   STRING; 746128.CADAFUBP00009400; -.
DR   EnsemblFungi; EAL84191; EAL84191; AFUA_6G00750.
DR   GeneID; 3503697; -.
DR   KEGG; afm:AFUA_6G00750; -.
DR   EuPathDB; FungiDB:Afu6g00750; -.
DR   HOGENOM; HOG000061334; -.
DR   InParanoid; Q4W928; -.
DR   KO; K01568; -.
DR   OMA; DVARWRY; -.
DR   OrthoDB; 560466at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
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   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; IPR012110; TPP_enzyme.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   PIRSF; PIRSF036565; Pyruvt_ip_decrb; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
PE   3: Inferred from homology;
DR   PRODOM; Q4W928.
DR   SWISS-2DPAGE; Q4W928.
KW   Lyase {ECO:0000313|EMBL:EAL84191.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR036565-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR036565-2};
KW   Pyruvate {ECO:0000313|EMBL:EAL84191.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          8..173
FT                   /note="TPP_enzyme_N"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          203..322
FT                   /note="TPP_enzyme_M"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          400..485
FT                   /note="TPP_enzyme_C"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   METAL           450
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   METAL           477
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   METAL           479
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ   SEQUENCE   575 AA;  64123 MW;  4BD70F7A5639F5CE CRC64;
     MDSDTLPLAQ YLFKRLRQLG VDSIFGVPGD YNLTLLDHVV PSGLKWVGNC NELNAGYAAD
     GYSRIKGIGA LVTTFGVGEL SAVNAIAGAY AERAPVVHIV GTPMRASQES RAMIHHTFID
     GEYQRFDRMQ EHVTVAQVSL SDHRTAPAEI DRILLQCLLH SRPVRITIPV DMVPVLVPTA
     GLASKIEIPP PVRQPQVEEA ALTAVLERIY NAKKPMILVD GETRAFGTVN EVNQFVTTTG
     WPTFTSGFGK GLVDETLPNV YGVYRPAHKE FVDSCDLVLA FGPHFSNTNT YIFMVRPQDE
     TSVLFNPTSV QVNKDIYRDL PAKYFIQQLT QRLDPSKIPV HQHNLVHPSA QVLPEVPPTD
     LVTQTAGFWR RLSPFFRSGD IVLGETGTPG YGANDFVLPP QTRLFKPVTW LSIGYMLPAT
     LGASYAQRDL IARNEYHNLS AARTILFIGD GSFQMTVQEL STIIHHKLDV IVFLINNDGY
     TIERCIHGRN QAYNDVARWR YLKAPELFGA DQEGEYASRT WEIRTWADCD AVLKDEQLVN
     GKGLRMVEVF MDKFDAPDVL MNLLNAQIAR DNAKK
//

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