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Database: UniProt
Entry: A0A0D2AQD6_9EURO
LinkDB: A0A0D2AQD6_9EURO
Original site: A0A0D2AQD6_9EURO 
ID   A0A0D2AQD6_9EURO        Unreviewed;       761 AA.
AC   A0A0D2AQD6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV06_05741 {ECO:0000313|EMBL:KIW42161.1};
OS   Exophiala oligosperma.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW42161.1, ECO:0000313|Proteomes:UP000053342};
RN   [1] {ECO:0000313|EMBL:KIW42161.1, ECO:0000313|Proteomes:UP000053342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW42161.1,
RC   ECO:0000313|Proteomes:UP000053342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN847336; KIW42161.1; -; Genomic_DNA.
DR   RefSeq; XP_016262377.1; XM_016406773.1.
DR   AlphaFoldDB; A0A0D2AQD6; -.
DR   STRING; 215243.A0A0D2AQD6; -.
DR   GeneID; 27357815; -.
DR   VEuPathDB; FungiDB:PV06_05741; -.
DR   HOGENOM; CLU_021479_0_0_1; -.
DR   OrthoDB; 2727909at2759; -.
DR   Proteomes; UP000053342; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   PANTHER; PTHR21708; PROBABLE 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR   PANTHER; PTHR21708:SF25; PROTEIN PAM1-RELATED; 1.
DR   Pfam; PF02558; ApbA; 1.
DR   Pfam; PF08546; ApbA_C; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053342}.
FT   DOMAIN          10..165
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          199..322
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   REGION          334..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          598..761
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..352
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..407
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        648..666
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        679..693
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        721..761
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   761 AA;  82353 MW;  B31EB4FBD8F6F740 CRC64;
     MAPAPPRLRI LSVGGNAVSA FLSWRLQATN ACDVTLVWKA NYQSVAQYGV SFKSQMFGNE
     RFKPRYVVQT PEDAAGQQTA FDYVILCVKA LPDVYNLADI IQSVVTPQHT CILVNTTNTL
     GVERQLEERF PTNVVLSLVS GADLVQLGSS EFEHRGSTEI WVGPSSQNSA IPEAIQRDMS
     EALAMTLNTA QVDCKVSSNI KQQQYERMVG PIAFHPASVL FETSNLAELL QMPGVHELIS
     DVIEELLSVA SAQNCIFPTD FKETTISSMI NSSQEPSTMY QDFSARRPME VETYLGAPVQ
     LAQAAGVKVP RIQTLYALLR HLNTVNKDRP VNAMASTAPL QSPVTAVQPP PRTISLSSPP
     PPRPPNGSFG GPPRIARGPP PMGPPVRRGP PPTNGFRGPP NSFPHRPGPM QRRPSYDENN
     LDEFSHVVLY DEMANNGDGP PEGYAENGGG PSLRERELML RERELQMKQH EMAMRRGAGG
     NGRRTSQNRH QDFDDDDDDD DYFDPMLARG PPPPSIDPDN FDMMSVTSRR TKRAPSQSQL
     RKDAFVNGAA MRPGSYGRPN MGRHRTSASI LSDMPVLGAN ILDNPMMGFS SNRYGNVDRK
     EMADESRANS LTASRLQEIG MISGPGMNGG PYPGPPSRRT SRSPGNPFGP PGRMPGGRPS
     PPNDPYMQPG GSRNGRPSPP GGMPAPMPRY PPGQSSMVPQ QVEQTGINKP FPPPKGPVKS
     LTGSASASAG SGDSGSANIE SEPSAHSSTS SFAQRQMLGA H
//
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