ID A0A0D2E8I6_9EURO Unreviewed; 759 AA.
AC A0A0D2E8I6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 02-APR-2025, entry version 32.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV05_10429 {ECO:0000313|EMBL:KIW51743.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW51743.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW51743.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW51743.1,
RC ECO:0000313|Proteomes:UP000054342};
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 xenobiotica CBS118157.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN847322; KIW51743.1; -; Genomic_DNA.
DR RefSeq; XP_013312327.1; XM_013456873.1.
DR AlphaFoldDB; A0A0D2E8I6; -.
DR STRING; 348802.A0A0D2E8I6; -.
DR GeneID; 25332337; -.
DR HOGENOM; CLU_021479_0_0_1; -.
DR OrthoDB; 5302359at2759; -.
DR Proteomes; UP000054342; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR FunFam; 1.10.1040.10:FF:000017; 2-dehydropantoate 2-reductase; 1.
DR FunFam; 3.40.50.720:FF:000424; Meiotically up-regulated gene 72 protein; 1.
DR Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
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; IPR051402; KPR-Related.
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:UP000054342}.
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 337..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..349
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..366
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..396
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..502
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..630
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..689
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..749
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 759 AA; 82244 MW; 159E75D8B49068B9 CRC64;
MAPAPPRLRI LSVGGNAVSA FLSWRLQATN ACDVTLVWKA NYQTVAQYGV SFKSQMFGNE
RFKPRYVVQT PEDAAGQQTA FDYVILCVKA LPDVYNLADI IQSVVTPQHT CILVNTTNTL
GVEKPLEERF PTNVVLSLVS GADLVQLGSS EFEHRGSTEI WVGPSSQNST IPESIQRDMS
EALAMTLTTA QVDCQVSSNI KQQQFERMIG PIAFYPASVL FETSNLGDLI RIPGVHDLLS
DVIEELLSVA HAQGCTFPNN FTETTISTMI DSSQEASTMY QDFTARRPME VETYLGSPVQ
LAKSAGVKVP RLQTLYTMLR HVNTVNKDRP IASAVSAAPV QAPVQSPVAV QPPPRTISLS
SPPPPRQTNG SLNGPLRPMR GPPPMGPPGR RGPPPVNGFR GPPNMYPQRP GQMQRRPSYD
ENNLDEFSHV VLYDEMADGE GPPAGYGENG GGPSMREREL MLREREIQLK QQEMAMRSRG
GRRPTHIRHQ DLDDDDDDDD YFDPMQARGP PPPSIDPDNF DMMSVTSRRT KRAPSQGQLR
KDAFANGGGM RPGSYGRPNM GRHRTSASIL SDMPMLGANI LDNPMMGFSS NRYGNVDRKE
MADESRANSL TASRLQEIGL NGGPGMTGGP YPGPPSRRTS RSPGNPFGPA GRMPGRPSPP
NDPYMQSGPP RNGRPSPPGA MPAPVPRYPP GQTNMIPQQV EQAGMNKPFP PPKPPVKSLT
GSASASAGSG DSGSANIESE PSAHSSTSSF AQRQMLGAH
//
