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Database: UniProt
Entry: A0A1Y2W1B7_9PEZI
LinkDB: A0A1Y2W1B7_9PEZI
Original site: A0A1Y2W1B7_9PEZI 
ID   A0A1Y2W1B7_9PEZI        Unreviewed;       771 AA.
AC   A0A1Y2W1B7;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Ketopantoate reductase C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=M426DRAFT_61482 {ECO:0000313|EMBL:OTB02911.1};
OS   Hypoxylon sp. CI-4A.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX   NCBI_TaxID=1001833 {ECO:0000313|EMBL:OTB02911.1, ECO:0000313|Proteomes:UP000242955};
RN   [1] {ECO:0000313|EMBL:OTB02911.1, ECO:0000313|Proteomes:UP000242955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CI-4A {ECO:0000313|EMBL:OTB02911.1,
RC   ECO:0000313|Proteomes:UP000242955};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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DR   EMBL; KZ111564; OTB02911.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2W1B7; -.
DR   STRING; 1001833.A0A1Y2W1B7; -.
DR   InParanoid; A0A1Y2W1B7; -.
DR   OrthoDB; 2727909at2759; -.
DR   Proteomes; UP000242955; 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:UP000242955}.
FT   DOMAIN          10..167
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          200..323
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   REGION          334..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          478..771
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..353
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..387
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..410
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        539..562
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        603..639
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        648..662
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        676..697
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        708..764
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   771 AA;  83082 MW;  8693BE96B5F55FF4 CRC64;
     MAPVAPRLKI LSVGGNAVSA FLSWRLQATN ACDVTLVWKS GFEAVHQYGI SFKSASFGNE
     RFKPRRVVRT PEEAAQSKEG AFDYVILCIK ALPDVYDLAS VIDAVVVPQH TCILVNTTHT
     LGVEAALEER FPTNVVLSLV SNAELNQLGS SEFEHSGSTE IWVGPANKKS SIPNAIQEDM
     AQALAMTLST GRVDCKVSSN IRQQQFERVI GPIAFHPASV IFDTPLHSAL LEKTGVRQLI
     SDVIDELIEL ATAQGCQLDA KFKENTIKEQ CEPSDSPSIM WQDYMARRPM EIETFLGSPI
     KLAQSSGVKV PRIETLYAIF HNLNIVNQSR PKEMNGLPAA SGSPTTASPM PRMSSAQPLR
     PVNGHPNGNS MSMPRPRPRN SSNFSGPPPG MRRPGPPPMN GGPPNGYRPP MNGAPNGHGP
     SRQPSRRGSF EDTDLGEFSH LVVYEDSADA GEGGYSADTS DMALREREMQ LRQRELALKE
     QEMRMRRGGP PPAGGRRRMP PPVRNGGGAY DDEEEEDDYF DPNSGPITPM VDPDNFDMMS
     VTSRKNRSKA PQSQSEIRMN PEGSNGPTAP RGGRWRPGFG SRNRSSQIMN SAPGLHDNIL
     DDPMMSFTSN RYGNVDRGQM HAGSRANSLT ASHLHELQSG PNGMSGPYPR RASQSPGQPY
     SPSIRGGGNG RPSPPNGFGG PGPNGRPSPP DGVRQPVPRY PPGQGNMVAP QQVEQRVGVS
     TLQPPNTKTA RSLTGSASAS AESGESTHLG SEPSAHSSQS SLGPRPPIGV R
//
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