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
//