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Database: UniProt
Entry: A0A1Y2UDV5_9PEZI
LinkDB: A0A1Y2UDV5_9PEZI
Original site: A0A1Y2UDV5_9PEZI 
ID   A0A1Y2UDV5_9PEZI        Unreviewed;       774 AA.
AC   A0A1Y2UDV5;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   13-SEP-2023, entry version 18.
DE   RecName: Full=Ketopantoate reductase C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=M434DRAFT_85510 {ECO:0000313|EMBL:OTA81434.1};
OS   Hypoxylon sp. CO27-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX   NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA81434.1, ECO:0000313|Proteomes:UP000194361};
RN   [1] {ECO:0000313|EMBL:OTA81434.1, ECO:0000313|Proteomes:UP000194361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO27-5 {ECO:0000313|EMBL:OTA81434.1,
RC   ECO:0000313|Proteomes:UP000194361};
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; KZ112641; OTA81434.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2UDV5; -.
DR   STRING; 1001938.A0A1Y2UDV5; -.
DR   Proteomes; UP000194361; 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:UP000194361}.
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          481..774
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        355..375
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..411
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        544..558
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        607..643
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        652..666
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        679..700
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        711..767
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   774 AA;  82764 MW;  FF7649F4C6A0AB08 CRC64;
     MAPVAPRLKI LSVGGNAVSA FLSWRLQATN ACDVTLVWKS GFEAVYQYGI SFKSATFGNE
     RFKPRRVVRT PEDAANNKDG AFDYVILCIK ALPDVYDLAS VIDAVVTPQH TCILVNTTHT
     LGVEDALEER FPTNVVLSLV SNAELNQLGS SEFEHSGSTE IWVGPANKSG KIPAAIQEDM
     AQALAMTLTS GRVDCKVSTN IRQQQFERVI GPIAFHPASV IFETPSHSAL LEKTGVRQLI
     SDVIDELIQL ASAQGCTLDA KFKENTIKEQ CEPSDSPSIM WQDYVARRPM EVETFLGSPI
     KLAQSSGVKL PRIETLYAIL HNLNIVNQSR PKEINGLPAA SGSPTAASPM PRMSSSGQPP
     RPPVNGHPNG NGMPMPRPRP RNSSNFSGPP PGMRRPPPMN GGGPPNGYRP PTNGAPNGHP
     SRQPSRRGSF DETDLGEFSH LVVYDDPADA GDGGYNADTS DIALRERELQ LRQRELALKE
     QEMRMRRGGP PGPGPGPGPV ARRRAPPVRN GGGMYDDEDE EDDYFDPNSG PITPMIDPDN
     FDMMSVTSRK NRSKAPPSQS ELRMHPEGPG QGGPSRGSRW RPGFGRNRSS QIISAAPGLH
     DNILDDPLMS FTSNRYGNVD RGQMQAGSRA NSLTASHLHE LSNGPNGMSG PFPRRASQSP
     GNPYSPSIRG GNGRPSPPNG FGGPGPNGRP SPPDGVRQPV PRYPPGQGNM VAPQQVEQRV
     GVSSLQPPNA KTARSLTGSA SASAGSGDST NLGSEPSAHS SSSSLGPRPP IGVR
//
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