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
//