ID W3WXB6_PESFW Unreviewed; 759 AA.
AC W3WXB6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Ketopantoate reductase C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PFICI_10557 {ECO:0000313|EMBL:ETS78495.1};
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS78495.1, ECO:0000313|Proteomes:UP000030651};
RN [1] {ECO:0000313|Proteomes:UP000030651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
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DR EMBL; KI912115; ETS78495.1; -; Genomic_DNA.
DR RefSeq; XP_007837329.1; XM_007839138.1.
DR AlphaFoldDB; W3WXB6; -.
DR GeneID; 19275570; -.
DR KEGG; pfy:PFICI_10557; -.
DR eggNOG; ENOG502QT3Z; Eukaryota.
DR HOGENOM; CLU_021479_0_0_1; -.
DR InParanoid; W3WXB6; -.
DR OMA; SFKSKAF; -.
DR OrthoDB; 2727909at2759; -.
DR Proteomes; UP000030651; 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:UP000030651}.
FT DOMAIN 9..166
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 199..321
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 328..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..352
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..685
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 759 AA; 81777 MW; 787566337670596F CRC64;
MADVELIRVC TVGGNAVSAF LSWRLQATNA CDVTLVWKTG FEAVHQYGIS FKSASFGNER
FKPRHVVRAP EEAGSTKDGP FDYVILCVKA LPDVYDLASV IDSVVTPQHT CILINTTATL
GIEALIEERY PTNVVLSLVS NAEITQIGTS EFEHKGSTEV WVGPANKNSN IPSAIQEDMA
QALAMTLSTG RVDCKVSSNI RQQQFERVIG PIAFHPASVI FETSSHTALL EKTGVRQLVS
DIIDELIELA KTQGCTLSAD FKENTIKEQC QTQESSIMWQ DYVARRPMEV ETYLGSPIKL
AKAANISLPR IETLYAVFHH LNVVNQSRPK EMNGVPPPHG SPSGPMPGPR MSSNGPPRSV
SNGIPNGMGR ARPRNSSNFS GPPPGMRRPP PGGPNGFRGP SGQYGPQSRQ PSRRGSMEET
DLGEFSHLVL YDDIPEGGDG GFPLDNGGDL DIRERELQLR QREMALKEQE MRMRRNGPPG
PRRRPPPRTA GGVYDDDDDE EGDYFDPDAL VTPSVDPDKV DMMSMTSRKN RIKAPSQSQI
RNDPEMGAAS GAPPARNSRW GRPSFGSRNR SSQIMNNSVP NLHSNIMDDP LLGYSSNRYG
NVDRGQMHHA ASSRANSLTA QHLDQLNGPG GMGGPYPRRA SQSPGNPYSP SIRGGNGRPS
PPNGFAGPGG PQGRPSPPNG MRQPVPRYPP GQGNSVAPQQ VEQRVGVSSL QPPRAKNVRS
LTGSASASAG SGDSTNTESE PSAHSSQSSL GPQVAIGVQ
//
