ID S3C4J8_OPHP1 Unreviewed; 783 AA.
AC S3C4J8;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=2-dehydropantoate 2-reductase-like protein {ECO:0000313|EMBL:EPE08444.1};
GN ORFNames=F503_01227 {ECO:0000313|EMBL:EPE08444.1};
OS Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE08444.1, ECO:0000313|Proteomes:UP000016923};
RN [1] {ECO:0000313|EMBL:EPE08444.1, ECO:0000313|Proteomes:UP000016923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE08444.1,
RC ECO:0000313|Proteomes:UP000016923};
RX PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA Robertson G., Birol I., Bohlmann J., Breuil C.;
RT "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT a comparison with the bark beetle-associated pine pathogen Grosmannia
RT clavigera.";
RL BMC Genomics 14:373-373(2013).
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DR EMBL; KE148149; EPE08444.1; -; Genomic_DNA.
DR AlphaFoldDB; S3C4J8; -.
DR STRING; 1262450.S3C4J8; -.
DR VEuPathDB; FungiDB:F503_01227; -.
DR eggNOG; ENOG502QT3Z; Eukaryota.
DR HOGENOM; CLU_021479_0_0_1; -.
DR OMA; RENAYDY; -.
DR OrthoDB; 2727909at2759; -.
DR Proteomes; UP000016923; 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:UP000016923}.
FT DOMAIN 12..167
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 201..324
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 331..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..683
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 783 AA; 84252 MW; E77C42E12A88AA8E CRC64;
MEGDFELMNV VSVGGNAVSA FLSWRLQATN ACDVTLVWKS GFEHVSQYGI SFKSPIFGNE
RFKPRHVVKS PEEAASRREG AYDYVILCIK ALPDVYDLAT IIDSVVTPQH TCILINTTHS
LGVEAAIEER FPTNVVLSLV SMAEVVQLGA SDFEHKGSAE IWVGPTNSLN DRIPQSIRED
MAQALAMTLT SGQVDCKVSS NIRQQQYERL IGPIAFHTTS VLFETPNHAQ LIEKVGVRQM
INGVLDELLA VAQSQGCTFP ADFKEQTITD MTKPQAAESV MWQDYTSRRP MEVETFLGSP
IRLAQEKGIA TPRIESLYAI LHNLNVVNQT RPKGDAMNRV PSSPAIMGNL PPRMSSQTNG
GPPNGVPNGM GGRPRMRNSS AGGPPGRRPP VSMNGGPPNG YGRPGPPNGH PSSRQQSRRG
SMEGTDLEEF SHLVLYDNIP EGGLATGPGP SQETELALRE RELQIRQREL ALREQEMRMR
RGGPPQGAPP PQRRGPPRAG VVDDEDEDDD FFDPNMAGPP NPMIDADNFD MMSVTSRKNR
KAANTNSGQF RKGSDLGAVP NSRNSRFRPF SRNRSSQLVD QLPSTHSNIL DDPMMAFTSN
RYANVDRSQM QAESRTNSLT ASRLDELQYN GAGPGPTGPM GPMAGMGGGA YPRRISQSPG
NPYGPGPRGV NGRPSPPNGY GGPPMNGAPM NGAPMNGRPS PPNGVRQPVP RYPPGQGNAV
APSQVEQHAG VSSLQPPMGK TVRSLTGSAS ASAGSGESTH LDSEPSANSS QSSLGPRQPI
GVR
//