ID A0A2C5XIP7_9HYPO Unreviewed; 729 AA.
AC A0A2C5XIP7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 13-SEP-2023, entry version 15.
DE RecName: Full=Ketopantoate reductase C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CDD81_5061 {ECO:0000313|EMBL:PHH64068.1};
OS Ophiocordyceps australis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=1399860 {ECO:0000313|EMBL:PHH64068.1, ECO:0000313|Proteomes:UP000226192};
RN [1] {ECO:0000313|EMBL:PHH64068.1, ECO:0000313|Proteomes:UP000226192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Map64 {ECO:0000313|EMBL:PHH64068.1,
RC ECO:0000313|Proteomes:UP000226192};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PHH64068.1}.
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DR EMBL; NJET01000037; PHH64068.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5XIP7; -.
DR STRING; 1399860.A0A2C5XIP7; -.
DR OrthoDB; 2727909at2759; -.
DR Proteomes; UP000226192; 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:UP000226192}.
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 325..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..355
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..429
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..704
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 729 AA; 79441 MW; 47FB2C0CC7A5C2E4 CRC64;
MAPMTPRLKI LSVGGNPVSA FLSWRLQATN ACDVTLVWKS GYEHVAQYGI SFKSPIFGNE
RFKPRHVVRN PEDASSSRDG PFDYVVLCVK ALPDVYDLAS VIDAVVTPQH TCILINTTHT
LGVEAAIEER FPTNVVLSLV SGAELTQLGQ SEFEHKGSSE IWVGPANRNS NIPQSIQEDM
AQALAMTLST GQVECKVSPN IRQQQYDRVI GPIAFHPISV LFETPNHAAL LEKIGVKDMI
SEVIDELLRL AAANGCEFPS GFKQKTIDDM TKPNLPESIM WQDYVARRPM EVETYLGSPI
KLARDSKVSL PRIETLYAIL HNINTNNRNR PKPGEGLPPP GILAPGSPVV PSPMPRIPSQ
QSHRPIMSGM PNGIPNGIPN GMPNGNGMPP RQPRPRNSSN FGPPGGMRRP PPMNGPGPNG
FPRPPPSVNG GSRAPSRRGS MDGNDLEEFS HLVLYDDIPE GHEPVVSGES DLALRERELQ
LRQRELALRE QEMRLRRGPP PGPMSRRGPH PMRHSHQAFD DDDDDDDLLD PTAITGIPTI
DPDNFDMMSV TSRKNRKAAP TAAQFRRNPE FDAPAPSRGS RFRPSFGRNR ASQLSQVPSM
TDNILEDPMM GFTSNRYATV DRGAMGAGSR ANSLTASRLD ELQYGPGPGG MPGMNGALPR
RASQSPGNPY SPSLRGGGRP SPPNGYGPPM NGRPSPPDGV RQPVPRYPPG HGNSVAPQQV
EQHVGRGQW
//