ID T5AHC1_OPHSC Unreviewed; 519 AA.
AC T5AHC1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Ketopantoate reductase ApbA/PanE {ECO:0000313|EMBL:EQL01994.1};
GN ORFNames=OCS_02297 {ECO:0000313|EMBL:EQL01994.1};
OS Ophiocordyceps sinensis (strain Co18 / CGMCC 3.14243) (Yarsagumba
OS caterpillar fungus) (Hirsutella sinensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=911162 {ECO:0000313|EMBL:EQL01994.1, ECO:0000313|Proteomes:UP000019374};
RN [1] {ECO:0000313|EMBL:EQL01994.1, ECO:0000313|Proteomes:UP000019374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Co18 / CGMCC 3.14243 {ECO:0000313|Proteomes:UP000019374};
RC TISSUE=Fruit-body {ECO:0000313|EMBL:EQL01994.1};
RX DOI=10.1007/s11434-013-5929-5;
RA Hu X., Zhang Y., Xiao G., Zheng P., Xia Y., Zhang X., St Leger R.J.,
RA Liu X., Wang C.;
RT "Genome survey uncovers the secrets of sex and lifestyle in caterpillar
RT fungus.";
RL Chin. Sci. Bull. 58:2846-2854(2013).
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DR EMBL; KE652378; EQL01994.1; -; Genomic_DNA.
DR AlphaFoldDB; T5AHC1; -.
DR eggNOG; ENOG502QT3Z; Eukaryota.
DR HOGENOM; CLU_021479_0_0_1; -.
DR Proteomes; UP000019374; 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:UP000019374}.
FT DOMAIN 4..158
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 191..314
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 317..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..340
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..412
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 519 AA; 57479 MW; A5245A40BD51ADE8 CRC64;
MDDIGGNPVS AFLSWRLQAS HACDVTLVWK SGFEHVAQYG ISFKSPIFGN ERFKPRHVVR
NPEDAANSRD GPFDYVVLCV KALPDVYDLA AVIDAVVTPQ HTCILINTTH TLGVEAAIEE
RFPTNVVLSL VSGAELTQLG QSEFEHKGST EIWVGPANKN SNISQSIQED MAQALAMTLS
TGQVDCKVSP NIRQQQYERV IGPIAFHPIS VLLETPNHAA LFEKVGVKDM ISDVIDELLR
LAGANGCKFS PDFKQRIMDD MTKPNMPESI MWQDFVARRP MEVETYLGSP LKLARDSQVS
LPRIETLYAI LHNINTVNRN RPKPGDGPQQ QPPPSSMPPG TPTLAAAAPR MPSQQGHRPM
MGGMPNGNGM PPRQPRPRNS ANFAPGGMRR APPMNGPPPN GYPRPPPSMN GGPRAPSRRN
SMDGNDLEEF SHLVLYDDIP EGQEPSIGGE DLGLREREMQ LRQREVALRE HEMRMRRGPP
PGSRRGAPPS IRNQPQSFDD DDDDDEFFRS QCGHWRPDH
//