ID A0A094BKG3_9PEZI Unreviewed; 704 AA.
AC A0A094BKG3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 13-SEP-2023, entry version 27.
DE RecName: Full=Ketopantoate reductase C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=V494_02488 {ECO:0000313|EMBL:KFY42271.1};
OS Pseudogymnoascus sp. VKM F-4513 (FW-928).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420907 {ECO:0000313|EMBL:KFY42271.1, ECO:0000313|Proteomes:UP000029288};
RN [1] {ECO:0000313|EMBL:KFY42271.1, ECO:0000313|Proteomes:UP000029288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4513 (FW-928) {ECO:0000313|Proteomes:UP000029288};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFY42271.1}.
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DR EMBL; JPJW01000863; KFY42271.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094BKG3; -.
DR STRING; 1420907.A0A094BKG3; -.
DR HOGENOM; CLU_021479_0_0_1; -.
DR OrthoDB; 2727909at2759; -.
DR Proteomes; UP000029288; 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:UP000029288}.
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 330..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..679
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 704 AA; 76532 MW; C5958ACD0AF78844 CRC64;
MAPTAPRLRI LSVGGNAVSA FLSWRLQATN ACDVTLVWKS GFDAVSQYGI SFKSSAFGNE
RFKPRHVVRT PEDAAAAKEG AFDYVLLCVK ALPDIYDLAA VIESVVTPQH TCILVNTTHT
LGVEAHLEQR FPTNVVLSLV SGAELTQLGV SEFEHKASTE VWVGAANKNA AIPASIQQDM
AEALAMTLST GQVDCKVSRN IRQQQYERMI GPIAFHPLSV LMETPSHATL LEKTAVEPMI
KDVMDELLRI AEAQGCTFPK DFKEKTVQDM VRPSESNSIM YQDFMARRPM EVETYLGSPI
KLAQSVGVKV PRIETLYALL HSVNIVNQQK PKEAPATPAV NGNGQFPTRL SSAPTPRPMN
GPNGAPNGMM NGMGRGRGRA PSMGPPPGMR RGGPMNGGPN GYGRPPPNGY GSRQQSRRGS
IDNDLADEFS HVVLYDDIPE GASNMGDDMA LRERELMLRQ REINMREQEM RMRRGPPPGP
RRGGATPSIR NGGFDDDDDD DDEYFDPTSR PAPPLIDPDN FDMMSVTSRR TRKAPSISQS
QMRNNPEGDS RRGYGGRGPM PSGRNRSSAR LIGNLPGAHD SIMDDPLMAY SSNRYGNVDR
QSLGQDSRAA SLTSARLDEL QLVGGGGMNG PFPRRTSQSP GNPYSPQLRG HGRPSPPNGH
MGYPPNGRPS PPGGMRQPVP QYPPGQGNTV APQQVEQHAG RGEW
//
