ID A0A093YR47_9PEZI Unreviewed; 703 AA.
AC A0A093YR47;
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=V492_07105 {ECO:0000313|EMBL:KFY07476.1};
OS Pseudogymnoascus sp. VKM F-4246.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420902 {ECO:0000313|EMBL:KFY07476.1, ECO:0000313|Proteomes:UP000029299};
RN [1] {ECO:0000313|EMBL:KFY07476.1, ECO:0000313|Proteomes:UP000029299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY07476.1,
RC ECO:0000313|Proteomes:UP000029299};
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:KFY07476.1}.
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DR EMBL; JPJU01002555; KFY07476.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093YR47; -.
DR STRING; 1420902.A0A093YR47; -.
DR HOGENOM; CLU_021479_0_0_1; -.
DR Proteomes; UP000029299; 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:UP000029299}.
FT DOMAIN 9..166
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 199..322
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 329..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..678
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 703 AA; 76377 MW; A476D35595F06699 CRC64;
MGDGMLMEVC VVGGNAVSAF LSWRLQATNA CDVTLVWKSG FDAVSQYGIS FKSSAFGNER
FKPRHVVRTP EDAAAAKEGA FDYVLLCVKA LPDIYDLAAV IESVVTPQHT CILVNTTHTL
GVEAHLEQRF PTNVVLSLVS GAELTQLGVS EFEHKASTEV WVGAANKNAA IPASIQQDMA
EALAMTLSTG QVDCKVSRNI RQQQYERMIG PIAFHPLSVL METSSHATLL EKTAVEPMIK
DVMDELLRIA EAQGCTFPKD FKEKTVQEMV RPSESNSIMY QDFMARRPME VETYLGSPIK
LAQSVGVKVP RIETLYALLH SVNIVNQQKP KEAPATPAVN GNGQFPTRLS SAPTPRPMNG
PNGAPNGMMN GMGRGRGRAP SMGPPPGMRR GGPMNGGPNG YGRPPPNGYG SRQQSRRGSI
DNDLADEFSH VVLYDDIPEG ASNLGDDMAL RERELMLRQR EINMREQEMR MRRGPPPGPR
RGGATPSIRN GGFDDDDDDD DEYFDPTSRP APPLIDPDNF DMMSVTSRRT RKAPSISQSQ
MRNNPEGDSR RGYGGRGPMP SGRNRSSARL IGNLPGAHDS IMDDPLMAYS SNRYGNVDRQ
SLGQDSRAAS LTSARLDELQ LVGGGGMNGP FPRRTSQSPG NPYSPQLRGH GRPSPPNGHM
GYPPNGRPSP PGGMRQPVPQ YPPGQGNTVA PQQVEQHAGR GEW
//
