ID K9G041_PEND2 Unreviewed; 748 AA.
AC K9G041;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=2-dehydropantoate 2-reductase, putative {ECO:0000313|EMBL:EKV15290.1};
GN ORFNames=PDIG_27280 {ECO:0000313|EMBL:EKV15290.1};
OS Penicillium digitatum (strain PHI26 / CECT 20796) (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1170229 {ECO:0000313|EMBL:EKV15290.1, ECO:0000313|Proteomes:UP000009882};
RN [1] {ECO:0000313|Proteomes:UP000009882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI26 / CECT 20796 {ECO:0000313|Proteomes:UP000009882};
RX PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT postharvest pathogen of citrus.";
RL BMC Genomics 13:646-646(2012).
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:EKV15290.1}.
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DR EMBL; AKCT01000122; EKV15290.1; -; Genomic_DNA.
DR AlphaFoldDB; K9G041; -.
DR STRING; 1170229.K9G041; -.
DR eggNOG; ENOG502QT3Z; Eukaryota.
DR HOGENOM; CLU_021479_0_0_1; -.
DR InParanoid; K9G041; -.
DR OMA; SFKSKAF; -.
DR OrthoDB; 2727909at2759; -.
DR Proteomes; UP000009882; 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:UP000009882}.
FT DOMAIN 9..164
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 197..319
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 323..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..347
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..389
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..644
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..669
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 748 AA; 81041 MW; 67F950B2BAA8C012 CRC64;
MVRHLIKACL VGGNAISAFL SWRLQATASC DVTLVWKSGY DSVSQYGVSF KSKAFGNERF
KPRHVVRAPE EASSREHVYD YVILCVKALP DVYDLASVIE SVVTPQHTCI LLNTTNTLGI
EAHLEQRYPT NVILSLVSNV EISQTGPSEF EHLSSSEIYV GATNKSSAIP TSVQSDMAAA
LAVTLNSGQV NCKVSDNIRQ EQFDRMIGPV AFHPASVVFD TPNHTQLLEK TGVRPLVMGI
LDEMMEIASA QGCSFPSDFR DKTVQKMIAL DSPTTMYSDF QGRRPMEVET FLGSPIKLAS
ESNVRVPRIE TMYAMLHHVN IANQKPRQES PPASVTGQPP PRMSSAPPQQ RPMMNGGPQS
LRGSRTPSGV GMPPQQRRGP PPGMMPRGPG GSMPPANRVQ RDPSLEGLEE FSHLVLYDEQ
GEPSVPQQNG NGHPEPAPGP VSELTLRERE LALRQRELQL REQEMNMRRP PPGPGRRGPP
PSRPATAFDE EDEDYFDPMD SMGIPHIDPD SVDMMSMTSR RGRKGLSHSQ IRKNPEFGVN
TGGSRPSSAF NRYFGRKRTS DRVMQEIPGL HDSLMDSPMM SYSSNRYGAV DRNQMHVESR
ANSLTASHKG DYPPRPFSQN RRNSQTPVPP FGGPPGPQGP PGTGGPRMSR PGGPHNAQPS
PPGNMRTPAP RYPPGQGNAA GPQQVDQHYG VSNAFPAKGP PKNQNLTSSA SASAGSGDSG
ASANLDSEPS SHSSQVSLGG QGVAAPVR
//
