ID   A0A2S4VV30_9BASI        Unreviewed;       453 AA.
AC   A0A2S4VV30;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   13-SEP-2023, entry version 18.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PSTT_03799 {ECO:0000313|EMBL:POW13382.1};
OS   Puccinia striiformis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=27350 {ECO:0000313|EMBL:POW13382.1, ECO:0000313|Proteomes:UP000239156};
RN   [1] {ECO:0000313|EMBL:POW13382.1, ECO:0000313|Proteomes:UP000239156}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-210 {ECO:0000313|EMBL:POW13382.1,
RC   ECO:0000313|Proteomes:UP000239156};
RA   Xia C.;
RT   "Gene loss provides genomic basis for host adaptation in cereal stripe rust
RT   fungi.";
RL   Submitted (DEC-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:POW13382.1}.
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DR   EMBL; PKSL01000025; POW13382.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S4VV30; -.
DR   VEuPathDB; FungiDB:PSHT_07102; -.
DR   VEuPathDB; FungiDB:PSTT_03799; -.
DR   Proteomes; UP000239156; 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:SF43; APBA_C DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR21708; PROBABLE 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR   Pfam; PF02558; ApbA; 1.
DR   Pfam; PF08546; ApbA_C; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000239156}.
FT   DOMAIN          8..156
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          263..446
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   REGION          345..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..385
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   453 AA;  49654 MW;  2B0D081513D84D0C CRC64;
     MSTEPVDVLL VGLGAIGGIY SFVLERSQRC RVTAIARSKY ESIQTHGLTI QSEKYGLIEN
     WRPYRLTRSA EEAADRDYRF IVCCVKSLPD VECISAILAP LLLPYHEDFP NSTCHPPPAV
     VLIQNGIGIE QELAEAFPLI HIISCVSWLG ANLITPPVVP GETSTPPISS TMPLGQIAPR
     IEHGPQDRLV FGLYEGEGFQ EARFNEAHSR TCNGYAEGLL ARDKTPLIGV ARVEKLQNGT
     NDINLFLELL TAGGCEAEAV EHIQPARWAK NLFNGAYSSM CTLSRSTISQ FLVPEVLPHT
     IPVARETMLE MLCVARALGY QEAELPAKTI DGIINFILQH YKPKGNVPET PSTLTTPPVI
     QETRHSESPD DAARNKGDGS AHVETAKDND TSAGSTSFKP SMLLDVEKNR PIELEPIVGA
     VLERARNKAV ETPRLDLLYA MLKVLQVQVT SNN
//