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Database: UniProt
Entry: A0A194WA55_9PEZI
LinkDB: A0A194WA55_9PEZI
Original site: A0A194WA55_9PEZI 
ID   A0A194WA55_9PEZI        Unreviewed;       539 AA.
AC   A0A194WA55;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Putative 2-dehydropantoate 2-reductase {ECO:0000313|EMBL:KUI73334.1};
GN   ORFNames=VM1G_08861 {ECO:0000313|EMBL:KUI73334.1};
OS   Valsa mali.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=105487 {ECO:0000313|EMBL:KUI73334.1};
RN   [1] {ECO:0000313|EMBL:KUI73334.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03-8 {ECO:0000313|EMBL:KUI73334.1};
RA   Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA   Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT   "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT   Colonization on Woody Bark.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870}.
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DR   EMBL; CM003107; KUI73334.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A194WA55; -.
DR   OrthoDB; 2486981at2759; -.
DR   Proteomes; UP000078559; Chromosome 10.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR   PANTHER; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE-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   3: Inferred from homology;
FT   DOMAIN          196..335
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          386..513
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   REGION          16..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          83..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   539 AA;  61336 MW;  86CB795B94BBC95C CRC64;
     MSPCYNIFFE ALLLPTETRD PTEPSSAKPE SSPGSPAWEA PGPKRIVLYR KDYLPRSRVF
     ARIPHRHTAW SYGSIVAGRG ARASRRSYSA EQAATTEQPP RPQPKKASYN HLSERPYLQR
     LLEQVEEDPL HKIDQAADKK YYPIGLPYTT AYTSDRRRGR DREEEAPETG GQVHILGYDP
     RAYFMAHQLG SYKYLDPVKL LIHKRVVMNS WRHEGEGVTL WKGTERSMLR GRAEAEWIGR
     GFNQPSNEHI QQLVVTLPCG VTKPALQNII HRIDNRTTIC FIQDGLGVIE QLNNTLFVDP
     TTRPNYILGH STASLGYNKK QFFSAILKKT GKLYLHSVER GIDLQPMFKM YPSVQNRRTS
     TQFLRTLVTT PGLNAGGFGL ENFLMKKLPA MVFSAIIEPM AIVLDTSYDQ VLLNERAILL
     ADELLEELFN VIMSLPELTN SSKVVEHCGV DALRKETLDR LVQKGVSNSL MLTRVRAGQW
     VDIDYLNGYF IRRGKDLGIK TPQNEMVVDV VKARIEQRKK DMKGLIPFEE SIDPNQYSF
//
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