ID   A0A1Z5TSQ3_HORWE        Unreviewed;       500 AA.
AC   A0A1Z5TSQ3;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   18-JUN-2025, entry version 25.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BTJ68_01024 {ECO:0000313|EMBL:OTA38961.1};
OS   Hortaea werneckii EXF-2000.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX   NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA38961.1, ECO:0000313|Proteomes:UP000194280};
RN   [1] {ECO:0000313|EMBL:OTA38961.1, ECO:0000313|Proteomes:UP000194280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA38961.1,
RC   ECO:0000313|Proteomes:UP000194280};
RA   Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA   Nislow C.E.;
RT   "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT   insights from long-read sequencing.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870}.
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:OTA38961.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MUNK01000006; OTA38961.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z5TSQ3; -.
DR   FunCoup; A0A1Z5TSQ3; 225.
DR   STRING; 1157616.A0A1Z5TSQ3; -.
DR   VEuPathDB; FungiDB:BTJ68_01024; -.
DR   InParanoid; A0A1Z5TSQ3; -.
DR   OrthoDB; 316762at147541; -.
DR   Proteomes; UP000194280; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:TreeGrafter.
DR   GO; GO:0050661; F:NADP binding; IEA:TreeGrafter.
DR   Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
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; IPR050838; Ketopantoate_reductase.
DR   InterPro; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR   PANTHER; PTHR43765; 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.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194280}.
FT   DOMAIN          154..280
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          349..478
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   REGION          143..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          283..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..167
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..293
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   500 AA;  54854 MW;  33A6D336AA9AC9D9 CRC64;
     MEKEQDPAIE SGSGDMYETD YSAAPAAAPA QLPRRIHMLG TGSIGKLVAH ALRGLPNPPP
     ISLIFHRYRL LEAWEQGKKV ITIEDSGHQE QRGGFDVELL PQVKKQHGII IEDGEEDVYE
     AAERLGVAPA EAADLIRRDR EERQLDEEAT DGQADGAGIG QQDQPDQLAT PSRQRRYRGD
     YAKKNEPIHN LIVTTKAPLT VSALLPLRHR LGPQSTICFL QNGMGAVDEV NKQLFPREED
     RPNYVQGIIT HGVNVPPAVA ERDPFYAVHA GHGTIALGLL PRAESKSQEH PSDPEQDGTP
     AANSSSSPTT PPSHRSQAQV EAWNTARYLL RTLTRTPVLA AVGFPPTELL QQQLEKLAVN
     SILNPLTALI DARNGAILHN FALTRTMRLM LAETSLVIRS LPELHALPNV NVRFSASRLE
     TLVVSVAHQT RDNVSSMLAD VRGGRRTEVE FINGYIVRRG EEMGIKCVVN YAMMQAVLGK
     SLITQREVGD DVPVKLDLNG
//