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Database: UniProt
Entry: A0A317SET6_9PEZI
LinkDB: A0A317SET6_9PEZI
Original site: A0A317SET6_9PEZI 
ID   A0A317SET6_9PEZI        Unreviewed;       456 AA.
AC   A0A317SET6;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   02-APR-2025, entry version 20.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00013014};
DE            EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014};
DE   AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024};
GN   ORFNames=C7212DRAFT_225614 {ECO:0000313|EMBL:PWW72954.1};
OS   Tuber magnatum (white Piedmont truffle).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Tuberaceae; Tuber.
OX   NCBI_TaxID=42249 {ECO:0000313|EMBL:PWW72954.1, ECO:0000313|Proteomes:UP000246991};
RN   [1] {ECO:0000313|EMBL:PWW72954.1, ECO:0000313|Proteomes:UP000246991}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=091103-1 {ECO:0000313|EMBL:PWW72954.1};
RA   Murat C., Payen T., Noel B., Kuo A., Martin F.M.;
RT   "Genomes of Pezizomycetes fungi and the evolution of truffles.";
RL   Submitted (MAR-2018) 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:PWW72954.1}.
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DR   EMBL; PYWC01000091; PWW72954.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317SET6; -.
DR   STRING; 42249.A0A317SET6; -.
DR   OrthoDB; 73846at2759; -.
DR   Proteomes; UP000246991; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:TreeGrafter.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:InterPro.
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; IPR003710; ApbA.
DR   InterPro; IPR050838; Ketopantoate_reductase.
DR   InterPro; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR00745; apbA_panE; 1.
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:UP000246991}.
FT   DOMAIN          50..234
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          302..432
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          252..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..42
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..273
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   456 AA;  49641 MW;  029A80B32FDA69E4 CRC64;
     MSTKQEWSAS PQDSRNISPP SPHDTTAAAA ATTTATATTT AASPVVPRRI HILGSGNVGN
     LVAHSLRTLP NPPPVTLLFH KFSKLEDFQT SGSRIELHRP LKEVSISYGY EAELTLPPNA
     VVAANTPLEA LVDPNTGATP PPPPQRRIAN LIITTKAHQT VAALRPISER LTKDSTVLIL
     QNGMGVLEEI KAEIFPDPAS RPNFVLGITT HGIYPEGPFT LVQKGMGTIS LGYVQRDHPE
     APDWKKEGVV RSWFTSSPPP PSEHPDKPPP LNTLPPSSGY LLSTLLSAKP LEAAHLSIAE
     LLSAQLEKLA INAVINPLTV LFNCKNGELL ENFYIVQNMR LILWEVSQVL CALPELAALP
     GRDVRLSPDR LYDLVIRVAR LSAGNYSSMF QDVRNGKQTE IDYINGYVLD RARDMELACT
     VNYMLVNMVK AKGKIVQERA AAQVPFVLFG HALCPL
//
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