ID   A0A1V1TNB4_9PEZI        Unreviewed;       490 AA.
AC   A0A1V1TNB4;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   05-FEB-2025, entry version 27.
DE   RecName: Full=Ketopantoate reductase C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ANO14919_119200 {ECO:0000313|EMBL:GAW22383.1};
OS   Xylariales sp. No.14919.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales.
OX   NCBI_TaxID=1813822 {ECO:0000313|EMBL:GAW22383.1, ECO:0000313|Proteomes:UP000189293};
RN   [1] {ECO:0000313|EMBL:GAW22383.1, ECO:0000313|Proteomes:UP000189293}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No.14919 {ECO:0000313|EMBL:GAW22383.1,
RC   ECO:0000313|Proteomes:UP000189293};
RG   Technology Reseach Association of Highly Efficient Gene Design;
RA   Itoh H., Matsui M., Shibata T.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAW22383.1, ECO:0000313|Proteomes:UP000189293}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No.14919 {ECO:0000313|EMBL:GAW22383.1,
RC   ECO:0000313|Proteomes:UP000189293};
RA   Itoh H., Matsui M., Kumagai T., Arita M., Machida M., Shibata T.;
RT   "Genome Sequence of Fungus Strain No.14919 Producing HMG-CoA Reductase
RT   Inhibitor FR901512.";
RL   Submitted (MAR-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:GAW22383.1}.
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DR   EMBL; BDMC01000049; GAW22383.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V1TNB4; -.
DR   STRING; 1813822.A0A1V1TNB4; -.
DR   OrthoDB; 73846at2759; -.
DR   Proteomes; UP000189293; 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:UP000189293}.
FT   DOMAIN          100..271
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          308..467
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   REGION          62..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..81
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   490 AA;  53516 MW;  CBB47FD5819AEE16 CRC64;
     MRVTRLSTPA STLRRQLVGM CGIPLRPMHS SARMRNINNP CEIPAEWLGR IMADNTTPPK
     LYAWTPKDLS AKGRTKPESG QDSRTGMEPN KRNEEERRRI YILGVGNIGR LYAMCLSKLA
     HSPPITLVVH RKELLERWAA EPGIELTRHG RVQRNVDFDV EWWTDMAPDG NDGAEVAAGG
     NIGNLIVATK ASDAIPQVDR VRRYLGGNST VAFVQNGMCK LWPPLGDVYV GARFADGNSP
     NWIACVTTHG VTSQGPFKSI HAAPANALVG PVMSGRGSDT GAGYLMRLIA KAPDLDAQEV
     SRKQLWVSQL EKLVVNAVIN PLTAVLRCKN GEIFIARDDA IPDIINRLLS EASETLGALV
     LSSRSEGLLL SESACKGTIP ENLTAEFLRA TREQLLGRFS FPRLRGLVLD VGVKVSANTS
     SMLQDLQAGK PTEVDDFNGW LVDTARLLDK GLQLPTHEKL IGLVKAKAKL TRNELCAEIL
     SREALLNADS
//