ID   A0A0P7AZ60_9HYPO        Unreviewed;       587 AA.
AC   A0A0P7AZ60;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, 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=AK830_g12397 {ECO:0000313|EMBL:KPM34175.1};
OS   Neonectria ditissima.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX   NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM34175.1, ECO:0000313|Proteomes:UP000050424};
RN   [1] {ECO:0000313|EMBL:KPM34175.1, ECO:0000313|Proteomes:UP000050424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R09/05 {ECO:0000313|EMBL:KPM34175.1,
RC   ECO:0000313|Proteomes:UP000050424};
RA   Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT   "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT   ditissima.";
RL   Submitted (SEP-2015) 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:KPM34175.1}.
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DR   EMBL; LKCW01000385; KPM34175.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7AZ60; -.
DR   STRING; 78410.A0A0P7AZ60; -.
DR   OrthoDB; 73846at2759; -.
DR   Proteomes; UP000050424; 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:UP000050424}.
FT   DOMAIN          291..390
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          421..552
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   REGION          36..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          89..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          153..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..178
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   587 AA;  65403 MW;  C1C2F1BA285BFEDC CRC64;
     MPSLRDTVFN SVTVSGIKVD DDQGYTRSTL KTGIGNPFIQ QSTHHHSTLR PSNSTPNTNA
     LADAIIYTIS PQPSQQTSLF ISVFSRHPSR PPSHARTQLL IPPFTGKPRG RHPVPRPYNP
     STSPFTAAKL ASLPNPRVSA RLPQKLSRCL RGNDWASRGS APSRCFASAA STPHQNKTPK
     AIPPELAGSP STRPWQSSDL NAQTLASSPT PSKFHIPSVI LPADAAKSGP VHKIHILGDD
     VRSRFIAHAL CGVYDSVELL GYRSMPKSRY RNVEAAQPER TRRSAYAEPN AVPVQTHVKA
     AKSHIDQLII TGRGFEAVKA MESVKDRVNE NTSVCLLNDG MGVLEDAREH IFKDTKSTPN
     FILGHMSHAL VYNRNRNSVK ELKSGRTVLT QTNPTLYTKD FAESLQEIKS LRTTSGSFEN
     WMRFKLPSMV FTAAVEPVCV LLEIPYQNLL ENRSAQSMMN QLLEEIVTVV DHMPELQGAM
     ELRRFIRGES LKKWCYQRIT GKASAPSDLL QRVEKGLQTD IKYQNGFFQK RAKTLGIDIP
     TNTLMVQMIK ARRAEALARR ESYIKMEEKS IDDLRALSPR RGTDEWL
//