ID A0A317X999_9EURO Unreviewed; 314 AA.
AC A0A317X999;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 02-APR-2025, entry version 16.
DE SubName: Full=2-dehydropantoate 2-reductase family protein {ECO:0000313|EMBL:PWY95184.1};
GN ORFNames=BO94DRAFT_562846 {ECO:0000313|EMBL:PWY95184.1};
OS Aspergillus sclerotioniger CBS 115572.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1450535 {ECO:0000313|EMBL:PWY95184.1, ECO:0000313|Proteomes:UP000246702};
RN [1] {ECO:0000313|EMBL:PWY95184.1, ECO:0000313|Proteomes:UP000246702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115572 {ECO:0000313|EMBL:PWY95184.1,
RC ECO:0000313|Proteomes:UP000246702};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) 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:PWY95184.1}.
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DR EMBL; MSFK01000003; PWY95184.1; -; Genomic_DNA.
DR RefSeq; XP_025471945.1; XM_025614316.1.
DR AlphaFoldDB; A0A317X999; -.
DR STRING; 1450535.A0A317X999; -.
DR GeneID; 37116459; -.
DR OrthoDB; 73846at2759; -.
DR Proteomes; UP000246702; 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:UP000246702}.
FT DOMAIN 6..175
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 183..308
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 314 AA; 35045 MW; 50999C21901C4B24 CRC64;
MASPRIHVLG LGSIGTFTAH GLKDIPNPPA VTLLLHRQSL YEYYLRNNRQ ITLTTLDGKS
IAHDNYDVEI YHPTGTWHTP SPSSITTSFI ETNTTITHLI LTVKATQAIS ALRSLKPRLT
SSSTILFLQN GCGMIDDVNE HLFPDPETRP NYITGVISHG VTLTSPFNAT HTGASKSYPY
TALLQIQLEK LSVNAFCNPV CALHDSKNAI LFNFPHLRRS ILSEISNIVL RLPELQGIPG
VEERFSVDRL EDTVNGILEK TRETVCSMVV DLRNGRETEV RFINGYWVRR GREVEVEVGV
NEGLMEQVLR RGSE
//
