ID A0A2G7FSM7_9EURO Unreviewed; 364 AA.
AC A0A2G7FSM7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 05-FEB-2025, entry version 21.
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=AARAC_005744 {ECO:0000313|EMBL:PIG83642.1};
OS Aspergillus arachidicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=656916 {ECO:0000313|EMBL:PIG83642.1, ECO:0000313|Proteomes:UP000231358};
RN [1] {ECO:0000313|EMBL:PIG83642.1, ECO:0000313|Proteomes:UP000231358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117610 {ECO:0000313|EMBL:PIG83642.1,
RC ECO:0000313|Proteomes:UP000231358};
RA Moore G., Beltz S.B., Mack B.M.;
RT "Genome sequence for an aflatoxigenic pathogen of Argentinian peanut,
RT Aspergillus arachidicola.";
RL Submitted (MAY-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:PIG83642.1}.
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DR EMBL; NEXV01000431; PIG83642.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G7FSM7; -.
DR STRING; 656916.A0A2G7FSM7; -.
DR Proteomes; UP000231358; 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 FunFam; 1.10.1040.10:FF:000038; Probable 2-dehydropantoate 2-reductase; 1.
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:UP000231358}.
FT DOMAIN 70..169
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 211..341
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 364 AA; 40619 MW; F94BEBCBA4EE6064 CRC64;
MHNPNLYRSW LERKKCLAIN TNGLDDVKTG FDVNVLNDKT WYSVPYWNKD GTAENGNDSI
DQHTEGVGNE ELLAQPADER IECLIVAVKG PVTVAAMDSV KRRLTPDSTI LFLQNGMGII
EELNEKVFRD PRRRPHYMCG VISHGLARRR EPFQVSHTGV GTTILGSVPP ADAVSPSNKG
DVDWAPSTKY LLRTLTLTPP LVAVAETPSS LMLYQLEKLA LNCVINPLTA IMNCKNGELL
YNYSFTRIMR LLLIEISSVI CALPELQGVP GIESRFSPER LRMMVVQLAN KTAKNHSSML
QDVLARKPTE IEYLNGYVVR RGEELGIKCV VNYMIKHLVL AKGLQTKQVE SGAIPIDLLR
EPQI
//
