ID A0A5N6G3P8_PETAA Unreviewed; 427 AA.
AC A0A5N6G3P8; A0A8H6E7T7;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 05-FEB-2025, entry version 14.
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=ETB97_011317 {ECO:0000313|EMBL:KAF5862679.1};
OS Petromyces alliaceus (Aspergillus alliaceus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=209559 {ECO:0000313|EMBL:KAF5862679.1, ECO:0000313|Proteomes:UP000541154};
RN [1] {ECO:0000313|EMBL:KAF5862679.1, ECO:0000313|Proteomes:UP000541154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FRR 5400 {ECO:0000313|EMBL:KAF5862679.1,
RC ECO:0000313|Proteomes:UP000541154};
RA Gilchrist C.L.M., Pitt J.I., Lange L., Lacey H.J., Vuong D., Midgley D.J.,
RA Greenfield P., Bradbury M., Lacey E., Busk P.K., Pilgaard B., Chooi Y.H.,
RA Piggott A.M.;
RT "Aspergillus burnettii sp. nov., novel species from soil in southeast
RT Queensland.";
RL Submitted (APR-2019) 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:KAF5862679.1}.
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DR EMBL; SPNV01000068; KAF5862679.1; -; Genomic_DNA.
DR OMA; RKEPFQV; -.
DR Proteomes; UP000541154; 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:UP000541154}.
SQ SEQUENCE 427 AA; 47229 MW; 7C028F32FE4F8E32 CRC64;
MAGDAQRGLN VRFLATWHQD ADEASRGSGK RRLSGRIHIL GLGNIGTFVA HSLASRSSPP
PVTLMMHTPN LYRSWLERKK CLAINTNGLD DIKTGFDVNV LNDKTWLSVP YWNQDGTTEN
GNESIDEYAQ QAATDGASAE DERIECLIVA VKAPVTATAM ESVKHRLTPD STVLFLQNGM
GAIDEVNEKV FPDPRYRPHY MCGIISHGLA RRKEPFQVSH TGVGTTILGS VPLAGAVTST
NEGDSNWAPS TKYLLRTLTL TPPLVAVAET PSSLILYQLE KLAMNSVINP LTAIMNCKNG
ELLYNYSFTR IMRLLLIEIS SVICALPELQ AVPGIESRFS PERLRMMVTQ LANKTAKNHS
SMLQDVLSRK TTEIEYMNGY IIRRGEELGI KCVVNYTIKH LVLAKHLQTK QMESGAIPID
LPREPKM
//
