ID A0A5N5QHW3_9AGAM Unreviewed; 432 AA.
AC A0A5N5QHW3;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 05-FEB-2025, entry version 15.
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=CTheo_5205 {ECO:0000313|EMBL:KAB5591332.1};
OS Ceratobasidium theobromae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Ceratobasidium.
OX NCBI_TaxID=1582974 {ECO:0000313|EMBL:KAB5591332.1, ECO:0000313|Proteomes:UP000383932};
RN [1] {ECO:0000313|EMBL:KAB5591332.1, ECO:0000313|Proteomes:UP000383932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT2 {ECO:0000313|EMBL:KAB5591332.1,
RC ECO:0000313|Proteomes:UP000383932};
RX PubMed=31583107;
RA Ali S.S., Asman A., Shao J., Firmansyah A.P., Susilo A.W., Rosmana A.,
RA McMahon P., Junaid M., Guest D., Kheng T.Y., Meinhardt L.W., Bailey B.A.;
RT "Draft genome sequence of fastidious pathogen Ceratobasidium theobromae,
RT which causes vascular-streak dieback in Theobroma cacao.";
RL Fungal Biol. Biotechnol. 6:14-14(2019).
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:KAB5591332.1}.
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DR EMBL; SSOP01000110; KAB5591332.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N5QHW3; -.
DR OrthoDB; 73846at2759; -.
DR Proteomes; UP000383932; 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 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:UP000383932}.
FT DOMAIN 3..197
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 273..422
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 432 AA; 47596 MW; D1A1441F05CA766F CRC64;
MNIHVLGVGS IGSLIAAHLR FSTSYPITLL VKRDSFAQTL TRDLEQTIVI EREGSVIRAT
GFSIQLTDPA AEIMRTMLRG PNGKLRANIL RPRSRSPSLA IPTPNEETSP IDSLIITTKA
PSTWRAVRAL SSRLTPNSTI TLIQNGMGVY EQLCAKVFPS SASRPHFIIA STTHGAWAKR
PFYTVHAGLG DLVFGVVPSE RVDLPLDLEK NYREIARKQG QSGESNEPTL EELQKEQEAL
LQKLTPHNSL YQTIRALLSL RGLSPSWVGA ADLQERLQRK LVTNSVINPL TAIMGCRNGK
LAGDPGAQRI ARGVCQEAEK VFRAQLLEDE NYTGSSNTNP PQYTEQDLAN ANLSRRLIAK
SLEAEFVRVA ELTAVNISSM LQDVKNGVET EVDYMNGYLI RMGVKYGIPT PVNEMLRTLV
QIKTRLPGGE EM
//
