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Database: UniProt
Entry: A0A0W0FB11_9AGAR
LinkDB: A0A0W0FB11_9AGAR
Original site: A0A0W0FB11_9AGAR 
ID   A0A0W0FB11_9AGAR        Unreviewed;       442 AA.
AC   A0A0W0FB11;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=WG66_14046 {ECO:0000313|EMBL:KTB33428.1};
OS   Moniliophthora roreri.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB33428.1, ECO:0000313|Proteomes:UP000054988};
RN   [1] {ECO:0000313|EMBL:KTB33428.1, ECO:0000313|Proteomes:UP000054988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB33428.1,
RC   ECO:0000313|Proteomes:UP000054988};
RA   Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT   "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT   pod rot of cacao.";
RL   Submitted (DEC-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:KTB33428.1}.
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DR   EMBL; LATX01002176; KTB33428.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W0FB11; -.
DR   eggNOG; ENOG502QPT5; Eukaryota.
DR   Proteomes; UP000054988; Unassembled WGS sequence.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:InterPro.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:InterPro.
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; 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; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR   PANTHER; PTHR43765:SF2; 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   Reference proteome {ECO:0000313|Proteomes:UP000054988}.
FT   DOMAIN          27..214
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          286..430
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   REGION          96..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   442 AA;  49269 MW;  25596B4748536A4A CRC64;
     MKLISGFQQE LYDQWKDSFS GSDMRFHVLG VGAIGSLLSH HLRRSLPAEH SVTLIHKTVR
     HARDAQNRGG IRVESGGISE LSGRFKAEIF EGGVAPRLSS RKETQEQTET SQTGTGLHVN
     HGDMHGNPIE SLFVTAKAHQ TVPAIRLLSP RLSANSTIVL MQNGMGVYEE LLQEIFRNPL
     SRPHFILASN THGVYPKGPF DVVHAGMGEI RFGIARDVEE RRNYEAGFFD ESVSRSDRRP
     RLTDITTSEA DPFFTRYKSL RNTVAALLLM DALQTSWIPM EEMQIAMRRK LVVNSVINPL
     TSVMGCKNGE IFSTPAGIEI MRSVCREAAK VFAAETRAAS QSYFDSIGAS EVDQEQITLD
     RVPRALSAES LQEECLRVAE ATKHNMSSTL ADIRKGVSRT EINYLNGHLV RLGRTYKVPT
     PTITTLWRLV YMRSAIPLDQ GF
//
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