ID A0A162JYI5_9HYPO Unreviewed; 470 AA.
AC A0A162JYI5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=2-dehydropantoate 2-reductase {ECO:0000313|EMBL:OAA50838.1};
GN ORFNames=BBO_00785 {ECO:0000313|EMBL:OAA50838.1};
OS Beauveria brongniartii RCEF 3172.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC Beauveria brongniartii.
OX NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA50838.1, ECO:0000313|Proteomes:UP000076863};
RN [1] {ECO:0000313|EMBL:OAA50838.1, ECO:0000313|Proteomes:UP000076863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA50838.1,
RC ECO:0000313|Proteomes:UP000076863};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:OAA50838.1}.
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DR EMBL; AZHA01000002; OAA50838.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162JYI5; -.
DR OrthoDB; 1354873at2759; -.
DR Proteomes; UP000076863; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; IPR013752; KPA_reductase.
DR InterPro; IPR013332; KPR_N.
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.
PE 3: Inferred from homology;
FT DOMAIN 89..265
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 305..453
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 470 AA; 50695 MW; 1AD0321B1DCC11BB CRC64;
MWGTASRPML SPCIRLATSH HPVRASITAS RSMTSQPSTP PWLSSLLREN NPAPKLYAWT
PAHLGLSTAL PSSPALSARP ADDADRRLYI LGLGNLGRMY ALYIRTRADP PPITLIVHRK
ELLSQWHESK GIEIACRDQV HTCKDFDIEW WAEEKPPETG GAAPVREAAD GSTIRNLLVT
TKAQAALPEV DRMRRYLDAQ STVAFAQNGM SKLWPPHGAS YMAARFPPDG AAGFHALLCV
TNHGLYSTGP FRSVFASPAG AYLGPVVASG IASAPPSSAA YLTAQVVDTE TLAARAFSSL
DVWVLQLEKL VVNTCINPLS AILRCKTGRL FASDSALRVM DLMLASSSRI LQAIVADSSS
AAILASDLQA GRSVGALRAE LAARFAQPRL RAMLHRVGAL VQDNKSSMLQ DVEAGKATTE
IGDFNGWLVD AAAYLGDDSI DVSVHEQVID LVERRVVMNE EQLAEHFLAT
//
