ID A0A1W2TJI4_ROSNE Unreviewed; 431 AA.
AC A0A1W2TJI4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 02-APR-2025, entry version 23.
DE SubName: Full=Putative 2-dehydropantoate 2-reductase {ECO:0000313|EMBL:GAP88355.1};
GN ORFNames=SAMD00023353_2900200 {ECO:0000313|EMBL:GAP88355.1};
OS Rosellinia necatrix (White root-rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Rosellinia.
OX NCBI_TaxID=77044 {ECO:0000313|EMBL:GAP88355.1};
RN [1] {ECO:0000313|EMBL:GAP88355.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W97 {ECO:0000313|EMBL:GAP88355.1};
RA Kanematsu S.;
RT "Draft genome sequence of Rosellinia necatrix.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DF977474; GAP88355.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2TJI4; -.
DR STRING; 77044.A0A1W2TJI4; -.
DR OMA; WDYVVVT; -.
DR OrthoDB; 3609at2759; -.
DR Proteomes; UP000054516; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR FunFam; 1.10.1040.10:FF:000017; 2-dehydropantoate 2-reductase; 1.
DR FunFam; 3.40.50.720:FF:000609; 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; IPR013752; KPA_reductase.
DR InterPro; IPR051402; KPR-Related.
DR InterPro; IPR013332; KPR_N.
DR PANTHER; PTHR21708:SF26; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR PANTHER; PTHR21708; PROBABLE 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR Pfam; PF02558; ApbA; 1.
DR Pfam; PF08546; ApbA_C; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000054516}.
FT DOMAIN 41..217
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 287..418
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..34
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..122
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..133
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 431 AA; 45597 MW; C0F4E7B06BA70963 CRC64;
MATPDPKHVG GISSSSSSNG SSTSTSTNGS TSTSPTRPVH ILFVGAGAVG CFYASRLHHP
SHNVYTSLTA RSNYAAIASS GVTLQTRSFG DYTFHPHAVF PSVAAAVAGA PPKRNTSSSS
STGDDDENNE EGGWDYVVVT TKALPDRTDD AAMIAPLVTP RRTCVVLIQN GVGVEAPYRA
RFPANPIVSG VTVVSAEQTS PGVVRQNRWT RISLGPYVRG LQPNTPTSTS TATATANANA
NANANTDTNT DDDDLAARGQ ACMERLAGWW TSPGGLRDAE PHTERELQAI RWHKLCINAA
FNSTAVLSGG RGNADQLTDA ELRRHVAGVM REVWDAAPAV LGGPSFPPEG LGGLATPERI
LRSTERNPGA RPSMLLDWDA GRPMELEVIL GNPVRLARAA GVEMPRLQSL YALLRSMQAV
REAARPREGK L
//
