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Database: UniProt
Entry: A0A0D2BY48_9EURO
LinkDB: A0A0D2BY48_9EURO
Original site: A0A0D2BY48_9EURO 
ID   A0A0D2BY48_9EURO        Unreviewed;       492 AA.
AC   A0A0D2BY48;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=PV08_06290 {ECO:0000313|EMBL:KIW16239.1};
OS   Exophiala spinifera.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW16239.1, ECO:0000313|Proteomes:UP000053328};
RN   [1] {ECO:0000313|EMBL:KIW16239.1, ECO:0000313|Proteomes:UP000053328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW16239.1,
RC   ECO:0000313|Proteomes:UP000053328};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala spinifera CBS89968.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870}.
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DR   EMBL; KN847495; KIW16239.1; -; Genomic_DNA.
DR   RefSeq; XP_016236455.1; XM_016380628.1.
DR   AlphaFoldDB; A0A0D2BY48; -.
DR   STRING; 91928.A0A0D2BY48; -.
DR   GeneID; 27333373; -.
DR   VEuPathDB; FungiDB:PV08_06290; -.
DR   HOGENOM; CLU_031468_10_3_1; -.
DR   OrthoDB; 1354873at2759; -.
DR   Proteomes; UP000053328; 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   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053328}.
FT   DOMAIN          162..245
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          309..441
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          468..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   492 AA;  54606 MW;  30A89E97BD95BBDD CRC64;
     MAQSHSWWSP VPSDEHASVS GQASFESKPL DEDVVSEPDE ERLLTRRVHI LGLGSIGTLV
     AHSMRCLPNP PPITLMMHKR EQYAEFKKAG RNIALIDQKN NINDEQTGYD VEVYEGEEPE
     AGPTWRFMPD FKSKPGRGAT PPVTNPLETG ESLPDGKVFI YCLIVAVKGH ATVAALRSVK
     DRVDSRTTIC FMQNGLGQID ELNRDVFTDP ATRPTYVLGI VSHGVYMADP CKVVHAGYGT
     IALGVSRDRD RHPLPPPALT RNISDLTDDE RRKFYPSDKD LFASMSSRYL LRTLTRSTVL
     ACAVFPYLDL LQLQLEKLAA NAVLNPLTAL LDVPNGALLE SNEISVVQRL LLAEVSLVIR
     GLPELEGIPN VKMRFSARRL EQLALAVTRR TAQNSSSMRE DLRHGKKPEI DYINGYIVRR
     GEEQGIKCAL NFMLMQLIKG KDGLQKRDYG IPQGIPYGTR HIGVQANPNQ PGIVTLSDES
     TPNPLRTTTN PR
//
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