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
//