ID N1JN32_BLUG1 Unreviewed; 603 AA.
AC N1JN32;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 18-JUN-2025, entry version 36.
DE SubName: Full=2-dehydropantoate 2-reductase {ECO:0000313|EMBL:CCU82001.1};
GN ORFNames=BGHDH14_bgh06166 {ECO:0000313|EMBL:CCU82001.1};
OS Blumeria graminis f. sp. hordei (strain DH14) (Barley powdery mildew)
OS (Oidium monilioides f. sp. hordei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Blumeria; Blumeria hordei.
OX NCBI_TaxID=546991 {ECO:0000313|EMBL:CCU82001.1, ECO:0000313|Proteomes:UP000015441};
RN [1] {ECO:0000313|EMBL:CCU82001.1, ECO:0000313|Proteomes:UP000015441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DH14 {ECO:0000313|EMBL:CCU82001.1};
RX PubMed=21148392; DOI=10.1126/science.1194573;
RA Spanu P.D., Abbott J.C., Amselem J., Burgis T.A., Soanes D.M., Stueber K.,
RA Ver Loren van Themaat E., Brown J.K.M., Butcher S.A., Gurr S.J.,
RA Lebrun M.-H., Ridout C.J., Schulze-Lefert P., Talbot N.J., Ahmadinejad N.,
RA Ametz C., Barton G.R., Benjdia M., Bidzinski P., Bindschedler L.V.,
RA Both M., Brewer M.T., Cadle-Davidson L., Cadle-Davidson M.M., Collemare J.,
RA Cramer R., Frenkel O., Godfrey D., Harriman J., Hoede C., King B.C.,
RA Klages S., Kleemann J., Knoll D., Koti P.S., Kreplak J., Lopez-Ruiz F.J.,
RA Lu X., Maekawa T., Mahanil S., Micali C., Milgroom M.G., Montana G.,
RA Noir S., O'Connell R.J., Oberhaensli S., Parlange F., Pedersen C.,
RA Quesneville H., Reinhardt R., Rott M., Sacristan S., Schmidt S.M.,
RA Schoen M., Skamnioti P., Sommer H., Stephens A., Takahara H.,
RA Thordal-Christensen H., Vigouroux M., Wessling R., Wicker T., Panstruga R.;
RT "Genome expansion and gene loss in powdery mildew fungi reveal tradeoffs in
RT extreme parasitism.";
RL Science 330:1543-1546(2010).
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:CCU82001.1}.
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DR EMBL; CAUH01005677; CCU82001.1; -; Genomic_DNA.
DR AlphaFoldDB; N1JN32; -.
DR FunCoup; N1JN32; 110.
DR STRING; 546991.N1JN32; -.
DR EnsemblFungi; BLGH_05936-mRNA-1; BLGH_05936-mRNA-1; BLGH_05936.
DR eggNOG; ENOG502QPT5; Eukaryota.
DR HOGENOM; CLU_452676_0_0_1; -.
DR InParanoid; N1JN32; -.
DR OrthoDB; 73846at2759; -.
DR Proteomes; UP000015441; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:TreeGrafter.
DR GO; GO:0050661; F:NADP binding; IEA:TreeGrafter.
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; IPR050838; Ketopantoate_reductase.
DR InterPro; IPR013752; KPA_reductase.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR PANTHER; PTHR43765; 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:UP000015441}.
FT DOMAIN 224..364
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 452..585
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 603 AA; 67787 MW; CCA614C429691E47 CRC64;
MEISTCSVAV DYVQKELSRN IFPLIGNEGN MNQKTSHSIS ACKPDNKVPR GQNININLNS
THTSLDSAHI HSLITNSSSI ISKRNERSDD LAYDLSTQPY ENNENVQNST NYNHIDNTMH
SKTTGKLTAT NLFDTRRENY QKNAIDETVN PNKQPPSASK LSTSLNIWGP QSHQVDSSTD
THKFISHPEQ SLNHSLEYQG SHVTPQKNAM NGSKLQNYIE SETIHILGMG PAGQFIAHSI
ARLEHAPPVV LLMHRPLQIQ LWHDEGAAIR IYRGGKIFSE SNFHVESSAN FRRTSPEQNF
VGFGENLQHT SEPPNYAIDT LIVATPASAT VSALLSVQHR IRPTTTICLI QDGMGMIHKI
NRIVFPDAEK RPIYVLGYMR HDLGPTDNFF SHFERSPSKL YCSKMPRISL TEPQNGATIE
RVDFSWSPQA RHLVGTLLRT PELNTAALGH KDFHKRQLSR LVVSAVIEPL AVAFDCVNGQ
LLENFGVANI MRGLIQEISV LIPVLPELRN IKNVQRDFSP ERLEKKILNR IQKSDVMVSS
MLAAIRQGKK ADIDFFTGYL LERARELNIP CPVNQVMYHL VKAKQTMKLR ESQNDIPYVV
NTT
//
