ID E5A671_LEPMJ Unreviewed; 384 AA.
AC E5A671;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 13-SEP-2023, entry version 60.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=LEMA_P083550.1 {ECO:0000313|EMBL:CBX99116.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|EMBL:CBX99116.1, ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870}.
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DR EMBL; FP929135; CBX99116.1; -; Genomic_DNA.
DR RefSeq; XP_003842595.1; XM_003842547.1.
DR AlphaFoldDB; E5A671; -.
DR STRING; 985895.E5A671; -.
DR EnsemblFungi; CBX99116; CBX99116; LEMA_P083550.1.
DR GeneID; 13282494; -.
DR eggNOG; ENOG502QT3Y; Eukaryota.
DR HOGENOM; CLU_031468_2_0_1; -.
DR InParanoid; E5A671; -.
DR OMA; NLGYHSG; -.
DR OrthoDB; 1548520at2759; -.
DR Proteomes; UP000002668; Genome.
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; PTHR21708:SF42; 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.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002668}.
FT DOMAIN 6..159
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 217..343
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 162..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 384 AA; 41542 MW; D1386D2C1F6D9002 CRC64;
MPPTTILIVG AGAIGAFYAS RLALAPNVSV SVICRSNYTA VSSSGFSLTS PQYGDYNFVP
AHTFRDTEEA RASGIAWDYI VVSTKALPDV SDDSAILTGL VGGETAIVLI QNGLGVEEPY
RTRFPQAPIC SAVTIASCAQ PQPGVIVHNR WTRINSGPYL PHLDTLPSTN STTTSPTTTN
GTPLPTDPTA IHKNETFIRL LVTGGIKDAT PYPHSKLQLL RWHKLAINAS FNPSSVLTLC
PPNHTLASDP ESRLHLLATM HEILATAPKI LGEPMPEDFA SPEQIIASTL RNTSGSRPSM
ALDWLGGKRL EMEVILGNPI RMARERGLEM PRLQSLYALV RMAQQVRERE GREAREERGG
SRMWMGGFGC VCVCVSFGTF SSLE
//