ID F4RQT2_MELLP Unreviewed; 367 AA.
AC F4RQT2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 13-SEP-2023, entry version 41.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=MELLADRAFT_64262 {ECO:0000313|EMBL:EGG05094.1};
OS Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7) (Poplar leaf
OS rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Melampsoraceae; Melampsora.
OX NCBI_TaxID=747676 {ECO:0000313|Proteomes:UP000001072};
RN [1] {ECO:0000313|Proteomes:UP000001072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=98AG31 / pathotype 3-4-7 {ECO:0000313|Proteomes:UP000001072};
RX PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA Grigoriev I.V., Szabo L.J., Martin F.;
RT "Obligate biotrophy features unraveled by the genomic analysis of rust
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
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DR EMBL; GL883114; EGG05094.1; -; Genomic_DNA.
DR RefSeq; XP_007411459.1; XM_007411397.1.
DR AlphaFoldDB; F4RQT2; -.
DR STRING; 747676.F4RQT2; -.
DR EnsemblFungi; EGG05094; EGG05094; MELLADRAFT_64262.
DR GeneID; 18930236; -.
DR KEGG; mlr:MELLADRAFT_64262; -.
DR VEuPathDB; FungiDB:MELLADRAFT_64262; -.
DR eggNOG; ENOG502QT3Y; Eukaryota.
DR HOGENOM; CLU_031468_2_0_1; -.
DR InParanoid; F4RQT2; -.
DR OrthoDB; 1548520at2759; -.
DR Proteomes; UP000001072; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; 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; IPR013752; KPA_reductase.
DR InterPro; IPR013332; KPR_N.
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.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001072}.
FT DOMAIN 19..177
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 227..357
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 367 AA; 41217 MW; 314141729BF15753 CRC64;
MSTQSQPSTS KPDPIHILIG AIGAFYGSRL HQPNHPQRPV LVSLTCRSNY KHVSSNGLSM
KTRSFGDYEF KPYRVYSSVI SASKNNSPKW DFVILCTKVL IGDINDSEIL LPLFNSTTQS
SNPTIVLIQN GVGIETIHRQ RFPNVPIISG VTVVNAEQIE LGVVRQNRWT RISLGSFLEF
EYDDQKIKSK THQNSELETK STHQIDLLVE LLKQGGIKDA EVYSERDLQL VRWHKLAINA
SMNPSSILCG GLTNPEMVAD PAIRIHLTEC MKEVLRAACV IFQLESMPTG FASPEEILES
ITRAKGEAIK PSMLVDWEQN RPLEIEAILA IPIRIAKRFG VELNRLQSMY AFLNQLQRQR
THGSAKL
//