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Database: UniProt
Entry: M7WR78_RHOT1
LinkDB: M7WR78_RHOT1
Original site: M7WR78_RHOT1 
ID   M7WR78_RHOT1            Unreviewed;       472 AA.
AC   M7WR78;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Protein of ketopantoate reductase family {ECO:0000313|EMBL:EMS20576.1};
GN   ORFNames=RHTO_02524 {ECO:0000313|EMBL:EMS20576.1};
OS   Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS20576.1, ECO:0000313|Proteomes:UP000016926};
RN   [1] {ECO:0000313|EMBL:EMS20576.1, ECO:0000313|Proteomes:UP000016926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NP11 {ECO:0000313|EMBL:EMS20576.1,
RC   ECO:0000313|Proteomes:UP000016926};
RX   PubMed=23047670; DOI=10.1038/ncomms2112;
RA   Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA   Ye M., Zou H., Zou H., Zhao Z.K.;
RT   "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL   Nat. Commun. 3:1112-1112(2012).
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DR   EMBL; KB722660; EMS20576.1; -; Genomic_DNA.
DR   RefSeq; XP_016271695.1; XM_016416198.1.
DR   AlphaFoldDB; M7WR78; -.
DR   GeneID; 27366537; -.
DR   eggNOG; ENOG502RYJ0; Eukaryota.
DR   HOGENOM; CLU_031468_2_1_1; -.
DR   OrthoDB; 1548520at2759; -.
DR   Proteomes; UP000016926; 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:SF43; APBA_C DOMAIN-CONTAINING PROTEIN; 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;
FT   DOMAIN          7..168
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          228..394
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   REGION          307..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          442..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..328
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   472 AA;  51814 MW;  323F629C4270AD2D CRC64;
     MSSPIDILIV GFGAVGTVYG WVLSQNSNVR VTAIARSSYD EMSNGIRIES EKYGEISGWK
     PYRLVRDADE ANDRAYKYII CSTKALPDLL PTASVLAPFL ESRHAQDTVD LEDGPCVVLI
     QNGIGIEHPL ASAYPSIPII SVVAWIGANL KPGGRVTHGM LEKLIMGLYT GEGSEPVEGE
     QVEDAFGDPH GYRKGPDGPE RLEEGKRRLK VFADLINNGG GTAVVVDDIQ SKRYEKNLWN
     AALSSLCTLS RCTVSQAVDP AVLPYTLPVV RRTMLEVMYV ARAWGYQEDV LPLRCVDEAI
     KITINNYQRP SQHSDPNTPF SPQRSDPSYG FPTEGDLAKE SFESSYNFKP SMLLDAEAGR
     PMELEPIIGS LLDRARAKGV PTPRLDMAYS ALKIQQDLAI RAYSSSATYQ EHIKNWLSRP
     PAVAGLGAAG RKAWERAVKK AELPEHEQGS VEMAGWRDKI PGKPVRADSK NI
//
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