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
//