ID A0A0J0XZL3_9TREE Unreviewed; 526 AA.
AC A0A0J0XZL3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00013014};
DE EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014};
DE AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024};
GN ORFNames=CC85DRAFT_281585 {ECO:0000313|EMBL:KLT46478.1};
OS Cutaneotrichosporon oleaginosum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT46478.1, ECO:0000313|Proteomes:UP000053611};
RN [1] {ECO:0000313|EMBL:KLT46478.1, ECO:0000313|Proteomes:UP000053611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBC0246 {ECO:0000313|EMBL:KLT46478.1,
RC ECO:0000313|Proteomes:UP000053611};
RG DOE Joint Genome Institute;
RA Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT T. oleaginosus allow insights into substrate utilization and the diverse
RT evolutionary trajectories of mating systems in fungi.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870}.
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DR EMBL; KQ087177; KLT46478.1; -; Genomic_DNA.
DR RefSeq; XP_018282969.1; XM_018421667.1.
DR AlphaFoldDB; A0A0J0XZL3; -.
DR STRING; 879819.A0A0J0XZL3; -.
DR GeneID; 28982270; -.
DR OrthoDB; 1354873at2759; -.
DR Proteomes; UP000053611; Unassembled WGS sequence.
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; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR PANTHER; PTHR43765:SF2; 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 Coiled coil {ECO:0000256|SAM:Coils}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053611}.
FT DOMAIN 5..189
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 263..398
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 482..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 421..448
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 501..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 526 AA; 56847 MW; FCD27AF599CD63F2 CRC64;
MMRLHVLGIG SVGTLLAHHL RLANPNTPIS LVFRNAAAFS KKRFRKDGVN RPTLKVTRTE
GDTLMTDGFD VDVAMSGKLP ALVEAAEQDG MDFVNAGGPI DSLIVCTKTQ ATAEAIEGLH
SRLSSSSVIT LLQNGMGVYD ELCAKFWPDP VTRPNFVLGT TTHGIAPAGE TGSVLHMSPP
GQGAIKWGVV PDPRKQIDFE TWLWGRPVGD LPTLTPPESP SLPLRTPPDG PGTENLHATL
EALLSITPLS PTLLPMPTLY NELLIKLALN AAINPLTAVL GGGYLQNGSL SRSAPGHRLV
QQVTKESSQV LTAYMHNLFA PHPAPADTVR LFSYESLLHR VQSVITATKG NTSSMANDVK
NGRMTEIDYI NGHLASLGHR LGVQTPVNRM LVQMVKFKAE VGGLGGTVYP RVRQTVREAE
EEALEARRLS LEERKVSLQE RAMLLKEERT AEAKRAKREW KRTVRRNAAV ARNLRAAEVE
AAIRGGADPT EVLRATEAEA SEASGSGNSE WTSASSDEGE GSSRRR
//