ID A0A1Q5QC34_9EURO Unreviewed; 438 AA.
AC A0A1Q5QC34;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=UA08_01983 {ECO:0000313|EMBL:OKL63441.1};
OS Talaromyces atroroseus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Trachyspermi.
OX NCBI_TaxID=1441469 {ECO:0000313|EMBL:OKL63441.1, ECO:0000313|Proteomes:UP000214365};
RN [1] {ECO:0000313|EMBL:OKL63441.1, ECO:0000313|Proteomes:UP000214365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 11181 {ECO:0000313|EMBL:OKL63441.1,
RC ECO:0000313|Proteomes:UP000214365};
RA Rasmussen K.B., Rasmussen S., Petersen B., Sicheritz-Ponten T.,
RA Mortensen U.H., Thrane U.;
RT "Talaromyces atroroseus IBT 11181 draft genome.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OKL63441.1}.
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DR EMBL; LFMY01000002; OKL63441.1; -; Genomic_DNA.
DR RefSeq; XP_020123562.1; XM_020261707.1.
DR AlphaFoldDB; A0A1Q5QC34; -.
DR STRING; 1441469.A0A1Q5QC34; -.
DR GeneID; 31001738; -.
DR OrthoDB; 1354873at2759; -.
DR Proteomes; UP000214365; 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 Reference proteome {ECO:0000313|Proteomes:UP000214365}.
FT DOMAIN 128..243
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 281..413
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 438 AA; 49211 MW; 991C6954401EC03F CRC64;
MQPSLVNPVQ KETLDDATHR SGSLSGRIHI IGLGNVGCFV AHSLASRKTR PPITLLLHNR
DMYSRWLQRK QSIALMTNGL DDIKTGFDVN VFNENTWHSL PYWNQHDNIN NSNVDNHEPE
ILISRRQEDP DLESTHAFET DEEMDLLTSE RDDEKIECII ITTKAPQTVQ ALSSVSHRLT
PDSTVLFLQN GMGVIDEVNK EIFPDPEKRP HYIQGVISHG LRMKRPFHVE YTGLGTTILG
ALPSRTTSDV QEEDWAPSTK YLLRTLTLTP PLVAVAESAV NVLQCQLEKL AMNCVINPFT
VLLDSQNGEL LYNYHITRSM RLLLAEISTV ICALPELEGV PGIQARFATE RLKNLAVNLA
NKTAANTSSM LQDVQALKRT EIEYINGYIV RRGDELGIRC VLNYMIMQLV LGKNHIMRLR
EAGAVPLDTS NLETEDEA
//
