ID A0A5N6T2X5_ASPPS Unreviewed; 344 AA.
AC A0A5N6T2X5;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 02-APR-2025, entry version 12.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|RuleBase:RU362068};
DE EC=1.1.1.169 {ECO:0000256|RuleBase:RU362068};
DE AltName: Full=Ketopantoate reductase {ECO:0000256|RuleBase:RU362068};
GN ORFNames=BDV38DRAFT_269170 {ECO:0000313|EMBL:KAE8140647.1};
OS Aspergillus pseudotamarii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=132259 {ECO:0000313|EMBL:KAE8140647.1, ECO:0000313|Proteomes:UP000325672};
RN [1] {ECO:0000313|EMBL:KAE8140647.1, ECO:0000313|Proteomes:UP000325672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117625 {ECO:0000313|EMBL:KAE8140647.1,
RC ECO:0000313|Proteomes:UP000325672};
RG DOE Joint Genome Institute;
RA Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA Baker S.E., Andersen M.R.;
RT "Friends and foes A comparative genomics study of 23 Aspergillus species
RT from section Flavi.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC pantoic acid. {ECO:0000256|RuleBase:RU362068}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantoate + NADP(+) = 2-dehydropantoate + NADPH + H(+);
CC Xref=Rhea:RHEA:16233, ChEBI:CHEBI:11561, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15980, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.169; Evidence={ECO:0000256|RuleBase:RU362068};
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870, ECO:0000256|RuleBase:RU362068}.
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DR EMBL; ML743561; KAE8140647.1; -; Genomic_DNA.
DR RefSeq; XP_031916710.1; XM_032056914.1.
DR AlphaFoldDB; A0A5N6T2X5; -.
DR GeneID; 43641124; -.
DR OrthoDB; 3609at2759; -.
DR Proteomes; UP000325672; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:InterPro.
DR FunFam; 1.10.1040.10:FF:000017; 2-dehydropantoate 2-reductase; 1.
DR Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
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; IPR051402; KPR-Related.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR00745; apbA_panE; 1.
DR PANTHER; PTHR21708:SF30; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 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.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000325672}.
FT DOMAIN 8..165
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 198..322
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 344 AA; 36702 MW; 031CF1BEEE312B98 CRC64;
MSTPKANILL IGSGGVGTIA ALNLEAGKLA QVTAVLRSNY QAVLSNGFNI TSCDHGVLKG
WKPTTITNLI PETKPESPKY DYIVCTTKVI TDCPPSTVDL IKPAVTPGHT VIVLIQNGLN
IEKPYFAAFP ENIVLSGISM IDSHEVAPGV IEHGSADDLV IGAFRNPNLD VGVEAAAAER
FVGLYSAAGK TKCILGPDVE YSRWRKLVFN ACLNPICALT GLDTGRIRLA GDAVDMLVRP
AMEEIRAAAR SVGVDLPEDV CEKVIGAYPV TMYLPPSMLE DVWKGNLVEV ESIVGEPLRV
GRANGVAMPT LSVLYNLLKG VQWRTKEKRG LIEIPAQGSD VADS
//
