ID A0A5N7DBG5_9EURO Unreviewed; 345 AA.
AC A0A5N7DBG5;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 02-APR-2025, entry version 13.
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=BDV37DRAFT_294422 {ECO:0000313|EMBL:KAE8403495.1};
OS Aspergillus pseudonomiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1506151 {ECO:0000313|EMBL:KAE8403495.1, ECO:0000313|Proteomes:UP000325579};
RN [1] {ECO:0000313|EMBL:KAE8403495.1, ECO:0000313|Proteomes:UP000325579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119388 {ECO:0000313|EMBL:KAE8403495.1,
RC ECO:0000313|Proteomes:UP000325579};
RG DOE Joint Genome Institute;
RA Mondo S., 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., Riley R.,
RA Salamov A., Simmons B.A., Magnuson J.K., Henrissat B., Mortensen U.H.,
RA Larsen T.O., Devries R.P., Grigoriev I.V., Machida M., Baker S.E.,
RA Andersen M.R., Cantor M.N., Hua S.X.;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ML736776; KAE8403495.1; -; Genomic_DNA.
DR RefSeq; XP_031940814.1; XM_032089625.1.
DR AlphaFoldDB; A0A5N7DBG5; -.
DR GeneID; 43674316; -.
DR OrthoDB; 3609at2759; -.
DR Proteomes; UP000325579; 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:UP000325579}.
FT DOMAIN 8..166
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 200..323
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 345 AA; 36570 MW; C710D5284CB1179A CRC64;
MSNTKANILL IGSGGVGTIA ALNLEAGNLA QVTAVLRSNY QAVASNGFNI TSCDHGTLKG
WKPTTTTNRI PEKMAPEAPK YDYIVCTTKV IADCPPLTAD LIKPAVTPGH TVIVLIQNGL
NIEKPYFAAF PENIVLSGIS MIDSHEVAPG VIEHGSADDL VIGAFRNPNL DCAVEVAAAE
RFVGLYSAAG KTKCILGLDV AYSRWRKLIF NACLNSICAL TGLDTGRIRL AGDAVEMLVR
PAMEEIRAAA GSVGVNLPAE VCEEVIGAYP VTMYLPPSML EDVWKGNLIE VESIVGEPLR
VGRANGVAMP TLSVLYNLLK GVQWKTKEQR GLIEIPAQGG SVAES
//
