ID A0A507AX43_9PEZI Unreviewed; 346 AA.
AC A0A507AX43;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 18-JUN-2025, entry version 18.
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=E0L32_009234 {ECO:0000313|EMBL:TPX09491.1};
OS Thyridium curvatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Thyridiales; Thyridiaceae; Thyridium.
OX NCBI_TaxID=1093900 {ECO:0000313|EMBL:TPX09491.1, ECO:0000313|Proteomes:UP000319257};
RN [1] {ECO:0000313|EMBL:TPX09491.1, ECO:0000313|Proteomes:UP000319257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D216 {ECO:0000313|EMBL:TPX09491.1,
RC ECO:0000313|Proteomes:UP000319257};
RA Varaljay V.A., Lyon W.J., Crouch A.L., Drake C.E., Hollomon J.M.,
RA Nadeau L.J., Nunn H.S., Stevenson B.S., Bojanowski C.L.,
RA Crookes-Goodson W.J.;
RT "Draft genome sequence of the filamentous fungus Phialemoniopsis curvata
RT isolated from diesel fuel.";
RL Submitted (JUN-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 -!- 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:TPX09491.1}.
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DR EMBL; SKBQ01000066; TPX09491.1; -; Genomic_DNA.
DR RefSeq; XP_030991202.1; XM_031144176.1.
DR AlphaFoldDB; A0A507AX43; -.
DR FunCoup; A0A507AX43; 27.
DR STRING; 1093900.A0A507AX43; -.
DR GeneID; 41976681; -.
DR InParanoid; A0A507AX43; -.
DR OrthoDB; 3609at2759; -.
DR Proteomes; UP000319257; 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 FunFam; 3.40.50.720:FF:000609; 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 NCBIfam; TIGR00745; apbA_panE; 1.
DR PANTHER; PTHR21708; PROBABLE 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR PANTHER; PTHR21708:SF40; REDUCTASE FAMILY PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G14497)-RELATED; 1.
DR Pfam; PF02558; ApbA; 1.
DR Pfam; PF08546; ApbA_C; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 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:UP000319257}.
FT DOMAIN 38..181
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 214..337
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 346 AA; 38239 MW; DA238F69D6ED3B07 CRC64;
MSSDITPPAY NTDSSPGRKH RDLPKFLDYD FSNLEFRIGS FYAFIFSRCK DANVTVVARS
NYETVKAHGL KLNSIVHGDH IVRFDRVLSS PAKAGRTFDY VVCAHKAIDE DNSAGSLACV
IDPQKITVVL IQNGIGIEEP FRQAFPPMTI ISCVTWTGAK QIELGVVQHL ERWEGLQIGL
YSGSACDESR DRQSLDIFAA LLQQGGTRYE VVPDIQQLRW KKIVSNAAWN PITTLTQMKT
HAWLQSSPDA LPLTRKLMTE VVTIAQKAGV DLDPNTPGLI LEEMINNASV GSSMFNDLVA
GKPMEVEPIL GKPLRKAREL GVDAPILETL YTLVTAVNIR SKQAVK
//
