ID A0A6A6YTS4_9PEZI Unreviewed; 333 AA.
AC A0A6A6YTS4;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 18-JUN-2025, entry version 24.
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=BDZ99DRAFT_569018 {ECO:0000313|EMBL:KAF2812322.1,
GN ECO:0000313|RefSeq:XP_033579286.1};
OS Mytilinidion resinicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Mytilinidiales; Mytilinidiaceae; Mytilinidion.
OX NCBI_TaxID=574789 {ECO:0000313|EMBL:KAF2812322.1};
RN [1] {ECO:0000313|EMBL:KAF2812322.1, ECO:0000313|RefSeq:XP_033579286.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 304.34 {ECO:0000313|EMBL:KAF2812322.1,
RC ECO:0000313|RefSeq:XP_033579286.1};
RA Haridas S., Albert R., Binder M., Bloem J., LaButti K., Salamov A.,
RA Andreopoulos B., Baker S., Barry K., Bills G., Bluhm B., Cannon C.,
RA Castanera R., Culley D., Daum C., Ezra D., Gonzalez J., Henrissat B.,
RA Kuo A., Liang C., Lipzen A., Lutzoni F., Magnuson J., Mondo S., Nolan M.,
RA Ohm R., Pangilinan J., Park H.-J., Ramirez L., Alfaro M., Sun H., Tritt A.,
RA Yoshinaga Y., Zwiers L.-H., Turgeon B., Goodwin S., Spatafora J., Crous P.,
RA Grigoriev I.;
RT "101 Dothideomycetes genomes: a test case for predicting lifestyles and
RT emergence of pathogens.";
RL Stud. Mycol. 0:0-0(2020).
RN [2] {ECO:0000313|RefSeq:XP_033579286.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 304.34 {ECO:0000313|RefSeq:XP_033579286.1};
RG NCBI Genome Project;
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:XP_033579286.1}
RP IDENTIFICATION.
RC STRAIN=CBS 304.34 {ECO:0000313|RefSeq:XP_033579286.1};
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
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; MU003697; KAF2812322.1; -; Genomic_DNA.
DR RefSeq; XP_033579286.1; XM_033727842.1.
DR GeneID; 54468735; -.
DR OrthoDB; 3609at2759; -.
DR Proteomes; UP000504636; Unplaced.
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:UP000504636}.
FT DOMAIN 8..164
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 191..320
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 333 AA; 35823 MW; 6B0F1E1191C63B14 CRC64;
MADRPNVLLF GTGAVGSVYL YLLSKHCDTT AICRSNYAAA KANGFTIHSP QIFGETLHFN
PRVARTCAEA TTLDVGSPAK PFDYIVICSK VTPNTIPALI APAVTPNHTV IVLLQNGINI
EAEYTAAFPT NPIISGVVYL PVTQTSPGVI QHGDIERLEL GAYPSSASSA PTTRFAELIQ
AGGGTAEVWD DVQFKRWAKL LVNGSWNPIC ALTRSSDVRF MASSAGATDF VFAMMLELVA
IAKAHGYANV DEKVARAQLE RFKKRIETSK GVGSEPSMLT DVREGRRMEV EAIVGNAVRM
AKEKGVDCVR LETVYFLAKG LDEAIGRALK GSK
//
