ID A0A2T4H119_FUSCU Unreviewed; 330 AA.
AC A0A2T4H119;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, 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=FCULG_00008444 {ECO:0000313|EMBL:PTD09503.1}, HYE67_007366
GN {ECO:0000313|EMBL:QPC65135.1};
OS Fusarium culmorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5516 {ECO:0000313|EMBL:PTD09503.1, ECO:0000313|Proteomes:UP000241587};
RN [1] {ECO:0000313|EMBL:PTD09503.1, ECO:0000313|Proteomes:UP000241587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV {ECO:0000313|EMBL:PTD09503.1,
RC ECO:0000313|Proteomes:UP000241587};
RA Schmidt R.;
RT "Fusarium culmorum secondary metabolites in fungal-bacterial-plant
RT interactions.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QPC65135.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Class2-1B {ECO:0000313|EMBL:QPC65135.1};
RA Yuan Z.;
RT "The chromosome-scale genome resource for two endophytic Fusarium species:
RT F. culmorum and F. pseudograminearum.";
RL Submitted (NOV-2020) 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 + H(+) + NADPH;
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; PVEM01000003; PTD09503.1; -; Genomic_DNA.
DR EMBL; CP064749; QPC65135.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4H119; -.
DR OMA; FKPSMLQ; -.
DR Proteomes; UP000241587; Unassembled WGS sequence.
DR Proteomes; UP000663297; Chromosome 3.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:UniProtKB-EC.
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; PTHR21708:SF30; 2-REDUCTASE FAMILY PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G00740)-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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000241587}.
FT DOMAIN 10..168
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 201..320
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 330 AA; 35943 MW; 8EDE573A695D3DFA CRC64;
MDKVNGKARI LVVGCGGIGC MAALNLEFGG QAQVTAVLRS SYQIVEKQGF TINSVDHGQV
RGFRPTEILS AVPDVSQSGI LPFDYIICAT KNTPDVSMPV AELIRPAVTT SYSTILLLQN
GLNIEVPLLE AFPDNVILSG ISVCGSSEPE SGTIEHNVHD ELWIGPFRDV GNVADRAKDI
VARYNAGGRC TCHYDSNVTF SRWKKLLYNA VYNPVSALTK LDTGDLQLCP GLVDEVVRPG
MKEIQAAAAA YGQEITDEMI EATITTEPIE AHVSPSMLVD VRKSQYIEFE NLIGEPLRCA
KAQKIATPIL QNHYSLAKSY QWKLKSKRAS
//
