ID A0A1S1NU47_9MYCO Unreviewed; 305 AA.
AC A0A1S1NU47;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 05-FEB-2025, entry version 23.
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=BKN37_00910 {ECO:0000313|EMBL:OHV06789.1};
OS Mycobacterium talmoniae.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Mycobacteriaceae; Mycobacterium.
OX NCBI_TaxID=1858794 {ECO:0000313|EMBL:OHV06789.1, ECO:0000313|Proteomes:UP000179734};
RN [1] {ECO:0000313|EMBL:OHV06789.1, ECO:0000313|Proteomes:UP000179734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NE-TNMC-100812 {ECO:0000313|Proteomes:UP000179734};
RA Greninger A.L., Elliott B., Vasireddy S., Vasireddy R.;
RT "Genome sequence of Mycobacterium talmonii.";
RL Submitted (OCT-2016) 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 -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC {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:OHV06789.1}.
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DR EMBL; MLQM01000002; OHV06789.1; -; Genomic_DNA.
DR RefSeq; WP_071019766.1; NZ_MLQM01000002.1.
DR AlphaFoldDB; A0A1S1NU47; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000179734; 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:UniProtKB-UniPathway.
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:SF26; 2-DEHYDROPANTOATE 2-REDUCTASE; 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 Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000179734}.
FT DOMAIN 3..151
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 177..301
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 305 AA; 31058 MW; 2C74D001F7CDBDD7 CRC64;
MKIAVIGCGA MGSVYAAKLA AAGHDVLAVD RADDHIAQIA AHGLRISGPG YDQVVAMRAA
TAAPAEEMDL VVLAVKAADV AAGAGDALPL LGATTPLLTI QNGLGSADTV ADIVGGHRVA
VGIASGFGAS RRAPGYVHHN AMRAMRFGAY SSLPFATVTE IAAAWSEAGF DAAAVADIAA
MQWEKLICNV AYSAPCALTG MTVGQVMDDP DMGPVSRAAA TEAWAVARAA GIAVDVTDPV
AHVRAFGAQL PEAKPSALLD HEARRVSEID VINGAVVRQA ARVGEPVPVN TTLTALVKAV
ERRWG
//
