ID A0A255I8A9_9FIRM Unreviewed; 306 AA.
AC A0A255I8A9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=C8E03_102349 {ECO:0000313|EMBL:PXV93580.1}, CG710_003650
GN {ECO:0000313|EMBL:RDY32537.1};
OS Lachnotalea glycerini.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnotalea.
OX NCBI_TaxID=1763509 {ECO:0000313|EMBL:RDY32537.1, ECO:0000313|Proteomes:UP000216411};
RN [1] {ECO:0000313|EMBL:RDY32537.1, ECO:0000313|Proteomes:UP000216411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCRI-19302 {ECO:0000313|EMBL:RDY32537.1,
RC ECO:0000313|Proteomes:UP000216411};
RX PubMed=29051240;
RA Maheux A.F., Boudreau D.K., Berube E., Boissinot M., Raymond F.,
RA Brodeur S., Corbeil J., Isabel S., Omar R.F., Bergeron M.G.;
RT "Draft Genome Sequence of a Sporulating and Motile Strain of Lachnotalea
RT glycerini Isolated from Water in Quebec City, Canada.";
RL Genome Announc. 5:e01059-17(2017).
RN [2] {ECO:0000313|EMBL:PXV93580.1, ECO:0000313|Proteomes:UP000247523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28816 {ECO:0000313|EMBL:PXV93580.1,
RC ECO:0000313|Proteomes:UP000247523};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:RDY32537.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCRI-19302 {ECO:0000313|EMBL:RDY32537.1};
RA Quirk P.G., Krulwich T.A.;
RL Submitted (JUL-2018) 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 -!- 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:RDY32537.1}.
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DR EMBL; QICS01000002; PXV93580.1; -; Genomic_DNA.
DR EMBL; NOKA02000003; RDY32537.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255I8A9; -.
DR OrthoDB; 9793586at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000216411; Unassembled WGS sequence.
DR Proteomes; UP000247523; Unassembled WGS sequence.
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 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: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|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362068};
KW Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000216411}.
FT DOMAIN 7..148
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 306 AA; 34456 MW; 9D1DDC8E0B705B5A CRC64;
MSIRNAALIG TGAVGGVYAM HLHNTYGMEF YVVAGDSRKK RIEQNGIKVN QMTYYPQLIE
PSETKHKMDL IIIAVKNYDL EQAIEDIQNL VKVGTIILPL LNGITASDRL CVAYPKAKIM
LGLSMGIDAI RTEEGIVNTD DGVIQFGYED NTVKAKEVED VLCYLTKAGI KAKVYSDMKR
MQWRKWMLNV GVNQASAITG AKFKYFGRNK ELFTLFRNAM MEVLELAKAA NVKITMEDIT
HIEEVILNFT PEGKTSMLQD VEAMRKTEID YFAGTVIEYG VKYHVPTPVN EVLYLALKAK
ENIYLD
//
