ID A0A7J5BSL2_9MICO Unreviewed; 332 AA.
AC A0A7J5BSL2;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 02-APR-2025, entry version 15.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465, ECO:0000256|RuleBase:RU362068};
DE EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014, ECO:0000256|RuleBase:RU362068};
DE AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024, ECO:0000256|RuleBase:RU362068};
GN ORFNames=F8O01_08620 {ECO:0000313|EMBL:KAB1657297.1};
OS Pseudoclavibacter chungangensis.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC Microbacteriaceae; Pseudoclavibacter.
OX NCBI_TaxID=587635 {ECO:0000313|EMBL:KAB1657297.1, ECO:0000313|Proteomes:UP000467240};
RN [1] {ECO:0000313|EMBL:KAB1657297.1, ECO:0000313|Proteomes:UP000467240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23821 {ECO:0000313|EMBL:KAB1657297.1,
RC ECO:0000313|Proteomes:UP000467240};
RA Li Y.;
RT "Phylogeny of genus Pseudoclavibacter and closely related genus.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC pantoic acid. {ECO:0000256|ARBA:ARBA00002919,
CC 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|ARBA:ARBA00048793,
CC 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|ARBA:ARBA00004994, 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:KAB1657297.1}.
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DR EMBL; WBJZ01000009; KAB1657297.1; -; Genomic_DNA.
DR RefSeq; WP_158040462.1; NZ_JACCFV010000001.1.
DR AlphaFoldDB; A0A7J5BSL2; -.
DR OrthoDB; 9796561at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000467240; 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:0050661; F:NADP binding; IEA:TreeGrafter.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR050838; Ketopantoate_reductase.
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; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR PANTHER; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362068};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655,
KW ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000467240}.
FT DOMAIN 3..147
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 174..315
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 332 AA; 33805 MW; 781974ED46B34250 CRC64;
MRIGVIGAGA VGTTVAALLA AAGHEVHVAA RRATAETIAA DGLHLDGAFG RHAVAVAADE
RLPPGLDLAL CATQAHDAAA ALAANADALV ATSVVALQNG LGGVDTAARV LGGRRDVHGA
LVLFAATGTA AGRAVATARG PVFVGAGSGW ASPASRRVAT ILASALPARA VDRFTGAQWA
KLLVNHVNAL PAITGSSVQA VSRDPGLVRV LARSLREAVL VAERQRVRIT GLGPLRQVDV
HALGHRPFDD AVDVARRLGH AFGPVPNPAS TLQAIRRGRR TEIDELNGRV ATLAAHHGID
APVERTLTRL VHEVERSGRF LAPGAVVAAV SA
//
