ID A0A0F4LZ30_9LACO Unreviewed; 311 AA.
AC A0A0F4LZ30;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 18-JUN-2025, entry version 35.
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=JG30_02940 {ECO:0000313|EMBL:KJY62831.1};
OS Bombilactobacillus mellifer.
OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Bombilactobacillus.
OX NCBI_TaxID=1218492 {ECO:0000313|EMBL:KJY62831.1, ECO:0000313|Proteomes:UP000033558};
RN [1] {ECO:0000313|EMBL:KJY62831.1, ECO:0000313|Proteomes:UP000033558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bin4 {ECO:0000313|EMBL:KJY62831.1,
RC ECO:0000313|Proteomes:UP000033558};
RA Ellegaard K.M., Tamarit D., Javelind E., Olofsson T., Andersson S.G.,
RA Vasquez A.;
RT "Comparative genomics of the lactic acid bacteria isolated from the honey
RT bee gut.";
RL Submitted (JAN-2015) 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:KJY62831.1}.
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DR EMBL; JXJQ01000003; KJY62831.1; -; Genomic_DNA.
DR RefSeq; WP_046315570.1; NZ_JAMBJK010000023.1.
DR AlphaFoldDB; A0A0F4LZ30; -.
DR STRING; 1218492.JG30_02940; -.
DR PATRIC; fig|1218492.5.peg.410; -.
DR HOGENOM; CLU_031468_0_0_9; -.
DR OrthoDB; 9800163at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000033558; 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 NCBIfam; NF005088; PRK06522.1-2; 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:UP000033558}.
FT DOMAIN 3..153
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 180..306
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 311 AA; 34640 MW; D9DC1442F3F705D8 CRC64;
MNITIVGAGG MGSRFAVMLK QAGNDVTLID GWKDNVQAIR EHGIQAQYNG DPLVVKLPIY
ELAEVDQIPA TSELVILFVK SNQLDQTCNQ IKKLLTPNTY ILCLLNGLGH EEVLQKYIDT
NRLLLGITMW TAGMQGPGHP ILQGNGNIEL QNFGDQGEDF AQKVVQVMDD AGLNAVYSQN
VKYSIWRKAC VNGTLNCLCS LLECNMKQLG QTKEAPEFLK TIIAEFAAVA SHEGVDLDQK
EVYQHIAETF DGDIAEHYPS MYQDLVQNHR LTEIDYINGA VWRKGQKYGV PTPYCQLITQ
LIHAKEQILC K
//
