ID A0A292YBA1_9BACT Unreviewed; 265 AA.
AC A0A292YBA1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 18-JUN-2025, entry version 38.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465};
DE EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014};
DE AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024};
GN ORFNames=LNAT_P0672 {ECO:0000313|EMBL:GAX87377.1};
OS Lebetimonas natsushimae.
OC Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
OC Nautiliales; Nautiliaceae; Lebetimonas.
OX NCBI_TaxID=1936991 {ECO:0000313|EMBL:GAX87377.1, ECO:0000313|Proteomes:UP000217944};
RN [1] {ECO:0000313|EMBL:GAX87377.1, ECO:0000313|Proteomes:UP000217944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS1857 {ECO:0000313|EMBL:GAX87377.1,
RC ECO:0000313|Proteomes:UP000217944};
RX PubMed=28690052; DOI=10.1016/j.syapm.2017.06.002;
RA Nagata R., Takaki Y., Tame A., Nunoura T., Muto H., Mino S., Sawayama S.,
RA Takai K., Nakagawa S.;
RT "Lebetimonas natsushimae sp. nov., a novel strictly anaerobic, moderately
RT thermophilic chemoautotroph isolated from a deep-sea hydrothermal vent
RT polychaete nest in the Mid-Okinawa Trough.";
RL Syst. Appl. Microbiol. 40:352-356(2017).
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 -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004994}.
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:GAX87377.1}.
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DR EMBL; BDME01000001; GAX87377.1; -; Genomic_DNA.
DR RefSeq; WP_096258517.1; NZ_BDME01000001.1.
DR AlphaFoldDB; A0A292YBA1; -.
DR OrthoDB; 5333395at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000217944; 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 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; IPR013752; KPA_reductase.
DR InterPro; IPR051402; KPR-Related.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:GAX87377.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000217944}.
FT DOMAIN 3..106
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 154..252
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 265 AA; 30848 MW; 802C8E72EF0A61B7 CRC64;
MKILVIGPGG VGGYFAYKLK KCGHYVSVIG SKGTVKKLKI KDVDKEEEIE FDDLIDKYDV
VFITTKSYHL DNVIKKYKDF LENSIVVPIL NGIGHFKKFK DFNYKKACIY ILSNKENGII
HKKTPLFYLC LEDDETLREV FKKCDDLKIK FSENIDKDIW KKYLFISTFA TLQSFYQKPT
GWIMENKKDE VEKFLGEVIR IAKNEGIDLS DEKIKVIKQA LNIPYNSKMS MQIDFEKGNK
TEVDNLTGFL AEKSDFINKF YKELK
//
