ID W7BIX7_9LIST Unreviewed; 296 AA.
AC W7BIX7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=MAQA_06028 {ECO:0000313|EMBL:EUJ19708.1};
OS Listeria aquatica FSL S10-1188.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1265818 {ECO:0000313|EMBL:EUJ19708.1, ECO:0000313|Proteomes:UP000019246};
RN [1] {ECO:0000313|EMBL:EUJ19708.1, ECO:0000313|Proteomes:UP000019246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL S10-1188 {ECO:0000313|EMBL:EUJ19708.1,
RC ECO:0000313|Proteomes:UP000019246};
RX PubMed=24599893; DOI=10.1099/ijs.0.052720-0;
RA den Bakker H.C., Warchocki S., Wright E.M., Allred A.F., Ahlstrom C.,
RA Manuel C.S., Stasiewicz M.J., Burrell A., Roof S., Strawn L., Fortes E.D.,
RA Nightingale K.K., Kephart D., Wiedmann M.;
RT "Listeria floridensis sp. nov., Listeria aquatica sp. nov., Listeria
RT cornellensis sp. nov., Listeria riparia sp. nov. and Listeria grandensis
RT sp. nov., from agricultural and natural environments.";
RL Int. J. Syst. Evol. Microbiol. 64:1882-1889(2014).
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 + 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|ARBA:ARBA00000784,
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:EUJ19708.1}.
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DR EMBL; AOCG01000006; EUJ19708.1; -; Genomic_DNA.
DR RefSeq; WP_036071934.1; NZ_AOCG01000006.1.
DR AlphaFoldDB; W7BIX7; -.
DR STRING; 1265818.MAQA_06028; -.
DR PATRIC; fig|1265818.5.peg.1203; -.
DR OrthoDB; 9800163at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000019246; 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; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR PANTHER; PTHR43765:SF2; 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|RuleBase:RU362068}.
FT DOMAIN 5..146
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 171..288
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 296 AA; 33026 MW; FC1C224CC8783B77 CRC64;
MKPKIGIIGG GAIGLFFAAR LSLYADVTVF VRRTEQQVRL NAEGIKLGTD TYSVRSEVTG
EQSFRHQDLL FVTVKSYQLA GLKAQLETFP KETPLAFLTN GIGHIEWLKE LSAETILLGI
TSHGVVRRSD REVESSGSGE TTLGIWCGSF DEGLKEYLTT LPDFPVSFSA NIFKEIYRKL
LINTAINPLT ALLNVPNGSL LTNKEFHGLL LEVVREANRV LQVENGIEVV EEICRNTAFN
WSSMAVDLLH KRKTEIDAIV LPVLKMLEEK ELSAERLTML YQLIKGKENE NAKLDD
//