ID A0A0R2CFZ0_9LACO Unreviewed; 327 AA.
AC A0A0R2CFZ0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=FD19_GL001433 {ECO:0000313|EMBL:KRM87275.1};
OS Lacticaseibacillus thailandensis DSM 22698 = JCM 13996.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1423810 {ECO:0000313|EMBL:KRM87275.1, ECO:0000313|Proteomes:UP000051789};
RN [1] {ECO:0000313|EMBL:KRM87275.1, ECO:0000313|Proteomes:UP000051789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22698 {ECO:0000313|EMBL:KRM87275.1,
RC ECO:0000313|Proteomes:UP000051789};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRM87275.1}.
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DR EMBL; AYZK01000003; KRM87275.1; -; Genomic_DNA.
DR RefSeq; WP_054750499.1; NZ_BBER01000003.1.
DR AlphaFoldDB; A0A0R2CFZ0; -.
DR STRING; 1423810.FD19_GL001433; -.
DR PATRIC; fig|1423810.4.peg.1472; -.
DR OrthoDB; 9800163at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000051789; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051789}.
FT DOMAIN 4..146
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 184..308
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 327 AA; 36480 MW; F4877894060CFCC5 CRC64;
MHYTVLGAGA MGLRYGVLLQ EVAGMKVDFV DNWDPEVDTI HSQGGVFVSR DGEDKHLVPI
NIYRPEEYTG DPDAYIIFCK QMGLQKMLTE CAHFFKPHQY AITCMNGMGH IEKINQYFPQ
EHVLGGTALI ATVLNGPGDV DFIGRPGAGT MNICPQTEVA DDFTHQVVTD FQAAHLNPNL
TDNFVGTLMA KVTFNSVVNT LCTMFEITMG EFIASPVAEK LSRQLIDEAY SACEAAGIQL
LNTREEEWQS VVHVSRDANP LHYPSMYQDM SKNRPTEVDY INGYIYEVGH AHGFEATTHN
FLRNLVHLAE FGKTFDMDAF RAAVLAR
//