ID D2Q968_BIFDB Unreviewed; 336 AA.
AC D2Q968;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 79.
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 OrderedLocusNames=BDP_0691 {ECO:0000313|EMBL:ADB09354.1};
OS Bifidobacterium dentium (strain ATCC 27534 / DSM 20436 / JCM 1195 / Bd1).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=401473 {ECO:0000313|EMBL:ADB09354.1, ECO:0000313|Proteomes:UP000008693};
RN [1] {ECO:0000313|EMBL:ADB09354.1, ECO:0000313|Proteomes:UP000008693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27534 / DSM 20436 / JCM 1195 / Bd1
RC {ECO:0000313|Proteomes:UP000008693};
RX PubMed=20041198; DOI=10.1371/journal.pgen.1000785;
RA Ventura M., Turroni F., Zomer A., Foroni E., Giubellini V., Bottacini F.,
RA Canchaya C., Claesson M.J., He F., Mantzourani M., Mulas L., Ferrarini A.,
RA Gao B., Delledonne M., Henrissat B., Coutinho P., Oggioni M., Gupta R.S.,
RA Zhang Z., Beighton D., Fitzgerald G.F., O'Toole P.W., van Sinderen D.;
RT "The Bifidobacterium dentium Bd1 genome sequence reflects its genetic
RT adaptation to the human oral cavity.";
RL PLoS Genet. 5:E1000785-E1000785(2009).
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}.
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DR EMBL; CP001750; ADB09354.1; -; Genomic_DNA.
DR RefSeq; WP_003836922.1; NC_013714.1.
DR AlphaFoldDB; D2Q968; -.
DR STRING; 401473.BDP_0691; -.
DR GeneID; 69534982; -.
DR KEGG; bde:BDP_0691; -.
DR eggNOG; COG1893; Bacteria.
DR HOGENOM; CLU_031468_0_0_11; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000008693; Chromosome.
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|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362068,
KW ECO:0000313|EMBL:ADB09354.1};
KW Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000008693}.
FT DOMAIN 3..146
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 189..312
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 336 AA; 37551 MW; 21526C33A009D381 CRC64;
MKYAVIGAGG MGIQYGVLLQ EFAHKDVDFI DTWKPNVEKI REQGGAYVSQ DGEDRHLVPI
DVYYPEEYTG EPDVWIVFVK QMQLDAVLKR CAHLFNDRQI VFSAMNGYGH FEKLNEYFSK
DRIYGGTALI GAYVYGPGDF NFTGGAHAKA MNLCSYADDP SEGVKAAEQV LFEDFTAATL
NPTIVENFIG MCMAKIVFNA VLNTLCTMYQ IRFGEFHAHP DARWLTEQLV DEAYGAAEAA
GYELLGTRET EVETILHTAG VAHPLHYPSM YQDLTKGRPT EVDYINGYIA KVGRENGYVC
KLHEFLTREV HLAERAFAIH NPDIVAQAEA DAEASK
//
