ID A0A087DX17_9BIFI Unreviewed; 345 AA.
AC A0A087DX17;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=BSTEL_1118 {ECO:0000313|EMBL:KFJ00068.1};
OS Bifidobacterium stellenboschense.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=762211 {ECO:0000313|EMBL:KFJ00068.1, ECO:0000313|Proteomes:UP000029004};
RN [1] {ECO:0000313|EMBL:KFJ00068.1, ECO:0000313|Proteomes:UP000029004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23968 {ECO:0000313|EMBL:KFJ00068.1,
RC ECO:0000313|Proteomes:UP000029004};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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 + 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:KFJ00068.1}.
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DR EMBL; JGZP01000005; KFJ00068.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087DX17; -.
DR STRING; 762211.BSTEL_1118; -.
DR eggNOG; COG1893; Bacteria.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000029004; 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|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362068,
KW ECO:0000313|EMBL:KFJ00068.1};
KW Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000029004}.
FT DOMAIN 5..150
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 188..312
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 345 AA; 38473 MW; E1F7BD247C73B69A CRC64;
MALSYAVLGS GGMGIQYGVL LQEFAHKHVD FIDTWRPNVE KIREQGGVYV SQDGEDRHLV
PIDIHYPEDY HGNPDVWIVF VKQQQLDGFL KRASHAGLFR DHQVVFSAMN GYGHFEKLGE
YFSRDRIFGG TALIGAYVYG PGDVNFTGGK HAKAMNMCAW DERRTPLEQE IHDDFAAATL
NPTIVDDFLG MCLAKIVFNS VLNTLCTMYE IRFGQFHANP GARWMTERIV DEAYTAAEKA
GITLLGTRET EVETILHTAG VAHPLHYPSM YQDLTKGRPT EVDYINGYIA RLAREHGAEA
PLNEFLVHEV HLAEQAYAIH HPDIAEAAAR NADRLAKDTA AALAA
//
