ID D6V3A4_9BRAD Unreviewed; 303 AA.
AC D6V3A4;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
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=AfiDRAFT_0420 {ECO:0000313|EMBL:EFI52434.1};
OS Afipia sp. 1NLS2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=666684 {ECO:0000313|EMBL:EFI52434.1, ECO:0000313|Proteomes:UP000004041};
RN [1] {ECO:0000313|EMBL:EFI52434.1, ECO:0000313|Proteomes:UP000004041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1NLS2 {ECO:0000313|EMBL:EFI52434.1,
RC ECO:0000313|Proteomes:UP000004041};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Prakah O.,
RA Elkins J.G., Brown S.D., Palumbo A.V., Hemme C., Zhou J., Watson D.B.,
RA Jardine P.M., Kostka J.E., Green S.J., Woyke T.J.;
RT "The draft genome of Afipia sp. 1NLS2.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC pantoic acid. {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:EFI52434.1}.
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DR EMBL; ADVZ01000001; EFI52434.1; -; Genomic_DNA.
DR RefSeq; WP_009337349.1; NZ_ADVZ01000001.1.
DR AlphaFoldDB; D6V3A4; -.
DR eggNOG; COG1893; Bacteria.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000004041; 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; 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 3: Inferred from homology;
KW NADP {ECO:0000256|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362068,
KW ECO:0000313|EMBL:EFI52434.1};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655,
KW ECO:0000256|RuleBase:RU362068}.
FT DOMAIN 3..149
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 173..293
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 303 AA; 31886 MW; 8E3C47E6FBB8A357 CRC64;
MKIAVMGAGA VGCFYGGMLA RGGHEVTLIG RPVHVEAITK RGGLRFESAI FDGVIPIGAN
TNPSAVAGAD VVLFCVKSAD TEEAGQQIAP HLKNDAVVIS LQNGVDNAER LAAVLKQVVL
PSVVYVAAGM GGPGHIQHHG RGDLIIGPSP RSDDIAKTFA DAAIPTVVSG EVLPRLWDKL
IINCAYNALS AIAQLPYGRL FEVEGTKEVM DSAILECIAV ASELGIAVSP DIREKTYALV
KVMPDQYAST AQDLARGRPT EIDFLNGHIV RKGAEFGIPT PSNLALQVAV KLRELERAGK
APR
//
