ID A1WNR8_VEREI Unreviewed; 343 AA.
AC A1WNR8;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
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=Veis_3557 {ECO:0000313|EMBL:ABM59275.1};
OS Verminephrobacter eiseniae (strain EF01-2).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Verminephrobacter.
OX NCBI_TaxID=391735 {ECO:0000313|EMBL:ABM59275.1, ECO:0000313|Proteomes:UP000000374};
RN [1] {ECO:0000313|Proteomes:UP000000374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EF01-2 {ECO:0000313|Proteomes:UP000000374};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-2.";
RL Submitted (DEC-2006) 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}.
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DR EMBL; CP000542; ABM59275.1; -; Genomic_DNA.
DR RefSeq; WP_011811266.1; NC_008786.1.
DR AlphaFoldDB; A1WNR8; -.
DR STRING; 391735.Veis_3557; -.
DR GeneID; 76461961; -.
DR KEGG; vei:Veis_3557; -.
DR eggNOG; COG1893; Bacteria.
DR HOGENOM; CLU_031468_0_0_4; -.
DR OrthoDB; 8555723at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000000374; 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:ABM59275.1};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655,
KW ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000000374}.
FT DOMAIN 5..154
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 183..323
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 343 AA; 37690 MW; 4096734AA2981B90 CRC64;
MNRDILIWGA GAIGGTVGAY LCRAGLDVTF VDIDAQHVAA IRDRKKGLSI SGPIDNFTVH
ADSFLPEELR GQWNRIFLCV KAHHTQQACE ELLPYLAPDG FVVSLQNGLC ERTIAEIAGR
ERTIGAFINF GADWIEAGAI MYGNRAAVVV GELKGEDTMR LRQLLADLKL FEPRAEATSN
IWAFLWGKLA YGSLLFAQAL GQDGIADCLE RPELLPLWRK MVAEVLAVAE AEGVAPSGFN
GFMPDAFAPA KGTVEASKKS VEKMAAFNRP NAKTHSGIWR DLAVRKRKTE VDAFIGQVVA
IGKIHQIQCP VLENLVEMIH EIENGRRIQS NANLTELWRK NAN
//
