ID Q0BU15_GRABC Unreviewed; 331 AA.
AC Q0BU15;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 87.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465};
DE EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014};
DE AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024};
GN OrderedLocusNames=GbCGDNIH1_0789 {ECO:0000313|EMBL:ABI61687.1};
OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Granulibacter.
OX NCBI_TaxID=391165 {ECO:0000313|EMBL:ABI61687.1, ECO:0000313|Proteomes:UP000001963};
RN [1] {ECO:0000313|EMBL:ABI61687.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGDNIH1 {ECO:0000313|EMBL:ABI61687.1};
RX PubMed=17827295; DOI=10.1128/JB.00793-07;
RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA Kupko J.J.III., Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT "Genome sequence analysis of the emerging human pathogenic acetic acid
RT bacterium Granulibacter bethesdensis.";
RL J. Bacteriol. 189:8727-8736(2007).
RN [2] {ECO:0000313|EMBL:ABI61687.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGDNIH1 {ECO:0000313|EMBL:ABI61687.1};
RA Zarember K.A., Porcella S.F., Chu J., Ding L., Dahlstrom E., Barbian K.,
RA Martens C., Sykora L., Kramer S., Pettinato A.M., Hong H., Wald G.,
RA Berg L.J., Rogge L.S., Greenberg D.E., Falcone E.L., Neves J.F.,
RA Simoes M.J., Casal M., Rodriguez-Lopez F.C., Zelazny A.M., Gallin J.I.,
RA Holland S.M.;
RT "Comparative genomic and phenotypic analysis of Granulibacter bethesdensis
RT clinical isolates from patients with chronic granulomatous disease.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004994}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000394; ABI61687.1; -; Genomic_DNA.
DR RefSeq; WP_011631496.1; NC_008343.2.
DR AlphaFoldDB; Q0BU15; -.
DR STRING; 391165.GbCGDNIH1_0789; -.
DR KEGG; gbe:GbCGDNIH1_0789; -.
DR eggNOG; COG1893; Bacteria.
DR HOGENOM; CLU_031468_6_1_5; -.
DR OMA; FKLWGNM; -.
DR OrthoDB; 247668at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000001963; 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; IPR013752; KPA_reductase.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR21708:SF42; 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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001963}.
FT DOMAIN 3..170
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 197..317
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 331 AA; 35199 MW; 7A395E7D8050A175 CRC64;
MKVAIFGAGA IGGLLGFKLA KAGVDVTLVA RGPQLAALQQ NGLTLIRDGE RDTVAVRAVG
SAAEAGIQDY VFVTLKAHSL PGAAPSIAQM MGPDSALVTG INGVPYWYFY GLEGEHANRR
VESVDPGGKL WDIIPPSQAI GSVVYPASEV VEPGVIEHTY GDRFSLGEPD GSRSPRIEAL
SKAMIAAGLK APIRPRIRDE IWVKLWGNLC FNPISALTGA TLDIITTRPD LRQTCRGMMG
EAQIVAEKLG VRFGIDLEKR IDGAAEVGVH KTSMLQDLER GRPMEIDALL GAVVELGHVT
GTPMPSCELV LALVRERARQ SGCYEDPQPA A
//