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Database: UniProt
Entry: Q0BU15_GRABC
LinkDB: Q0BU15_GRABC
Original site: Q0BU15_GRABC 
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}.
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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
//
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