PANE_CAUVC
ID PANE_CAUVC Reviewed; 290 AA.
AC Q9ABG6;
DT 21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000250|UniProtKB:P0A9J4};
DE EC=1.1.1.169 {ECO:0000250|UniProtKB:P0A9J4};
DE AltName: Full=Ketopantoate reductase {ECO:0000250|UniProtKB:P0A9J4};
DE Short=KPR {ECO:0000250|UniProtKB:P0A9J4};
GN OrderedLocusNames=CC_0261;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC pantoic acid. {ECO:0000250|UniProtKB:P0A9J4}.
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:0000250|UniProtKB:P0A9J4};
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC {ECO:0000250|UniProtKB:P0A9J4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A9J4}.
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000305}.
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DR EMBL; AE005673; AAK22248.1; -; Genomic_DNA.
DR PIR; D87281; D87281.
DR RefSeq; NP_419080.1; NC_002696.2.
DR RefSeq; WP_010918150.1; NC_002696.2.
DR AlphaFoldDB; Q9ABG6; -.
DR SMR; Q9ABG6; -.
DR STRING; 190650.CC_0261; -.
DR EnsemblBacteria; AAK22248; AAK22248; CC_0261.
DR KEGG; ccr:CC_0261; -.
DR PATRIC; fig|190650.5.peg.256; -.
DR eggNOG; COG1893; Bacteria.
DR HOGENOM; CLU_031468_4_0_5; -.
DR OMA; GMFSRGD; -.
DR BioCyc; CAULO:CC0261-MON; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000001816; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 1.10.1040.10; -; 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 Pfam; PF02558; ApbA; 1.
DR Pfam; PF08546; ApbA_C; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00745; apbA_panE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; NADP; Oxidoreductase; Pantothenate biosynthesis;
KW Reference proteome.
FT CHAIN 1..290
FT /note="2-dehydropantoate 2-reductase"
FT /id="PRO_0000157312"
FT ACT_SITE 175
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 8..13
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 98
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 124
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 256
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
SQ SEQUENCE 290 AA; 30189 MW; F4E50CC43D2EB746 CRC64;
MTSIAVIGPG AVGGTLAAWL AQKPDHVVTV CVRTPFEALA VETPEGAISA TPRVATSPES
LAPVDWVLVT TKTYDTDATW TWLDALVGPQ TRVAILRNGV EHVAPFVGKI AAERLVPAVV
DIPAERSAPG RMLQRRNGWI KVPVGPAGEA FAALFAHTPI ELHVVEDFVT EAWKKLALNC
AGAVNALVLK PAGIAHDEGA AQVMRSLVRE CVAVGRAEGA DLSDDLPDQV IAGYRAADPG
SVNSLHADRA AGRAMELDAR NGVIVRRGAA HGIATPANAM VVALLNAAAL
