PANE_PYRAE
ID PANE_PYRAE Reviewed; 279 AA.
AC Q8ZT70;
DT 21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000250|UniProtKB:Q5JGC2};
DE EC=1.1.1.169 {ECO:0000250|UniProtKB:Q5JGC2};
DE AltName: Full=Ketopantoate reductase {ECO:0000250|UniProtKB:Q5JGC2};
DE Short=KPR {ECO:0000250|UniProtKB:Q5JGC2};
GN OrderedLocusNames=PAE3409;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
CC -!- FUNCTION: Catalyzes the NAD(P)H-dependent reduction of ketopantoate
CC into pantoic acid. {ECO:0000250|UniProtKB:Q5JGC2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantoate + NAD(+) = 2-dehydropantoate + H(+) + NADH;
CC Xref=Rhea:RHEA:61292, ChEBI:CHEBI:11561, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15980, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000250|UniProtKB:Q5JGC2};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:61294;
CC Evidence={ECO:0000250|UniProtKB:Q5JGC2};
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:Q5JGC2};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16235;
CC Evidence={ECO:0000250|UniProtKB:Q5JGC2};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC {ECO:0000250|UniProtKB:Q5JGC2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5JGC2}.
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000305}.
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DR EMBL; AE009441; AAL64893.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8ZT70; -.
DR SMR; Q8ZT70; -.
DR STRING; 178306.PAE3409; -.
DR EnsemblBacteria; AAL64893; AAL64893; PAE3409.
DR KEGG; pai:PAE3409; -.
DR PATRIC; fig|178306.9.peg.2562; -.
DR eggNOG; arCOG04139; Archaea.
DR HOGENOM; CLU_031468_0_0_2; -.
DR InParanoid; Q8ZT70; -.
DR OMA; NYSSMYQ; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000002439; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IBA:GO_Central.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:InterPro.
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 Coenzyme A biosynthesis; Cytoplasm; NAD; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..279
FT /note="2-dehydropantoate 2-reductase"
FT /id="PRO_0000157324"
FT ACT_SITE 158
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 6..11
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 66
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 86
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 225..228
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 240
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
SQ SEQUENCE 279 AA; 29732 MW; 8A0A50DA29CD1328 CRC64;
MLRVIGLGAV GSLFTYFLNR AGVVPEVVQR RRCGEFLFCV EGDCEKLKFR EGGAADDVGY
TIVAVKAYDS RSVVPHLKGV AVVAQNGIGG YEEIKEAYPN SVPAVVTYGV YREGCRAELR
GVGEIYLPSA VSTLAELLER GGGRVRLVED IEPYRWLKLA VNAAINAITA LLQAPNGVII
SSPYAQTLAL EVAQEVLNVA TALGVKMPRN PVEEVLRVAS ATAKNLSSTA RDVAACAKTE
IDYINGAVVK YGEALGVATP VNKALFNLIK ARESLCNSG
