PANE_ARCFU
ID PANE_ARCFU Reviewed; 294 AA.
AC O28578;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
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=AF_1695;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
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; AE000782; AAB89553.1; -; Genomic_DNA.
DR PIR; F69461; F69461.
DR RefSeq; WP_010879191.1; NC_000917.1.
DR AlphaFoldDB; O28578; -.
DR SMR; O28578; -.
DR STRING; 224325.AF_1695; -.
DR DNASU; 1484918; -.
DR EnsemblBacteria; AAB89553; AAB89553; AF_1695.
DR GeneID; 1484918; -.
DR KEGG; afu:AF_1695; -.
DR eggNOG; arCOG04139; Archaea.
DR HOGENOM; CLU_031468_0_1_2; -.
DR OMA; NYSSMYQ; -.
DR OrthoDB; 57213at2157; -.
DR PhylomeDB; O28578; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000002199; 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: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..294
FT /note="2-dehydropantoate 2-reductase"
FT /id="PRO_0000157322"
FT ACT_SITE 178
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 10..15
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 34
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 74
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 98
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 122
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 243..246
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 258
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
SQ SEQUENCE 294 AA; 31885 MW; A0AFE175763A4184 CRC64;
MRVQRVQIMG AGALGSLVGA LIQLAGYDVI FVARGKQLEA LKKGLRVSGL KNAELKVYCT
SQPEDADITF VTVKAYDTET VAKKLAEVDA GVVCSLQNGV GNEEILAKYC RKVLGGVTTY
GANLKDYGHV VYAGEGYTYV GEMDGRVSGE AEMVAEVLRD AGMRAEAVND IEFRIWAKAV
VNAAINPITA ICRVKNGEVV RNPHLWEVAR AVADEGRQVM ARMGYEFDAA SEVRKVAEMT
AENRSSMLQD LERGKRTEVE FINGAIVKKG EEFGIDCAVN RTLLNLVRGV ESGL
