PANE_PYRAB
ID PANE_PYRAB Reviewed; 300 AA.
AC Q9V0N0; G8ZGW0;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
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 Name=apbA; OrderedLocusNames=PYRAB07590; ORFNames=PAB0512;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248285; CAB49673.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70155.1; -; Genomic_DNA.
DR PIR; H75119; H75119.
DR RefSeq; WP_010867881.1; NC_000868.1.
DR AlphaFoldDB; Q9V0N0; -.
DR SMR; Q9V0N0; -.
DR STRING; 272844.PAB0512; -.
DR EnsemblBacteria; CAB49673; CAB49673; PAB0512.
DR GeneID; 1496099; -.
DR KEGG; pab:PAB0512; -.
DR PATRIC; fig|272844.11.peg.799; -.
DR eggNOG; arCOG04139; Archaea.
DR HOGENOM; CLU_031468_6_1_2; -.
DR OMA; NYSSMYQ; -.
DR PhylomeDB; Q9V0N0; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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.
FT CHAIN 1..300
FT /note="2-dehydropantoate 2-reductase"
FT /id="PRO_0000157325"
FT ACT_SITE 179
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 7..12
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 99
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 123
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 246..249
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 261
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
SQ SEQUENCE 300 AA; 32773 MW; F559625B73F691DC CRC64;
MKIYILGAGA IGSLFGGLLA NAGEDVLLIG RDPHVSAINE KGLKIVGIKD LNVKVEATTR
VPEEKPDLIV LATKSYSTIE ALKSARHIVK GSWVLSIQNG IGNEDKIIEF GGKAIGGITT
NGAMVEAPGV IKWTGKGVTI IGLYPQGKEK FIEKVADVFN SADIETHVSE NIISWIWAKA
IVNSAINPIG TLLEVKNKVI RENDFLLSMA MEVVKEGCRV ALQNGIEFDV PPMDLFFQTL
EQTRENYNSM LQDIWRGKKT EVDYINGKIV EYAKAVNLEA PMNLLLWGLI KGKEALEGKK
