PANE_PYRHO
ID PANE_PYRHO Reviewed; 301 AA.
AC O50098;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
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=PH1390; ORFNames=PHAA019;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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; BA000001; BAA30496.1; -; Genomic_DNA.
DR PIR; H71011; H71011.
DR RefSeq; WP_010885478.1; NC_000961.1.
DR AlphaFoldDB; O50098; -.
DR SMR; O50098; -.
DR STRING; 70601.3257813; -.
DR EnsemblBacteria; BAA30496; BAA30496; BAA30496.
DR GeneID; 1443716; -.
DR KEGG; pho:PH1390; -.
DR eggNOG; arCOG04139; Archaea.
DR OMA; NYSSMYQ; -.
DR OrthoDB; 57213at2157; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000000752; 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..301
FT /note="2-dehydropantoate 2-reductase"
FT /id="PRO_0000157326"
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 301 AA; 32811 MW; E2354787F603880C CRC64;
MKIYILGAGA IGSLVGGLLA NVGEDVTLIG RGRHIEAINK RGLMIEGLTN LKINTKATTS
IPGAKPDLII LTTKSYSTDD ALNSAKDIVR DTWVLSLQNG IGNEEKIMEL GGRPIGGITT
NGAVLKEPGV VEWRGRGITL IGLYPKGRNE FVEEVKETFN RAGLETEVTE NIIGWKWAKT
IVNSAINPIG AILEVKNGAI KDNDYLLSIA VEVVKEGCKI ALQNGIKFDI SPMELLIQTL
EQTRENYNSM LQDIWRGKRT EIDFINGKII EYAKLVNLEA PLNFLLWALV KAKESLGGGS
K
