ID A2BMY5_HYPBU Unreviewed; 314 AA.
AC A2BMY5;
DT 20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 20-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00013014, ECO:0000256|RuleBase:RU362068};
DE EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014, ECO:0000256|RuleBase:RU362068};
DE AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024, ECO:0000256|RuleBase:RU362068};
GN OrderedLocusNames=Hbut_1524 {ECO:0000313|EMBL:ABM81346.1};
OS Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Hyperthermus.
OX NCBI_TaxID=415426 {ECO:0000313|EMBL:ABM81346.1, ECO:0000313|Proteomes:UP000002593};
RN [1] {ECO:0000313|EMBL:ABM81346.1, ECO:0000313|Proteomes:UP000002593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5456 / JCM 9403 / PLM1-5
RC {ECO:0000313|Proteomes:UP000002593};
RX PubMed=17350933;
RA Brugger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA She Q., Garrett R.A., Klenk H.P.;
RT "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL Archaea 2:127-135(2007).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC pantoic acid. {ECO:0000256|RuleBase:RU362068}.
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:0000256|ARBA:ARBA00000108};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:61294;
CC Evidence={ECO:0000256|ARBA:ARBA00000108};
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:0000256|ARBA:ARBA00000825};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16235;
CC Evidence={ECO:0000256|ARBA:ARBA00000825};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004724, ECO:0000256|RuleBase:RU362068}.
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870, ECO:0000256|RuleBase:RU362068}.
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DR EMBL; CP000493; ABM81346.1; -; Genomic_DNA.
DR RefSeq; WP_011822664.1; NC_008818.1.
DR AlphaFoldDB; A2BMY5; -.
DR STRING; 415426.Hbut_1524; -.
DR EnsemblBacteria; ABM81346; ABM81346; Hbut_1524.
DR GeneID; 4781604; -.
DR KEGG; hbu:Hbut_1524; -.
DR eggNOG; arCOG04139; Archaea.
DR HOGENOM; CLU_031468_0_0_2; -.
DR OrthoDB; 201845at2157; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000002593; Chromosome.
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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 NCBIfam; TIGR00745; apbA_panE; 1.
DR PANTHER; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR PANTHER; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR Pfam; PF02558; ApbA; 1.
DR Pfam; PF08546; ApbA_C; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Coenzyme A biosynthesis {ECO:0000256|RuleBase:RU362068};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000002593}.
FT DOMAIN 7..151
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 179..301
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 314 AA; 33534 MW; 048D0818C5AEA83E CRC64;
MSLNIDVVVV GCGAVGSTVA LALARAGVQV AAVTRSGTDG CRWDMVLVEG LGFGELLVCG
WTGAARLRPR LVVYAVKAYD LTSAVEDSLQ AGWNPEAVVS LQNGLGSLEL LSKTYGVDRA
IGGVVYFGAV GVAPCRARLL GRGGLLLGCW ARGGSCSFWS HQLAEALTAG GLPSSHVGDV
EPYRWLKLAV NAAINPVTVL AWSRNKVILE NPDAGKLAAQ LAREVALVAW RRGVELPGDP
VEEVFRVARA TGDNCSSMLQ DVARRGRSEV DYINGSVARE AWRLGLRAPF NEAMWRAVRL
LERWLAGRRL PCEI
//
