ID F2L174_THEU7 Unreviewed; 278 AA.
AC F2L174;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
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=TUZN_1334 {ECO:0000313|EMBL:AEA12810.1};
OS Thermoproteus uzoniensis (strain 768-20).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Thermoproteus.
OX NCBI_TaxID=999630 {ECO:0000313|EMBL:AEA12810.1, ECO:0000313|Proteomes:UP000008138};
RN [1] {ECO:0000313|EMBL:AEA12810.1, ECO:0000313|Proteomes:UP000008138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=768-20 {ECO:0000313|EMBL:AEA12810.1,
RC ECO:0000313|Proteomes:UP000008138};
RX PubMed=21478349; DOI=10.1128/JB.00409-11;
RA Mardanov A.V., Gumerov V.M., Beletsky A.V., Prokofeva M.I.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of the thermoacidophilic crenarchaeon
RT Thermoproteus uzoniensis 768-20.";
RL J. Bacteriol. 193:3156-3157(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=768-20;
RA Mardanov A.V., Gumerov V.M., Beletsky A.V., Prokofeva M.I.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of the thermoacidophilic crenarchaeon
RT Thermoproteus uzoniensis 768-20.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002590; AEA12810.1; -; Genomic_DNA.
DR RefSeq; WP_013680146.1; NC_015315.1.
DR AlphaFoldDB; F2L174; -.
DR STRING; 999630.TUZN_1334; -.
DR GeneID; 10360861; -.
DR KEGG; tuz:TUZN_1334; -.
DR eggNOG; arCOG04139; Archaea.
DR HOGENOM; CLU_031468_0_0_2; -.
DR OrthoDB; 201845at2157; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000008138; 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}.
FT DOMAIN 4..127
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 149..272
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 278 AA; 29550 MW; F6F081212B55C394 CRC64;
MFRIVGLGAV GSLFAYFLNR AGYAPGVVQR RVCDEYLFCA DGACERLRLA AAGAEGAKYT
VVAVKAYDSL SAVPHLRGTA VVAQNGIGGY EAIREVYPSS VAAVVTYGVY REGCRSELRG
RGEIYLPRAV SDFADVLERG GARAVVVDDV EPYRWLKLAV NAAINAITAL LQAPNGVIAS
VDHARDLARA VVAEVARVAE AAGVRMPADP FEEVLRVASA TAENVSSTAR DLARCAKTEV
DFINGAVVKY GERLGVYTPV NAALYSLIKA KESLCGRE
//
