ID V4XVL6_9ARCH Unreviewed; 293 AA.
AC V4XVL6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
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 ORFNames=A07HB70_01788 {ECO:0000313|EMBL:ESS06238.1};
OS uncultured archaeon A07HB70.
OC Archaea; environmental samples.
OX NCBI_TaxID=1412872 {ECO:0000313|EMBL:ESS06238.1, ECO:0000313|Proteomes:UP000030648};
RN [1] {ECO:0000313|Proteomes:UP000030648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24335829;
RA Podell S., Emerson J.B., Jones C.M., Ugalde J.A., Welch S.,
RA Heidelberg K.B., Banfield J.F., Allen E.E.;
RT "Seasonal fluctuations in ionic concentrations drive microbial succession
RT in a hypersaline lake community.";
RL ISME J. 0:0-0(2013).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KI543181; ESS06238.1; -; Genomic_DNA.
DR AlphaFoldDB; V4XVL6; -.
DR STRING; 1412872.A07HB70_01788; -.
DR PATRIC; fig|1412872.3.peg.1859; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000030648; Unassembled WGS sequence.
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|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362068,
KW ECO:0000313|EMBL:ESS06238.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030648}.
FT DOMAIN 3..143
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 171..290
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 293 AA; 29610 MW; 5C3D3A4DF707B94B CRC64;
MNVVVFGAGS LGSLVGAVLA RRHDVTLVGR APHVEAVRAD GLRVEGEESF VAHPSATTGG
EGLSADLAVV TVKSFDTGEA AAALATGDVG AALSLANGMG NEATLAGTLD APVVAGATAL
GASLRGPGRV AWLGRGRTTV GPWTDDAGRA AHRAGGALRV AGFPTTVTDA VRRRLWEKLA
ANAAINPLTA LAGVRNGAVA DPPLAATAAA AARETARAAR HAGVDLRDDR AVETATRVAR
ATAENRSSMA RDLEAGRRTE VDAINGHVVD RIGAERAPVN AALSALVRAR DDR
//
