PANE_HALSA
ID PANE_HALSA Reviewed; 303 AA.
AC Q9HRF0;
DT 21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=VNG_0730C;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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; AE004437; AAG19208.1; -; Genomic_DNA.
DR PIR; D84230; D84230.
DR RefSeq; WP_010902504.1; NC_002607.1.
DR AlphaFoldDB; Q9HRF0; -.
DR SMR; Q9HRF0; -.
DR STRING; 64091.VNG_0730C; -.
DR PaxDb; Q9HRF0; -.
DR EnsemblBacteria; AAG19208; AAG19208; VNG_0730C.
DR GeneID; 5952666; -.
DR GeneID; 62884173; -.
DR KEGG; hal:VNG_0730C; -.
DR PATRIC; fig|64091.14.peg.557; -.
DR HOGENOM; CLU_031468_0_0_2; -.
DR InParanoid; Q9HRF0; -.
DR OMA; NYSSMYQ; -.
DR OrthoDB; 57213at2157; -.
DR PhylomeDB; Q9HRF0; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000000554; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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;
KW Reference proteome.
FT CHAIN 1..303
FT /note="2-dehydropantoate 2-reductase"
FT /id="PRO_0000157323"
FT ACT_SITE 185
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 78
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 103
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 129
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 252..255
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT BINDING 267
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q5JGC2"
SQ SEQUENCE 303 AA; 31124 MW; B373143F2822DC94 CRC64;
MRVVVQGPGS LGSLVGGVLA GGETAVTLLG HQSEHLTRVR EDGLRVVQPD GTTRVTRPSV
ATDPSVVADA DLVVVCVKSY DTASAARALG RQCDGAMVLT LQNGLGNAAV LAEHVPADTV
LVGTTTHGAA RTEPGVVRHA GGGETTIGRY RGANDARVAS VAAAFSTGGM ETTVTASPQR
AVWEKVLVNV GINAATALAD VDNGALVECP PGERVLERAV TEGVRVAEAE GVSVSESVVE
RARQVAARTA SNESSMRQDL AGGARTEVES LHGAVVERAR DHDIAVPVIR TLADLVRLAQ
RDG
