PANE_YEAST
ID PANE_YEAST Reviewed; 379 AA.
AC P38787; D3DL12;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=2-dehydropantoate 2-reductase;
DE EC=1.1.1.169;
DE AltName: Full=Ketopantoate reductase;
DE Short=KPA reductase;
DE Short=KPR;
GN Name=PAN5; OrderedLocusNames=YHR063C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC pantoic acid. {ECO:0000250}.
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;
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC -!- MISCELLANEOUS: Present with 2600 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000305}.
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DR EMBL; U00061; AAB68390.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06756.1; -; Genomic_DNA.
DR PIR; S46711; S46711.
DR RefSeq; NP_011930.1; NM_001179193.1.
DR AlphaFoldDB; P38787; -.
DR SMR; P38787; -.
DR BioGRID; 36495; 47.
DR DIP; DIP-5591N; -.
DR IntAct; P38787; 5.
DR MINT; P38787; -.
DR STRING; 4932.YHR063C; -.
DR iPTMnet; P38787; -.
DR MaxQB; P38787; -.
DR PaxDb; P38787; -.
DR PRIDE; P38787; -.
DR EnsemblFungi; YHR063C_mRNA; YHR063C; YHR063C.
DR GeneID; 856460; -.
DR KEGG; sce:YHR063C; -.
DR SGD; S000001105; PAN5.
DR VEuPathDB; FungiDB:YHR063C; -.
DR eggNOG; ENOG502QPT5; Eukaryota.
DR GeneTree; ENSGT00940000176320; -.
DR HOGENOM; CLU_031468_10_2_1; -.
DR InParanoid; P38787; -.
DR OMA; ASTTHGC; -.
DR BioCyc; YEAST:MON3O-214; -.
DR UniPathway; UPA00028; UER00004.
DR PRO; PR:P38787; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38787; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; ISS:SGD.
DR GO; GO:0050661; F:NADP binding; IBA:GO_Central.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IC:SGD.
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 1: Evidence at protein level;
KW NADP; Oxidoreductase; Pantothenate biosynthesis; Reference proteome.
FT CHAIN 1..379
FT /note="2-dehydropantoate 2-reductase"
FT /id="PRO_0000157328"
FT ACT_SITE 224
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 13..18
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 328
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 379 AA; 42821 MW; 22BCAB56B2AE1AF3 CRC64;
MTAPHRSTIH ILGLGAMGTV LAVDLLRFTN ALVVPLFRSQ ERLAQFQKTN GNNISIRKLY
LEGSPIFSYP VEKCECPETF SKKPIDNLVV TTKTYQTKEA LAPYLPYINK NTNLILIQNG
LGVLELLREE IFTDSKNRPH LFQGVISHGV YQDKAGVFNH AGWAGMKIAK LPWTEEEMIQ
KKSVVEDDAA NNSLVKLLTE PKFAKEFGIE HSTYQEMLFG QLFKFLVNAC MNPVTAILDC
VNGEMKASCG PVFTSIIDEC LQILRVAYRP LFQYHEKYSG NEEYPEMDVN AVLTTDNMVS
EVTRIGCDIN SRNSSSMRQD TLFLRDIEIE YINGYVVKLA DNLNLDPNCC KVNKTIGELA
TMRLALNRSR SINGDWRKD
