PANE_SCHPO
ID PANE_SCHPO Reviewed; 350 AA.
AC Q9HDU6;
DT 21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Probable 2-dehydropantoate 2-reductase;
DE EC=1.1.1.169;
DE AltName: Full=Ketopantoate reductase;
DE Short=KPA reductase;
DE Short=KPR;
GN ORFNames=SPBPB2B2.09c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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 -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAC21411.1; -; Genomic_DNA.
DR RefSeq; NP_596855.1; NM_001023878.2.
DR AlphaFoldDB; Q9HDU6; -.
DR SMR; Q9HDU6; -.
DR BioGRID; 277900; 52.
DR STRING; 4896.SPBPB2B2.09c.1; -.
DR MaxQB; Q9HDU6; -.
DR PaxDb; Q9HDU6; -.
DR EnsemblFungi; SPBPB2B2.09c.1; SPBPB2B2.09c.1:pep; SPBPB2B2.09c.
DR GeneID; 2541389; -.
DR KEGG; spo:SPBPB2B2.09c; -.
DR PomBase; SPBPB2B2.09c; -.
DR VEuPathDB; FungiDB:SPBPB2B2.09c; -.
DR eggNOG; ENOG502QPT5; Eukaryota.
DR HOGENOM; CLU_031468_10_2_1; -.
DR InParanoid; Q9HDU6; -.
DR OMA; ASTTHGC; -.
DR PhylomeDB; Q9HDU6; -.
DR UniPathway; UPA00028; UER00004.
DR PRO; PR:Q9HDU6; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; ISS:PomBase.
DR GO; GO:0050661; F:NADP binding; IBA:GO_Central.
DR GO; GO:0015940; P:pantothenate biosynthetic process; ISS:PomBase.
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 NADP; Oxidoreductase; Pantothenate biosynthesis; Reference proteome.
FT CHAIN 1..350
FT /note="Probable 2-dehydropantoate 2-reductase"
FT /id="PRO_0000157327"
FT ACT_SITE 213
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 9..14
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 350 AA; 39114 MW; 1129E750CB1BA754 CRC64;
MNNTIYILGA GSIGSLLAYE LASLKSINNR VILLLRDKSR VNSFKDKNST LKIDRLFEEN
VPHLCCQVTA SEPSQLNVQS IENMIVTTKA GQTENALSKY LPYLSKNSNI LFVQNGMGAV
ENVCGKLWPE EQNKPSIYQG VISHGCFQTA PFHFSHAGLG DLKISKVPKN PKKILPDEAA
ETPCEMIKSL GKSELLRLRY MNYPELLVNQ CEKLVINACI NPTTATLDCV NGELYNDESA
KELFRCIIKE CVDIFFKCIP LFKNNEEAEK ILNVNRLLDR VMFVGTKVNG ANSSSTRQDC
LLLRETEIDA INGYVVKLAE NNGFQATVNK TMMLLTKSRL GLNRCRAHAR
