Reviewed, UniProtKB/Swiss-Prot Q9HDU6 (PANE_SCHPO)

Names and origin

Protein names

Recommended name:
    Probable 2-dehydropantoate 2-reductase
    EC=1.1.1.169
Alternative name(s):
    Ketopantoate reductase
      Short name=KPA reductase
      Short name=KPR

Gene names

ORF Names:

SPBPB2B2.09c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	350 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid By similarity.
Catalytic activity	(R)-pantoate + NADP+ = 2-dehydropantoate + NADPH.
Pathway	Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
Sequence similarities	Belongs to the ketopantoate reductase family.

Ontologies

Keywords
Biological process	Pantothenate biosynthesis Pyrimidine biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pantothenate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW pyrimidine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe nucleus Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	2-dehydropantoate 2-reductase activity Inferred from electronic annotation. Source: EC NADP or NADPH binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 350	350	Probable 2-dehydropantoate 2-reductase		PRO_0000157327
Regions
	Nucleotide binding	9 – 14	6	NADP By similarity
Sites
	Active site	213	1	Proton donor By similarity
	Binding site	115	1	NADP; via amide nitrogen By similarity
	Binding site	115	1	Substrate By similarity
	Binding site	217	1	Substrate By similarity
	Binding site	221	1	Substrate By similarity
	Binding site	295	1	Substrate By similarity
	Binding site	307	1	NADP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9HDU6-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 1129E750CB1BA754	FASTA	350	39,114
	10 20 30 40 50 60 MNNTIYILGA GSIGSLLAYE LASLKSINNR VILLLRDKSR VNSFKDKNST LKIDRLFEEN 70 80 90 100 110 120 VPHLCCQVTA SEPSQLNVQS IENMIVTTKA GQTENALSKY LPYLSKNSNI LFVQNGMGAV 130 140 150 160 170 180 ENVCGKLWPE EQNKPSIYQG VISHGCFQTA PFHFSHAGLG DLKISKVPKN PKKILPDEAA 190 200 210 220 230 240 ETPCEMIKSL GKSELLRLRY MNYPELLVNQ CEKLVINACI NPTTATLDCV NGELYNDESA 250 260 270 280 290 300 KELFRCIIKE CVDIFFKCIP LFKNNEEAEK ILNVNRLLDR VMFVGTKVNG ANSSSTRQDC 310 320 330 340 350 LLLRETEIDA INGYVVKLAE NNGFQATVNK TMMLLTKSRL GLNRCRAHAR

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329671 Genomic DNA. Translation: CAC21411.1.
RefSeq	NP_596855.1.
3D structure databases
SMR	Q9HDU6. Positions 4-333.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9HDU6.
Genome annotation databases
GeneID	2541389.
KEGG	spo:SPBPB2B2.09c.
NMPDR	fig|4896.1.peg.2721.
Organism-specific databases
GeneDB_Spombe	SPBPB2B2.09c.
Phylogenomic databases
eggNOG	fuNOG09713.
HOGENOM	HBG397471.
OMA	QGVISHG.
OrthoDB	EOG9NW12N.
PhylomeDB	Q9HDU6.
Enzyme and pathway databases
BRENDA	1.1.1.169. 653.
Gene expression databases
ArrayExpress	Q9HDU6.
Family and domain databases
InterPro	IPR008927. 6-PGluconate_DH_C-like. IPR003710. ApbA. IPR013752. ApbA_C. IPR013332. ApbA_N. IPR013328. DH_multihelical. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 1 hit.
PANTHER	PTHR21708:SF21. ApbA. 1 hit.
Pfam	PF02558. ApbA. 1 hit. PF08546. ApbA_C. 1 hit. [Graphical view]
TIGRFAMs	TIGR00745. apbA_panE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PANE_SCHPO

Accession

Primary (citable) accession number: Q9HDU6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2002
Last sequence update:	March 1, 2001
Last modified:	February 9, 2010
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)