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Protein

Probable 2-dehydropantoate 2-reductase

Gene

SPBPB2B2.09c

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.By similarity

Catalytic activityi

(R)-pantoate + NADP+ = 2-dehydropantoate + NADPH.

Pathway:i(R)-pantothenate biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes (R)-pantoate from 3-methyl-2-oxobutanoate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Probable 3-methyl-2-oxobutanoate hydroxymethyltransferase (SPAC5H10.09c)
  2. Probable 2-dehydropantoate 2-reductase (SPBPB2B2.09c)
This subpathway is part of the pathway (R)-pantothenate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-pantoate from 3-methyl-2-oxobutanoate, the pathway (R)-pantothenate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei115 – 1151NADP; via amide nitrogenBy similarity
Binding sitei115 – 1151SubstrateBy similarity
Active sitei213 – 2131Proton donorBy similarity
Binding sitei217 – 2171SubstrateBy similarity
Binding sitei221 – 2211SubstrateBy similarity
Binding sitei295 – 2951SubstrateBy similarity
Binding sitei307 – 3071NADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi9 – 146NADPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pantothenate biosynthesis, Pyrimidine biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00028; UER00004.

Names & Taxonomyi

Protein namesi
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 namesi
ORF Names:SPBPB2B2.09c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBPB2B2.09c.
PomBaseiSPBPB2B2.09c.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 350350Probable 2-dehydropantoate 2-reductasePRO_0000157327Add
BLAST

Proteomic databases

MaxQBiQ9HDU6.

Interactioni

Protein-protein interaction databases

BioGridi277900. 50 interactions.
MINTiMINT-4702481.

Structurei

3D structure databases

ProteinModelPortaliQ9HDU6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ketopantoate reductase family.Curated

Phylogenomic databases

eggNOGiCOG1893.
HOGENOMiHOG000000875.
InParanoidiQ9HDU6.
KOiK00077.
OMAiGIECPVN.
OrthoDBiEOG7VQJPR.
PhylomeDBiQ9HDU6.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR003710. ApbA.
IPR013752. KPA_reductase.
IPR013332. KPR_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF02558. ApbA. 1 hit.
PF08546. ApbA_C. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
TIGRFAMsiTIGR00745. apbA_panE. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9HDU6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNTIYILGA GSIGSLLAYE LASLKSINNR VILLLRDKSR VNSFKDKNST
60 70 80 90 100
LKIDRLFEEN VPHLCCQVTA SEPSQLNVQS IENMIVTTKA GQTENALSKY
110 120 130 140 150
LPYLSKNSNI LFVQNGMGAV ENVCGKLWPE EQNKPSIYQG VISHGCFQTA
160 170 180 190 200
PFHFSHAGLG DLKISKVPKN PKKILPDEAA ETPCEMIKSL GKSELLRLRY
210 220 230 240 250
MNYPELLVNQ CEKLVINACI NPTTATLDCV NGELYNDESA KELFRCIIKE
260 270 280 290 300
CVDIFFKCIP LFKNNEEAEK ILNVNRLLDR VMFVGTKVNG ANSSSTRQDC
310 320 330 340 350
LLLRETEIDA INGYVVKLAE NNGFQATVNK TMMLLTKSRL GLNRCRAHAR
Length:350
Mass (Da):39,114
Last modified:March 1, 2001 - v1
Checksum:i1129E750CB1BA754
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAC21411.1.
RefSeqiNP_596855.1. NM_001023878.2.

Genome annotation databases

EnsemblFungiiSPBPB2B2.09c.1; SPBPB2B2.09c.1:pep; SPBPB2B2.09c.
GeneIDi2541389.
KEGGispo:SPBPB2B2.09c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAC21411.1.
RefSeqiNP_596855.1. NM_001023878.2.

3D structure databases

ProteinModelPortaliQ9HDU6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277900. 50 interactions.
MINTiMINT-4702481.

Proteomic databases

MaxQBiQ9HDU6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBPB2B2.09c.1; SPBPB2B2.09c.1:pep; SPBPB2B2.09c.
GeneIDi2541389.
KEGGispo:SPBPB2B2.09c.

Organism-specific databases

EuPathDBiFungiDB:SPBPB2B2.09c.
PomBaseiSPBPB2B2.09c.

Phylogenomic databases

eggNOGiCOG1893.
HOGENOMiHOG000000875.
InParanoidiQ9HDU6.
KOiK00077.
OMAiGIECPVN.
OrthoDBiEOG7VQJPR.
PhylomeDBiQ9HDU6.

Enzyme and pathway databases

UniPathwayiUPA00028; UER00004.

Miscellaneous databases

NextBioi20802498.
PROiQ9HDU6.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR003710. ApbA.
IPR013752. KPA_reductase.
IPR013332. KPR_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF02558. ApbA. 1 hit.
PF08546. ApbA_C. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
TIGRFAMsiTIGR00745. apbA_panE. 1 hit.
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiPANE_SCHPO
AccessioniPrimary (citable) accession number: Q9HDU6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2002
Last sequence update: March 1, 2001
Last modified: July 22, 2015
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.