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Protein

6-phosphogluconate dehydrogenase, decarboxylating

Gene

SPBC660.16

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO2, with concomitant reduction of NADP to NADPH.By similarity

Catalytic activityi

6-phospho-D-gluconate + NADP+ = D-ribulose 5-phosphate + CO2 + NADPH.

Pathwayi: pentose phosphate pathway

This protein is involved in step 3 of the subpathway that synthesizes D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage).
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Glucose-6-phosphate 1-dehydrogenase (zwf1), Probable glucose-6-phosphate 1-dehydrogenase C794.01c (SPCC794.01c), Probable glucose-6-phosphate 1-dehydrogenase C7.13c (SPAC3C7.13c)
  2. Probable 6-phosphogluconolactonase (SPCC16C4.10)
  3. 6-phosphogluconate dehydrogenase, decarboxylating (SPBC660.16)
This subpathway is part of the pathway pentose phosphate pathway, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage), the pathway pentose phosphate pathway and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei106NADPBy similarity1
Binding sitei106SubstrateBy similarity1
Active sitei187Proton acceptorBy similarity1
Active sitei194Proton donorBy similarity1
Binding sitei195SubstrateBy similarity1
Binding sitei264Substrate; via amide nitrogenBy similarity1
Binding sitei291SubstrateBy similarity1
Binding sitei449Substrate; shared with dimeric partnerBy similarity1
Binding sitei455Substrate; shared with dimeric partnerBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi13 – 18NADPBy similarity6
Nucleotide bindingi36 – 38NADPBy similarity3
Nucleotide bindingi78 – 80NADPBy similarity3

GO - Molecular functioni

  • NADP binding Source: PomBase
  • phosphogluconate dehydrogenase (decarboxylating) activity Source: PomBase

GO - Biological processi

  • D-gluconate metabolic process Source: UniProtKB-KW
  • generation of precursor metabolites and energy Source: PomBase
  • pentose-phosphate shunt, oxidative branch Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Gluconate utilization, Pentose shunt

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiR-SPO-71336. Pentose phosphate pathway (hexose monophosphate shunt).
UniPathwayiUPA00115; UER00410.

Names & Taxonomyi

Protein namesi
Recommended name:
6-phosphogluconate dehydrogenase, decarboxylating (EC:1.1.1.44)
Gene namesi
ORF Names:SPBC660.16
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC660.16.
PomBaseiSPBC660.16.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000900741 – 4926-phosphogluconate dehydrogenase, decarboxylatingAdd BLAST492

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei107Phosphoserine1 Publication1
Modified residuei215Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP78812.
PRIDEiP78812.

PTM databases

iPTMnetiP78812.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi277661. 3 interactors.
MINTiMINT-4691318.

Structurei

3D structure databases

ProteinModelPortaliP78812.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni132 – 134Substrate bindingBy similarity3
Regioni190 – 191Substrate bindingBy similarity2

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000255147.
InParanoidiP78812.
KOiK00033.
OMAiEGEPCVT.
OrthoDBiEOG092C1NQM.
PhylomeDBiP78812.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
1.20.5.320. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR012284. 6PGD_dom_3.
IPR006114. 6PGDH_C.
IPR006113. 6PGDH_Gnd/GntZ.
IPR006115. 6PGDH_NADP-bd.
IPR006184. 6PGdom_BS.
IPR016040. NAD(P)-bd_dom.
IPR006183. Pgluconate_DH.
[Graphical view]
PfamiPF00393. 6PGD. 1 hit.
PF03446. NAD_binding_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000109. 6PGD. 1 hit.
PRINTSiPR00076. 6PGDHDRGNASE.
SMARTiSM01350. 6PGD. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00873. gnd. 1 hit.
PROSITEiPS00461. 6PGD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P78812-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQKEVADFG LIGLAVMGQN LILNGADKGF TVCCYNRTTS RVDEFLANEA
60 70 80 90 100
KGKSIVGAHS LEEFVSKLKK PRVCILLVKA GKPVDYLIEG LAPLLEKGDI
110 120 130 140 150
IVDGGNSHYP DTTRRCEELA KKGILFVGSG VSGGEEGARY GPSLMPGGNP
160 170 180 190 200
AAWPRIKPIF QTLAAKAGNN EPCCDWVGEQ GAGHYVKMVH NGIEYGDMQL
210 220 230 240 250
ICETYDIMKR GLGMSCDEIA DVFEKWNTGK LDSFLIEITR DVLRYKADDG
260 270 280 290 300
KPLVEKILDA AGQKGTGKWT AQNALEMGTP VSLITEAVFA RCLSSLKSER
310 320 330 340 350
VRASKKLTGP NTKFTGDKKQ LIDDLEDALY ASKIISYAQG FMLMREAAKE
360 370 380 390 400
YGWKLNNAGI ALMWRGGCII RSVFLKDITE AFREDPNLES ILFHPFFTNG
410 420 430 440 450
VEKAQAGWRR VVAQAAMLGI PVPATSTGLS FYDGYRSAVL PANLLQAQRD
460 470 480 490
YFGAHTFRVL PEAADKSLPA DKDIHINWTG HGGNISATTY DA
Length:492
Mass (Da):53,680
Last modified:January 11, 2001 - v2
Checksum:iF55F342957A9D3E1
GO

Sequence cautioni

The sequence BAA13823 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti219 – 220IA → ST in BAA13823 (PubMed:9501991).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89161 mRNA. Translation: BAA13823.1. Different initiation.
CU329671 Genomic DNA. Translation: CAA22536.1.
PIRiT40628.
T42523.
RefSeqiNP_595095.1. NM_001021002.2.

Genome annotation databases

EnsemblFungiiSPBC660.16.1; SPBC660.16.1:pep; SPBC660.16.
GeneIDi2541146.
KEGGispo:SPBC660.16.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89161 mRNA. Translation: BAA13823.1. Different initiation.
CU329671 Genomic DNA. Translation: CAA22536.1.
PIRiT40628.
T42523.
RefSeqiNP_595095.1. NM_001021002.2.

3D structure databases

ProteinModelPortaliP78812.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277661. 3 interactors.
MINTiMINT-4691318.

PTM databases

iPTMnetiP78812.

Proteomic databases

MaxQBiP78812.
PRIDEiP78812.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC660.16.1; SPBC660.16.1:pep; SPBC660.16.
GeneIDi2541146.
KEGGispo:SPBC660.16.

Organism-specific databases

EuPathDBiFungiDB:SPBC660.16.
PomBaseiSPBC660.16.

Phylogenomic databases

HOGENOMiHOG000255147.
InParanoidiP78812.
KOiK00033.
OMAiEGEPCVT.
OrthoDBiEOG092C1NQM.
PhylomeDBiP78812.

Enzyme and pathway databases

UniPathwayiUPA00115; UER00410.
ReactomeiR-SPO-71336. Pentose phosphate pathway (hexose monophosphate shunt).

Miscellaneous databases

PROiP78812.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
1.20.5.320. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR012284. 6PGD_dom_3.
IPR006114. 6PGDH_C.
IPR006113. 6PGDH_Gnd/GntZ.
IPR006115. 6PGDH_NADP-bd.
IPR006184. 6PGdom_BS.
IPR016040. NAD(P)-bd_dom.
IPR006183. Pgluconate_DH.
[Graphical view]
PfamiPF00393. 6PGD. 1 hit.
PF03446. NAD_binding_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000109. 6PGD. 1 hit.
PRINTSiPR00076. 6PGDHDRGNASE.
SMARTiSM01350. 6PGD. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00873. gnd. 1 hit.
PROSITEiPS00461. 6PGD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry namei6PGD_SCHPO
AccessioniPrimary (citable) accession number: P78812
Secondary accession number(s): Q9UQW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 11, 2001
Last modified: October 5, 2016
This is version 128 of the entry and version 2 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

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 one 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.