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Protein

6-phosphogluconate dehydrogenase, decarboxylating

Gene

6-PGD

Organism
Cunninghamella elegans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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. no protein annotated in this organism
  2. no protein annotated in this organism
  3. 6-phosphogluconate dehydrogenase, decarboxylating (6-PGD)
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 sitei105NADPBy similarity1
Binding sitei105SubstrateBy similarity1
Active sitei186Proton acceptorBy similarity1
Active sitei193Proton donorBy similarity1
Binding sitei194SubstrateBy similarity1
Binding sitei263Substrate; via amide nitrogenBy similarity1
Binding sitei290SubstrateBy similarity1
Binding sitei449Substrate; shared with dimeric partnerBy similarity1
Binding sitei455Substrate; shared with dimeric partnerBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi12 – 17NADPBy similarity6
Nucleotide bindingi35 – 37NADPBy similarity3
Nucleotide bindingi77 – 79NADPBy similarity3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Gluconate utilization, Pentose shunt

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00115; UER00410.

Names & Taxonomyi

Protein namesi
Recommended name:
6-phosphogluconate dehydrogenase, decarboxylating (EC:1.1.1.44)
Gene namesi
Name:6-PGD
OrganismiCunninghamella elegans
Taxonomic identifieri4853 [NCBI]
Taxonomic lineageiEukaryotaFungiFungi incertae sedisMucoromycotinaMucoralesCunninghamellaceaeCunninghamella

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000900731 – 4856-phosphogluconate dehydrogenase, decarboxylatingAdd BLAST485

Proteomic databases

PRIDEiO60037.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO60037.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni131 – 133Substrate bindingBy similarity3
Regioni189 – 190Substrate bindingBy similarity2

Sequence similaritiesi

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.

O60037-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVEAVADIGL IGLAVMGQNL ILNMNDHGFV VCAYNRTTSK VDDFLANEAK
60 70 80 90 100
GTNVVGAHSV EELCAKLKRP RKVMLLVKAG SAVDAFIDQL LPHLEEGDII
110 120 130 140 150
IDGGNSHFPD SIRRTKELEA KGILFVGSGV SGGEEGARYG PSLMPGGNSK
160 170 180 190 200
AWEHIQPIFQ AIAAKAPDGA SCCEWVGETG AGHYVKMVHN GIEYGDMQLI
210 220 230 240 250
TEVYQILHEG LGLSHDEMAD IFEEWNKGDL DSFLIEITRD ILRFKDTDGQ
260 270 280 290 300
PLVTKIRDTA GQKGTGKWTA IDSLDRGIPV TLIGEAVYSR CLSSLKDERV
310 320 330 340 350
RASKILQGPS SSKFTGDKKT FIAQLGQALY AAKIVSYAQG YMLMRQAAKD
360 370 380 390 400
YEWKLNNAGI ALMWRGGCII RSVFLGKIRD AYTKNPELEN LLFDDFFKDA
410 420 430 440 450
TAKAQDAWRN VTAQAVLMGI PTPALSTALN FYDGLRHEIL PANLLQAQRD
460 470 480
YFGAHTYELL HTPGKWVHTN WTGRGGNVSA STYDA
Length:485
Mass (Da):53,102
Last modified:August 1, 1998 - v1
Checksum:iF7E6DDFF3D21EFB2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y17297 mRNA. Translation: CAA76734.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y17297 mRNA. Translation: CAA76734.1.

3D structure databases

ProteinModelPortaliO60037.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO60037.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00115; UER00410.

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_CUNEL
AccessioniPrimary (citable) accession number: O60037
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: August 1, 1998
Last modified: October 5, 2016
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.