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Protein

6-phosphogluconate dehydrogenase, decarboxylating

Gene

DOR14

Organism
Candida albicans (Yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 (DOR14)
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 sitei128NADPBy similarity1
Binding sitei128SubstrateBy similarity1
Active sitei208Proton acceptorBy similarity1
Active sitei215Proton donorBy similarity1
Binding sitei216SubstrateBy similarity1
Binding sitei286Substrate; via amide nitrogenBy similarity1
Binding sitei313SubstrateBy similarity1
Binding sitei474Substrate; shared with dimeric partnerBy similarity1
Binding sitei480Substrate; shared with dimeric partnerBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi35 – 40NADPBy similarity6
Nucleotide bindingi58 – 60NADPBy similarity3
Nucleotide bindingi100 – 102NADPBy 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:DOR14
OrganismiCandida albicans (Yeast)
Taxonomic identifieri5476 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000900721 – 5176-phosphogluconate dehydrogenase, decarboxylatingAdd BLAST517

Proteomic databases

PRIDEiO13287.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO13287.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni154 – 156Substrate bindingBy similarity3
Regioni211 – 212Substrate 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.

O13287-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNFNALSRL SILSKQLSFN NTNSSIARGD IGLIGLAVMG QNLILNMADH
60 70 80 90 100
GYTVVAYNRT TAKVDRFLEN EAKGKSILGA HSIKELVDQL KRPRRIMLLV
110 120 130 140 150
KAGAPVDEFI NQLLPYLEEG DIIIDGGNSH FPDSNRRYEE LAKKGILFVG
160 170 180 190 200
SGVSGGEEGA RTGPSLMPGG NEKAWPHIKE IFQDVAAKSD GEPCCDWVGD
210 220 230 240 250
AGAGHYVKMV HNGIEYGDMQ LICEAYDLMK RVGKFEDKEI GDVFATWNKG
260 270 280 290 300
VLDSFLIEIT RDILYYNDPT DGKPLVEKIL DTAGQKGTGK WTAVNALDLG
310 320 330 340 350
IPVTLIGEAV FSRCLSAMKA ERVEASKALK GPQVTGESPI TDKKQFIDDL
360 370 380 390 400
EQALYASKII SYTQGFMLMN QAAKDYGWKL NNAGIALMWR GGCIIRSVFL
410 420 430 440 450
AEITAAYRKK PDLENLLLYP FFNDAITKAQ SGWRASVGKA IQYGIPTPAF
460 470 480 490 500
STALAFYDGL RSERLPANLL QAQRDYFGAH TFKVLPGQEN ELLKKDEWIH
510
INWTGRGGDV SSTTYDA
Length:517
Mass (Da):56,924
Last modified:January 1, 1998 - v1
Checksum:i91E3F520FFCABF7A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB006102 Genomic DNA. Translation: BAA21690.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB006102 Genomic DNA. Translation: BAA21690.1.

3D structure databases

ProteinModelPortaliO13287.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO13287.

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_CANAX
AccessioniPrimary (citable) accession number: O13287
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: October 5, 2016
This is version 88 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.