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Protein

6-phosphogluconate dehydrogenase, decarboxylating

Gene

AN10233

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
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.

Pathway:ipentose 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 (gsdA)
  2. no protein annotated in this organism
  3. 6-phosphogluconate dehydrogenase, decarboxylating (AN10233), 6-phosphogluconate dehydrogenase, decarboxylating (AN3954.2), 6-phosphogluconate dehydrogenase, decarboxylating (ANIA_03954)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei96 – 961NADPBy similarity
Binding sitei96 – 961SubstrateBy similarity
Active sitei178 – 1781Proton acceptorBy similarity
Active sitei185 – 1851Proton donorBy similarity
Binding sitei300 – 3001SubstrateBy similarity
Binding sitei468 – 4681Substrate; shared with dimeric partnerBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 186NADPBy similarity
Nucleotide bindingi24 – 263NADPBy similarity
Nucleotide bindingi68 – 703NADPBy similarity

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
ORF Names:AN10233
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560 Componenti: Chromosome VII

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4964966-phosphogluconate dehydrogenase, decarboxylatingPRO_0000415144Add
BLAST

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliC8VP36.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni122 – 1243Substrate bindingBy similarity
Regioni181 – 1822Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

InParanoidiC8VP36.
OMAiLDGGNEW.
OrthoDBiEOG7F252Z.

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.
IPR006115. 6PGDH_NADP-bd.
IPR016040. NAD(P)-bd_dom.
IPR006183. Pgluconate_DH.
[Graphical view]
PfamiPF00393. 6PGD. 1 hit.
PF03446. NAD_binding_2. 1 hit.
[Graphical view]
PRINTSiPR00076. 6PGDHDRGNASE.
SUPFAMiSSF48179. SSF48179. 1 hit.

Sequencei

Sequence statusi: Complete.

C8VP36-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSMMAFAFS EIGLDVSIWD VKYDNVQQLL ESAKNTNYKG KIEGFKDVSK
60 70 80 90 100
FTQSLEGKAE RKIFLFSITH GDPADSVLDM IKKDLKKGDI ILDGGNENYR
110 120 130 140 150
RTEARQKICE KIGVSWIGLG VSGGYQSARR GPSLSPGGDK EALDLVMPLL
160 170 180 190 200
ELYAGKDAKS GQPCVTRIGP KGSGHFVKMV HNGIEGGMLS TLAEAWSLLH
210 220 230 240 250
YGRGMGYEEI ADLFESWNKE GVLRNNYLLE IGAELLRVKK TPQGDGNGEG
260 270 280 290 300
VGDGGFVLDD VLDKVVQDDD NTEGTPYWSV MESASRHISA PTLATAHFMR
310 320 330 340 350
IASGNRIERL EVAKQLRIPS PSPIRGMKDI EAFKEHLHSA VYSSFLASFC
360 370 380 390 400
QGLELIARAS EDEGWDIDLG KCLQIWRSGC IIRSEGIADI LQPAVSGNKG
410 420 430 440 450
IKNMKYIDTV AQELHRTYPS LKEIVMAATD SDHYIPAISA TLEYLKYEGG
460 470 480 490
TNLPTKFMEA QMDFFGAHGY NLPGVPGEDP GPVSKGPHHY EWRPAK
Length:496
Mass (Da):54,500
Last modified:November 3, 2009 - v1
Checksum:iE7D424769A85EAC4
GO

Sequence cautioni

The sequence EAA64021.1 differs from that shown. Reason: Erroneous gene model prediction. The predicted gene AN1735 has been split into 2 genes: AN10230 and AN10233.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACD01000027 Genomic DNA. Translation: EAA64021.1. Sequence problems.
BN001307 Genomic DNA. Translation: CBF85462.1.

Genome annotation databases

EnsemblFungiiCADANIAT00008380; CADANIAP00008380; CADANIAG00008380.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACD01000027 Genomic DNA. Translation: EAA64021.1. Sequence problems.
BN001307 Genomic DNA. Translation: CBF85462.1.

3D structure databases

ProteinModelPortaliC8VP36.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00008380; CADANIAP00008380; CADANIAG00008380.

Phylogenomic databases

InParanoidiC8VP36.
OMAiLDGGNEW.
OrthoDBiEOG7F252Z.

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.
IPR006115. 6PGDH_NADP-bd.
IPR016040. NAD(P)-bd_dom.
IPR006183. Pgluconate_DH.
[Graphical view]
PfamiPF00393. 6PGD. 1 hit.
PF03446. NAD_binding_2. 1 hit.
[Graphical view]
PRINTSiPR00076. 6PGDHDRGNASE.
SUPFAMiSSF48179. SSF48179. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  2. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Entry informationi

Entry namei6PGD_EMENI
AccessioniPrimary (citable) accession number: C8VP36
Secondary accession number(s): Q5BCJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: November 3, 2009
Last modified: July 22, 2015
This is version 34 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. 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.