Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9PKX7 (6PGD_CHLMU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
6-phosphogluconate dehydrogenase, decarboxylating

EC=1.1.1.44
Gene names
Name:gnd
Ordered Locus Names:TC_0333
OrganismChlamydia muridarum (strain MoPn / Nigg) [Complete proteome] [HAMAP]
Taxonomic identifier243161 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

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

Pathway

Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 3/3.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the 6-phosphogluconate dehydrogenase family.

Ontologies

Keywords
   Biological processGluconate utilization
Pentose shunt
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processD-gluconate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

pentose-phosphate shunt

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionNADP binding

Inferred from electronic annotation. Source: InterPro

phosphogluconate dehydrogenase (decarboxylating) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4794796-phosphogluconate dehydrogenase, decarboxylating
PRO_0000090031

Regions

Nucleotide binding10 – 156NADP By similarity
Nucleotide binding33 – 353NADP By similarity
Nucleotide binding75 – 773NADP By similarity
Region129 – 1313Substrate binding By similarity
Region186 – 1872Substrate binding By similarity

Sites

Active site1831Proton acceptor By similarity
Active site1901Proton donor By similarity
Binding site1031NADP By similarity
Binding site1031Substrate By similarity
Binding site1911Substrate By similarity
Binding site2601Substrate; via amide nitrogen By similarity
Binding site2871Substrate By similarity
Binding site4471Substrate; shared with dimeric partner By similarity
Binding site4531Substrate; shared with dimeric partner By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PKX7 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 3501DD6DAA0B8F8B

FASTA47952,689
        10         20         30         40         50         60 
MAPADIGLIG LAVMGKNLVL NMIDHGFAVS VYNRSPEKTE EFLKEHGENI SLQGFTAIEE 

        70         80         90        100        110        120 
FVQSLKRPRK IMIMIKAGAP VDEMISSLLP FLEEGDILID GGNSYYLDSE RRYIDLKKKG 

       130        140        150        160        170        180 
ILFVGMGVSG GEEGARKGPS IMPGGNIEAW PVIAPIFQSI AAQVDGQPCC SWIGTGGAGH 

       190        200        210        220        230        240 
FVKAVHNGIE YGDIQLICET YEILKSRLDL SLEQIGNIFF EWNQTDLNSY LMGASAAVLT 

       250        260        270        280        290        300 
AKDENGVAVA STILDVAGQK GTGRWVAEDA IKAGVPMSLI IESVLARYLS AWKEVRRQAA 

       310        320        330        340        350        360 
REFPVASLLY QPSQEASVLI EDAREALYAA KIISYAQGFM LLKQISEERN WDLNLGELAL 

       370        380        390        400        410        420 
IWRGGCIIQS AFLDKIHQGF ESCPDAHSLM LQDYFKNVLL NSETGFRRAI LHAVGAGVAI 

       430        440        450        460        470 
PCLASALAFY DGYRTENSPL FLVQGLRDYF GAHGYERQDR PRGEFYHTDW LGSKNASRM 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE002160 Genomic DNA. Translation: AAF39196.1.
PIRA81714.
RefSeqNP_296712.1. NC_002620.2.

3D structure databases

ProteinModelPortalQ9PKX7.
SMRQ9PKX7. Positions 2-473.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243161.TC0333.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF39196; AAF39196; TC_0333.
GeneID1246377.
KEGGcmu:TC_0333.
PATRIC20372076. VBIChlMur19118_0362.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0362.
KOK00033.
OMAEAYFFMK.
OrthoDBEOG6MSS4W.

Enzyme and pathway databases

BioCycCMUR243161:GHYU-349-MONOMER.
UniPathwayUPA00115; UER00410.

Family and domain databases

Gene3D1.10.1040.10. 1 hit.
1.20.5.320. 1 hit.
3.40.50.720. 1 hit.
InterProIPR008927. 6-PGluconate_DH_C-like.
IPR006114. 6PGDH_C.
IPR006113. 6PGDH_decarbox.
IPR006115. 6PGDH_NADP-bd.
IPR006184. 6PGdom_BS.
IPR013328. DH_multihelical.
IPR012284. Fibritin/6PGD_C-extension.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00393. 6PGD. 1 hit.
PF03446. NAD_binding_2. 1 hit.
[Graphical view]
PIRSFPIRSF000109. 6PGD. 1 hit.
SUPFAMSSF48179. SSF48179. 1 hit.
TIGRFAMsTIGR00873. gnd. 1 hit.
PROSITEPS00461. 6PGD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry name6PGD_CHLMU
AccessionPrimary (citable) accession number: Q9PKX7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways