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P31072 (6PGD_TRYBB) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
OrganismTrypanosoma brucei brucei
Taxonomic identifier5702 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Ref.2

Sequence similarities

Belongs to the 6-phosphogluconate dehydrogenase family.

Ontologies

Keywords
   Biological processGluconate utilization
Pentose shunt
   LigandNADP
   Molecular functionOxidoreductase
   Technical term3D-structure
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_0000090071

Regions

Nucleotide binding9 – 146NADP By similarity
Nucleotide binding32 – 343NADP By similarity
Nucleotide binding77 – 793NADP By similarity
Region131 – 1333Substrate binding By similarity
Region189 – 1902Substrate binding By similarity

Sites

Active site1861Proton acceptor By similarity
Active site1931Proton donor By similarity
Binding site1051NADP By similarity
Binding site1051Substrate By similarity
Binding site1941Substrate By similarity
Binding site2631Substrate; via amide nitrogen By similarity
Binding site2901Substrate By similarity
Binding site4541Substrate; shared with dimeric partner By similarity
Binding site4601Substrate; shared with dimeric partner By similarity

Secondary structure

................................................................. 479
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P31072 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 64FED260915ABC2F

FASTA47952,154
        10         20         30         40         50         60 
MSMDVGVVGL GVMGANLALN IAEKGFKVAV FNRTYSKSEE FMKANASAPF AGNLKAFETM 

        70         80         90        100        110        120 
EAFAASLKKP RKALILVQAG AATDSTTEQL KKVFEKGDIL VDTGNAHFKD QGRRAQQLEA 

       130        140        150        160        170        180 
AGLRFLGMGI SGGEEGARKG PAFFPGGTLS VWEEIRPIVE AAAAKADDGR PCVTMNGSGG 

       190        200        210        220        230        240 
AGSCVKMYHN SGEYAILQIW GEVFDILRAM GLNNDEVAAV LEDWKSKNFL KSYMLDISIA 

       250        260        270        280        290        300 
AARAKDKDGS YLTEHVMDRI GSKGTGLWSA QEALEIGVPA PSLNMAVVSR QFTMYKTERQ 

       310        320        330        340        350        360 
ANASNAPGIT QSPGYTLKNK SPSGPEIKQL YDSVCIAIIS CYAQMFQCLR EMDKVHNFGL 

       370        380        390        400        410        420 
NLPATIATFR AGCILQGYLL KPMTEAFEKN PNISNLMCAF QTEIRAGLQN YRDMVALITS 

       430        440        450        460        470 
KLEVSIPVLS ASLNYVTAMF TPTLKYGQLV SLQRDVFGRH GYERVDKDGR ESFQWPELQ 

« Hide

References

[1]"A 6-phosphogluconate dehydrogenase gene from Trypanosoma brucei."
Barrett M.P., le Page R.W.F.
Mol. Biochem. Parasitol. 57:89-100(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 427.
[2]"A 2.8-A resolution structure of 6-phosphogluconate dehydrogenase from the protozoan parasite Trypanosoma brucei: comparison with the sheep enzyme accounts for differences in activity with coenzyme and substrate analogues."
Phillips C., Dohnalek J., Gover S., Barrett M.P., Adams M.J.
J. Mol. Biol. 282:667-681(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X65623 Genomic DNA. Translation: CAA46577.1.
PIRA48565.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PGJX-ray2.82A/B2-479[»]
ProteinModelPortalP31072.
SMRP31072. Positions 2-479.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

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...

Other

EvolutionaryTraceP31072.

Entry information

Entry name6PGD_TRYBB
AccessionPrimary (citable) accession number: P31072
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: October 16, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways