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P37754 (6PGD9_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 77. 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
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length468 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4684686-phosphogluconate dehydrogenase, decarboxylating
PRO_0000090038

Regions

Nucleotide binding10 – 156NADP By similarity
Nucleotide binding33 – 353NADP By similarity
Nucleotide binding74 – 763NADP By similarity
Region128 – 1303Substrate binding By similarity
Region186 – 1872Substrate binding By similarity

Sites

Active site1831Proton acceptor By similarity
Active site1901Proton donor By similarity
Binding site1021NADP By similarity
Binding site1021Substrate By similarity
Binding site1911Substrate By similarity
Binding site2601Substrate; via amide nitrogen By similarity
Binding site2871Substrate By similarity
Binding site4451Substrate; shared with dimeric partner By similarity
Binding site4511Substrate; shared with dimeric partner By similarity

Sequences

Sequence LengthMass (Da)Tools
P37754 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: C13D94CFD78BFF3A

FASTA46851,625
        10         20         30         40         50         60 
MSKQQIGVVG MAVMGRNLAL NIESRGYTVS VFNRSREKTE EVIAENPGKK LVPYYTVQEF 

        70         80         90        100        110        120 
VESLETPRRI LLMVKAGSGT DSAIDSLKPY LDKGDIIIDG GNTFFQDTIR RNRELSAEGF 

       130        140        150        160        170        180 
NFIGTGVSGG EEGALKGPSI MPGGQKEAYE LVAPILKQIA AVAEDGEPCV TYIGADGAGH 

       190        200        210        220        230        240 
YVKMVHNGIE YGDMQLIAEA YALLKGGLTL SNEELAQTFT EWNEGELSSY LYDITKDIFT 

       250        260        270        280        290        300 
KKDEEGKYLV DVILDEAANK GTGKWTSQSS LDLGEPLSLI TESVFPRYIS SLKDQRVAAS 

       310        320        330        340        350        360 
KVLSGPQAQP AGDKAEFIEK VRRALYLGKI VSYAQGFSQL RAASDEYNWE LNYAEIAKIF 

       370        380        390        400        410        420 
RAGCIIRAQF LQKITDAYAQ NAGIANLLLA PYFKQIADDY QQALRDVVAY AVQNGIRVPT 

       430        440        450        460 
FSAAIAYYDS YRSAVLPANL IQAQRDYFGA HTYKRTDKEG VFHTEWLE 

« Hide

References

[1]"Cloning and analysis of duplicated rfbM and rfbK genes involved in the formation of GDP-mannose in Escherichia coli O9:K30 and participation of rfb genes in the synthesis of the group I K30 capsular polysaccharide."
Jayaratne P., Bronner D., Maclachlan R.P., Dodgson C., Kido N., Whitfield C.
J. Bacteriol. 176:3126-3139(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: O9:K30:H12 / E69.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L27646 Genomic DNA. Translation: AAA21136.1.
PIRI41250.

3D structure databases

ProteinModelPortalP37754.
SMRP37754. Positions 1-466.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbP37754.
PRIDEP37754.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0362.

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...

Entry information

Entry name6PGD9_ECOLX
AccessionPrimary (citable) accession number: P37754
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: October 16, 2013
This is version 77 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