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Q7VMX4 (6PGD_HAEDU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 73. 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:HD_0833
OrganismHaemophilus ducreyi (strain 35000HP / ATCC 700724) [Complete proteome] [HAMAP]
Taxonomic identifier233412 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length484 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 – 4844846-phosphogluconate dehydrogenase, decarboxylating
PRO_0000090040

Regions

Nucleotide binding11 – 166NADP By similarity
Nucleotide binding34 – 363NADP By similarity
Nucleotide binding76 – 783NADP By similarity
Region130 – 1323Substrate binding By similarity
Region188 – 1892Substrate binding By similarity

Sites

Active site1851Proton acceptor By similarity
Active site1921Proton donor By similarity
Binding site1041NADP By similarity
Binding site1041Substrate By similarity
Binding site1931Substrate By similarity
Binding site2621Substrate; via amide nitrogen By similarity
Binding site2891Substrate By similarity
Binding site4471Substrate; shared with dimeric partner By similarity
Binding site4531Substrate; shared with dimeric partner By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VMX4 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: BA23A9A770615B23

FASTA48453,272
        10         20         30         40         50         60 
MSIKGDIGVI GLAVMGQNLI LNMNDNGFKV VAYNRTASKV DEFLAGEAKD TNIIGAYSLE 

        70         80         90        100        110        120 
DLAAKLEKPR KIMLMVRAGE VVDQFIDALL PHLEAGDIII DGGNSNYPDT NRRTITLAEK 

       130        140        150        160        170        180 
GIRFIGTGVS GGEEGARHGP SIMPGGNEEA WPFVKPILQA ISAKTDKDEP CCDWVGKEGA 

       190        200        210        220        230        240 
GHFVKMVHNG IEYGDMQLIC EAYQFLKDGL GLNYEEMHAI FADWKNTELD SYLIDITADI 

       250        260        270        280        290        300 
LAYKDADGEP LVEKILDTAG QKGTGKWTGI NALDFGIPLT LITEAVFARC VSAFKDQRVA 

       310        320        330        340        350        360 
VSQLFNKTIT PISDDKKEWI EAVRKALLAS KIISYAQGFM LIREASENFE WNINYGATAL 

       370        380        390        400        410        420 
LWREGCIIRS AFLGNIRDAY EANPGLVFLG SDPYFQNILQ SAMADWRKVV AKSIEIGIPM 

       430        440        450        460        470        480 
PCMAAAITFL DGYSSEHLPA NLLQAQRDYF GAHTYERTDK PRCSFFHTNW TGRGGNTAST 


TYDV 

« Hide

References

[1]"The complete genome sequence of Haemophilus ducreyi."
Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L., Nguyen D., Wang J., Forst C., Hood L.
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 35000HP / ATCC 700724.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017143 Genomic DNA. Translation: AAP95728.1.
RefSeqNP_873339.1. NC_002940.2.

3D structure databases

ProteinModelPortalQ7VMX4.
SMRQ7VMX4. Positions 4-475.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING233412.HD0833.

Proteomic databases

PRIDEQ7VMX4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP95728; AAP95728; HD_0833.
GeneID1490785.
KEGGhdu:HD0833.
PATRIC20178083. VBIHaeDuc133973_0685.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0362.
KOK00033.
OMAKQQIGVI.
OrthoDBEOG6MSS4W.
ProtClustDBPRK09287.

Enzyme and pathway databases

BioCycHDUC233412:GH5F-763-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_HAEDU
AccessionPrimary (citable) accession number: Q7VMX4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: October 1, 2003
Last modified: November 13, 2013
This is version 73 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