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Q9Z8I3 (6PGD_CHLPN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 103. 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:CPn_0360, CP_0398, CpB0369
OrganismChlamydia pneumoniae (Chlamydophila pneumoniae) [Complete proteome] [HAMAP]
Taxonomic identifier83558 [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_0000090032

Regions

Nucleotide binding9 – 146NADP By similarity
Nucleotide binding32 – 343NADP By similarity
Nucleotide binding74 – 763NADP By similarity
Region128 – 1303Substrate binding By similarity
Region185 – 1862Substrate binding By similarity

Sites

Active site1821Proton acceptor By similarity
Active site1891Proton donor By similarity
Binding site1021NADP By similarity
Binding site1021Substrate By similarity
Binding site1901Substrate By similarity
Binding site2591Substrate; via amide nitrogen By similarity
Binding site2861Substrate By similarity
Binding site4461Substrate; shared with dimeric partner By similarity
Binding site4521Substrate; shared with dimeric partner By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9Z8I3 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 0FD301D3378E11F4

FASTA47952,939
        10         20         30         40         50         60 
MQTNIGLIGL AVMGKNLVLN MIDHGFSVSV YNRTPEKTRD FLKEYPNHRE LVGFESLEDF 

        70         80         90        100        110        120 
VNSLERPRKI MLMIQAGKPV DQSIHALLPF LEPGDVIIDG GNSYFKDSER RCKELQEKGI 

       130        140        150        160        170        180 
LFLGVGISGG EEGARHGPSI MPGGNPEAWP LVAPIFQSIA AKVQGRPCCS WVGTGGAGHY 

       190        200        210        220        230        240 
VKAVHNGIEY GDIQLICEAY GILRDFLKLS ATAVATILKE WNTLELESYL IRIASEVLAL 

       250        260        270        280        290        300 
KDPEGIPVID TILDVVGQKG TGKWTAIDAL NSGVPLSLII GAVLARFLSS WKEIREQAAR 

       310        320        330        340        350        360 
NYPGTPLIFE MPHDPSVFIQ DVFHALYASK IISYAQGFML LGEASKEYNW GLDLGEIALM 

       370        380        390        400        410        420 
WRGGCIIQSA FLDVIHKGFA ANPENTSLIF QEYFRGALRH AEMGWRRTVV TAIGAGLPIP 

       430        440        450        460        470 
CLAAAITFYD GYRTASSSMS LAQGLRDYFG AHTYERNDRP RGEFYHTDWV HTKTTERVK 

« Hide

References

[1]"Comparative genomes of Chlamydia pneumoniae and C. trachomatis."
Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., Olinger L., Grimwood J., Davis R.W., Stephens R.S.
Nat. Genet. 21:385-389(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CWL029.
[2]"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39."
Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. expand/collapse author list , Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.
Nucleic Acids Res. 28:1397-1406(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AR39.
[3]"Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA."
Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.
Nucleic Acids Res. 28:2311-2314(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J138.
[4]"The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis."
Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TW-183.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001363 Genomic DNA. Translation: AAD18504.1.
AE002161 Genomic DNA. Translation: AAF38243.1.
BA000008 Genomic DNA. Translation: BAA98568.1.
AE009440 Genomic DNA. Translation: AAP98300.1.
PIRC72088.
F86535.
RefSeqNP_224560.1. NC_000922.1.
NP_300417.1. NC_002491.1.
NP_444947.1. NC_002179.2.
NP_876643.1. NC_005043.1.

3D structure databases

ProteinModelPortalQ9Z8I3.
SMRQ9Z8I3. Positions 2-471.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING115713.CPn0360.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD18504; AAD18504; CPn_0360.
AAF38243; AAF38243; CP_0398.
AAP98300; AAP98300; CpB0369.
BAA98568; BAA98568; BAA98568.
GeneID1467050.
895135.
919866.
963777.
KEGGcpa:CP0398.
cpj:CPj0360.
cpn:CPn0360.
cpt:CpB0369.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0362.
HOGENOMHOG000255147.
KOK00033.
OMAKQQIGVI.
OrthoDBEOG6MSS4W.
ProtClustDBPRK09287.

Enzyme and pathway databases

BioCycCPNE115711:GI7B-413-MONOMER.
CPNE115713:GHEY-374-MONOMER.
CPNE138677:GH8N-369-MONOMER.
CPNE182082:GH4N-379-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_CHLPN
AccessionPrimary (citable) accession number: Q9Z8I3
Secondary accession number(s): Q9JQC1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: November 13, 2013
This is version 103 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