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A4QE39 (A4QE39_CORGB) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
6-phosphogluconate dehydrogenase, decarboxylating PIRNR PIRNR000109 RuleBase RU000485

EC=1.1.1.44 PIRNR PIRNR000109 RuleBase RU000485
Gene names
Ordered Locus Names:cgR_1513
OrganismCorynebacterium glutamicum (strain R) [Complete proteome] [HAMAP]
Taxonomic identifier340322 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length492 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. PIRNR PIRNR000109

Catalytic activity

6-phospho-D-gluconate + NADP+ = D-ribulose 5-phosphate + CO2 + NADPH. PIRNR PIRNR000109 RuleBase RU000485

Pathway

Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 3/3. PIRNR PIRNR000109

Subunit structure

Homodimer By similarity. PIRNR PIRNR000109

Sequence similarities

Belongs to the 6-phosphogluconate dehydrogenase family. PIRNR PIRNR000109 RuleBase RU000485

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding22 – 276NADP By similarity PIRSR PIRSR000109-3
Nucleotide binding45 – 473NADP By similarity PIRSR PIRSR000109-3
Nucleotide binding87 – 893NADP By similarity PIRSR PIRSR000109-3
Region141 – 1433Substrate binding By similarity PIRSR PIRSR000109-2
Region198 – 1992Substrate binding By similarity PIRSR PIRSR000109-2

Sites

Active site1951Proton acceptor By similarity PIRSR PIRSR000109-1
Active site2021Proton donor By similarity PIRSR PIRSR000109-1
Binding site1151NADP By similarity PIRSR PIRSR000109-3
Binding site1151Substrate By similarity PIRSR PIRSR000109-2
Binding site2031Substrate By similarity PIRSR PIRSR000109-2
Binding site2731Substrate; via amide nitrogen By similarity PIRSR PIRSR000109-2
Binding site3001Substrate By similarity PIRSR PIRSR000109-2
Binding site4621Substrate; shared with dimeric partner By similarity PIRSR PIRSR000109-2
Binding site4681Substrate; shared with dimeric partner By similarity PIRSR PIRSR000109-2

Sequences

Sequence LengthMass (Da)Tools
A4QE39 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: B3BEF808693F0E77

FASTA49252,602
        10         20         30         40         50         60 
MPSSTINNMT NGDNLAQIGV VGLAVMGSNL ARNFARNGHT VAVYNRSTDK TDKLIADHGS 

        70         80         90        100        110        120 
EGNFIPSATV EEFVASLEKP RRAIIMVQAG NATDAVINQL ADAMDEGDII IDGGNALYTD 

       130        140        150        160        170        180 
TIRREKEISA RGLHFVGAGI SGGEEGALNG PSIMPGGPAK SYESLGPLLE SIAANVDGTP 

       190        200        210        220        230        240 
CVTHIGPDGA GHFVKMVHNG IEYADMQVIG EAYHLLRYAA GMQPAEIAEV FKEWNAGDLD 

       250        260        270        280        290        300 
SYLIEITAEV LSQVDAETGK PLIDVIVDAA GQKGTGRWTV KAALDLGIAT TGIGEAVFAR 

       310        320        330        340        350        360 
ALSGATSQRA AAQGNLPAGV LTDLEALGVD KAQFVEDVRR ALYASKLVAY AQGFDEIKAG 

       370        380        390        400        410        420 
SDENNWDVDP RDLATIWRGG CIIRAKFLNR IVEAYDANAE LESLLLDPYF KSELGDLIDS 

       430        440        450        460        470        480 
WRRVIVTATQ LGLPIPVFAS SLSYYDSLRA ERLPAALIQG QRDFFGAHTY KRIDKDGSFH 

       490 
TEWSGDRSEV EA 

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References

[1]"Comparative analysis of the Corynebacterium glutamicum group and complete genome sequence of strain R."
Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M., Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.
Microbiology 153:1042-1058(2007) [PubMed: 17379713] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: R.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009044 Genomic DNA. Translation: BAF54505.1.
RefSeqYP_001138407.1. NC_009342.1.

3D structure databases

ProteinModelPortalA4QE39.
SMRA4QE39. Positions 16-484.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4QE39.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4993244.
GenomeReviewsGene locus cgR_1513 in contig AP009044_GR.
KEGGcgt:cgR_1513.
PATRIC21507614. VBICorGlu58097_1560.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0362.
HOGENOMHBG286913.
OMASNYPDTN.
ProtClustDBPRK09287.

Family and domain databases

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]
Gene3DG3DSA:1.20.5.320. Fibritin/6PGD_C-extension. 1 hit.
G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
G3DSA:1.10.1040.10. Opine_DH. 1 hit.
KOK00033.
PfamPF00393. 6PGD. 1 hit.
PF03446. NAD_binding_2. 1 hit.
[Graphical view]
PIRSFPIRSF000109. 6PGD. 1 hit.
SUPFAMSSF48179. 6DGDH_C_like. 1 hit.
TIGRFAMsTIGR00873. Gnd. 1 hit.
PROSITEPS00461. 6PGD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA4QE39_CORGB
AccessionPrimary (citable) accession number: A4QE39
Entry history
Integrated into UniProtKB/TrEMBL: May 15, 2007
Last sequence update: May 15, 2007
Last modified: January 25, 2012
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)