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A3Q0E2 (A3Q0E2_MYCSJ) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 39. 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:Mjls_2839
OrganismMycobacterium sp. (strain JLS) [Complete proteome] [HAMAP]
Taxonomic identifier164757 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length486 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 binding18 – 236NADP By similarity PIRSR PIRSR000109-3
Nucleotide binding41 – 433NADP By similarity PIRSR PIRSR000109-3
Nucleotide binding83 – 853NADP By similarity PIRSR PIRSR000109-3
Region137 – 1393Substrate binding By similarity PIRSR PIRSR000109-2
Region194 – 1952Substrate binding By similarity PIRSR PIRSR000109-2

Sites

Active site1911Proton acceptor By similarity PIRSR PIRSR000109-1
Active site1981Proton donor By similarity PIRSR PIRSR000109-1
Binding site1111NADP By similarity PIRSR PIRSR000109-3
Binding site1111Substrate By similarity PIRSR PIRSR000109-2
Binding site1991Substrate By similarity PIRSR PIRSR000109-2
Binding site2691Substrate; via amide nitrogen By similarity PIRSR PIRSR000109-2
Binding site2961Substrate By similarity PIRSR PIRSR000109-2
Binding site4541Substrate; shared with dimeric partner By similarity PIRSR PIRSR000109-2
Binding site4601Substrate; shared with dimeric partner By similarity PIRSR PIRSR000109-2

Sequences

Sequence LengthMass (Da)Tools
A3Q0E2 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: A1C7DE6872E8D774

FASTA48652,428
        10         20         30         40         50         60 
MSSSEKSTAG TAQIGVTGLA VMGSNIARNF ARHGYTVALH NRSVAKTDAL LAEHGSEGSF 

        70         80         90        100        110        120 
VRTETIPEFL AALEKPRRVL IMVKAGEATD AVINELADAM EDGDIIIDGG NALYTDTIRR 

       130        140        150        160        170        180 
EKAIRERGLH FVGAGISGGE EGALNGPSIM PGGPAESYES LGPLLEEISA HVDGVPCCTH 

       190        200        210        220        230        240 
IGPDGAGHFV KMVHNGIEYS DMQLIGEAYQ LLRDGLGKSA PEIAEVFDEW NRGDLDSFLV 

       250        260        270        280        290        300 
EITAQVLRQI DEKTGKPLVD LILDEAEQKG TGRWTVKSAL DLGVPVTGIA EAVFARALSG 

       310        320        330        340        350        360 
SVAQRQATTG LASGDLGEKP SDAEQFTEDI RQALYASKII AYAQGFNQIQ AGSAEYDWGI 

       370        380        390        400        410        420 
TPGDMATIWR GGCIIRAKFL NRIKDAFDND PDLPTLIVDP YFRDAIENAI DSWRRVVVKA 

       430        440        450        460        470        480 
TELGIPIPGF SSALSYYDGL RTERLPAALT QGLRDFFGAH TYGRIDTDRD KRFHTLWSGD 


RSEVEA 

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References

[1]"Complete sequence of Mycobacterium sp. JLS."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J., Sims R.C., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JLS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000580 Genomic DNA. Translation: ABN98619.1.
RefSeqYP_001071110.1. NC_009077.1.

3D structure databases

ProteinModelPortalA3Q0E2.
SMRA3Q0E2. Positions 12-478.
ModBaseSearch...

Protein-protein interaction databases

STRINGA3Q0E2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000052000; EBMYCP00000050281; EBMYCG00000051995.
GeneID4878553.
GenomeReviewsGene locus Mjls_2839 in contig CP000580_GR.
KEGGmjl:Mjls_2839.
PATRIC18091845. VBIMycSp51234_2858.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0362.
GeneTreeEBGT00050000015862.
HOGENOMHBG286913.
OMASNYPDTN.
PhylomeDBA3Q0E2.
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 nameA3Q0E2_MYCSJ
AccessionPrimary (citable) accession number: A3Q0E2
Entry history
Integrated into UniProtKB/TrEMBL: April 3, 2007
Last sequence update: April 3, 2007
Last modified: January 25, 2012
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)