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P52207 (6PGD_BACLI) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 74. 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:gntZ
OrganismBacillus licheniformis
Taxonomic identifier1402 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length467 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
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 – 4674676-phosphogluconate dehydrogenase, decarboxylating
PRO_0000090025

Regions

Nucleotide binding9 – 146NADP By similarity
Nucleotide binding32 – 343NADP By similarity
Nucleotide binding73 – 753NADP By similarity
Region127 – 1293Substrate binding By similarity
Region184 – 1852Substrate binding By similarity

Sites

Active site1811Proton acceptor By similarity
Active site1881Proton donor By similarity
Binding site1011NADP By similarity
Binding site1011Substrate By similarity
Binding site1891Substrate By similarity
Binding site2591Substrate; via amide nitrogen By similarity
Binding site2861Substrate By similarity
Binding site4511Substrate; shared with dimeric partner By similarity

Sequences

Sequence LengthMass (Da)Tools
P52207 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 3F14CFF0320D8E52

FASTA46751,642
        10         20         30         40         50         60 
MRNTIGVIGL GVMGSNIALN MASKGEQVAV YNYTRDLTDQ LVQKTGGQTV KPYYELEDFV 

        70         80         90        100        110        120 
QSLEKPRKIF LMVTAGKPVD SVIDSLVPLL EEGDVIMDGG NSHYEDTERR YDSLKAKGIG 

       130        140        150        160        170        180 
YLGIGISGGE VGALKGPSIM PGGDRDVYEK AAPILTKIAA QVEGDPCCVY IGPKGAGHFV 

       190        200        210        220        230        240 
KMVHNGIEYA DMQLIAEAYT FLREKLLLPI DEIADIFDTW NQGELKSYLI EITAEILRKK 

       250        260        270        280        290        300 
DERTGAPLID VILDKTGQKG TGKWTSLQAI DNGIPSSIIT ESLFARYLSS LKDERTAAEN 

       310        320        330        340        350        360 
VLAGPETEER PLDQNVWIDR VRQALYMGKV CAYAQGFAQY KMTSDLNGWH LPLKDIALIF 

       370        380        390        400        410        420 
RGGCIIRAQF LNLISEVYDK QPDLSNLLVA PDFAEKLKEY QSGLRKVVCE GISSGISFPC 

       430        440        450        460 
LSTALSYYDG YRTGRSNANL LQAQANYFGA HTYERTDMEG VFHTDWY 

« Hide

References

[1]"Nucleotide sequence and features of the Bacillus licheniformis gnt operon."
Yoshida K., Seki S., Fujita Y.
DNA Res. 1:157-162(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BGSC5A2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D31631 Genomic DNA. Translation: BAA06504.1.
PIRJC2306.

3D structure databases

ProteinModelPortalP52207.
SMRP52207. Positions 3-467.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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 name6PGD_BACLI
AccessionPrimary (citable) accession number: P52207
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 16, 2013
This is version 74 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