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P00349 (6PGD_SHEEP) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:PGD
OrganismOvis aries (Sheep) [Reference proteome]
Taxonomic identifier9940 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis

Protein attributes

Sequence length483 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO2, with concomitant reduction of NADP to NADPH.

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. Ref.5 Ref.6

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the 6-phosphogluconate dehydrogenase family.

Sequence caution

The sequence described in Ref.2 differs from that shown. Reason: Incorrect CNBR peptide order. Many sequencing errors.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 4834826-phosphogluconate dehydrogenase, decarboxylating
PRO_0000090066

Regions

Nucleotide binding10 – 156NADP
Nucleotide binding33 – 353NADP
Nucleotide binding75 – 773NADP
Nucleotide binding478 – 4814NADP; shared with dimeric partner By similarity
Region129 – 1313Substrate binding
Region187 – 1882Substrate binding

Sites

Active site1841Proton acceptor
Active site1911Proton donor
Binding site1031NADP
Binding site1031Substrate
Binding site1291Substrate
Binding site1921Substrate
Binding site2611Substrate; via amide nitrogen
Binding site2881Substrate
Binding site4471Substrate; shared with dimeric partner By similarity
Binding site4531Substrate; shared with dimeric partner By similarity

Amino acid modifications

Modified residue381N6-acetyllysine By similarity
Modified residue2571Phosphoserine By similarity
Modified residue2631Phosphothreonine By similarity
Modified residue2671Phosphothreonine By similarity
Modified residue2701Phosphoserine By similarity

Secondary structure

................................................................. 483
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00349 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: F4AC5DB414385F11

FASTA48352,970
        10         20         30         40         50         60 
MAQADIALIG LAVMGQNLIL NMNDHGFVVC AFNRTVSKVD DFLANEAKGT KVLGAHSLEE 

        70         80         90        100        110        120 
MVSKLKKPRR IILLVKAGQA VDNFIEKLVP LLDIGDIIID GGNSEYRDTM RRCRDLKDKG 

       130        140        150        160        170        180 
ILFVGSGVSG GEDGARYGPS LMPGGNKEAW PHIKAIFQGI AAKVGTGEPC CDWVGDDGAG 

       190        200        210        220        230        240 
HFVKMVHNGI EYGDMQLICE AYHLMKDVLG LGHKEMAKAF EEWNKTELDS FLIEITASIL 

       250        260        270        280        290        300 
KFQDADGKHL LPKIRDSAGQ KGTGKWTAIS ALEYGVPVTL IGEAVFARCL SSLKDERIQA 

       310        320        330        340        350        360 
SKKLKGPQNI PFEGDKKSFL EDIRKALYAS KIISYAQGFM LLRQAATEFG WTLNYGGIAL 

       370        380        390        400        410        420 
MWRGGCIIRS VFLGKIKDAF DRNPGLQNLL LDDFFKSAVE NCQDSWRRAI STGVQAGIPM 

       430        440        450        460        470        480 
PCFTTALSFY DGYRHAMLPA NLIQAQRDYF GAHTYELLAK PGQFIHTNWT GHGGSVSSSS 


YNA 

« Hide

References

[1]"Sheep 6-phosphogluconate dehydrogenase. Revised protein sequence based upon the sequences of cDNA clones obtained with the polymerase chain reaction."
Somers D.O., Medd S.M., Walker J.E., Adams M.J.
Biochem. J. 288:1061-1067(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Amino acid sequence of ovine 6-phosphogluconate dehydrogenase."
Carne A., Walker J.E.
J. Biol. Chem. 258:12895-12906(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-483, CLEAVAGE OF INITIATOR METHIONINE.
Tissue: Liver.
[3]"The three dimensional structure of sheep liver 6-phosphogluconate dehydrogenase at 2.6-A resolution."
Adams M.J., Archibald I.G., Bugg C.E., Carne A., Gover S., Helliwell J.R., Pickersgill R.W., White S.W.
EMBO J. 2:1009-1014(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[4]"The structure of 6-phosphogluconate dehydrogenase refined at 2.5-A resolution."
Adams M.J., Gover S., Leaback R., Phillips C., Somers D.O.
Acta Crystallogr. B 47:817-820(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[5]"Crystallographic study of coenzyme, coenzyme analogue and substrate binding in 6-phosphogluconate dehydrogenase: implications for NADP specificity and the enzyme mechanism."
Adams M.J., Ellis G.H., Gover S., Naylor C.E., Phillips C.
Structure 2:651-668(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-483 IN COMPLEXES WITH NADP AND SUBSTRATE, SUBUNIT.
[6]"Structure of 6-phosphogluconate dehydrogenase refined at 2-A resolution."
Phillips C., Gover S., Adams M.J.
Acta Crystallogr. D 51:290-304(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-483, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X60195 mRNA. Translation: CAA42751.1.
PIRS15280.
DESHGC. S27359.
RefSeqNP_001009467.1. NM_001009467.2.
UniGeneOar.419.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PGNX-ray2.30A2-483[»]
1PGOX-ray2.50A2-483[»]
1PGPX-ray2.50A2-483[»]
1PGQX-ray3.17A2-483[»]
2PGDX-ray2.00A2-483[»]
ProteinModelPortalP00349.
SMRP00349. Positions 2-474.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP00349.
ChEMBLCHEMBL1169597.

Proteomic databases

PRIDEP00349.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID443541.

Organism-specific databases

CTD5226.

Phylogenomic databases

HOVERGENHBG000029.

Enzyme and pathway databases

SABIO-RKP00349.
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...

Other

EvolutionaryTraceP00349.

Entry information

Entry name6PGD_SHEEP
AccessionPrimary (citable) accession number: P00349
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 121 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways