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Reviewed, UniProtKB/Swiss-Prot P11411 (G6PD_LEUME)

Last modified November 25, 2008. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Glucose-6-phosphate 1-dehydrogenase
      Short name=G6PD
    EC=1.1.1.49
Gene names
Name: zwf
OrganismLeuconostoc mesenteroides
Taxonomic identifier1245 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Leuconostoc

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Protein attributes

Sequence length486 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

D-glucose 6-phosphate + NADP(+) = D-glucono-1,5-lactone 6-phosphate + NADPH.

Pathway

Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the glucose-6-phosphate dehydrogenase family.

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Ontologies

Keywords

   Biological processCarbohydrate metabolism
Glucose metabolism
   LigandNAD
NADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Direct protein sequencing

Gene Ontology (GO)

   Biological processglucose metabolic process

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionbinding

Inferred from electronic annotation. Source: InterPro

glucose-6-phosphate dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 486485Glucose-6-phosphate 1-dehydrogenase
PRO_0000068125

Sites

Active site2411Proton acceptor
Binding site151NADP
Binding site471NADP
Binding site1791Substrate
Binding site1831Substrate
Binding site3441Substrate

Experimental info

Mutagenesis221K → Q: Decreases KM for substrate over 30-fold
Mutagenesis471R → A: Strongly reduces affinity for NADP
Mutagenesis1781D → N: Decreases Kcat over 100-fold
Mutagenesis1791H → N: Decreases KM for substrate over 200-fold
Mutagenesis1831K → Q: Decreases KM for substrate 1000-fold
Mutagenesis2411H → N: Decreases Kcat over 10000-fold
Mutagenesis3441K → Q: Decreases KM for substrate over 300-fold
Sequence conflict154 – 1563SYD → HYI AA sequence Ref.2
Sequence conflict1651L → F AA sequence Ref.2

Secondary structure

1 ....................................................................................... 486
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P11411-1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: AA43433F83ED091D

FASTA48654,441
        10         20         30         40         50         60 
MVSEIKTLVT FFGGTGDLAK RKLYPSVFNL YKKGYLQKHF AIVGTARQAL NDDEFKQLVR 

        70         80         90        100        110        120 
DSIKDFTDDQ AQAEAFIEHF SYRAHDVTDA ASYAVLKEAI EEAADKFDID GNRIFYMSVA 

       130        140        150        160        170        180 
PRFFGTIAKY LKSEGLLADT GYNRLMIEKP FGTSYDTAAE LQNDLENAFD DNQLFRIDHY 

       190        200        210        220        230        240 
LGKEMVQNIA ALRFGNPIFD AAWNKDYIKN VQVTLSEVLG VEERAGYYDT AGALLDMIQN 

       250        260        270        280        290        300 
HTMQIVGWLA MEKPESFTDK DIRAAKNAAF NALKIYDEAE VNKYFVRAQY GAGDSADFKP 

       310        320        330        340        350        360 
YLEELDVPAD SKNNTFIAGE LQFDLPRWEG VPFYVRSGKR LAAKQTRVDI VFKAGTFNFG 

       370        380        390        400        410        420 
SEQEAQEAVL SIIIDPKGAI ELKLNAKSVE DAFNTRTIDL GWTVSDEDKK NTPEPYERMI 

       430        440        450        460        470        480 
HDTMNGDGSN FADWNGVSIA WKFVDAISAV YTADKAPLET YKSGSMGPEA SDKLLAANGD 


AWVFKG

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References

[1]"Cloning of the gene and amino acid sequence for glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides."
Lee W.T., Flynn T.G., Lyons C., Levy H.R.
J. Biol. Chem. 266:13028-13034(1991) [PubMed: 2071589] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequence identity between a lysine-containing peptide from Leuconostoc mesenteroides glucose-6-phosphate dehydrogenase and an active site peptide from human erythrocyte glucose-6-phosphate dehydrogenase."
Bhadbhade M.M., Adams M.J., Flynn T.G., Levy H.R.
FEBS Lett. 211:243-246(1987) [PubMed: 3100332] [Abstract]
Cited for: PROTEIN SEQUENCE OF 147-188.
[3]"Lysine-21 of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase participates in substrate binding through charge-charge interaction."
Lee W.T., Levy H.R.
Protein Sci. 1:329-334(1992) [PubMed: 1304341] [Abstract]
Cited for: IMPORTANCE OF LYS-22 FOR SUBSTRATE-BINDING.
[4]"Delineation of the roles of amino acids involved in the catalytic functions of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase."
Vought V., Ciccone T., Davino M.H., Fairbairn L., Lin Y., Cosgrove M.S., Adams M.J., Levy H.R.
Biochemistry 39:15012-15021(2000) [PubMed: 11106479] [Abstract]
Cited for: MUTAGENESIS OF LYS-22; ARG-47; LYS-183 AND LYS-344.
[5]"The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides refined at 2.0-A resolution."
Rowland P., Basak A.K., Gover S., Levy H.R., Adams M.J.
Structure 2:1073-1087(1994) [PubMed: 7881907] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[6]"On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase."
Cosgrove M.S., Naylor C., Paludan S., Adams M.J., Levy H.R.
Biochemistry 37:2759-2767(1998) [PubMed: 9485426] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT ASN-241, MUTAGENESIS OF ASP-178; HIS-179 AND HIS-241.
[7]"An examination of the role of asp-177 in the His-Asp catalytic dyad of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: X-ray structure and pH dependence of kinetic parameters of the D177N mutant enzyme."
Cosgrove M.S., Gover S., Naylor C.E., Vandeputte-Rutten L., Adams M.J., Levy H.R.
Biochemistry 39:15002-15011(2000) [PubMed: 11106478] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANTS ASN-178 AND CYS-366 IN COMPLEX WITH NAD; NADP AND SUBSTRATE.
+Additional computationally mapped references.

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Cross-references

Sequence databases

M64446 Genomic DNA. Translation: AAA25265.1.
PIRA39864.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1DPGX-ray2.00A/B1-486[»]
1E77X-ray2.69A1-486[»]
1E7MX-ray2.54A1-486[»]
1E7YX-ray2.48A1-486[»]
1H93X-ray2.20A1-486[»]
1H94X-ray2.50A1-486[»]
1H9AX-ray2.16A1-486[»]
1H9BX-ray2.40A1-486[»]
2DPGX-ray2.50A1-486[»]
ModBaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MON-13060.

Family and domain databases

InterProIPR001282. Glc-6-P_DHase.
IPR016040. NAD(P)-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR23429. G6PDH. 1 hit.
PfamPF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
[Graphical view]
PIRSFPIRSF000110. G6PD. 1 hit.
PRINTSPR00079. G6PDHDRGNASE.
ProDomPD001129. G6PD. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00871. zwf. 1 hit.
PROSITEPS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

LinkHubP11411.