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UniProtKB/Swiss-Prot entry P11411


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name G6PD_LEUME
Primary accession number P11411
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1989
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    July 22, 2008 (Entry version 83)
Name and origin of the protein
Protein name Glucose-6-phosphate 1-dehydrogenase
Synonyms G6PD
EC 1.1.1.49
Gene name
Name: zwf
From
Leuconostoc mesenteroides [TaxID: 1245] 
Taxonomy Bacteria; Firmicutes; Lactobacillales; Leuconostoc.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2071589 [NCBI, ExPASy, EBI, Israel, Japan]
Lee W.T., Flynn T.G., Lyons C., Levy H.R.;
"Cloning of the gene and amino acid sequence for glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides.";
J. Biol. Chem. 266:13028-13034(1991).
[2]
PROTEIN SEQUENCE OF 147-188.
DOI=10.1016/0014-5793(87)81445-X; PubMed=3100332 [NCBI, ExPASy, EBI, Israel, Japan]
Bhadbhade M.M., Adams M.J., Flynn T.G., Levy H.R.;
"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.";
FEBS Lett. 211:243-246(1987).
[3]
IMPORTANCE OF LYS-22 FOR SUBSTRATE-BINDING.
PubMed=1304341 [NCBI, ExPASy, EBI, Israel, Japan]
Lee W.T., Levy H.R.;
"Lysine-21 of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase participates in substrate binding through charge-charge interaction.";
Protein Sci. 1:329-334(1992).
[4]
MUTAGENESIS OF LYS-22; ARG-47; LYS-183 AND LYS-344.
DOI=10.1021/bi0014610; PubMed=11106479 [NCBI, ExPASy, EBI, Israel, Japan]
Vought V., Ciccone T., Davino M.H., Fairbairn L., Lin Y., Cosgrove M.S., Adams M.J., Levy H.R.;
"Delineation of the roles of amino acids involved in the catalytic functions of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase.";
Biochemistry 39:15012-15021(2000).
[5]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
DOI=10.1016/S0969-2126(94)00110-3; PubMed=7881907 [NCBI, ExPASy, EBI, Israel, Japan]
Rowland P., Basak A.K., Gover S., Levy H.R., Adams M.J.;
"The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides refined at 2.0-A resolution.";
Structure 2:1073-1087(1994).
[6]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT ASN-241, AND MUTAGENESIS OF ASP-178; HIS-179 AND HIS-241.
DOI=10.1021/bi972069y; PubMed=9485426 [NCBI, ExPASy, EBI, Israel, Japan]
Cosgrove M.S., Naylor C., Paludan S., Adams M.J., Levy H.R.;
"On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase.";
Biochemistry 37:2759-2767(1998).
[7]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANTS ASN-178 AND CYS-366 IN COMPLEX WITH NAD; NADP AND SUBSTRATE.
DOI=10.1021/bi0014608; PubMed=11106478 [NCBI, ExPASy, EBI, Israel, Japan]
Cosgrove M.S., Gover S., Naylor C.E., Vandeputte-Rutten L., Adams M.J., Levy H.R.;
"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.";
Biochemistry 39:15002-15011(2000).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M64446; AAA25265.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A39864; A39864.
3D structure databases
PDB
1DPG; X-ray; 2.00 A; A/B=1-486.[ExPASy / RCSB / EBI]
1E77; X-ray; 2.69 A; A=1-486.[ExPASy / RCSB / EBI]
1E7M; X-ray; 2.54 A; A=1-486.[ExPASy / RCSB / EBI]
1E7Y; X-ray; 2.48 A; A=1-486.[ExPASy / RCSB / EBI]
1H93; X-ray; 2.20 A; A=1-486.[ExPASy / RCSB / EBI]
1H94; X-ray; 2.50 A; A=1-486.[ExPASy / RCSB / EBI]
1H9A; X-ray; 2.16 A; A=1-486.[ExPASy / RCSB / EBI]
1H9B; X-ray; 2.40 A; A=1-486.[ExPASy / RCSB / EBI]
2DPG; X-ray; 2.50 A; A=1-486.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1DPG; -.
1E77; -.
1E7M; -.
1E7Y; -.
1H93; -.
1H94; -.
1H9A; -.
1H9B; -.
2DPG; -.
ModBase P11411.
Enzyme and pathway databases
BioCyc MetaCyc:MON-13060; -.
Family and domain databases
InterPro IPR001282; Glc-6-P_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR23429; G6PDH; 1.
Pfam PF02781; G6PD_C; 1.
PF00479; G6PD_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000110; G6PD; 1.
PRINTS PR00079; G6PDHDRGNASE.
ProDom PD001129; G6PD; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00871; zwf; 1.
PROSITE PS00069; G6P_DEHYDROGENASE; 1.
BLOCKS P11411.
Other
LinkHub P11411; -.
ProtoNet P11411.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Carbohydrate metabolism; Direct protein sequencing; Glucose metabolism; NAD; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   486  485     Glucose-6-phosphate 1-dehydrogenase. PRO_0000068125
ACT_SITE   241   241        Proton acceptor. 
BINDING   15    15        NADP. 
BINDING   47    47        NADP. 
BINDING   179   179        Substrate. 
BINDING   183   183        Substrate. 
BINDING   344   344        Substrate. 
MUTAGEN   22    22        K->Q: Decreases KM for substrate over 30-fold. 
MUTAGEN   47    47        R->A: Strongly reduces affinity for NADP. 
MUTAGEN   178   178        D->N: Decreases Kcat over 100-fold. 
MUTAGEN   179   179        H->N: Decreases KM for substrate over 200-fold. 
MUTAGEN   183   183        K->Q: Decreases KM for substrate 1000-fold. 
MUTAGEN   241   241        H->N: Decreases Kcat over 10000-fold. 
MUTAGEN   344   344        K->Q: Decreases KM for substrate over 300-fold. 
CONFLICT   154   156        SYD -> HYI (in Ref. 2; AA sequence). 
CONFLICT   165   165        L -> F (in Ref. 2; AA sequence). 
STRAND   7    12  6      
TURN   13    15  3      
HELIX   17    21  5      
HELIX   23    32  10      
STRAND   38    48  11      
HELIX   52    63  12      
HELIX   64    66  3      
HELIX   70    77  8      
STRAND   80    84  5      
HELIX   92   106  15      
STRAND   113   117  5      
HELIX   121   123  3      
HELIX   124   133  10      
STRAND   139   141  3      
STRAND   143   147  5      
HELIX   155   165  11      
TURN   166   168  3      
HELIX   171   173  3      
STRAND   174   176  3      
HELIX   179   182  4      
HELIX   184   188  5      
HELIX   189   194  6      
HELIX   197   200  4      
TURN   205   207  3      
STRAND   208   216  9      
HELIX   225   236  12      
TURN   237   240  4      
HELIX   241   250  10      
STRAND   255   258  4      
HELIX   259   270  12      
HELIX   278   284  7      
STRAND   285   290  6      
HELIX   301   303  3      
STRAND   315   321  7      
HELIX   326   328  3      
STRAND   333   343  11      
STRAND   345   352  8      
STRAND   361   363  3      
STRAND   369   377  9      
STRAND   379   387  9      
STRAND   389   392  4      
STRAND   395   403  9      
HELIX   406   411  6      
HELIX   415   425  11      
HELIX   434   452  19      
STRAND   459   461  3      
STRAND   465   467  3      
HELIX   469   476  8      
TURN   477   479  3      
Sequence information
Length: 486 AA [This is the length of the unprocessed precursor] Molecular weight: 54441 Da [This is the MW of the unprocessed precursor] CRC64: AA43433F83ED091D [This is a checksum on the sequence]
        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 

P11411 in FASTA format

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