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UniProtKB/Swiss-Prot entry P11411


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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 August 1, 1992 (Sequence version 3)
Annotations were last modified on    March 21, 2006 (Entry version 63)
Name and origin of the protein
Protein name Glucose-6-phosphate 1-dehydrogenase
Synonyms EC 1.1.1.49
G6PD
Gene name
Name:  zwf
From
Leuconostoc mesenteroides  [TaxID: 1245]  
Taxonomy Bacteria; Firmicutes; Lactobacillales; Leuconostoc.
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 146-187.
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-21 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-21; ARG-46; LYS-182 AND LYS-343.
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).
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-240, AND MUTAGENESIS OF ASP-177; HIS-178 AND HIS-240.
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-177 AND CYS-365 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; A/B=1-485. [ExPASy / RCSB / EBI]
1E77; X-ray; A=1-485. [ExPASy / RCSB / EBI]
1E7M; X-ray; A=1-485. [ExPASy / RCSB / EBI]
1E7Y; X-ray; A=1-485. [ExPASy / RCSB / EBI]
1H93; X-ray; A=1-485. [ExPASy / RCSB / EBI]
1H94; X-ray; A=1-485. [ExPASy / RCSB / EBI]
1H9A; X-ray; A=1-485. [ExPASy / RCSB / EBI]
1H9B; X-ray; A=1-485. [ExPASy / RCSB / EBI]
2DPG; X-ray; @=1-485. [ExPASy / RCSB / EBI]
Detailed list of linked structures.
ModBase P11411.
Protein-protein interaction databases
DIP P11411.
2D gel databases
SWISS-2DPAGE Get region on 2D PAGE.
Organism-specific gene databases
HOGENOM [Family / Alignment / Tree]
Family and domain databases
InterPro IPR001282; G6PDH.
Graphical view of domain structure.
PANTHER PTHR10097; G6PD; 1.
PTHR10097:SF2; G6PD; 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
Key From   To  Length   Description  FTId
INIT_MET    0     0            
CHAIN    1   485   485       Glucose-6-phosphate 1-dehydrogenase.  PRO_0000068125
ACT_SITE    240   240           Proton acceptor.  
BINDING    14    14           NADP.  
BINDING    46    46           NADP.  
BINDING    178   178           Substrate.  
BINDING    182   182           Substrate.  
BINDING    343   343           Substrate.  
MUTAGEN    21    21           K->Q: Decreases Km for substrate over 30-fold.  
MUTAGEN    46    46           R->A: Strongly reduces affinity for NADP.  
MUTAGEN    177   177           D->N: Decreases Kcat over 100-fold.  
MUTAGEN    178   178           H->N: Decreases Km for substrate over 200-fold.  
MUTAGEN    182   182           K->Q: Decreases Km for substrate 1000-fold.  
MUTAGEN    240   240           H->N: Decreases Kcat over 10000-fold.  
MUTAGEN    343   343           K->Q: Decreases Km for substrate over 300-fold.  
CONFLICT    153   155           SYD -> HYI (in Ref. 2).  
CONFLICT    164   164           L -> F (in Ref. 2).  
STRAND    6    11   6        
TURN    12    14   3        
STRAND    15    15   1        
HELIX    16    20   5        
TURN    21    21   1        
HELIX    22    31   10        
TURN    32    33   2        
STRAND    34    35   2        
STRAND    37    47   11        
HELIX    51    65   15        
STRAND    67    67   1        
HELIX    69    76   8        
TURN    77    78   2        
STRAND    79    83   5        
TURN    86    87   2        
TURN    89    90   2        
HELIX    91   105   15        
TURN    106   107   2        
STRAND    110   110   1        
STRAND    112   116   5        
STRAND    118   118   1        
HELIX    120   132   13        
TURN    133   134   2        
STRAND    136   136   1        
STRAND    138   140   3        
STRAND    142   146   5        
STRAND    148   148   1        
STRAND    152   153   2        
HELIX    154   164   11        
TURN    165   167   3        
HELIX    170   172   3        
STRAND    173   175   3        
HELIX    178   181   4        
STRAND    182   182   1        
HELIX    183   193   11        
TURN    194   194   1        
HELIX    196   199   4        
TURN    200   201   2        
STRAND    202   203   2        
TURN    204   206   3        
STRAND    207   215   9        
STRAND    217   217   1        
TURN    221   222   2        
HELIX    224   235   12        
TURN    236   239   4        
HELIX    240   249   10        
STRAND    254   257   4        
HELIX    258   269   12        
TURN    270   271   2        
STRAND    272   272   1        
HELIX    277   283   7        
STRAND    284   289   6        
STRAND    293   294   2        
TURN    295   296   2        
HELIX    300   302   3        
STRAND    303   303   1        
TURN    304   305   2        
TURN    308   309   2        
STRAND    314   320   7        
STRAND    322   322   1        
STRAND    324   324   1        
HELIX    325   327   3        
TURN    328   329   2        
STRAND    332   342   11        
STRAND    344   351   8        
STRAND    360   362   3        
STRAND    368   376   9        
STRAND    378   386   9        
STRAND    388   391   4        
STRAND    394   402   9        
HELIX    405   410   6        
HELIX    414   424   11        
TURN    425   425   1        
TURN    428   429   2        
STRAND    430   431   2        
HELIX    433   451   19        
TURN    452   453   2        
STRAND    455   455   1        
STRAND    458   460   3        
TURN    462   463   2        
STRAND    464   466   3        
HELIX    468   475   8        
TURN    476   478   3        
STRAND    482   482   1        
Sequence information
Length: 485 AA [This is the length of the unprocessed precursor] Molecular weight: 54310 Da [This is the MW of the unprocessed precursor] CRC64: 9BBB5CBE7BE314BC [This is a checksum on the sequence]
        10         20         30         40         50         60 
VSEIKTLVTF FGGTGDLAKR KLYPSVFNLY KKGYLQKHFA IVGTARQALN DDEFKQLVRD 

        70         80         90        100        110        120 
SIKDFTDDQA QAEAFIEHFS YRAHDVTDAA SYAVLKEAIE EAADKFDIDG NRIFYMSVAP 

       130        140        150        160        170        180 
RFFGTIAKYL KSEGLLADTG YNRLMIEKPF GTSYDTAAEL QNDLENAFDD NQLFRIDHYL 

       190        200        210        220        230        240 
GKEMVQNIAA LRFGNPIFDA AWNKDYIKNV QVTLSEVLGV EERAGYYDTA GALLDMIQNH 

       250        260        270        280        290        300 
TMQIVGWLAM EKPESFTDKD IRAAKNAAFN ALKIYDEAEV NKYFVRAQYG AGDSADFKPY 

       310        320        330        340        350        360 
LEELDVPADS KNNTFIAGEL QFDLPRWEGV PFYVRSGKRL AAKQTRVDIV FKAGTFNFGS 

       370        380        390        400        410        420 
EQEAQEAVLS IIIDPKGAIE LKLNAKSVED AFNTRTIDLG WTVSDEDKKN TPEPYERMIH 

       430        440        450        460        470        480 
DTMNGDGSNF ADWNGVSIAW KFVDAISAVY TADKAPLETY KSGSMGPEAS DKLLAANGDA 


WVFKG 

P11411 in FASTA format

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View entry in raw text format (no links)
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