SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P11411

- G6PD_LEUME

UniProt

P11411 - G6PD_LEUME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Glucose-6-phosphate 1-dehydrogenase
Gene
zwf
Organism
Leuconostoc mesenteroides
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone. Can utilize either NADP+ or NAD+.4 Publications

Catalytic activityi

D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH.5 Publications

Kineticsi

  1. KM=114 µM for glucose 6-phosphate (with NADP)2 Publications
  2. KM=69 µM for glucose 6-phosphate (with NAD)
  3. KM=8.0 µM for NADP
  4. KM=160 µM for NAD

pH dependencei

Optimum pH is 5.4-8.9.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei47 – 471NADP
Binding sitei149 – 1491NADP
Binding sitei179 – 1791Substrate
Binding sitei183 – 1831Substrate
Binding sitei217 – 2171Substrate
Binding sitei236 – 2361Substrate
Active sitei241 – 2411Proton acceptor1 Publication
Binding sitei339 – 3391Substrate
Binding sitei344 – 3441Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 208NADPUniRule annotation
Nucleotide bindingi86 – 872NADPUniRule annotation

GO - Molecular functioni

  1. NADP binding Source: UniProtKB-HAMAP
  2. glucose-6-phosphate dehydrogenase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. pentose-phosphate shunt Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13060.
SABIO-RKP11411.
UniPathwayiUPA00115; UER00408.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose-6-phosphate 1-dehydrogenase (EC:1.1.1.49)
Short name:
G6PD
Gene namesi
Name:zwf
OrganismiLeuconostoc mesenteroides
Taxonomic identifieri1245 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLeuconostocaceaeLeuconostoc

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi15 – 151T → A: Decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication
Mutagenesisi15 – 151T → S: Decreases catalytic efficiency toward glucose 6-phosphate (with NAD). 1 Publication
Mutagenesisi22 – 221K → E: Almost loss of activity. 2 Publications
Mutagenesisi22 – 221K → Q: Strongly decreases catalytic efficiency toward glucose 6-phosphate. 2 Publications
Mutagenesisi22 – 221K → R: Decreases catalytic efficiency toward glucose 6-phosphate. 2 Publications
Mutagenesisi47 – 471R → A: Decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication
Mutagenesisi48 – 481Q → A or E: Decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication
Mutagenesisi150 – 1501P → G or V: Strongly decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication
Mutagenesisi178 – 1781D → N: Strongly decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication
Mutagenesisi179 – 1791H → N: Strongly decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication
Mutagenesisi180 – 1801Y → F: Decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication
Mutagenesisi183 – 1831K → Q or R: Strongly decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication
Mutagenesisi241 – 2411H → N: Strongly decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication
Mutagenesisi344 – 3441K → Q or R: Strongly decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication
Mutagenesisi375 – 3751D → Q: Strongly decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication
Mutagenesisi416 – 4161Y → F: Decreases catalytic efficiency toward glucose 6-phosphate. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedUniRule annotation
Chaini2 – 486485Glucose-6-phosphate 1-dehydrogenaseUniRule annotation
PRO_0000068125Add
BLAST

Proteomic databases

PRIDEiP11411.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 126
Turni13 – 153
Helixi17 – 215
Helixi23 – 3210
Beta strandi38 – 4811
Helixi52 – 6312
Helixi64 – 663
Helixi70 – 778
Beta strandi80 – 845
Helixi92 – 10615
Beta strandi113 – 1175
Helixi121 – 1233
Helixi124 – 13310
Beta strandi139 – 1413
Beta strandi143 – 1475
Helixi155 – 16511
Turni166 – 1683
Helixi171 – 1733
Beta strandi174 – 1763
Helixi179 – 1824
Helixi184 – 1885
Helixi189 – 1946
Helixi197 – 2004
Turni205 – 2073
Beta strandi208 – 2169
Helixi222 – 2243
Helixi225 – 23612
Turni237 – 2404
Helixi241 – 25010
Beta strandi255 – 2584
Helixi259 – 27012
Helixi278 – 2847
Beta strandi285 – 2906
Beta strandi294 – 2985
Helixi301 – 3033
Beta strandi315 – 3217
Helixi326 – 3283
Beta strandi333 – 34311
Beta strandi345 – 3528
Beta strandi361 – 3633
Beta strandi369 – 3779
Beta strandi379 – 3879
Beta strandi389 – 3924
Beta strandi395 – 4039
Helixi406 – 4116
Helixi415 – 42511
Helixi428 – 4303
Helixi434 – 45219
Beta strandi459 – 4613
Beta strandi465 – 4673
Helixi469 – 4768
Turni477 – 4793

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DPGX-ray2.00A/B2-486[»]
1E77X-ray2.69A2-486[»]
1E7MX-ray2.54A2-486[»]
1E7YX-ray2.48A2-486[»]
1H93X-ray2.20A2-486[»]
1H94X-ray2.50A2-486[»]
1H9AX-ray2.16A2-486[»]
1H9BX-ray2.40A2-486[»]
2DPGX-ray2.50A2-486[»]
ProteinModelPortaliP11411.
SMRiP11411. Positions 2-486.

Miscellaneous databases

EvolutionaryTraceiP11411.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00966. G6PD.
InterProiIPR001282. G6P_DH.
IPR019796. G6P_DH_AS.
IPR022675. G6P_DH_C.
IPR022674. G6P_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR23429. PTHR23429. 1 hit.
PfamiPF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000110. G6PD. 1 hit.
PRINTSiPR00079. G6PDHDRGNASE.
TIGRFAMsiTIGR00871. zwf. 1 hit.
PROSITEiPS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11411-1 [UniParc]FASTAAdd to Basket

« Hide

MVSEIKTLVT FFGGTGDLAK RKLYPSVFNL YKKGYLQKHF AIVGTARQAL    50
NDDEFKQLVR DSIKDFTDDQ AQAEAFIEHF SYRAHDVTDA ASYAVLKEAI 100
EEAADKFDID GNRIFYMSVA PRFFGTIAKY LKSEGLLADT GYNRLMIEKP 150
FGTSYDTAAE LQNDLENAFD DNQLFRIDHY LGKEMVQNIA ALRFGNPIFD 200
AAWNKDYIKN VQVTLSEVLG VEERAGYYDT AGALLDMIQN HTMQIVGWLA 250
MEKPESFTDK DIRAAKNAAF NALKIYDEAE VNKYFVRAQY GAGDSADFKP 300
YLEELDVPAD SKNNTFIAGE LQFDLPRWEG VPFYVRSGKR LAAKQTRVDI 350
VFKAGTFNFG SEQEAQEAVL SIIIDPKGAI ELKLNAKSVE DAFNTRTIDL 400
GWTVSDEDKK NTPEPYERMI HDTMNGDGSN FADWNGVSIA WKFVDAISAV 450
YTADKAPLET YKSGSMGPEA SDKLLAANGD AWVFKG 486
Length:486
Mass (Da):54,441
Last modified:January 23, 2007 - v4
Checksum:iAA43433F83ED091D
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti154 – 1563SYD → HYI AA sequence 1 Publication
Sequence conflicti165 – 1651L → F AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M64446 Genomic DNA. Translation: AAA25265.1.
PIRiA39864.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M64446 Genomic DNA. Translation: AAA25265.1 .
PIRi A39864.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DPG X-ray 2.00 A/B 2-486 [» ]
1E77 X-ray 2.69 A 2-486 [» ]
1E7M X-ray 2.54 A 2-486 [» ]
1E7Y X-ray 2.48 A 2-486 [» ]
1H93 X-ray 2.20 A 2-486 [» ]
1H94 X-ray 2.50 A 2-486 [» ]
1H9A X-ray 2.16 A 2-486 [» ]
1H9B X-ray 2.40 A 2-486 [» ]
2DPG X-ray 2.50 A 2-486 [» ]
ProteinModelPortali P11411.
SMRi P11411. Positions 2-486.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P11411.
ChEMBLi CHEMBL1741173.

Proteomic databases

PRIDEi P11411.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00115 ; UER00408 .
BioCyci MetaCyc:MONOMER-13060.
SABIO-RK P11411.

Miscellaneous databases

EvolutionaryTracei P11411.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_00966. G6PD.
InterProi IPR001282. G6P_DH.
IPR019796. G6P_DH_AS.
IPR022675. G6P_DH_C.
IPR022674. G6P_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PANTHERi PTHR23429. PTHR23429. 1 hit.
Pfami PF02781. G6PD_C. 1 hit.
PF00479. G6PD_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000110. G6PD. 1 hit.
PRINTSi PR00079. G6PDHDRGNASE.
TIGRFAMsi TIGR00871. zwf. 1 hit.
PROSITEi PS00069. G6P_DEHYDROGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 12291.
  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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 147-188.
  3. "Glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides. Kinetic studies."
    Olive C., Geroch M.E., Levy H.R.
    J. Biol. Chem. 246:2047-2057(1971) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  4. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-22.
  5. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF THR-15; LYS-22; ARG-47; GLN-48; PRO-150; TYR-180; LYS-183; LYS-344; ASP-375 AND TYR-416.
  6. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  7. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT ASN-241 IN COMPLEX WITH NADP, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, MUTAGENESIS OF ASP-178; HIS-179 AND HIS-241.
  8. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANTS ASN-178 AND CYS-366 IN COMPLEXES WITH NAD; NADP AND GLUCOSE 6-PHOSPHATE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
  9. "NADP+ and NAD+ binding to the dual coenzyme specific enzyme Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: different interdomain hinge angles are seen in different binary and ternary complexes."
    Naylor C.E., Gover S., Basak A.K., Cosgrove M.S., Levy H.R., Adams M.J.
    Acta Crystallogr. D 57:635-648(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) IN COMPLEXES WITH NAD AND NADP.

Entry informationi

Entry nameiG6PD_LEUME
AccessioniPrimary (citable) accession number: P11411
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 114 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi