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Protein

Glucose-6-phosphate 1-dehydrogenase

Gene

zwf

Organism
Leuconostoc mesenteroides
Status
Reviewed-Annotation score: 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+.UniRule annotation4 Publications

Catalytic activityi

D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH.UniRule annotation5 Publications

Kineticsi

  1. KM=114 µM for glucose 6-phosphate (with NADP)2 Publications
  2. KM=69 µM for glucose 6-phosphate (with NAD)2 Publications
  3. KM=8.0 µM for NADP2 Publications
  4. KM=160 µM for NAD2 Publications

    pH dependencei

    Optimum pH is 5.4-8.9.2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei47 – 471NADPUniRule annotation1 Publication
    Binding sitei149 – 1491NADPUniRule annotation1 Publication
    Binding sitei179 – 1791Substrate
    Binding sitei183 – 1831Substrate
    Binding sitei217 – 2171Substrate
    Binding sitei236 – 2361Substrate
    Active sitei241 – 2411Proton acceptorUniRule annotation1 Publication
    Binding sitei339 – 3391Substrate
    Binding sitei344 – 3441Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi13 – 208NADPUniRule annotation1 Publication
    Nucleotide bindingi86 – 872NADPUniRule annotation1 Publication

    GO - Molecular functioni

    GO - Biological processi

    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.
    BRENDAi1.1.1.363. 839.
    SABIO-RKP11411.
    UniPathwayiUPA00115; UER00408.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucose-6-phosphate 1-dehydrogenaseUniRule annotation (EC:1.1.1.49UniRule annotation)
    Short name:
    G6PDUniRule annotation
    Gene namesi
    Name:zwfUniRule annotation
    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 – 11Removed
    Chaini2 – 486485Glucose-6-phosphate 1-dehydrogenasePRO_0000068125Add
    BLAST

    Proteomic databases

    PRIDEiP11411.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Structurei

    Secondary structure

    1
    486
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 126Combined sources
    Turni13 – 153Combined sources
    Helixi17 – 215Combined sources
    Helixi23 – 3210Combined sources
    Beta strandi38 – 4811Combined sources
    Helixi52 – 6312Combined sources
    Helixi64 – 663Combined sources
    Helixi70 – 778Combined sources
    Beta strandi80 – 845Combined sources
    Helixi92 – 10615Combined sources
    Beta strandi113 – 1175Combined sources
    Helixi121 – 1233Combined sources
    Helixi124 – 13310Combined sources
    Beta strandi139 – 1413Combined sources
    Beta strandi143 – 1475Combined sources
    Helixi155 – 16511Combined sources
    Turni166 – 1683Combined sources
    Helixi171 – 1733Combined sources
    Beta strandi174 – 1763Combined sources
    Helixi179 – 1824Combined sources
    Helixi184 – 1885Combined sources
    Helixi189 – 1946Combined sources
    Helixi197 – 2004Combined sources
    Turni205 – 2073Combined sources
    Beta strandi208 – 2169Combined sources
    Helixi222 – 2243Combined sources
    Helixi225 – 23612Combined sources
    Turni237 – 2404Combined sources
    Helixi241 – 25010Combined sources
    Beta strandi255 – 2584Combined sources
    Helixi259 – 27012Combined sources
    Helixi278 – 2847Combined sources
    Beta strandi285 – 2906Combined sources
    Beta strandi294 – 2985Combined sources
    Helixi301 – 3033Combined sources
    Beta strandi315 – 3217Combined sources
    Helixi326 – 3283Combined sources
    Beta strandi333 – 34311Combined sources
    Beta strandi345 – 3528Combined sources
    Beta strandi361 – 3633Combined sources
    Beta strandi369 – 3779Combined sources
    Beta strandi379 – 3879Combined sources
    Beta strandi389 – 3924Combined sources
    Beta strandi395 – 4039Combined sources
    Helixi406 – 4116Combined sources
    Helixi415 – 42511Combined sources
    Helixi428 – 4303Combined sources
    Helixi434 – 45219Combined sources
    Beta strandi459 – 4613Combined sources
    Beta strandi465 – 4673Combined sources
    Helixi469 – 4768Combined sources
    Turni477 – 4793Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11411.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glucose-6-phosphate dehydrogenase family.UniRule annotation

    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

            10         20         30         40         50
    MVSEIKTLVT FFGGTGDLAK RKLYPSVFNL YKKGYLQKHF AIVGTARQAL
    60 70 80 90 100
    NDDEFKQLVR DSIKDFTDDQ AQAEAFIEHF SYRAHDVTDA ASYAVLKEAI
    110 120 130 140 150
    EEAADKFDID GNRIFYMSVA PRFFGTIAKY LKSEGLLADT GYNRLMIEKP
    160 170 180 190 200
    FGTSYDTAAE LQNDLENAFD DNQLFRIDHY LGKEMVQNIA ALRFGNPIFD
    210 220 230 240 250
    AAWNKDYIKN VQVTLSEVLG VEERAGYYDT AGALLDMIQN HTMQIVGWLA
    260 270 280 290 300
    MEKPESFTDK DIRAAKNAAF NALKIYDEAE VNKYFVRAQY GAGDSADFKP
    310 320 330 340 350
    YLEELDVPAD SKNNTFIAGE LQFDLPRWEG VPFYVRSGKR LAAKQTRVDI
    360 370 380 390 400
    VFKAGTFNFG SEQEAQEAVL SIIIDPKGAI ELKLNAKSVE DAFNTRTIDL
    410 420 430 440 450
    GWTVSDEDKK NTPEPYERMI HDTMNGDGSN FADWNGVSIA WKFVDAISAV
    460 470 480
    YTADKAPLET YKSGSMGPEA SDKLLAANGD AWVFKG
    Length:486
    Mass (Da):54,441
    Last modified:January 23, 2007 - v4
    Checksum:iAA43433F83ED091D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti154 – 1563SYD → HYI AA sequence (PubMed:3100332).Curated
    Sequence conflicti165 – 1651L → F AA sequence (PubMed:3100332).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M64446 Genomic DNA. Translation: AAA25265.1.
    PIRiA39864.

    Cross-referencesi

    Web resourcesi

    Worthington enzyme manual

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M64446 Genomic DNA. Translation: AAA25265.1.
    PIRiA39864.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry

    BindingDBiP11411.
    ChEMBLiCHEMBL1741173.

    Proteomic databases

    PRIDEiP11411.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00115; UER00408.
    BioCyciMetaCyc:MONOMER-13060.
    BRENDAi1.1.1.363. 839.
    SABIO-RKP11411.

    Miscellaneous databases

    EvolutionaryTraceiP11411.

    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]
    ProtoNetiSearch...

    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: May 27, 2015
    This is version 120 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

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.