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P11411

- G6PD_LEUME

UniProt

P11411 - G6PD_LEUME

Protein

Glucose-6-phosphate 1-dehydrogenase

Gene

zwf

Organism
Leuconostoc mesenteroides
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    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 – 471NADP1 PublicationUniRule annotation
    Binding sitei149 – 1491NADP1 PublicationUniRule annotation
    Binding sitei179 – 1791Substrate
    Binding sitei183 – 1831Substrate
    Binding sitei217 – 2171Substrate
    Binding sitei236 – 2361Substrate
    Active sitei241 – 2411Proton acceptor1 PublicationUniRule annotation
    Binding sitei339 – 3391Substrate
    Binding sitei344 – 3441Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi13 – 208NADP1 PublicationUniRule annotation
    Nucleotide bindingi86 – 872NADP1 PublicationUniRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. pentose-phosphate shunt Source: UniProtKB-HAMAP

    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-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 – 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.
    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

    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

    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:
    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: October 1, 2014
    This is version 115 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